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Description:

Toll-Interleukin 1 Receptor (TIR) Domain Containing Adaptor Protein Human Recombinant

Toll-interleukin 1 receptor (TIR) domain containing adaptor protein, adapter protein wyatt, BACTS1, Mal, wyatt, Toll-like receptor adaptor protein, TIR domain-containing adapter protein, MyD88 adapter-like protein.

Product # :

PRO-1181

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Description

TIRAP Human Recombinant produced in E. coli is a single polypeptide chain containing 244 amino acids (1-221) and having a molecular mass of 26.3 kDa.TIRAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TIRAP solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Toll-interleukin1 receptor (TIR) domain containing adaptor protein (TIRAP) contains 1 TIR domain. TIRAP is an adapter molecule linked with toll-like receptors. TIRAP is required in TLR2 and TLR4 signaling pathways in the innate immune response. TIRAP activates NF-kappa-B, MAPK1, MAPK3 and JNK, which subsequently results in cytokine secretion and the inflammatory response. TIRAP is highly expressed in the liver, kidney, spleen, skeletal muscle and heart. TIRAP is also found in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.
Synonyms
Toll-interleukin 1 receptor (TIR) domain containing adaptor protein, adapter protein wyatt, BACTS1, Mal, wyatt, Toll-like receptor adaptor protein, TIR domain-containing adapter protein, MyD88 adapter-like protein.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASSTSL PAPGSRPKKP LGKMADWFRQ TLLKKPKKRP NSPESTSSDA SQPTSQDSPL PPSLSSVTSP SLPPTHASDS GSSRWSKDYD VCVCHSEEDL VAAQDLVSYL EGSTASLRCF LQLRDATPGG AIVSELCQAL SSSHCRVLLI TPGFLQDPWC KYQMLQALTE APGAEGCTIP LLSGLSRAAY PPELRFMYYV DGRGPDGGFR QVKEAVMRYL QTLS

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Angiopoietin-like Protein 4 Human Recombinant

ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.

Product # :

CYT-249

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Description

The ANGPTL4 Human Recombinant is manufactured with N-terminal fusion of His Tag. The Angiopoietin-like Protein 4 His -Tagged Fusion Protein is 25 kDa protein containing 204 amino acid residues of the Angiopoietin-like Protein 4 and 16 additional amino acid residues - His Tag (underlined).

Source

Escherichia Coli.

Formulation

Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
FIAF (fasting-induced adipose factor) a.k.a ANGPTL4 or PGAR or HFARP is an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. ANGPTL4 is found in human and mouse blood plasma both as a native protein and in a truncated form. In human white adipose tissue and SGBS adipocytes, only the native form of ANGPTL4 could be detected, whereas in mice the differentiation of mouse 3T3-L1 adipocytes is associated with the production of truncated ANGPTL4. However, the truncated ANGPTL4 is produced by human liver. In human blood plasma FIAF is mainly presented in a truncated form (FIAF-S2), whose levels treatment increases (as shown by experimental data). There is an inter individual variation in ANGPTL4 levels of both the truncated and the native form, however those levels were not influenced by prolonged semistarvation and are not associated with body mass index.
Synonyms
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Angiopoietin-like Protein 4 Human recombinant at -20°C. Aliquot the ANGPTL4 after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted ANGPTL4 can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add 0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
Amino Acid Sequence
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
Background
Angiopoietin-like Protein 4 Human Recombinant: A Promising Therapeutic Approach for Metabolic Disorders
Abstract:

Angiopoietin-like protein 4 (ANGPTL4) is a multifunctional protein involved in the regulation of lipid metabolism and energy homeostasis. It has emerged as a potential therapeutic target for metabolic disorders, including obesity, dyslipidemia, and insulin resistance. The availability of human recombinant ANGPTL4 protein has provided researchers with a valuable tool to investigate its biological functions and explore its therapeutic potential. This concise review provides an overview of the role of ANGPTL4 in metabolic regulation and discusses the potential of ANGPTL4 human recombinant protein as a therapeutic intervention.
Introduction:

Metabolic disorders are a global health challenge with significant implications for cardiovascular health. ANGPTL4, a member of the angiopoietin-like protein family, has gained attention for its role in lipid metabolism and energy balance. ANGPTL4 influences the uptake, storage, and utilization of lipids, as well as glucose metabolism, making it an attractive target for therapeutic interventions.
Mechanisms of ANGPTL4 Action:

ANGPTL4 exerts its effects through multiple mechanisms. It inhibits lipoprotein lipase (LPL) activity, reducing the hydrolysis of triglycerides and leading to elevated plasma triglyceride levels. ANGPTL4 also promotes adipose tissue lipolysis, facilitating the release of fatty acids for energy utilization. Moreover, ANGPTL4 affects glucose metabolism by modulating insulin signaling and glucose uptake in various tissues.
Role of ANGPTL4 in Metabolic Regulation:

ANGPTL4 plays a critical role in lipid and glucose metabolism. It regulates plasma lipid levels by modulating LPL activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL4 also influences energy homeostasis by promoting lipid mobilization from adipocytes and regulating fatty acid oxidation. Additionally, ANGPTL4 impacts glucose metabolism by modulating insulin sensitivity and glucose uptake in skeletal muscle and adipose tissue.
Therapeutic Potential of ANGPTL4 Human Recombinant Protein:

The availability of ANGPTL4 human recombinant protein opens new avenues for therapeutic interventions targeting metabolic disorders. Administration of ANGPTL4 recombinant protein or modulation of ANGPTL4 activity offers potential strategies to improve lipid profiles, reduce adiposity, and enhance insulin sensitivity. Preclinical studies have shown promising results, demonstrating the potential of ANGPTL4 as a therapeutic target for metabolic disorders.
Conclusion:

ANGPTL4 represents a promising target for therapeutic interventions in metabolic disorders. Its involvement in the regulation of lipid and glucose metabolism makes it an attractive candidate for the development of novel treatment approaches. The availability of ANGPTL4 human recombinant protein enables further exploration of its therapeutic potential and may contribute to the development of effective interventions for metabolic disorders.
What is the molecular weight/Mw of ANGPTL4 Protein?
ANGPTL4 Protein has a total Mw of 25kDa.

What is the source or expression system of ANGPTL4 Protein?
Escherichia Coli.

What is the Purity of ANGPTL4 Protein?
ANGPTL4 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPTL4 Protein?
The biological functionality of ANGPTL4 Protein will be determined in the future.

What is the amino acid sequence of ANGPTL4 Protein?
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.

What applications can ANGPTL4 Protein be used in?
ANGPTL4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPTL4 Protein?
The endotoxin level is minimal, ANGPTL4 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Angiopoietin-like Protein 7 Human Recombinant

angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 protein

Product # :

CYT-1208

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Description

ANGPTL7 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-346a.a) containing 553amino acids and having a molecular mass of 63.2kDa.ANGPTL7 is fused to a 233 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

ANGPTL7 protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Angiopoietin-related protein 7 (ANGPTL7), belongs to the angiopoietin-like family of molecules. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera. ANGPTL7 production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-Beta and in cartilage by TNF-alpha.
Synonyms
angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 protein
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK
Background
Angiopoietin-like Protein 7 Human Recombinant: An Emerging Player in Metabolic Regulation and Therapeutic Potential
Abstract:
Angiopoietin-like protein 7 (ANGPTL7) is a multifunctional protein that has recently gained attention for its potential role in metabolic regulation and as a therapeutic target for metabolic disorders. ANGPTL7 is involved in the modulation of lipid metabolism, adipogenesis, and insulin signaling. The availability of human recombinant ANGPTL7 protein has provided researchers with a valuable tool to unravel its biological functions and explore its therapeutic applications. This review provides an overview of the current knowledge on ANGPTL7 and discusses its potential as a therapeutic intervention in metabolic disorders.
Introduction:
Metabolic disorders, including obesity and type 2 diabetes, pose significant health challenges worldwide. ANGPTL7, a member of the angiopoietin-like protein family, has recently emerged as a potential regulator of metabolic processes. ANGPTL7 affects lipid metabolism, adipose tissue biology, and insulin signaling pathways, making it an intriguing target for therapeutic interventions in metabolic disorders.
Role of ANGPTL7 in Metabolic Regulation:
ANGPTL7 plays a multifaceted role in metabolic regulation. It influences lipid metabolism by regulating lipoprotein lipase (LPL) activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL7 also affects adipocyte biology and adipogenesis, potentially contributing to the development of obesity and related metabolic complications. Furthermore, ANGPTL7 modulates insulin signaling and glucose metabolism, suggesting its involvement in insulin resistance and diabetes pathogenesis.
Mechanisms of ANGPTL7 Action:
ANGPTL7 exerts its effects through various mechanisms. It interacts with extracellular matrix components, influencing cell adhesion and migration. ANGPTL7 also regulates angiogenesis and vascular remodeling, potentially linking it to metabolic regulation and tissue homeostasis.
Therapeutic Potential of ANGPTL7 Human Recombinant Protein:
The availability of ANGPTL7 human recombinant protein offers new avenues for therapeutic interventions in metabolic disorders. Modulating ANGPTL7 activity through recombinant protein administration or targeted interventions may have significant implications for lipid metabolism, adipose tissue function, and insulin sensitivity. Exploring ANGPTL7 as a therapeutic target holds promise for the development of novel strategies to tackle metabolic disorders.
Conclusion:
ANGPTL7 is an emerging player in metabolic regulation with potential therapeutic implications for metabolic disorders. Its involvement in lipid metabolism, adipose tissue biology, and insulin signaling pathways highlights its importance in maintaining metabolic homeostasis. The availability of ANGPTL7 human recombinant protein opens up new possibilities for further investigations and the development of targeted interventions for metabolic disorders.
What is the molecular weight/Mw of ANGPTL7 Protein?
ANGPTL7 Protein has a total Mw of 63.2kDa.

What is the source or expression system of ANGPTL7 Protein?
HEK293 cells.

What is the Purity of ANGPTL7 Protein?
ANGPTL7 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPTL7 Protein?
The biological functionality of ANGPTL7 Protein will be determined in the future.

What is the amino acid sequence of ANGPTL7 Protein?
QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK

What applications can ANGPTL7 Protein be used in?
ANGPTL7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPTL7 Protein?
The endotoxin level is minimal, ANGPTL7 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Monocyte Chemotactic Protein-1 Mouse Recombinant (CCL2)

Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11, Platelet-derived growth factor-inducible protein JE.

Product # :

CHM-313

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Description

Monocyte Chemotactic Protein-1 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14 kDa. The MCP-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity was determined by calculating its ability to chemoattract Balb/C mouse spleen MNCs at 1.0-20.0 ng/ml.

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Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acidsand a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11, Platelet-derived growth factor-inducible protein JE.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Monocyte Chemotactic Protein-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Pro-Asp-Ala-Val.
Background
What is the molecular weight/Mw of CCL2 MOUSE Protein?
CCL2 MOUSE Protein has a total Mw of 14kDa.

What is the source or expression system of CCL2 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL2 MOUSE Protein?
CCL2 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 MOUSE Protein?
The biological activity was determined by calculating its ability to chemoattract Balb/C mouse spleen MNCs at 1.0-20.0 ng/ml.

What is the amino acid sequence of CCL2 MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Pro-Asp-Ala-Val.

What applications can CCL2 MOUSE Protein be used in?
CCL2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL2 MOUSE Protein?
The endotoxin level is minimal, CCL2 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL2 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL2 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Retinol Binding Protein-4, Mouse Anti Human

Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

Product # :

ANT-371

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
Retinol binding protein 4(RBP4) belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. This protein was found to be expressed and secreted by adipose tissue, and was strongly associated with insulin resistance. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli. RBP4 delivers retinol from the liver to the peripheral tissues. In plasma, the rbp-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.
Synonyms
Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
Immunogen
Anti-human RBP4 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human RBP4 amino acids 19-201 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
PAT2B4AT.
Applications
RBP4 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1000. Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
RBP4 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Erythropoietin clone PAT1C12AT, Mouse Anti Human

EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

Product # :

ANT-744

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
EPO is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of 4 alpha helical bundles. EPO is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
Synonyms
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Physical Appearance
Sterile filtered colorless solution.
Stability
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT1C12AT.
Type
Mouse Anti Human Monoclonal.
Purification Method
EPO antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Eotaxin Rhesus Macaque Recombinant (CCL11)

Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

Product # :

CHM-022

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Shipped at Room temp

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Description

Recombinant Eotaxin Rhesus Macaque produced in E.coli cells is a non-glycosylated, homodimeric protein containing 74 amino acid chain and having a molecular mass of 8.4kDa. The Eotaxin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Eotaxin was lyophilized from a 0.2µm filtered concentrated solution in 2×PBS, pH 7.0.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood eosinophils is in a concentration range of 0.1-10.0 ng/ml corresponding to a specific activity of 1.0 × 10⁵ - 1.0 × 10⁷ IU/mg.

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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Eotaxin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Eotaxin Recombinant in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPDSVATTCC FTLTNKKIPL QRLESYRRII SGKCPQKAVI FKTKLAKDIC ADPKKKWVQD SMKYLDRKSP TPKP
Background
What is the molecular weight/Mw of EOTAXIN RHESUS MACAQUE Protein?
EOTAXIN RHESUS MACAQUE Protein has a total Mw of 8.4kDa.

What is the source or expression system of EOTAXIN RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of EOTAXIN RHESUS MACAQUE Protein?
EOTAXIN RHESUS MACAQUE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EOTAXIN RHESUS MACAQUE Protein?
Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood eosinophils is in a concentration range of 0.1-10.0 ng/ml corresponding to a specific activity of 1.0 × 105 - 1.0 × 107 IU/mg.

What is the amino acid sequence of EOTAXIN RHESUS MACAQUE Protein?
GPDSVATTCC FTLTNKKIPL QRLESYRRII SGKCPQKAVI FKTKLAKDIC ADPKKKWVQD SMKYLDRKSP TPKP

What applications can EOTAXIN RHESUS MACAQUE Protein be used in?
EOTAXIN RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EOTAXIN RHESUS MACAQUE Protein?
The endotoxin level is minimal, EOTAXIN RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

Who supplies recombinant EOTAXIN RHESUS MACAQUE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of EOTAXIN RHESUS MACAQUE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Macrophage Inflammatory Protein-1 beta Mouse Recombinant (CCL4)

Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA2, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.

Product # :

CHM-321

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Description

Macrophage Inflammatory Protein-1 beta Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7808 Dalton. The MIP-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1 mg/ml) solution in water containing no additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Mouse MIP-1 beta activity is calculated by the ability to chemoattract Human blood monocytes at 20-100ng/ml corresponding to a Specific Activity of 10,000-50,000IU/mg.

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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1? and MIP-1? that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-? from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
Synonyms
Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA2, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse MIP-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CCL4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Mouse MIP-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APYGADTPTA CCFSYSRKIP RQFIVDYFET SSLCSQPGVI FLTKRNRQIC ADSKETWVQE YITDLELNA.
Background
What is the molecular weight/Mw of MIP 1B MOUSE Protein?
MIP 1B MOUSE Protein has a total Mw of 7.8kDa.

What is the source or expression system of MIP 1B MOUSE Protein?
Escherichia Coli.

What is the Purity of MIP 1B MOUSE Protein?
MIP 1B MOUSE Protein is > 98% pure as determined by SDS-PAGE.

What is the Biological Activity of MIP 1B MOUSE Protein?
Mouse MIP-1 beta activity is calculated by the ability to chemoattract Human blood monocytes at 20-100ng/ml corresponding to a Specific Activity of 10,000-50,000IU/mg.

What is the amino acid sequence of MIP 1B MOUSE Protein?
APYGADTPTA CCFSYSRKIP RQFIVDYFET SSLCSQPGVI FLTKRNRQIC ADSKETWVQE YITDLELNA.

What applications can MIP 1B MOUSE Protein be used in?
MIP 1B MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for MIP 1B MOUSE Protein?
The endotoxin level is minimal, MIP 1B MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Neuregulin1 isoform HRG-beta3, Mouse Anti Human

Product # :

ANT-458

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
NRG1 is one of 4 proteins in the neuregulin family which act on the EGFR family of receptors. NRG1 was initially identified as a 44kDa glycoprotein that interacts with the ERBB2 receptor tyrosine kinase to increase its phosphorylation on tyrosine residues. In various brain areas, NRG1 is expressed at synaptic regions and its processing can be regulated by neuronal activity. The HRG-beta3variant of NRG1, along with HRG-alpha, beta1 and beta2 variants, was identified in various normal tissues and cancer cell lines.
Immunogen
Anti-human NRG1 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NRG1 amino acids 20-241 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
Pk1G13AT.
Applications
NRG1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
NRG1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Macrophage-Colony Stimulating Factor Mouse Recombinant

CSF-1, Lanimostim, MCSF, M-CSF.

Product # :

CYT-439

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Description

Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5x10⁵ units/mg.

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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
CSF-1, Lanimostim, MCSF, M-CSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized M-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.
Background
Macrophage-Colony Stimulating Factor Mouse Recombinant: An In-Depth Analysis
Abstract:
Macrophage-Colony Stimulating Factor (M-CSF) is a crucial cytokine involved in the regulation of macrophage biology, including their differentiation, survival, and function. This research paper provides an in-depth analysis of M-CSF Mouse Recombinant, focusing on its structure, signaling pathways, and diverse functions in the context of human research. Additionally, the paper explores the therapeutic potential of M-CSF modulation in various diseases.
Introduction:
M-CSF plays a vital role in the development and maintenance of macrophages, key immune cells involved in innate immunity and tissue homeostasis. This paper aims to provide a comprehensive analysis of M-CSF Mouse Recombinant, highlighting its importance in human macrophage biology and its potential therapeutic applications.
Structure and Function of M-CSF:
M-CSF is a homodimeric protein that binds to its receptor, CSF-1R, leading to the activation of downstream signaling pathways. It regulates the proliferation, survival, and activation of macrophages, influencing immune responses and tissue remodeling processes.
Signaling Pathways:
Upon binding to CSF-1R, M-CSF triggers various intracellular signaling pathways, including the MAPK pathway, PI3K/Akt pathway, and JAK/STAT pathway. These pathways regulate gene expression and mediate cellular responses, impacting macrophage functions.
Role in Macrophage Development and Function:
M-CSF is essential for the differentiation and maturation of macrophages from hematopoietic progenitor cells. It promotes the survival, proliferation, and activation of macrophages, enhancing their phagocytic activity, cytokine production, and antigen presentation capabilities.
Therapeutic Potential:
Given its crucial role in macrophage biology, M-CSF modulation has emerged as a potential therapeutic strategy. M-CSF inhibitors and CSF-1R antagonists have shown promise in the treatment of inflammatory and autoimmune diseases, as well as certain cancers. Targeting M-CSF signaling can modulate immune responses and affect disease progression.
Clinical Applications and Future Directions:
The therapeutic potential of M-CSF modulation is being explored in various clinical settings. Clinical trials investigating M-CSF inhibitors as monotherapy or combination therapy are underway in diseases such as rheumatoid arthritis and cancer. Future research should focus on understanding the intricate mechanisms of M-CSF signaling, optimizing therapeutic strategies, and developing personalized treatment approaches.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Stromal Cell-Derived Factor-1 beta Human Recombinant (CXCL12), His Tag

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

Product # :

CHM-249

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Description

SDF-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 93 amino acids (22-93 a.a.) and having a molecular mass of 10.8 KDa. The SDF-1b is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SDF-1 beta His Tag protein contains 20mM Tris-HCl buffer pH-8 and 10% glycerol.

Purity

Greater than 90% as determined by Analysis by SDS-PAGE.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor. The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM.
Background
What is the molecular weight/Mw of CXCL12 HUMAN BETA, HIS Protein?
CXCL12 HUMAN BETA, HIS Protein has a total Mw of 10.8kDa.

What is the source or expression system of CXCL12 HUMAN BETA, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL12 HUMAN BETA, HIS Protein?
CXCL12 HUMAN BETA, HIS Protein is > 90% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 HUMAN BETA, HIS Protein?
The biological functionality of CXCL12 HUMAN BETA, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL12 HUMAN BETA, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM.

What applications can CXCL12 HUMAN BETA, HIS Protein be used in?
CXCL12 HUMAN BETA, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL12 HUMAN BETA, HIS Protein?
The endotoxin level is minimal, CXCL12 HUMAN BETA, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL12 HUMAN BETA, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL12 HUMAN BETA, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-8 Canine Recombinant

Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8.

Product # :

CHM-009

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Shipped at Room temp

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Description

Interleukin-8 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 79 amino acids and having a molecular mass of 9.1kDa. The IL8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected murine BaF3 cells is in a concentration range of 0.15-0.75 ng/ml.

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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVLSRVSSEL RCQCIKTHST PFHPKYIKEL RVIDSGPHCE NSEIIVKLFN GNEVCLDPKE KWVQKVVQIF LKKAEKQDP.
Background
What is the molecular weight/Mw of CXCL8 CANINE Protein?
CXCL8 CANINE Protein has a total Mw of 9.1kDa.

What is the source or expression system of CXCL8 CANINE Protein?
Escherichia Coli.

What is the Purity of CXCL8 CANINE Protein?
CXCL8 CANINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 CANINE Protein?
The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected murine BaF3 cells is in a concentration range of 0.15-0.75 ng/ml.

What is the amino acid sequence of CXCL8 CANINE Protein?
AVLSRVSSEL RCQCIKTHST PFHPKYIKEL RVIDSGPHCE NSEIIVKLFN GNEVCLDPKE KWVQKVVQIF LKKAEKQDP.

What applications can CXCL8 CANINE Protein be used in?
CXCL8 CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 CANINE Protein?
The endotoxin level is minimal, CXCL8 CANINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL8 CANINE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL8 CANINE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-8 (1-72 a.a.) Human Recombinant (CXCL8)

IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

Product # :

CHM-231

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Shipped at Room temp

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Citations

Description

Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 72 amino acids and having a molecular mass of 8452 Dalton. The IL-8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL-8 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

sds-page

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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.
Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein has a total Mw of 8.45kDa.

What is the source or expression system of CXCL8 HUMAN (1-72) Protein?
Escherichia Coli.

What is the Purity of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 HUMAN (1-72) Protein?
Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CXCL8 HUMAN (1-72) Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.

What applications can CXCL8 HUMAN (1-72) Protein be used in?
CXCL8 HUMAN (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 HUMAN (1-72) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-72) Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL8 HUMAN (1-72) that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL8 HUMAN (1-72)?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Adiponectin Mouse Recombinant, Trimeric form

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-247

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Quantity :

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Shipped at Room temp

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Description

Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.

Source

HEK293 (Human embryonic kidney cell line).

Formulation

Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.

Purity

Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.

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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered white lyophilized (freeze-dried) powder.
Stability
Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.

What is the source or expression system of ADIPONECTIN Protein?
HEK293

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.

What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Tumor Necrosis Factor Receptor 13B Human Recombinant, Sf9

Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.

Product # :

CYT-982

Price :

Quantity :

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Shipped with Ice Packs

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Description

TACI produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 407 amino acids (1-165a.a.) and having a molecular mass of 45.8kDa (Molecular size on SDS-PAGE will appear at approximately 25-50kDa). TACI is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

TACI a protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADLMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYSLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Bone Morphogenetic Protein-2 Human Recombinant

BMP-2, BMP2A.

Product # :

CYT-261

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Quantity :

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Description

Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing 2x115 amino acids and having a molecular mass of 26kDa. The BMP-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP2 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM sodium citrate pH=3.5.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by its ability to induce alkaline phosphatase production by ATDC-5 cells is 0.5-1.0 µg/ml.

More Info

Introduction
BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.
Synonyms
BMP-2, BMP2A.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bone Morphogenetic Protein-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Bone Morphogenetic Protein-2 in sterile 20mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISM LYLDENEKVV LKNYQDMVVE GCGCR.
Background
What is the molecular weight/Mw of BMP2 Protein?
BMP2 Protein has a total Mw of 26kDa.

What is the source or expression system of BMP2 Protein?
Escherichia Coli.

What is the Purity of BMP2 Protein?
BMP2 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP2 Protein?
The ED50 as determined by its ability to induce alkaline phosphatase production by ATDC-5 cells is 0.5-1.0 µg/ml.

What is the amino acid sequence of BMP2 Protein?
MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISM LYLDENEKVV LKNYQDMVVE GCGCR.

What applications can BMP2 Protein be used in?
BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP2 Protein?
The endotoxin level is minimal, BMP2 Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.4 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of BMP-2 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Natural Cytotoxicity Receptor NKp46 Human Recombinant

Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.

Product # :

PRO-432

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Description

NKp46 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (22-255) and having a molecular mass of 26.6kDa. NKp46 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NKp46 (1mg/ml) contains phosphate buffered saline (pH7.4) & 1mM EDTA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.
Synonyms
Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MQQQTLPKPF IWAEPHFMVP KEKQVTICCQ GNYGAVEYQL HFEGSLFAVD RPKPPERINKVKFYIPDMNS RMAGQYSCIY RVGELWSEPS NLLDLVVTEM YDTPTLSVHP GPEVISGEEV TFYCRLDTAT SMFLLLKEGR SSHVQRGYGK VQAEFPLGPV TTAHRGTYRX FGSYNNHAWSFPSEPVKLLV TGDIENTSLA PEDPTFSADT WGTYLLTTET GLQKDHALWD HTAQN.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Apolipoprotein L 4 Human Recombinant

APOL-IV, APOLIV, Apolipoprotein L4, ApoL-IV.

Product # :

CYT-785

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Description

APOH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (1-348 a.a.) and having a molecular mass of 41.1kDa.APOH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

APOH protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

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Introduction
Apolipoprotein L 4 (APOL4) belongs to the apolipoprotein L family. APOL4 plays a role in lipid exchange and transport through the body, in addition to reverse cholesterol transport from peripheral cells to the liver. Two transcript variants encoding two different isoforms have been found for this gene. APOL4 is highly expressed in spinal cord, placenta, adrenal gland; also detected in spleen, bone marrow, uterus, trachea, mammary gland and testis
Synonyms
APOL-IV, APOLIV, Apolipoprotein L4, ApoL-IV.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGSWVQL ITSVGVQQNH PGWTVAGQFQ EKKRFTEEVI EYFQKKVSPV HLKILLTSDE AWKRFVRVAE LPREEADALY EALKNLTPYV AIEDKDMQQK EQQFREWFLK EFPQIRWKIQ ESIERLRVIA NEIEKVHRGC VIANVVSGST GILSVIGVML APFTAGLSLS ITAAGVGLGI ASATAGIASS IVENTYTRSA ELTASRLTAT STDQLEALRD ILRDITPNVL SFALDFDEAT KMIANDVHTL RRSKATVGRP LIAWRYVPIN VVETLRTRGA PTRIVRKVAR NLGKATSGVL VVLDVVNLVQ DSLDLHKGAK SESAESLRQW AQELEENLNE LTHIHQSLKA G.
Background
Clusterin Human Recombinant: Unraveling the Molecular Chaperone's Multifaceted Roles in Health and Disease
Abstract:

Clusterin, a versatile molecular chaperone, is involved in diverse physiological and pathological processes, making it an intriguing target for biomedical research. This paper provides a comprehensive analysis of Clusterin human recombinant, exploring its structure, functions, and potential applications. Understanding the intricacies of Clusterin sheds light on its significance in various biological contexts and highlights its potential as a therapeutic agent. This article offers a concise yet comprehensive examination of Clusterin, emphasizing its impact on human health.
Introduction:

The multifunctional protein Clusterin has emerged as a fascinating molecule with diverse roles in cellular homeostasis, neuroprotection, and tissue repair. This paper delves into the intricate nature of Clusterin, unveiling its structural features, molecular interactions, and involvement in various physiological processes.
Structure and Function of Clusterin:

Clusterin exhibits a complex structure, comprising multiple isoforms and domains that enable its interactions with a wide range of ligands. It functions as a molecular chaperone, aiding in protein folding, clearance of cellular debris, and regulation of apoptosis. Clusterin also plays a role in lipid transport and immune modulation.
Biological Implications of Clusterin:

Clusterin's involvement in diverse biological processes highlights its significance in health and disease. It contributes to the maintenance of tissue homeostasis, participates in neuroprotection, and influences immune responses. Moreover, Clusterin has been implicated in various diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases.
Clusterin Human Recombinant Production:

Cutting-edge biotechnological techniques, such as recombinant DNA technology and protein expression systems, allow for the production of Clusterin human recombinant. These methods facilitate large-scale production, purification, and characterization of Clusterin, offering opportunities for therapeutic applications.
Therapeutic Potential of Clusterin Human Recombinant:

Harnessing the therapeutic potential of Clusterin holds promise in various clinical scenarios. Its chaperone-like properties make it an attractive target for the development of therapies against protein misfolding diseases. Additionally, Clusterin's involvement in tissue repair and immune modulation opens avenues for therapeutic interventions in neurodegenerative diseases and cancer.
Conclusion:

Clusterin human recombinant represents a captivating field of research, unraveling the multifaceted roles of this molecular chaperone in health and disease. Understanding the structure, functions, and biological implications of Clusterin is essential in advancing our knowledge and exploring its potential therapeutic applications. Continued investigation into the mechanisms of Clusterin will likely pave the way for innovative therapeutic strategies in diverse fields of medicine.
What is the molecular weight/Mw of APOL4 Protein?
APOL4 Protein has a total Mw of 41.1kDa.

What is the source or expression system of APOL4 Protein?
Escherichia Coli.

What is the Purity of APOL4 Protein?
APOL4 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of APOL4 Protein?
The biological functionality of APOL4 Protein will be determined in the future.

What is the amino acid sequence of APOL4 Protein?
MGSSHHHHHH SSGLVPRGSH MGSMGSWVQL ITSVGVQQNH PGWTVAGQFQ EKKRFTEEVI EYFQKKVSPV HLKILLTSDE AWKRFVRVAE LPREEADALY EALKNLTPYV AIEDKDMQQK EQQFREWFLK EFPQIRWKIQ ESIERLRVIA NEIEKVHRGC VIANVVSGST GILSVIGVML APFTAGLSLS ITAAGVGLGI ASATAGIASS IVENTYTRSA ELTASRLTAT STDQLEALRD ILRDITPNVL SFALDFDEAT KMIANDVHTL RRSKATVGRP LIAWRYVPIN VVETLRTRGA PTRIVRKVAR NLGKATSGVL VVLDVVNLVQ DSLDLHKGAK SESAESLRQW AQELEENLNE LTHIHQSLKA G.

What applications can APOL4 Protein be used in?
APOL4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOL4 Protein?
The endotoxin level is minimal, APOL4 Protein was purified using conventional chromatography techniques..

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Apolipoprotein A-V Human Recombinant, HEK

Apolipoprotein A-V, Apo-AV, ApoA-V, Apolipoprotein A5, Regeneration-associated protein 3, APOA5, RAP3, APOAV.

Product # :

CYT-025

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Shipped at Room temp

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Description

APOA5 Human Recombinant Flag-Tagged Fusion Protein is 40.1 kDa protein containing 354 amino acid residues of the APOA5 Human and 11 additional amino acid residues of flagTag.

Source

HEK293

Formulation

APOA5 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 20mM TRIS and 50mM NaCl, pH 7.5

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
ApoA5 is an important regulator of serum triglyceride concentrations. An ApoA5 mouse nock-out model produced an approximately four fold increase in serum triglycerides, whereas a knock-in model human ApoA5 produced 50-70% lower concentrations of mouse serum triglycerides. Furthermore, peroxisome proliferators-activated receptoragonists, which are used clinically to lower serum triglyceride concentrations, cause increased ApoA5 mRNA expression. There is very little known about ApoA5 protein in human serum. Lately, it was established that ApoA5 is present in the human serum and it can be detected by polyclonal antibodies against both the HN2 and COOH termini, but at much lower concentration than other apolipoproteins.
Synonyms
Apolipoprotein A-V, Apo-AV, ApoA-V, Apolipoprotein A5, Regeneration-associated protein 3, APOA5, RAP3, APOAV.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized APOA5 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted APOA5 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
RKGFWDYFSQ TSGDKGRVEQ IHQQKMAREP ATLKDSLEQD LNNMNKFLEK LRPLSGSEAP RLPQDPVGMR RQLQEELEEV KARLQPYMAE AHELVGWNLE GLRQQLKPYT MDLMEQVALR VQELQEQLRV VGEDTKAQLL GGVDEAWALL QGLQSRVVHH TGRFKELFHP YAESLVSGIG RHVQELHRSV APHAPASPAR LSRCVQVLSR KLTLKAKALH ARIQQNLDQL REELSRAFAG TGTEEGAGPD PQMLSEEVRQ RLQAFRQDTY LQIAAFTRAI DQETEEVQQQ LAPPPPGHSA FAPEFQQTDS GKVLSKLQAR LDDLWEDITH SLHDQGHSHL GDPAAADYKD DDDK
Background
What is the molecular weight/Mw of APOA5 Protein?
APOA5 Protein has a total Mw of 40.1kDa.

What is the source or expression system of APOA5 Protein?
HEK293
What is the Purity of APOA5 Protein?
APOA5 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of APOA5 Protein?
The biological functionality of APOA5 Protein will be determined in the future.

What is the amino acid sequence of APOA5 Protein?
RKGFWDYFSQ TSGDKGRVEQ IHQQKMAREP ATLKDSLEQD LNNMNKFLEK LRPLSGSEAP RLPQDPVGMR RQLQEELEEV KARLQPYMAE AHELVGWNLE GLRQQLKPYT MDLMEQVALR VQELQEQLRV VGEDTKAQLL GGVDEAWALL QGLQSRVVHH TGRFKELFHP YAESLVSGIG RHVQELHRSV APHAPASPAR LSRCVQVLSR KLTLKAKALH ARIQQNLDQL REELSRAFAG TGTEEGAGPD PQMLSEEVRQ RLQAFRQDTY LQIAAFTRAI DQETEEVQQQ LAPPPPGHSA FAPEFQQTDS GKVLSKLQAR LDDLWEDITH SLHDQGHSHL GDPAAADYKD DDDK
What applications can APOA5 Protein be used in?
APOA5 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOA5 Protein?
The endotoxin level is minimal, APOA5 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Bone Morphogenetic Protein-7 Human Recombinant, Plant

Osteogenic Protein 1, BMP-7.

Product # :

CYT-039

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Shipped at Room temp

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Description

Bone Morphogenetic Protein-7 Human Recombinant produced in Plant is a monomeric, glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 16.5kDa, and fused to a 6xHis-tag at the N-terminus. The BMP-7 is purified by proprietary chromatographic techniques.

Source

Nicotiana benthamiana.

Formulation

BMP-7 was lyophilized from a solution containing Tris-HCl 0.05M buffer at pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The biological activity of BMP-7 was measured by its ability to induce alkaline phosphatase production by ATDC5 cells, ED₅₀ is less than 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

More Info

Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
Synonyms
Osteogenic Protein 1, BMP-7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMP-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP 7 Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
Lyophilized BMP-7 protein should be reconstituted in distilled water to a concentration of 50 ng/µl.
Amino Acid Sequence
HHHHHHSTGSKQRSQNRSKTPKNQEALRMANVAEN
SSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAY
YCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKP
CCAPTQLNAISVLYFDDSSVILKKYRNMVVRACGCH.
Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, Plant, Monomer, HEK
Abstract:
Welcome to our research paper exploring the incredible world of Bone Morphogenetic Protein-7 Human Recombinant, Plant, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this study, we embark on a captivating journey to unravel the wonders of BMP-7 HR and its significance in cellular differentiation. As a key member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR plays a pivotal role in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells, while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Step into the fascinating world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its crucial role in guiding cellular differentiation. Meet our trusted companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, paving the way for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatility, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR from plant sources opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.5kDa.

What is the source or expression system of BMP7 Protein?
Escherichia Coli.

What is the Purity of BMP7 Protein?
BMP7 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP7 Protein?
The biological activity of BMP-7 was measured by its ability to induce alkaline phosphatase production by ATDC5 cells, ED50 is less than 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

What is the amino acid sequence of BMP7 Protein?
HHHHHHSTGSKQRSQNRSKTPKNQEALRMANVAEN
SSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAY
YCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKP
CCAPTQLNAISVLYFDDSSVILKKYRNMVVRACGCH.

What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

B-type Natriuretic Peptide Human Recombinant

NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

Product # :

CYT-327

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Description

B-type Natriuretic Peptide Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 32 amino acids and having a molecular mass of 3,500 Dalton. NPPB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Natriuretic Peptide Precursor B was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized B-type Natriuretic Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NPPB should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized B-type Natriuretic Peptide in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
Background
What is the molecular weight / Mw of BNP Protein?
BNP Protein has a total Mw of 3.5kDa.

What is the source or expression system of BNP Protein?
Escherichia Coli.

What is the Purity of BNP Protein?
BNP Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of BNP Protein?
The biological functionality of BNP Protein will be determined in the future.

What is the amino acid sequence of BNP Protein?
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.

What applications can BNP Protein Protein be used in?
BNP Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BNP Protein?
The endotoxin level is minimal, BNP Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Uteroglobin Human Recombinant, His Tag

Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

Product # :

CYT-752

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Uteroglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 9.2kDa (calculated).

Source

Escherichia Coli.

Formulation

Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
Synonyms
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SCGB1A1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASEICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Bone Morphogenetic Protein-7 Human Recombinant, His Tag

Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.

Product # :

CYT-629

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Shipped with Ice Packs

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Description

BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
Synonyms
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK
Abstract:
Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.8kDa.

What is the source or expression system of BMP7 Protein?
Escherichia Coli.

What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.

What is the amino acid sequence of BMP7 Protein?
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.

What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Apolipoprotein-M Human Recombinant, HEK

G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

Product # :

CYT-026

Price :

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Shipping Method :

Shipped at Room temp

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Description

APOM HEK Human Recombinant Protein is 20 kDa protein containing 179 amino acid residues of the APOM Human and 13 additional amino acid residues of flag Tag.

Source

HEK293.

Formulation

APOM Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 20mM TRIS and 50mM NaCl, pH 7.5.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
APOM is belongs to the lipocalin protein family and is associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it takes part in lipid transport.
Synonyms
G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Store lyophilized APOM Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted APOM Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
HVDYKDDDDK PAGCPEHSQL TTLGVDGKEF PEVHLGQWYF IAGAAPTKEE LATFDPVDNI VFNMAAGSAP MQLHLRATIR MKDGLCVPRK WIYHLTEGST DLRTEGRPDM KTELFSSSCP GGIMLNETGQ GYQRFLLYNR SPHPPEKCVE EFKSLTSCLD SKAFLLTPRN QEACELSNN
Applications
Cell culture and/or animal studies, ELISA and Western blotting.
Background
What is the molecular weight/Mw of APOM Protein?
APOM Protein has a total Mw of 20kDa.

What is the source or expression system of APOM Protein?
HEK293.

What is the Purity of APOM Protein?
APOM Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of APOM Protein?
The biological functionality of APOM Protein will be determined in the future.

What is the amino acid sequence of APOM Protein?
HVDYKDDDDK PAGCPEHSQL TTLGVDGKEF PEVHLGQWYF IAGAAPTKEE LATFDPVDNI VFNMAAGSAP MQLHLRATIR MKDGLCVPRK WIYHLTEGST DLRTEGRPDM KTELFSSSCP GGIMLNETGQ GYQRFLLYNR SPHPPEKCVE EFKSLTSCLD SKAFLLTPRN QEACELSNN

What applications can APOM Protein be used in?
APOM Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOM Protein?
The endotoxin level is minimal, APOM Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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