Search: 625 results found for "otoraplin"

Description:

Thrombopoietin Human Recombinant

Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO

Product # :

CYT-1178

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Description

TPO Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 343 amino acids (22-353 a.a) and having a molecular mass of 36.8kDa.TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range is ≤10ng/ml. It is measured by cell proliferation assay using MO7e human megakaryocytic leukemic cells.

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Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets.
Synonyms
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO
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
DGSHMSPAPP ACDLRVLSKL LRDSHVLHSR LSQCPEVHPL PTPVLLPAVD FSLGEWKTQM EETKAQDILG AVTLLLEGVM AARGQLGPTC LSSLLGQLSG QVRLLLGALQ SLLGTQLPPQ GRTTAHKDPN AIFLSFQHLL RGKVRFLMLV GGSTLCVRRA PPTTAVPSRT SLVLTLNELP NRTSGLLETN FTASARTTGS GLLKWQQGFR AKIPGLLNQT SRSLDQIPGY LNRIHELLNG TRGLFPGPSR RTLGAPDISS GTSDTGSLPP NLQPGYSPSP THPPTGQYTL FPLPPTLPTP VVQLHPLLPD PSAPTPTPTS PLLNTSYTHS QNLSQEGHHH HHH

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:

Heat Shock Protein 90kDa Beta (GRP94) Member 1 Human Recombinant

ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.

Product # :

HSP-091

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Description

HSP90B1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 819 amino acids (22-803 a.a.) and having a molecular mass of 94.4 kDa.HSP90B1 is expressed with a 36 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GRP94 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM EDTA, 0.1M NaCl, 1mM DTT and 10% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
HSP90B1 is an abundant molecular chaperone resident endoplasmic reticulum (ER) lumenal stress protein which is part of the Hsp90 family. HSP90B1 is involved in maintaining protein homeostasis in the secretory pathway as well as functioning in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. HSP90B1 has key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90B1 protein associates with numerous cochaperones and involved in folding of newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is highly expressed in human gastric carcinoma BGC-823 cells during the whole cell cycle.
Synonyms
ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDDE VDVDGTVEED LGKSREGSRT DDEVVQREEE AIQLDGLNAS QIRELREKSE KFAFQAEVNR MMKLIINSLY KNKEIFLREL ISNASDALDK IRLISLTDEN ALSGNEELTV KIKCDKEKNL LHVTDTGVGM TREELVKNLG TIAKSGTSEF LNKMTEAQED GQSTSELIGQ FGVGFYSAFL VADKVIVTSK HNNDTQHIWE SDSNEFSVIA DPRGNTLGRG TTITLVLKEE ASDYLELDTI KNLVKKYSQF INFPIYVWSS KTETVEEPME EEEAAKEEKE ESDDEAAVEE EEEEKKPKTK KVEKTVWDWE LMNDIKPIWQ RPSKEVEEDE YKAFYKSFSK ESDDPMAYIH FTAEGEVTFK SILFVPTSAP RGLFDEYGSK KSDYIKLYVR RVFITDDFHD MMPKYLNFVK GVVDSDDLPL NVSRETLQQH KLLKVIRKKL VRKTLDMIKK IADDKYNDTF WKEFGTNIKL GVIEDHSNRT RLAKLLRFQS SHHPTDITSL DQYVERMKEK QDKIYFMAGS SRKEAESSPF VERLLKKGYE VIYLTEPVDE YCIQALPEFD GKRFQNVAKE GVKFDESEKT KESREAVEKE FEPLLNWMKD KALKDKIEKA VVSQRLTESP CALVASQYGW SGNMERIMKA QAYQTGKDIS TNYYASQKKT FEINPRHPLI RDMLRRIKED EDDKTVLDLA VVLFETATLR SGYLLPDTKA YGDRIERMLR LSLNIDPDAK VEEEPEEEPE ETAEDTTEDT EQDEDEEMDV GTDEEEETAK ESTAEKDEL.

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:

Activin-A Human Recombinant, Active

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-145

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Description

Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Formulation

Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 10⁵ units/mg.

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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.

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:

Growth and Differentiation factor 7 Mouse Recombinant

Growth/differentiation factor 7, GDF-7, Gdf7.

Product # :

CYT-946

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Shipped at Room temp

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Description

GDF7 Mouse Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 146 amino acids and having a molecular mass of 29.8kDa.The GDF-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF7 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

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 inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.

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Introduction
Growth Differentiation Factor-7 (GDF-7) belongs to the BMP family of TGF-b superfamily proteins. GDF7 elicits its bioactivity via a heterodimeric receptor complex comprised of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor. GDF7 signaling results in the phosphorylation and activation of Smad proteins. GDF-7 is also involved in tendon and ligament formation and repair. In addition, GDF7 regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance.
Synonyms
Growth/differentiation factor 7, GDF-7, Gdf7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-7 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 GDF-7 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.
Background
What is the molecular weight/Mw of GDF7 Protein?
GDF7 Protein has a total Mw of 29.8kDa.

What is the source or expression system of GDF7 Protein?
Escherichia Coli.

What is the Purity of GDF7 Protein?
GDF7 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF7 Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.

What is the amino acid sequence of GDF7 Protein?
TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.

What applications can GDF7 Protein be used in?
GDF7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF7 Protein?
The endotoxin level is minimal, GDF7 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:

Galectin-4 Mouse Recombinant

gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 4.

Product # :

CYT-187

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Description

LGALS4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-326a.a) and having a molecular mass of 38.8kDa.LGALS4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LGALS4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.

SDS-PAGE

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Introduction
Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 & IL-17.
Synonyms
gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 4.
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 MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.
Background
What is the molecular weight/Mw of LGALS4 MOUSE Protein?
LGALS4 MOUSE Protein has a total Mw of 38.8kDa.

What is the source or expression system of LGALS4 MOUSE Protein?
Escherichia Coli.

What is the Purity of LGALS4 MOUSE Protein?
LGALS4 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS4 MOUSE Protein?
The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.

What is the amino acid sequence of LGALS4 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.

What applications can LGALS4 MOUSE Protein be used in?
LGALS4 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS4 MOUSE Protein?
The endotoxin level is minimal, LGALS4 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:

Adiponectin (108-244 a.a.) Human Recombinant

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

Product # :

CYT-073

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sds-page
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Description

Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Acrp30 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

sds-page

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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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 MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN.
Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 18.1kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >80% 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 is the amino acid sequence of ADIPONECTIN Protein? MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN..

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:

MIG Human Recombinant (CXCL9)

Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.

Product # :

CHM-333

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

MIG (monokine induced by gamma-INF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 103 amino acids and having a molecular mass of 11700 Dalton. The MIG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.

Purity

Greater than 97.0% 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 peripheral blood T-lymphocytes is in a concentration range of 10-100 ng/ml.

More Info

Introduction
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belonging to the CXC chemokine family that is also known as Monokine induced by gamma INF (MIG). CXCL9 is a T-cell chemoattractant, which is induced by IFN-?. It is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
Synonyms
Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL9 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 MIG in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TPVVRKGRCSCISTNQGTIHLQSLKDLKQFAPSPSCEKIEIIATLKNGVQTCLNPDS
ADVKELIKKWEKQVSQKKKQKNGKKHQKKKVLKVRKSQRSRQKKTT.
Background
What is the molecular weight/Mw of CXCL9 HUMAN Protein?
CXCL9 HUMAN Protein has a total Mw of 11.7kDa.

What is the source or expression system of CXCL9 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL9 HUMAN Protein?
CXCL9 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL9 HUMAN Protein?
The biological activity determined by a chemotaxis bioassay using human peripheral blood T-lymphocytes is in a concentration range of 10-100 ng/ml.

What is the amino acid sequence of CXCL9 HUMAN Protein?
TPVVRKGRCSCISTNQGTIHLQSLKDLKQFAPSPSCEKIEIIATLKNGVQTCLNPDS
ADVKELIKKWEKQVSQKKKQKNGKKHQKKKVLKVRKSQRSRQKKTT.

What applications can CXCL9 HUMAN Protein be used in?
CXCL9 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL9 HUMAN Protein?
The endotoxin level is minimal, CXCL9 HUMAN 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:

Macrophage Inflammatory Protein-3 alpha Mouse Recombinant (CCL20)

Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.

Product # :

CHM-236

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Quantity :

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Description

Macrophage Inflammatory Protein-3 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.9 kDa. The MIP-3a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The Activity is calculated by its ability to chemoattract primary human T cells at 2-20ng/ml, corresponding to a specific activity of 50,000-500,000 units/mg.

More Info

Introduction
CCL20 is a chemotactic factor that draws lymphocytes & neutrophils, rather than monocytes. MIP-3 alpha inhibits proliferation of myeloid progenitors in colony formation assays. MIP3A plays a role in the formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. CCL20 holdes antibacterial activity e.coli atcc 25922 and s.aureus atcc 29213. CCL20 gene transcription is activated by H. pylori, which activates NF-kappaB through intracellular signal pathway which involves IkappaB kinase and NF-kappaB-inducing kinase. MIP-3 alpha is invloved in chemokine-mediated lymphocyte trafficking during gastric inflammation in Helicobacter infection. CCL20 expression is involved in the recruitment of CD45R0-positive T cell subsets into the intestinal lamina propria.
MIP-3A is in charge of the advancement of pulpal inflammation through the recruitment of C-C motif Receptor 6-expressing lymphocytes Vaginal epithelial cells respond to factors present in semen by secreting MIP-3 alpha, which increases langerhans cells recruitment during HIV transmission.
Synonyms
Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-3a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL-20 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 MIP-3a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ASNYDCCLSY IQTPLPSRAI VGFTRQMADE ACDINAIIFH TKKRKSVCAD PKQNWVKRAV NLLSLRVKKM.
Background
What is the molecular weight/Mw of CCL20 MOUSE Protein?
CCL20 MOUSE Protein has a total Mw of 7.9kDa.

What is the source or expression system of CCL20 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL20 MOUSE Protein?
CCL20 MOUSE Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL20 MOUSE Protein?
The Activity is calculated by its ability to chemoattract primary human T cells at 2-20ng/ml, corresponding to a specific activity of 50,000-500,000 units/mg.

What is the amino acid sequence of CCL20 MOUSE Protein?
ASNYDCCLSY IQTPLPSRAI VGFTRQMADE ACDINAIIFH TKKRKSVCAD PKQNWVKRAV NLLSLRVKKM.

What applications can CCL20 MOUSE Protein be used in?
CCL20 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL20 MOUSE Protein?
The endotoxin level is minimal, CCL20 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:

Macrophage Inflammatory protein-3 (CCL19) Human Recombinant, T7 Tag

Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433, Epstein-Barr virus-induced molecule 1 ligand chemokine, EBI1-ligand chemokine.

Product # :

CHM-374

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Description

MIP3b Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (22-98 a.a.) and having a molecular mass of 10.4kDa.MIP3b is fused to a 16 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MIP3b protein solution (0.5mg/ml) containing Phosphate Buffered Saline pH7.4 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Chemokine (C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). CCL19 is expressed abundantly in thymus and lymph nodes, with moderate levels in trachea and colon and low levels in stomach, small intestine, lung, kidney and spleen. The gene for CCL19 is located on human chromosome 9. This chemokine elicits its effects on its target cells by binding to the chemokine receptor chemokine receptor CCR7. It attracts certain cells of the immune system, including dendritic cells and antigen-engaged B cells.
Synonyms
Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433, Epstein-Barr virus-induced molecule 1 ligand chemokine, EBI1-ligand chemokine.
Physical Appearance
Sterile Filtered clear 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
MASMTGGQQM GRGSHMGTND AEDCCLSVTQ KPIPGYIVRN FHYLLIKDGC RVPAVVFTTL RGRQLCAPPD QPWVERIIQR LQRTSAKMKR RSS.
Background
What is the molecular weight/Mw of CCL19 HUMAN, T7 Protein?
CCL19 HUMAN, T7 Protein has a total Mw of 10.4kDa.

What is the source or expression system of CCL19 HUMAN, T7 Protein?
Escherichia Coli.

What is the Purity of CCL19 HUMAN, T7 Protein?
CCL19 HUMAN, T7 Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL19 HUMAN, T7 Protein?
The biological functionality of CCL19 HUMAN, T7 Protein will be determined in the future.

What is the amino acid sequence of CCL19 HUMAN, T7 Protein?
MASMTGGQQM GRGSHMGTND AEDCCLSVTQ KPIPGYIVRN FHYLLIKDGC RVPAVVFTTL RGRQLCAPPD QPWVERIIQR LQRTSAKMKR RSS.

What applications can CCL19 HUMAN, T7 Protein be used in?
CCL19 HUMAN, T7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL19 HUMAN, T7 Protein?
The endotoxin level is minimal, CCL19 HUMAN, T7 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:

Agouti–Related Protein Human Recombinant

ART, AGRT, ASIP2, MGC118963, AGRP.

Product # :

HOR-283

Price :

Quantity :

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Shipped at Room temp

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Description

The Human Agouti-related protein is created as a recombinant protein with N-terminal fusion of His Tag.The Human Agouti-related protein His-Tagged Fusion Protein, produced in E. coli, is 14.4 kDa (calculated) protein containing 112 amino acid residues of the human AGRP and 16 additional amino acid residues - His Tag, thrombin cleavage site (highlighted).The AGRP is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AGRP protein was lyophilized from 0.5mg/ml in 5mM TRIS, 25mM NaCl, pH 7.5.

Purity

Purity of Agouti–related protein recombinant human is >95% as determined by SDS-PAGE.

More Info

Introduction
Agouti-related protein is an endogenous antagonist of hypothalamic alpha-melanocortin receptors MC3R and MC4R with potent orexigenic activity. Although a complete deletion of the AGRP gene does not produce any significant metabolic phenotypes, reduction in AGRP expression by RNA interference is associated with increased metabolic rate along with reduced weight gain. In hypothalamus, it is produced by neurons in the medial portion of arcuate nucleus, which produce also the potent orexigenic peptide Neuropeptide Y (NP-Y). Another site of central AGRP production is the hypothalamic nucleus. AGRP encompasses 132 amino acid residues and its alpha-melanocortin inhibiting activity results in a 34 amino acid cystine knot domain within the C-terminal (87-132) portion of the protein. Both AGRP and NP-Y expression was shown to be suppressed by leptin. Central administration of AGRP induces hyperphagia and increased gain in body weight in rodents, but may also exert metabolic effects even when hyperphagia is prevented. In the absence of hyperphagia, intracerebralventricular administration of AGRP caused significant increases in plasma leptin and insulin concentrations (twofold and 1.5-fold, respectively) and fat pad mass.
In the periphery, AGRP mRNA was found in adrenal glands, lung, testis, ovary, skeletal muscle and adipose tissue in humans or rodents. In the adrenals, it was shown that AGRP antagonizes glucosteroid production mediated by MC4R. AGRP could then modulate locally the functions of some peripheral tissues such as adrenals.
In human and rat serum, detectable levels of AGRP-like activity were reported in the lower picogram range. The serum AGRP levels were elevated in obese humans compared to lean controls and increased with fasting in rats.
Synonyms
ART, AGRT, ASIP2, MGC118963, AGRP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized AGRP 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
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MKHHHHHHHM LVPRGSAQMG LAPMEGIRRP DQALLPELPG LGLRAPLKKT TAEQAEEDLL QEAQALAEVL DLQDREPRSS RRCVRLHESC LGQQVPCCDP CATCYCRFFN AFCYCRKLGT AMNPCSRT.

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:

Septin-3 Human Recombinant

Septin 3, SEP3, Neuronal-Specific Septin 3, Neuronal-Specific Septin-3, BK250D10.3, Neuronal-specific septin-3.

Product # :

PRO-2152

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Description

SEPT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 43.1kDa. SEPT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SEPT3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Septin-3, also known as SEPT3 is a member of the septin family of GTPases. Members of this family are essential for cytokinesis. Furthermore, expression is up regulated by retinoic acid in a human teratocarcinoma cell line. The exact role of SEPT3 has not been determined yet. In addition, among its related pathways are Bacterial invasion of epithelial cells.
Synonyms
Septin 3, SEP3, Neuronal-Specific Septin 3, Neuronal-Specific Septin-3, BK250D10.3, Neuronal-specific septin-3.
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 MGSMSKGLPE TRTDAAMSEL VPEPRPKPAV PMKPMSINSN LLGYIGIDTI IEQMRKKTMK TGFDFNIMVV GQSGLGKSTL VNTLFKSQVS RKASSWNREE KIPKTVEIKA IGHVIEEGGV KMKLTVIDTP GFGDQINNEN CWEPIEKYIN EQYEKFLKEE VNIARKKRIP DTRVHCCLYF ISPTGHSLRP LDLEFMKHLS KVVNIIPVIA KADTMTLEEK SEFKQRVRKE LEVNGIEFYP QKEFDEDLED KTENDKIRQE SMPFAVVGSD KEYQVNGKRV LGRKTPWGII EVENLNHCEF ALLRDFVIRT HLQDLKEVTH NIHYETYRAK RLNDNGGLPP GEGLLGTVLP PVPATPCPTA E.

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:

Alpha Synuclein A53T Human Recombinant

Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

Product # :

PRO-159

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Description

A-Synuclein A53T Human Recombinant which is a Parkinson’s disease-related point mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A53T is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5) and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.

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:

IFN-Tau Ovine Recombinant

IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.

Product # :

CYT-377

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Quantity :

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Shipped at Room temp

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Description

IFN-Tau Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19914.7 Dalton.The IFN-Tau is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from (1mg/ml) solution containing PBS pH-7.4.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.

More Info

Introduction
IFN-tau is also known as TP-1 (trophoblast protein-1) is a new class of type I IFN that is secreted by the trophoblast and is the signal for maternal recognition of pregnancy in sheep. IFN- tau has potent immunosuppressive and antiviral activities similar to other type I IFN but is less cytotoxic than IFN-alpha and IFN-beta. The current investigation concerns the effect of recombinant ovine IFN- tau (rOIFN- tau) on the modulation of MHC class I and II expression on cloned mouse cerebrovascular endothelial (CVE) cells.
IFN-tau induced tyrosine phosphorylation of Stat1 and upregulated the expression of MHC class I on CVE. One proposed action by which type I IFN reduces the relapse rate in MS is via interference with IFN-?-induced MHC class II expression. IFN- tau was shown to downregulate IFN-?-induced MHC class II expression on CVE and, hence, may be of potential therapeutic value in downregulating inflammation in the central nervous system (CNS). IFN- tau did not upregulate the expression of MHC class II on CVE. IFN- tau also inhibited the replication of Theiler's virus in CVE.
Synonyms
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-Tau although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Tau 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 IFN Tau 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 Cys-Tyr-Leu-Ser-Arg.
Background
What is the molecular weight/Mw of IFN TAU OVINE Protein?
IFN TAU OVINE Protein has a total Mw of 19.9kDa.

What is the source or expression system of IFN TAU OVINE Protein?
Escherichia Coli.

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

What is the Biological Activity of IFN TAU OVINE Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.

What is the amino acid sequence of IFN TAU OVINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.

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

What is the endotoxin level for IFN TAU OVINE Protein?
The endotoxin level is minimal, IFN TAU OVINE 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:

Insulin-Like Growth Factor Binding Protein-7 Human Recombinant

Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.

Product # :

CYT-788

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Recombinant Human IGFBP7 produced in E.coli cells is a non-glycosylated, homodimeric protein containing 2x256 amino acid chains and having a molecular mass of 26.4kDa. The IGFBP-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IGFBP7 was lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.5 and 150mM NaCl.

Purity

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

More Info

Introduction
Insulin-like Growth Factor-Binding Protein 7 (IGFBP7) is a member of the IGFBP family. IGFBP family members are all cysteine rich proteins with conserved cysteine and have an IGFBP domain, a Kazal-like domain and an Ig-like C2-type domain. IGFBP7 is expressed in a broad range of normal human tissues and it mostly shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. IGFBP7 has a role in skeletal myogenesis by binding to IGF in a manner which inhibits IGF induced differentiation of skeletal myoblasts, without disturbing IGF induced proliferation. Moreover, IGFBP7 suppresses growth and colony formation of prostate and breast cancer cell lines via an IGF independent mechanism, which triggers a delay in the G1 phase of the cell cycle, and increased apoptosis.
Synonyms
Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGFBP7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP-7 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 IGFBP-7 in sterile 20mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SSSDTCGPCE PASCPPLPPL GCLLGETRDA CGCCPMCARG EGEPCGGGGA GRGYCAPGME CVKSRKRRKG KAGAAAGGPG VSGVCVCKSR YPVCGSDGTT YPSGCQLRAA SQRAESRGEK AITQVSKGTC EQGPSIVTPP KDIWNVTGAQ VYLSCEVIGI PTPVLIWNKV KRGHYGVQRT ELLPGDRDNL AIQTRGGPEK HEVTGWVLVS PLSKEDAGEY ECHASNSQGQ ASASAKITVV DALHEIPVKK GEGAEL.
Background
What is the molecular weight/Mw of IGFBP7 HUMAN Protein?
IGFBP7 HUMAN Protein has a total Mw of 26.4kDa.

What is the source or expression system of IGFBP7 HUMAN Protein?
Escherichia Coli.

What is the Purity of IGFBP7 HUMAN Protein?
IGFBP7 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IGFBP7 HUMAN Protein?
The biological functionality of IGFBP7 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IGFBP7 HUMAN Protein?
SSSDTCGPCE PASCPPLPPL GCLLGETRDA CGCCPMCARG EGEPCGGGGA GRGYCAPGME CVKSRKRRKG KAGAAAGGPG VSGVCVCKSR YPVCGSDGTT YPSGCQLRAA SQRAESRGEK AITQVSKGTC EQGPSIVTPP KDIWNVTGAQ VYLSCEVIGI PTPVLIWNKV KRGHYGVQRT ELLPGDRDNL AIQTRGGPEK HEVTGWVLVS PLSKEDAGEY ECHASNSQGQ ASASAKITVV DALHEIPVKK GEGAEL.

What applications can IGFBP7 HUMAN Protein be used in?
IGFBP7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGFBP7 HUMAN Protein?
The endotoxin level is minimal, IGFBP7 HUMAN 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:

BCA-1/BLC Mouse Recombinant (CXCL13)

C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.

Product # :

CHM-030

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

CXCL13 Mouse Recombinant (22-109) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10kDa.The BCA-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The BCA1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

More Info

Introduction
BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.
Synonyms
C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA1 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 CXCL13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.
Background
What is the molecular weight/Mw of CXCL13 MOUSE Protein?
CXCL13 MOUSE Protein has a total Mw of 10kDa.

What is the source or expression system of CXCL13 MOUSE Protein?
Escherichia Coli.

What is the Purity of CXCL13 MOUSE Protein?
CXCL13 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL13 MOUSE Protein?
The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

What is the amino acid sequence of CXCL13 MOUSE Protein?
ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.

What applications can CXCL13 MOUSE Protein be used in?
CXCL13 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL13 MOUSE Protein?
The endotoxin level is minimal, CXCL13 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL13 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 CXCL13 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:

Interleukin-1 alpha Mouse Recombinant

Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

Product # :

CYT-523

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Interleukin-1A Mouse Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 156 amino acids and having a molecular mass of 17.9 kDa. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS, pH=7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependant stimulation of murine D10S cells is < 0.002 ng/ml.

More Info

Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS.
Background
What is the molecular weight/Mw of IL1A MOUSE Protein?
IL1A MOUSE Protein has a total Mw of 17.9kDa.

What is the source or expression system of IL1A MOUSE Protein?
Escherichia Coli.

What is the Purity of IL1A MOUSE Protein?
IL1A MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A MOUSE Protein?
The biological functionality of IL1A MOUSE Protein will be determined in the future.

What is the amino acid sequence of IL1A MOUSE Protein?
SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS.
What applications can IL1A MOUSE Protein be used in?
IL1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A MOUSE Protein?
The endotoxin level is minimal, IL1A 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:

Interleukin-1 alpha Mouse Recombinant, His Tag

Interleukin-1 alpha, IL-1 alpha, Il1a.

Product # :

CYT-848

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

IL 1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.4kDa.IL 1 alpha is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IL 1 alpha protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Interleukin-1 alpha, IL-1 alpha, Il1a.
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 MGSSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQIS.
Background
What is the molecular weight/Mw of IL1A MOUSE, HIS Protein?
IL1A MOUSE, HIS Protein has a total Mw of 20.4kDa.

What is the source or expression system of IL1A MOUSE, HIS Protein?
Escherichia Coli.

What is the Purity of IL1A MOUSE, HIS Protein?
IL1A MOUSE, HIS Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A MOUSE, HIS Protein?
The biological functionality of IL1A MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1A MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQIS.

What applications can IL1A MOUSE, HIS Protein be used in?
IL1A MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A MOUSE, HIS Protein?
The endotoxin level is minimal, IL1A MOUSE, HIS 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:

Interleukin-28A Human Recombinant

Interleukin-28A, IL-28A, IFN-Lambda 2, IFN-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.

Product # :

CYT-602

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

IL-28A human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 19.6 kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 μm filtered solution containing no additives.

Purity

Greater than 85% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
IL-28A is distantly related to type I IFNs and the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
Synonyms
Interleukin-28A, IL-28A, IFN-Lambda 2, IFN-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-Lambda 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 2 Recombinant 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-28A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPVAR LHGALPDARG CHIAQFKSLS PQELQAFKRAKDALEESLLL KDCRCHSRLF PRTWDLRQLQ VRERPMALEA ELALTLKVLE ATADTDPALV DVLDQPLHTL HHILSQFRAC IQPQPTAGPR TRGRLHHWLY RLQEAPKKES PGCLEASVTFNLFRLLTRDL NCVASGDLCV.

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-28A Mouse Recombinant

IFN-lambda-2, Interleukin-28A, IL-28A, Ifnl2, Il28a, EG330496.

Product # :

CYT-741

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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biological activity
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Description

Recombinant Mouse Interleukin-28A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a total molecular mass of 19.7kDa.The IL-28A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse IL-28A is lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 and 5% trehalose.

Purity

Greater than 95% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by an anti-viral assay using human HepG2 cells infected with encephalomyocarditis(EMC) virus is less than 3 ng/ml, corresponding to a specific activity of > 3.3 × 10⁵ IU/mg.

More Info

Introduction
IL-28A is distantly related to the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
Synonyms
IFN-lambda-2, Interleukin-28A, IL-28A, Ifnl2, Il28a, EG330496.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-Lambda 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 2 Recombinant 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-28A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DPVPRATRLP VEAKDCHIAQ FKSLSPKELQ AFKKAKDAIE KRLLEKDMRC SSHLISRAWD LKQLQVQERP KALQAEVALT LKVWENMTDS ALATILGQPL HTLSHIHSQL QTCTQLQATA EPKPPSRRLS RWLHRLQEAQ SKETPGCLED SVTSNLFRLL TRDLKCVASG DQCV.

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-28B Mouse Recombinant

Interferon lambda-3, IFN-lambda-3, Interleukin-28B, IL-28B, Ifnl3, Il28, Il28b.

Product # :

CYT-732

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

IL-28B Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.6kDa.The IL28B is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL28B protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by an anti-viral assay using human HepG2 cells infected with encephalomyocarditis is less than 30 ng/ml, corresponding to a specific activity of > 3.3 × 10⁴ IU/mg.

More Info

Introduction
IL-28B is a cytokine remotely related to type I interferons and the IL-10 family. Interleukin-28B, interleukin 28A (IL28A), and interleukin 29 (IL29) are 3 closely related cytokine genes which form a cytokine gene cluster on a chromosomal region mapped to 19q13. Expression of the cytokines encoded by these 3 genes can be induced by viral infection. All 3 cytokines interact with a heterodimeric class II cytokine receptor which consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha (IL28RA).
Synonyms
Interferon lambda-3, IFN-lambda-3, Interleukin-28B, IL-28B, Ifnl3, Il28, Il28b.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-28B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL28B 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-28B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DPVPRATRLP VEAKDCHIAQ FKSLSPKELQ AFKKAKGAIE KRLLEKDMRC SSHLISRAWD LKQLQVQERP KALQAEVALT LKVWENINDS ALTTILGQPL HTLSHIHSQL QTCTQLQATA EPKPPSRRLS RWLHRLQEAQ SKETPGCLED SVTSNLFQLL LRDLKCVASG DQCV.

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:

Syntaxin-4 Human Recombinant

Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.

Product # :

PRO-1176

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Quantity :

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Shipped with Ice Packs

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Description

STX4 Human Recombinant produced in E. coli is a single polypeptide chain containing 300 amino acids (1-275) and having a molecular mass of 34.7 kDa.STX4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The STX4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Syntaxin 4 (STX4) is a member of the syntaxin/epimorphin family of proteins. The Syntaxin family is cellular receptors for transport vesicles which participate in exocytosis in neutrophils. Syntaxin 4 is vital for normal regulation of glucose metabolism uptake in skeletal muscle and decline in STX4 protein levels lead to reduction of whole-body hormone-stimulated glucose metabolism. STX4 is expressed in neutrophils and neutrophil-differentiated HL-60 cells. The STX4 expression in neutrophils increases with differentiation.
Synonyms
Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.
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 MGSHMMRDRT HELRQGDDSS DEEDKERVAL VVHPGTARLG SPDEEFFHKV RTIRQTIVKL GNKVQELEKQ QVTILATPLP EESMKQELQN LRDEIKQLGR EIRLQLKAIE PQKEEADENY NSVNTRMRKT QHGVLSQQFV ELINKCNSMQ SEYREKNVER IRRQLKITNA GMVSDEELEQ MLDSGQSEVF VSNILKDTQV TRQALNEISA RHSEIQQLER SIRELHDIFT FLATEVEMQG EMINRIEKNI LSSADYVERG QEHVKTALEN QKKARKKKVL

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:

Parkinson Disease Protein 7 Mouse Recombinant

Protein deglycase DJ-1, Parkinson disease protein 7 homolog.

Product # :

PRO-2226

Price :

Quantity :

Shipping Method :

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source
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Description

PARK7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189 a.a) and having a molecular mass of 22.4kDa. PARK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PARK7 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).
Synonyms
Protein deglycase DJ-1, Parkinson disease protein 7 homolog.
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 MGSMASKRAL VILAKGAEEM ETVIPVDVMR RAGIKVTVAG LAGKDPVQCS RDVMICPDTS LEDAKTQGPY DVVVLPGGNL GAQNLSESPM VKEILKEQES RKGLIAAICA GPTALLAHEV GFGCKVTTHP LAKDKMMNGS HYSYSESRVE KDGLILTSRG PGTSFEFALA IVEALVGKDM ANQVKAPLVL KD.

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-17D Human Recombinant

Interleukin 17D, Interleukin 27, IL-17D, IL-27, IL27, Interleukin-17D, Interleukin-27, IL17D.

Product # :

CYT-876

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Interleukin-17D Human Recombinant (18-202) produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 polypeptide chains of 185 amino acids each and having a molecular mass of 40kDa.The IL-17D is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

Immobilized rHuIL-17D binds to rHuIL-17BR with EC₅₀ less than 2µg/ml.

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Introduction
IL17D modulates immune responses indirectly by stimulating the production of myeloid growth factors and chemokines, as well as suppressing the proliferation of myeloid progenitors. IL17D is expressed in the skeletal muscle, heart, adipose tissue, lung, pancreas, and nervous system. Among IL-17 family members, IL17D is most closely related to IL17B, sharing 27% aa sequence identity. The treatment of endothelial cells with IL17D cytokine stimulates the production of other cytokines including IL6, IL8 and CSF2/ GM-CSF. The increased expression of IL8 induced by IL17D cytokine is NF-kappa B-dependent.
Synonyms
Interleukin 17D, Interleukin 27, IL-17D, IL-27, IL27, Interleukin-17D, Interleukin-27, IL17D.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL17D although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-17D 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-17D in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APRAGRRPAR PRGCADRPEE LLEQLYGRLA AGVLSAFHHT LQLGPREQAR NASCPAGGRP ADRRFRPPTN LRSVSPWAYR ISYDPARYPR YLPEAYCLCR GCLTGLFGEE DVRFRSAPVY MPTVVLRRTP ACAGGRSVYT EAYVTIPVGC TCVPEPEKDA DSINSSIDKQ GAKLLLGPND APAGP.

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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