Search: 1000 results found for "other cytokines"

Description:

Epithelial Neutrophil-Activating Protein 78 Rat Recombinant (CXCL5)

C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

Product # :

CHM-267

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Description

Epithelial Neutrophil-Activating Protein 78 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids and having a molecular mass of 10.0kDa.The CXCL5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.

Purity

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

Biological Activity

Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

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Introduction
Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.
Synonyms
C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ENA-78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.
Background
What is the molecular weight/Mw of CXCL5 RAT Protein?
CXCL5 RAT Protein has a total Mw of 10.0kDa.

What is the source or expression system of CXCL5 RAT Protein?
Escherichia Coli.

What is the Purity of CXCL5 RAT Protein?
CXCL5 RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL5 RAT Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

What is the amino acid sequence of CXCL5 RAT Protein?
APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.

What applications can CXCL5 RAT Protein be used in?
CXCL5 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL5 RAT Protein?
The endotoxin level is minimal, CXCL5 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL5 RAT 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 CXCL5 RAT?
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:

Serum Amyloid A (APO-SAA) Human Recombinant

Product # :

CYT-942

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Description

APO-SAA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 104 amino acids and having a molecular mass of 11.7kDa. Recombinant Apo-SAA is a consensus SAA molecule corresponding to human Apo-SAA1a, except for the presence of an N-terminal methionine, the substitution of asparagine for aspartic acid at position 60, and arginine for histidine at position 71 (the latter two substituted residues are present in Apo-SAA2b).The Human APO-SAA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Human SAA was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris-HCl, pH 9.0 and 150mM NaCl.

Purity

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

Biological Activity

The biological activity determined by its ability to down-regulate lipid biosynthesis in aortic smooth muscle cells. The effective concentration was found to be 4µM.

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Introduction
Serum amyloid A protein which is a member of the SAA family is encoded by the SAA gene in humans. SAA is expressed by the liver and secreted in plasma. Serum amyloid A is the main acute phase reactant and apolipoprotein of the HDL complex. Elevated serum SAA protein levels may be linked with lung cancer. The level of Apo-SAA, which is ordinarily 1-5 ?g/ml in plasma, increases 500-1000 fold within 24 hours of an inflammatory stimulus and, under these conditions, is the most abundant HDL Apolipoprotein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human SAA 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 SAA Human in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RSFFSFLGEA FDGARDMWRA YSDMREANYI GSDKYFHARG NYDAAKRGPG GVWAAEAISN ARENIQRFFG RGAEDSLADQ AANEWGRSGK DPNHFRPAGL PEKY.

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-Cell Maturation Antigen Human Recombinant

BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.

Product # :

CYT-598

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Description

TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.3 kDa. The TNFRSF17 is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

1mg of TNFRSF17 Human contain 20mM sodium phosphate buffer, pH-7.4, and 130mM NaCl.

Purity

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

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Introduction
TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.
Synonyms
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFRSF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFRSF17 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 TNFRSF17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AGQCSQNEYF DSLLHACIPC QLRCSSNTPP LTCQRYCNAS VTNSVKGTNA.

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:

TNF Ligand Receptor Superfamily Member 25 Recombinant Human

Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

Product # :

CYT-980

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Description

TNFRSF25 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 417 amino acids (25-199) and having a molecular mass of 46.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF25 is fused to a 242 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF25 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Biological Activity

Determined by the binding ability in a functional ELISA with Human VEGI (CAT# cyt-589). The ED50 range ≤ 5ug/ml.

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Introduction
TNF Ligand Receptor Superfamily Member 25 (TNFRSF25) belongs to the TNF receptor superfamily that binds to the TNF-like protein TL1A. TNFRSF25 interacts directly with the adapter TRADD and regulates lymphocyte homeostasis. TNFRSF25 is also mediates activation of NF-kappa-B and induces apoptosis. TNFRSF25 signals are vital to exert T helper cell 2 effector activity in Th2-polarized CD4 cells and co-stimulate interleukin-13 production by glycosphingolipid-activated NKT cells.
Synonyms
Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.
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
ADPQGGTRSP RCDCAGDFHK KIGLFCCRGC PAGHYLKAPC TEPCGNSTCL VCPQDTFLAW ENHHNSECAR CQACDEQASQ VALENCSAVA DTRCGCKPGW FVECQVSQCV SSSPFYCQPC LDCGALHRHT RLLCSRRDTD CGTCLPGFYE HGDGCVSCPT STLGSCPERC AAVCGWRQLE 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:

Apolipoprotein C-I Human Recombinant

Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.

Product # :

CYT-812

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Description

APOC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids (27-83 a.a.) and having a molecular mass of 9.0kDa. APOC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

APOC1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

sds-page

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Introduction
Apolipoprotein C-I (APOC1) which expressed mainly in the liver is a part of the apolipoprotein C family. APOC1 which is usually found in plasma and responsible for the activation of esterified lechitin cholesterol takes an important part in the exchange of esterified cholesterol among lipoproteins and in removal of cholesterol from tissues. APOC1 is activated when monocytes differentiate into macrophages. APOC1 protein’s main role is to inhibit CETP by altering the electric charge of HDL molecules. APOC1 is also binds free fatty acids and reduces their intracellular esterification.
Synonyms
Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.
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
MGSSHHHHHH SSGLVPRGSH MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.
Background
Apolipoprotein C-I Human Recombinant: Unraveling the Complexity of Lipid Regulation
Abstract:
Apolipoprotein C-I (ApoC-I) is a remarkable protein that plays a significant role in lipid metabolism and cardiovascular health. It is primarily synthesized in the liver and is associated with lipoproteins involved in lipid transport. This research paper aims to provide a comprehensive overview of ApoC-I human recombinant, shedding light on its physiological functions, production methods, and potential therapeutic applications. By delving into the intricacies of ApoC-I, we can gain valuable insights into its role as a key player in lipid regulation and its potential as a therapeutic target.
Introduction:
The prevalence of lipid disorders and cardiovascular diseases necessitates a deeper understanding of the mechanisms governing lipid metabolism. ApoC-I, a critical component of lipoproteins, offers unique insights into the regulation of lipid levels and its implications for cardiovascular health.
Structure and Function of Apolipoprotein C-I:
ApoC-I exhibits a complex molecular structure, comprising functional domains that enable its interaction with lipoproteins. It plays a crucial role in regulating lipoprotein metabolism by inhibiting the activity of lipoprotein lipase and modulating the clearance of triglyceride-rich lipoproteins.
Regulation of Apolipoprotein C-I Expression:
The synthesis and secretion of ApoC-I are tightly regulated processes influenced by various factors, including nutritional status and hormonal signals. Understanding the regulatory mechanisms underlying ApoC-I expression can provide insights into its role in maintaining lipid homeostasis.
Apolipoprotein C-I and Cardiovascular Diseases:
Dysregulation of ApoC-I has been associated with various lipid disorders and cardiovascular diseases. Altered levels of ApoC-I have been observed in conditions such as hypertriglyceridemia and atherosclerosis, highlighting its potential as a biomarker for cardiovascular risk assessment.
Production of Apolipoprotein C-I Human Recombinant:
Recombinant ApoC-I can be produced using advanced biotechnological approaches, including recombinant DNA technology and protein expression systems. These methods enable large-scale production, purification, and characterization of ApoC-I, facilitating its potential therapeutic applications.
Therapeutic Potential of Apolipoprotein C-I Human Recombinant:
Targeting ApoC-I opens up exciting avenues for therapeutic interventions in lipid disorders and cardiovascular diseases. Modulating ApoC-I expression or function holds promise for restoring lipid balance and reducing the risk of cardiovascular complications.
Conclusion:
Apolipoprotein C-I human recombinant represents a fascinating area of research in the field of lipid metabolism and cardiovascular health. By unraveling the intricate interplay between ApoC-I, lipoproteins, and cardiovascular diseases, we can pave the way for novel therapeutic strategies and improved risk assessment. Further studies are required to fully understand the therapeutic potential of ApoC-I human recombinant and translate these findings into clinical applications.
What is the molecular weight/Mw of APOC1 Protein?
APOC1 Protein has a total Mw of 9kDa.

What is the source or expression system of APOC1 Protein?
Escherichia Coli.

What is the Purity of APOC1 Protein?
APOC1 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of APOC1 Protein?
The biological functionality of APOC1 Protein will be determined in the future.

What is the amino acid sequence of APOC1 Protein?
MGSSHHHHHH SSGLVPRGSH MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.

What applications can APOC1 Protein be used in?
APOC1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOC1 Protein?
The endotoxin level is minimal, APOC1 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:

CTLA-4 (CD152), Hamster Anti-Mouse

GSE, CD152, IDDM12, CELIAC3, CTLA-4.

Product # :

ANT-116

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Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.
Synonyms
GSE, CD152, IDDM12, CELIAC3, CTLA-4.
Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
mixture of mouse activated T cells.
Ig Subclass
Hamster IgG.
Clone
RYNmCTLA-4.
Applications
Blocking and staining antibody. For staining, use for blocking CTLA-4 function should be determined by the investigator.
Available Conjugates
This antibody is only available as purified antibody.
Type
Hamster Anti Mouse Monoclonal.
Storage Procedures
Lyophilized: store at 4oC. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion exchange column.

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 Mouse Anti Human, (NYRhEPO)

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

Product # :

ANT-196

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Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein 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.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human erythropoietin.
Ig Subclass
Mouse IgG1.
Clone
NYRhEPO.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion exchange.

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 11 Human Recombinant, His Tag

Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.

Product # :

CYT-887

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Shipped with Ice Packs

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Description

GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
Synonyms
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
Background
What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.

What is the source or expression system of GDF11 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF11 HUMAN, HIS Protein?
The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.

What applications can GDF11 HUMAN, HIS Protein be used in?
GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF11 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF11 HUMAN, 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:

Betacellulin Human Recombinant

Product # :

CYT-330

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Quantity :

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Description

Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Betacellulin Human Recombinant was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Betacellulin Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC 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
It is recommended to reconstitute the lyophilized BTC Human in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY
Background
Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine
Introduction
In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.
BTC: The Architect of Cellular Revitalization
BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.
Crafting the Alchemist: Pioneering Methodologies
Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.
Unveiling the Biological Tapestry
Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.
A Flourish of Results
The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.
Charting a Transformative Future
As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.
What is the molecular weight/Mw of BTC Protein?
BTC Protein has a total Mw of 9kDa.

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

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

What is the Biological Activity of BTC Protein?
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

What is the amino acid sequence of BTC Protein?
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

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

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

TRAIL/APO 2 Ligand (114-281 a.a.) Human Recombinant

Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

Product # :

CYT-546

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Soluble TNF-related apoptosis-inducing ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (114-281) and having a molecular mass of 19.6 kDa. The sTRAIL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1mg/ml in 20mM Tris-HCl pH-7.5, 300mM NaCl, 0.1mM DTT & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26.
TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Physical Appearance
Sterile Filtered colorless liquid.
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
MVRERGPQRV AAHITGTRGR SNTLSSPNSK NEKALGRKIN SWESSRSGHS FLSNLHLRNGELVIHEKGFY YIYSQTYFRF QEEIKENTKN DKQMVQYIYK YTSYPDPILL MKSARNSCWSKDAEYGLYSI YQGGIFELKE NDRIFVSVTN EHLIDMDHEA SFFGAFLVG.

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:

RELM-Beta Human Recombinant

Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

Product # :

CYT-780

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

RELM-b Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 19kDa. RELM-b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RELM-b was lyophilized from a solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.
Synonyms
Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized RELM-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM-b Human 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 RELM-b in sterile 0.1% TFA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQCSLDSVMD KKIKDVLNSL EYSPSPISKK LSCASVKSQG RPSSCPAGMA VTGCACGYGC GSWDVQLETT CHCQCSVVDW TTARCCHLT.

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:

BAFF (BLyS) Receptor Human Recombinant, HEK

TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

Product # :

CYT-1224

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

BAFFR Human Recombinant is a single, glycosylated, polypeptide chain (1-78 a.a) containing a total of 314 amino acids and having a molecular mass of 34.4 kDa. BAFFR is fused to 233 a.a hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The BAFFR solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

More Info

Synonyms
TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.
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
DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.
Background
B-cell Activating Factor (BAFF) and its corresponding receptor, BAFF-R, are integral components of the immune system, orchestrating crucial processes in B-cell survival, maturation, and differentiation. As we delve into the intricate world of immunology, the study of BAFF and its receptor has unveiled essential pathways that govern the immune responses in health and disease. This research investigates the multifaceted role of BAFF Receptor Protein, shedding light on its structural complexities, signaling mechanisms, and its pivotal contributions to immune regulation. By exploring the interactions between BAFF and its receptor, scientists aim to decipher the delicate balance that underlies immune homeostasis and explore potential therapeutic avenues.
Structural Architecture of BAFF Receptor Protein:
BAFF Receptor, a transmembrane protein predominantly expressed on B cells, belongs to the tumor necrosis factor receptor (TNFR) superfamily. Its intricate structure involves various domains, each playing a unique role in ligand binding, receptor activation, and downstream signaling. Understanding the structural intricacies of BAFF Receptor is paramount to unraveling the molecular events that govern B-cell fate decisions and immune responses.
Physiological Significance in B-Cell Biology:
BAFF Receptor, upon binding with its ligand BAFF, initiates a cascade of events critical for B-cell survival and function. This interaction promotes B-cell maturation, prevents premature apoptosis, and influences the formation of immune synapses. Additionally, BAFF Receptor signaling is tightly regulated to prevent excessive B-cell activation, ensuring immune tolerance and preventing autoimmune responses. Disruptions in these pathways can lead to autoimmune disorders, underscoring the crucial role of BAFF Receptor in maintaining immune equilibrium.
Regulation of Immune Responses:
BAFF Receptor signaling not only affects B-cell development but also has broader implications for immune responses. By modulating antibody production, B-cell activation, and immune memory, BAFF Receptor plays a vital role in shaping adaptive immunity. Its dysregulation has been implicated in various autoimmune conditions, making it an attractive target for therapeutic interventions aimed at restoring immune balance.
BAFF Receptor as a Therapeutic Target:
The intricate involvement of BAFF Receptor in autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, has positioned it as a promising therapeutic target. Researchers are exploring monoclonal antibodies and other targeted therapies that aim to modulate BAFF Receptor signaling, providing a new frontier in autoimmune disease management. Additionally, understanding the BAFF-BAFF Receptor axis offers potential insights into the development of vaccines and immunotherapies, fostering innovative approaches in the fight against infectious diseases and malignancies.
BAFF Receptor Protein, as a key player in immune regulation, embodies the complexities of immunology. Its interactions with BAFF orchestrate fundamental processes in B-cell biology and adaptive immunity. As scientists unravel the intricate signaling pathways and structural nuances of BAFF Receptor, they pave the way for novel therapeutic strategies and innovative treatments for autoimmune disorders and beyond. This research not only deepens our understanding of immune regulation but also holds the promise of transformative advancements in immunotherapy, ultimately shaping the future of immune-related healthcare.
What is the molecular weight/Mw of BAFF-R Protein?
BAFF-R Protein has a total Mw of 34.4kDa.

What is the source or expression system of BAFF-R Protein?
HEK293 Cells.

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

What is the Biological Activity of BAFF-R Protein?
The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

What is the amino acid sequence of BAFF-R Protein?
DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.

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

What is the endotoxin level for BAFF-R Protein?
The endotoxin level is minimal, BAFF-R 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:

Beta Defensin-2 Human Recombinant

BD-2, hBD-2, Defensin beta 2, Skin-antimicrobial peptide 1, SAP1, DEFB4, DEFB102, DEFB2, DEFB4P, Beta-defensin 2.

Product # :

CYT-571

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Beta Defensin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.3 kDa. The BD-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Human BD-2 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution containing 20mM PB pH-7.4 and 130mM NaCl.

Purity

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

Biological Activity

Determined by the ability to chemoattract human dendritic immature cells at a concentration of 10-100ng/ml.

More Info

Synonyms
BD-2, hBD-2, Defensin beta 2, Skin-antimicrobial peptide 1, SAP1, DEFB4, DEFB102, DEFB2, DEFB4P, Beta-defensin 2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-2 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-2 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 Beta Defensin-2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GIGDPVTCLK SGAICHPVFC PRRYKQIGTC GLPGTKCCKK P.
Background
Beta Defensin-2 Human Recombinant: Unveiling its Role in Innate Immunity and Therapeutic Potential
Abstract:

Beta Defensin-2 (BD-2), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-2 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-2 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-2, highlighting its impact on innate immunity and its therapeutic potential.
Introduction:

Innate immunity serves as the first line of defense against invading pathogens. BD-2, a key antimicrobial peptide within the defensin family, plays a vital role in immune responses at epithelial surfaces. This paper provides an overview of BD-2, shedding light on its structure, function, and therapeutic potential.
BD-2 Structure and Function:

BD-2 is a cationic peptide that exhibits a conserved cysteine motif, conferring its antimicrobial activity. It acts by disrupting microbial cell membranes, exerting a broad spectrum of antimicrobial effects against bacteria, fungi, and viruses. Additionally, BD-2 possesses immunomodulatory properties, regulating inflammatory responses and promoting wound healing.
Antimicrobial Properties and Therapeutic Applications:

BD-2 demonstrates potent antimicrobial activity against a wide range of pathogens, including drug-resistant strains. Its ability to combat biofilm formation and enhance immune cell recruitment makes it a promising candidate for developing novel antimicrobial therapies. Furthermore, BD-2's immunomodulatory effects hold potential in treating inflammatory disorders.
Therapeutic Potential of BD-2 Human Recombinant:

BD-2 human recombinant offers exciting prospects in immunotherapy. Strategies aimed at enhancing BD-2 expression or delivering exogenous BD-2 may boost innate immune responses in individuals with compromised immunity or chronic infections. BD-2-based therapeutics could be developed for wound healing, infectious diseases, and inflammatory conditions.
Challenges and Future Directions:

While BD-2 shows great promise, challenges remain. Further research is needed to optimize delivery methods of BD-2 and evaluate its safety and efficacy in clinical settings. Understanding the interplay between BD-2 and other immune factors will enable the development of synergistic therapies for enhanced therapeutic outcomes.
Conclusion:

BD-2 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-2 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize immunotherapy and improve patient outcomes.
What is the molecular weight/Mw of BD2 Protein?
BD2 Protein has a total Mw of 4.3kDa.

What is the source or expression system of BD2 Protein?
Escherichia Coli.

What is the Purity of BD2 Protein?
BD2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD2 Protein?
Determined by the ability to chemoattract human dendritic immature cells at a concentration of 10-100ng/ml.

What is the amino acid sequence of BD2 Protein?
GIGDPVTCLK SGAICHPVFC PRRYKQIGTC GLPGTKCCKK P.

What applications can BD2 Protein be used in?
BD2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD2 Protein?
The endotoxin level is minimal, BD2 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:

Beta Defensin-2 Mouse Recombinant

Beta-defensin 2, BD-2, mBD-2, Defensin beta 2, Defb2, MGC129140, MGC129141.

Product # :

CYT-035

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

Beta Defensin-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5.5kDa. The BD-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse BD-2 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

Purity

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

Biological Activity

Determined by the ability to chemoattract immature human dendritic cells at a concentration of 10-100ng/ml.

More Info

Introduction
The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
BBeta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.
Variation in human Beta Defensin-1 contributes to asthma diagnosis, with apparent gender-specific effects. Human Beta Defensin-3 is a dimer, while Human BD-1 and Human BD-2 are monomeric. The expression of Human BD1 is correlated with induction profiles in gingival keratinocytes.
The level of expression of human DEFB1 mRNA is lower than that of human BD3 and human BD-2 in reconstructed epidermis.
Human BD1 is down-regulated in human prostatic and renal carcinomas.
Synonyms
Beta-defensin 2, BD-2, mBD-2, Defensin beta 2, Defb2, MGC129140, MGC129141.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-2 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-2 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 Beta Defensin-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K.
Background
What is the molecular weight/Mw of BD2 Protein?
BD2 Protein has a total Mw of 5.5kDa.

What is the source or expression system of BD2 Protein?
Escherichia Coli.

What is the Purity of BD2 Protein?
BD2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD2 Protein?
Determined by the ability to chemoattract immature human dendritic cells at a concentration of 10-100ng/ml.

What is the amino acid sequence of BD2 Protein?
AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K.

What applications can BD2 Protein be used in?
BD2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD2 Protein?
The endotoxin level is minimal, BD2 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 (72-244) Human Recombinant

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

Product # :

CYT-1231

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

The Adiponectin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 24kDa protein containing 173 amino acid residues of the Acrp30 Human, 72-244 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Adiponectin 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
IGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN
Background
Adiponectin is a protein produced and secreted by adipose tissue. Adiponectin takes part in regulating glucose levels as well as fatty acid breakdown.
Adiponectin ‘s Functions:
Anti-Inflammatory Effects - Adiponectin has anti-inflammatory properties that helps mitigate chronic inflammation.
Regulation of Glucose and Lipid Metabolism - Adiponectin Enhances insulin sensitivity, helping in regulation of blood sugar levels and also promotes fatty acid oxidation, which helps reduce fat accumulation.
Cardiovascular Health - It may influence vascular health and is associated with a lower risk of cardiovascular diseases.
Levels and Health Implications:
Normal Levels - usually, higher levels of adiponectin are associated with a lower risk of metabolic syndrome, cardiovascular diseases and type 2 diabetes.
Low Levels - Reduced adiponectin levels are often linked with obesity, insulin resistance, and other metabolic disorders.
Factors Influencing on the Adiponectin Levels:
Weight - High body fat (especially visceral fat) can lower adiponectin levels.
Diet and Exercise - Regular physical activity and a healthy diet can increase adiponectin levels.
Genetics - Genetic factors might also be an influence on an individual adiponectin level.
Adiponectin is an important component in metabolic health, therefore continuing the research of its functions and regulation keeps advance our understanding of its role in diseases like diabetes and cardiovascular conditions.
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

What is the Purity of ADIPONECTIN Protein?
ADIPONECTINProtein is >90% 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?
IGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN.

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:

Serum Amyloid A (APO-SAA) Feline Recombinant

Product # :

CYT-1221

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

SAA Feline produced in E.coli is a single, non-glycosylated polypeptide chain (1-111 a.a) containing 121 a.a and having a molecular mass of 13,838 Dalton. SAA s fused with a 10 amino acids His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SAA was lyophilized from 0.01M HCl (pH 2.0).

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serum Amyloid A (APO-SAA) 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 SAA in 0.01M HCl (pH 2.0) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
In response to infection, injury, or inflammation, SAA levels rapidly rise in the bloodstream. Acting as a chemoattractant, SAA recruits immune cells to the site of injury, facilitating the innate immune response. Additionally, SAA modulates the activities of immune cells, influencing cytokine production and phagocytosis. These immunomodulatory functions highlight SAA's significance in shaping the immune landscape during inflammatory events. SAA participates in lipid metabolism by interacting with HDL particles. In the acute-phase response, SAA displaces apolipoprotein A1 from HDL, transforming it into a pro-inflammatory particle. This alteration in HDL composition affects its cardioprotective functions, potentially contributing to atherosclerosis and cardiovascular diseases. Understanding these interactions is crucial for deciphering the intricate relationship between inflammation and cardiovascular health.

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 Type Human Recombinant, His Tag

Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, Tumor necrosis factor receptor type I, TNF-R1, TNF-RI, TNFR-I, p60, p55, CD120a, TNFRSF1A, TNFAR, TNFR1, FPF, TBP1, TNF-R, p55-R, TNFR55, TNFR60, TNF-R-I, TNF-R55, MGC19588.

Product # :

CYT-673

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

TNFR Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 161 amino acids fragment (41-201) having a molecular weight of 22.68kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TNFR His Tag is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFR His Tag protein is supplied in 1xPBS, 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene.
Synonyms
Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, Tumor necrosis factor receptor type I, TNF-R1, TNF-RI, TNFR-I, p60, p55, CD120a, TNFRSF1A, TNFAR, TNFR1, FPF, TBP1, TNF-R, p55-R, TNFR55, TNFR60, TNF-R-I, TNF-R55, MGC19588.
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. Please avoid freeze thaw cycles.
Amino Acid Sequence
DSVCPQGKYIHPQNNSICCTKCHKGTYLYNDCPGPGQ
DTDCRECESGSFTASENHLRHCLSCSKCRKEMGQVE
ISSCTVDRDTVCGCRKNQYRHYWSENLFQCFNCSLCL
NGTVHLSCQEKQNTVCTCHAGFFLRENECVSCSNCKK
SLECTKLCLPQIEN.

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:

Leukemia Inhibitory Factor Human Recombinant, His tag

CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

Product # :

CYT-1082

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Description

LIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 23-202) containing 189 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 20.9kDa (calculated).

Source

Escherichia Coli.

Formulation

LIF filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 20 mM Tris buffer, 20 mM NaCl and 5% w/v trehalose, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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.
Amino Acid Sequence
MKHHHHHHAS PLPITPVNAT CAIRHPCHNN LMNQIRSQLA QLNGSANALF ILYYTAQGEP FPNNLDKLCG PNVTDFPPFH ANGTEKAKLV ELYRIVVYLG TSLGNITRDQ KILNPSALSL HSKLNATADI LRGLLSNVLC RLCSKYHVGH VDVTYGPDTS GKDVFQKKKL GCQLLGKYKQ IIAVLAQAF.

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:

Lymphotactin (XCL1) Mouse Recombinant

XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

Product # :

CHM-037

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Quantity :

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Description

Lymphotactin (XCL1) Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.1kDa.Lymphotactin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm 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.

Biological Activity

The ED50 as determined by a chemotaxis bioassay using human XCR1 transfected murine BaF3 cells is < 100 ng/ml, corresponding to a specific activity of > 1.0 × 10⁴ IU/mg.

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Introduction
XCL1 is a small cytokine belongs to the XC chemokine family that is also known as lymphotactin. XCL1 is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized XCL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lymphotactin 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 Lymphotactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VGTEVLEESS CVNLQTQRLP VQKIKTYIIW EGAMRAVIFV TKRGLKICAD PEAKWVKAAI KTVDGRASTR KNMAETVPTG AQRSTSTAIT LTG.
Background
What is the molecular weight/Mw of LYMPHOTACTIN MOUSE Protein?
LYMPHOTACTIN MOUSE Protein has a total Mw of 10.1kDa.

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

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

What is the Biological Activity of LYMPHOTACTIN MOUSE Protein?
The ED50 as determined by a chemotaxis bioassay using human XCR1 transfected murine BaF3 cells is < 100 ng/ml, corresponding to a specific activity of > 1.0 × 104 IU/mg.

What is the amino acid sequence of LYMPHOTACTIN MOUSE Protein?
VGTEVLEESS CVNLQTQRLP VQKIKTYIIW EGAMRAVIFV TKRGLKICAD PEAKWVKAAI KTVDGRASTR KNMAETVPTG AQRSTSTAIT LTG.

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

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

Who supplies recombinant LYMPHOTACTIN 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 LYMPHOTACTIN 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:

4-1BB Receptor Human Recombinant, His Tag

Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor T-cell, antigen 4-1BB homolog, T-cell antigen ILA, CD137 antigen, CDw137, ILA, 4-1BB, MGC2172, 4-1BBR, TNFRSF9.

Product # :

CYT-137

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Description

4-1BBR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (18-186 a.a) and having a molecular mass of 20kDa.4-1BBR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

4-1BBR 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% as determined by SDS-PAGE.

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Introduction
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.
Synonyms
Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor T-cell, antigen 4-1BB homolog, T-cell antigen ILA, CD137 antigen, CDw137, ILA, 4-1BB, MGC2172, 4-1BBR, TNFRSF9.
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
MGSSHHHHHH SSGLVPRGSH MGSMFERTRS LQDPCSNCPA GTFCDNNRNQ ICSPCPPNSF SSAGGQRTCD ICRQCKGVFR TRKECSSTSN AECDCTPGFH CLGAGCSMCE QDCKQGQELT KKGCKDCCFG TFNDQKRGIC RPWTNCSLDG KSVLVNGTKE RDVVCGPSPA DLSPGASSVT
PPAPAREPGH SPQ.

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 differentiation factor 5 Mouse Recombinant, His Tag

Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.

Product # :

CYT-852

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Description

GDF5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (376-495 a.a) and having a molecular mass of 16kDa.GDF5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
Synonyms
Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.
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 MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.
Background
What is the molecular weight/Mw of GDF5 MOUSE Protein?
GDF5 MOUSE Protein has a total Mw of 16kDa.

What is the source or expression system of GDF5 MOUSE Protein?
Escherichia Coli.

What is the Purity of GDF5 MOUSE Protein?
GDF5 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF5 MOUSE Protein?
The biological functionality of GDF5 MOUSE Protein will be determined in the future.

What is the amino acid sequence of GDF5 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.

What applications can GDF5 MOUSE Protein be used in?
GDF5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF5 MOUSE Protein?
The endotoxin level is minimal, GDF5 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:

Angiopoietin Like Protein 3 Human Recombinant, HEK

Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.

Product # :

CYT-766

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

ANGPTL3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 17-460) containing a total of 450 amino acids, having a molecular mass of 52.6kDa (calculated) and fused to a 6 aa His tag at C-Terminus.The Human ANGPTL3 is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.
Synonyms
Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.
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.
Solubility
It is recommended to add deionized water to a working concentration of 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 in the cell culture.
Amino Acid Sequence
SRIDQDNSSF DSLSPEPKSR FAMLDDVKIL ANGLLQLGHG LKDFVHKTKG QINDIFQKLN IFDQSFYDLS LQTSEIKEEE KELRRTTYKL QVKNEEVKNM SLELNSKLES LLEEKILLQQ KVKYLEEQLT NLIQNQPETP EHPEVTSLKT FVEKQDNSIK DLLQTVEDQY KQLNQQHSQI KEIENQLRRT SIQEPTEISL SSKPRAPRTT PFLQLNEIRN VKHDGIPAEC TTIYNRGEHT SGMYAIRPSN SQVFHVYCDV ISGSPWTLIQ HRIDGSQNFN ETWENYKYGF GRLDGEFWLG LEKIYSIVKQ SNYVLRIELE DWKDNKHYIE YSFYLGNHET NYTLHLVAIT GNVPNAIPEN KDLVFSTWDH KAKGHFNCPE GYSGGWWWHD ECGENNLNGK YNKPRAKSKP ERRRGLSWKS QNGRLYSIKS TKMLIHPTDS ESFEHHHHHH.
Background
What is the molecular weight/Mw of ANGPTL3 Protein?
ANGPTL3 Protein has a total Mw of 52.6kDa.

What is the source or expression system of ANGPTL3 Protein?
HEK 293.

What is the Purity of ANGPTL3 Protein?
ANGPTL3 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPTL3 Protein?
The biological functionality of ANGPTL3 Protein will be determined in the future.

What is the amino acid sequence of ANGPTL3 Protein?
SRIDQDNSSF DSLSPEPKSR FAMLDDVKIL ANGLLQLGHG LKDFVHKTKG QINDIFQKLN IFDQSFYDLS LQTSEIKEEE KELRRTTYKL QVKNEEVKNM SLELNSKLES LLEEKILLQQ KVKYLEEQLT NLIQNQPETP EHPEVTSLKT FVEKQDNSIK DLLQTVEDQY KQLNQQHSQI KEIENQLRRT SIQEPTEISL SSKPRAPRTT PFLQLNEIRN VKHDGIPAEC TTIYNRGEHT SGMYAIRPSN SQVFHVYCDV ISGSPWTLIQ HRIDGSQNFN ETWENYKYGF GRLDGEFWLG LEKIYSIVKQ SNYVLRIELE DWKDNKHYIE YSFYLGNHET NYTLHLVAIT GNVPNAIPEN KDLVFSTWDH KAKGHFNCPE GYSGGWWWHD ECGENNLNGK YNKPRAKSKP ERRRGLSWKS QNGRLYSIKS TKMLIHPTDS ESFEHHHHHH.

What applications can ANGPTL3 Protein be used in?
ANGPTL3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPTL3 Protein?
The endotoxin level is minimal, ANGPTL3 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 Hormone-1, Mouse Anti Human

GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

ANT-230

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% sodium azide.

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered solution.
Immunogen
GH Antibody is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant Growth hormone.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PG3H5AT.
Applications
The GH antibody has been tested by ELISA and by Western blot analysis to assure specificity and reactivity. Since application vary, however, each investigation should titrate the reagent to obtain optimal results. Recommended dilution range for Western blot analysis: 1:500 ~ 1:1000. Recommended starting dilution: 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
GH 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:

Angiopoietin-like Protein 7 Mouse Recombinant

Angiopoietin-related protein 7, Angiopoietin-like protein 7.

Product # :

CYT-914

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Description

ANGPTL7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 324 amino acids (22-337 a.a.) and having a molecular mass of 37.5kDa. ANGPTL7 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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-related protein 7, Angiopoietin-like protein 7.
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
QKPHKRKTQL KAAGCCEEMR ELKAQVANLS SLLGELSRKQ ESDWVSVVMQ VMELESSSKH MESRLSTAES KYSEMNNQID IMQLQAAQTV TQTSADAIYD CSSLYQKNYR ISGVYKLPPD EFLGSPELEV FCDMETSGGG WTIIQRRKSG LVSFYQDWRQ YKQGFGSIRG DFWLGNEHIH RLTRQPSRLR VELEDWEGNA RYAEYSYFAL GNELNSYRLF LGNYSGNVGK DALLYHNNTV FSTKDKDNDN CLDKCAQLRK GGYWYNCCTD SNLNGVYYRL GEHRKHMDGI SWYGWHGANY SLKRVEMKIR PEAFKPLEHH HHHH.
Background
What is the molecular weight/Mw of ANGPTL7 Protein?
ANGPTL7 Protein has a total Mw of 37.5kDa.

What is the source or expression system of ANGPTL7 Protein?
Sf9, Baculovirus 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?
QKPHKRKTQL KAAGCCEEMR ELKAQVANLS SLLGELSRKQ ESDWVSVVMQ VMELESSSKH MESRLSTAES KYSEMNNQID IMQLQAAQTV TQTSADAIYD CSSLYQKNYR ISGVYKLPPD EFLGSPELEV FCDMETSGGG WTIIQRRKSG LVSFYQDWRQ YKQGFGSIRG DFWLGNEHIH RLTRQPSRLR VELEDWEGNA RYAEYSYFAL GNELNSYRLF LGNYSGNVGK DALLYHNNTV FSTKDKDNDN CLDKCAQLRK GGYWYNCCTD SNLNGVYYRL GEHRKHMDGI SWYGWHGANY SLKRVEMKIR PEAFKPLEHH HHHH.
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.

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