Search: 1000 results found for "interleukin 8 (cxcl8)"

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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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.

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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.
Who supplies recombinant CCL20 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 CCL20 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-19 Human Recombinant

Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19.

Product # :

CYT-363

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Description

Interleukin-19 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids and having a molecular mass of 17913 Dalton. The IL-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 10mM sodium citrate pH-5.

Purity

Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity is determined by it's ability to activate STAT following receptor-ligand interaction.

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Introduction
IL19 is a cytokine that belongs to the IL10 cytokine subfamily. IL-19 is found to be preferentially expressed in monocytes. It can bind the IL20 receptor complex and lead to the activation of the signal transducer and activator of transcription 3 (STAT3). A similar cytokine in mouse is reported to up-regulate the expression of IL6 and TNF-alpha and induce apoptosis, which suggests a role of this cytokine in inflammatory responses. Alternatively spliced transcript variants encoding the distinct isoforms have been described.
Synonyms
Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-19 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL19 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 -19 in sterile 18MΩ-cm H2O at a concentration of 0.5mg/ml or less.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Arg-Arg-Cys.

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 10 Receptor Alpha Human Recombinant

Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.

Product # :

CYT-892

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Description

IL10RA Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated, polypeptide chain containing 220 amino acids (22-235 a.a.) and having a molecular mass of 25.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).IL10RA is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL10RA protein solution (0.2mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
Synonyms
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
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
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS LLTSGEVGEF CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH
Background
What is the molecular weight/Mw of IL10RA HUMAN Protein?
IL10RA HUMAN Protein has a total Mw of 25.2kDa.

What is the source or expression system of IL10RA HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL10RA HUMAN Protein?
IL10RA HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10RA HUMAN Protein?
The biological functionality of IL10RA HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL10RA HUMAN Protein?
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS LLTSGEVGEF CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH.

What applications can IL10RA HUMAN Protein be used in?
IL10RA HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10RA HUMAN Protein?
The endotoxin level is minimal, IL10RA HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10RA HUMAN 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 IL10RA HUMAN?
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:

Recombinant Human Interleukin 10 Receptor Beta

Interleukin-10 receptor subunit beta, IL-10 receptor subunit beta, IL-10R subunit beta, IL-10RB, Cytokine receptor class-II member 4, Cytokine receptor family 2 member 4, CRF2-4, Interleukin-10 receptor subunit 2, IL-10R subunit 2, IL-10R2, CDw210b, IL10RB.

Product # :

CYT-1025

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Description

IL10RB Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 440 amino acids (20-220 a.a.) and having a molecular mass of 50.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).IL10RB is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

IL10RB protein solution (1.0mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
Synonyms
Interleukin-10 receptor subunit beta, IL-10 receptor subunit beta, IL-10R subunit beta, IL-10RB, Cytokine receptor class-II member 4, Cytokine receptor family 2 member 4, CRF2-4, Interleukin-10 receptor subunit 2, IL-10R subunit 2, IL-10R2, CDw210b, IL10RB.
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
MVPPPENVRM NSVNFKNILQ WESPAFAKGN LTFTAQYLSY RIFQDKCMNT TLTECDFSSL SKYGDHTLRV RAEFADEHSD WVNITFCPVD DTIIGPPGMQ VEVLADSLHM RFLAPKIENE YETWTMKNVY NSWTYNVQYW KNGTDEKFQI TPQYDFEVLR NLEPWTTYCV QVRGFLPDRN KAGEWSEPVC EQTTHDETVP SLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.
Background
What is the molecular weight/Mw of IL10RB HUMAN Protein?
IL10RB HUMAN Protein has a total Mw of 50.5kDa.

What is the source or expression system of IL10RB HUMAN Protein?
Sf9, Insect cells.

What is the Purity of IL10RB HUMAN Protein?
IL10RB HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10RB HUMAN Protein?
The biological functionality of IL10RB HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL10RB HUMAN Protein?
MVPPPENVRM NSVNFKNILQ WESPAFAKGN LTFTAQYLSY RIFQDKCMNT TLTECDFSSL SKYGDHTLRV RAEFADEHSD WVNITFCPVD DTIIGPPGMQ VEVLADSLHM RFLAPKIENE YETWTMKNVY NSWTYNVQYW KNGTDEKFQI TPQYDFEVLR NLEPWTTYCV QVRGFLPDRN KAGEWSEPVC EQTTHDETVP SLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.

What applications can IL10RB HUMAN Protein be used in?
IL10RB HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10RB HUMAN Protein?
The endotoxin level is minimal, IL10RB HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10RB HUMAN 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 IL10RB HUMAN?
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-22 Receptor Antagonist (Y51A) Mouse Recombinant

IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

Product # :

CYT-1239

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Shipped at Room temp

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Description

IL22RA (Y51A) Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids and having a molecular mass of 16.7 kDa. IL22RA (Y51A) is purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with NaHCO3.

Purity

Greater than 98.0% as determined by:

(a) Gel filtration chromatography.

(b) Analysis by SDS-PAGE.

Biological Activity

IL22RA (Y51A) Is capable of full inhibition of STAT3 phosphorylation induced by mouse interleukin 22 in HepG cells. Its affinity toward immobilized mIL-22 receptor α1 extracellular domain (mIL-22 Rα1-ECD) or IL-22 binding protein is similar to the non-mutated mouse interleukin 22. Mouse IL-22 antagonist (Y51A) has no agonistic activity in this bioassay.

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Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL22RA (Y51A) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22RA (Y51A) 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 IL22RA (Y51A) in sterile 18MΩ-cm 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 Ala-Leu-Pro-Val-Asn.
Background
IL-22 belongs to the IL-10 family of regulatory cytokines and produced by several populations of immune cells at a site of inflammation. Members of this family share partial homology in their amino acid sequences, but varies in their biological functions. IL-22 takes effect on non-hematopoietic cells. IL-22 takes pat in wound healing and in protection against microbs.Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the pancreas and liver.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

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-32, Mouse Anti Human

NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.

Product # :

ANT-007

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Formulation

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

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Introduction
IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function. Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine,
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human IL32 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human IL32 amino acids 1-331 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
PAT2F9AT.
Applications
IL32 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
IL32 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:

Interleukin-15 PAT7G9AT Mouse Anti-Human

IL-15, MGC9721, Interleukin-15.

Product # :

ANT-776

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Formulation

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

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Synonyms
IL-15, MGC9721, Interleukin-15.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human IL15 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IL15 protein 49-162 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and Kappa light chain.
Clone
PAT7G9T.
Applications
The antibody has been tested by ELISA, Western blot analysis, FACS and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Background
Interleukin-15 which is produced by a wide variety of cells and tissues is a pleiotropic cytokine which takes part in innate and adaptive immunity. IL- 15 is well known due to its involvement in a trans-signaling mechanism where IL-15 receptor alpha from 1 subset of cells presents IL-15 to close cells that express IL-2Rβ/γc. IL-15 like IL-2, stimulates the proliferation of Tlymphocytes and induces the generation of cytotoxic T-lymphocytes (CTLs) and lymphokine-activated killer (LAK) cells. IL-15 and IL-2 may also compete for the same receptor, and thus negatively regulate each other's activity.
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
IL15 antibody was purified by protein-A affinity chromatography.

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

Description:

Interleukin-2 Porcine Recombinant

T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.

Product # :

CYT-397

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Description

Interleukin2 Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids and having a molecular mass of 15217 Dalton. The IL-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using murine CTLL-2 cells is less than 0.5ng/ml, corresponding to a specific activity of > 2.0 × 10⁶IU/mg.

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Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
Synonyms
T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-2 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 2 in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APTSSSTKNT KKQLEPLLLD LQLLLKEVKN YENADLSRML TFKFYMPKQA TELKHLQCLV EELKALEGVL NLGQSKNSDS ANIKESMNNI NVTVLELKGS ETSFKCEYDD ETVTAVEFLN KWITFCQSIY STLT.
Background
What is the molecular weight/Mw of IL 2 PORCINE Protein?
IL 2 PORCINE Protein has a total Mw of 15.2kDa.

What is the source or expression system of IL 2 PORCINE Protein?
Escherichia Coli.

What is the Purity of IL 2 PORCINE Protein?
IL 2 PORCINE Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 PORCINE Protein?
The ED50 as determined by a cell proliferation assay using murine CTLL-2 cells is less than 0.5ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.

What is the amino acid sequence of IL 2 PORCINE Protein?
APTSSSTKNT KKQLEPLLLD LQLLLKEVKN YENADLSRML TFKFYMPKQA TELKHLQCLV EELKALEGVL NLGQSKNSDS ANIKESMNNI NVTVLELKGS ETSFKCEYDD ETVTAVEFLN KWITFCQSIY STLT.

What applications can IL 2 PORCINE Protein be used in?
IL 2 PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 PORCINE Protein?
The endotoxin level is minimal, IL 2 PORCINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 PORCINE 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 IL 2 PORCINE?
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-7 Human Recombinant, sf9

Interleukin 7, IL-7, Interleukin-7.

Product # :

CYT-975

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Shipped with Ice Packs

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Description

IL7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 161 amino acids (26-177 a.a.) and having a molecular mass of 18.4kDa. IL7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL7 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
Synonyms
Interleukin 7, IL-7, Interleukin-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
ADPDCDIEGK DGKQYESVLM VSIDQLLDSM KEIGSNCLNN EFNFFKRHIC DANKEGMFLF RAARKLRQFL KMNSTGDFDL HLLKVSEGTT ILLNCTGQVK GRKPAALGEA QPTKSLEENK SLKEQKKLND LCFLKRLLQE IKTCWNKILM GTKEHHHHHH H
Background
What is the molecular weight/Mw of IL7 HUMAN, SF9 Protein?
IL7 HUMAN, SF9 Protein has a total Mw of 18.4kDa.

What is the source or expression system of IL7 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL7 HUMAN, SF9 Protein?
IL7 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL7 HUMAN, SF9 Protein?
The biological functionality of IL7 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of IL7 HUMAN, SF9 Protein?
ADPDCDIEGK DGKQYESVLM VSIDQLLDSM KEIGSNCLNN EFNFFKRHIC DANKEGMFLF RAARKLRQFL KMNSTGDFDL HLLKVSEGTT ILLNCTGQVK GRKPAALGEA QPTKSLEENK SLKEQKKLND LCFLKRLLQE IKTCWNKILM GTKEHHHHHH H.

What applications can IL7 HUMAN, SF9 Protein be used in?
IL7 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL7 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL7 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL7 HUMAN, SF9 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 IL7 HUMAN, SF9?
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:

Stromal Cell-Derived Factor-1 beta Feline Recombinant (CXCL12)

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

Product # :

CHM-247

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Stromal Cell-Derived Factor-1 beta Feline Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8526 Dalton. The SDF-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.

Purity

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

Biological Activity

The specific activity as determined by its ability to chemoattract human peripheral T cells stimulated with IL-2 and PHA in a concentration range from 10-75 ng/ml corresponding to a Specific Activity of 13,334-100,000IU/mg.

More Info

Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 SDF-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM.
Background
What is the molecular weight/Mw of CXCL12 FELINE BETA Protein?
CXCL12 FELINE BETA Protein has a total Mw of 8.5kDa.

What is the source or expression system of CXCL12 FELINE BETA Protein?
Escherichia Coli.

What is the Purity of CXCL12 FELINE BETA Protein?
CXCL12 FELINE BETA Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 FELINE BETA Protein?
The specific activity as determined by its ability to chemoattract human peripheral T cells stimulated with IL-2 and PHA in a concentration range from 10-75 ng/ml corresponding to a Specific Activity of 13,334-100,000IU/mg.

What is the amino acid sequence of CXCL12 FELINE BETA Protein?
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM.

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

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

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

Where can I order bulk mg quantities of CXCL12 FELINE BETA?
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:

Canine IL-6 Recombinant

IL6, IL-6, Interleukin-6.

Product # :

CYT-1006

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL6 Canine Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 195 amino acids (21-207a.a.) and having a molecular mass of 22.0kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL6 is expressed with an 8 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL6 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
Synonyms
IL6, IL-6, Interleukin-6.
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
FPTPGPLAGD SKDDATSNSL PLTSANKVEE LIKYILGKIS ALRKEMCDKF NKCEDSKEAL AENNLHLPKL EGKDGCFQSG FNQETCLTRI TTGLVEFQLH LNILQNNYEG DKENVKSVHM STKILVQMLK SKVKNQDEVT TPDPTTDASL QAILQSQDEC VKHTTIHLIL RSLEDFLQFS LRAVRIMLEH HHHHH.
Background
Canine IL-6 Recombinant: Implications for Immunotherapy and Veterinary Medicine
Abstract:
Interleukin-6 (IL-6) plays a pivotal role in the immune response and inflammation regulation in various species, including canines. The advent of recombinant DNA technology has enabled the production of Canine IL-6 Recombinant (cIL-6r), opening new avenues for research in immunotherapy and veterinary medicine. This paper delves into the significance of cIL-6r, its production methods, and its potential applications in the treatment of inflammatory and autoimmune diseases in dogs.
Introduction:
Interleukin-6 is a multifunctional cytokine that exerts its effects on a wide range of physiological processes, including immune responses, hematopoiesis, and inflammation. In the canine immune system, IL-6 plays a crucial role in coordinating immune cell activation, antibody production, and acute phase responses. Recombinant IL-6 production has emerged as a promising strategy to harness its therapeutic potential.
Methods:
The production of cIL-6r involves recombinant DNA technology, where the canine IL-6 gene is inserted into an expression vector and transfected into a suitable host cell line, typically bacterial or mammalian cells. The recombinant protein is then purified using various chromatographic techniques to ensure high purity and biological activity.
Applications:
Canine IL-6 Recombinant holds immense promise in various applications within veterinary medicine. Its immunomodulatory properties make it a potential candidate for treating conditions such as immune-mediated diseases, inflammatory disorders, and certain types of cancer in dogs. Additionally, cIL-6r can be utilized to stimulate immune responses in vaccines, thereby enhancing their efficacy.
Challenges and Future Directions:
While cIL-6r shows great potential, its therapeutic use requires comprehensive studies to establish optimal dosages, safety profiles, and potential side effects. Long-term effects and potential interactions with existing treatments must also be explored.
Conclusion:
The advent of Canine IL-6 Recombinant marks a significant advancement in veterinary medicine, offering new avenues for immunotherapy and disease management in dogs. With further research and development, cIL-6r could become an invaluable tool in treating various conditions, ultimately enhancing the health and well-being of our canine companions.
What is the molecular weight/Mw of IL6 CANINE Protein?
IL6 CANINE Protein has a total Mw of 22kDa.

What is the source or expression system of IL6 CANINE Protein?
Sf9, Baculovirus cells.
What is the Purity of IL6 CANINE Protein?
IL6 CANINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6 CANINE Protein?
The biological functionality of IL6 CANINE Protein will be determined in the future.

What is the amino acid sequence of IL6 CANINE Protein?
FPTPGPLAGD SKDDATSNSL PLTSANKVEE LIKYILGKIS ALRKEMCDKF NKCEDSKEAL AENNLHLPKL EGKDGCFQSG FNQETCLTRI TTGLVEFQLH LNILQNNYEG DKENVKSVHM STKILVQMLK SKVKNQDEVT TPDPTTDASL QAILQSQDEC VKHTTIHLIL RSLEDFLQFS LRAVRIMLEH HHHHH.

What applications can IL6 CANINE Protein be used in?
IL6 CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL6 CANINE Protein?
The endotoxin level is minimal, IL6 CANINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL6 CANINE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL6 CANINE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-2 Human Recombinant

T-cell growth factor (TCGF), Lymphokine, IL-2.

Product # :

CYT-209

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15.4kDa. The IL-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a 0.2μm filtered concentrated solution (1.0mg/ml) in PBS, pH 5.0.

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-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x10⁷IU/mg.

More Info

Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
Synonyms
T-cell growth factor (TCGF), Lymphokine, IL-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 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-2 in sterile distilled water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.
Background
IL 2 HUMAN: A Vital Tool for Advancing Immunotherapy Research
IL 2 HUMAN refers to the human form of Interleukin-2, a critical cytokine in the immune system. This protein is crucial for the growth and activity of T and B lymphocytes, the cells responsible for the body's immune defense against infections.
By promoting the growth of these cells, IL 2 plays a vital role in maintaining and activating the immune response.
Production and Characteristics
Typically, IL 2 is produced through recombinant DNA technology using E. coli bacteria. This method allows for creating large quantities of pure and functional IL 2 protein.
The product appears as a sterile, white lyophilized powder that is non-glycosylated and consists of 133 amino acids with a molecular mass of approximately 15.4 kDa.
Reconstituting IL-2 Human for Laboratory Use
To dissolve the lyophilized IL-2 effectively, it should be reconstituted with sterile distilled water to achieve a minimum 100µg/ml concentration. This makes the protein readily usable for further experimental procedures.
Moreover, the concentration allows for easy adjustment in solubility and ensures optimal conditions for the protein's activity in various research setups. Proper dissolution and storage are crucial to maintain the protein's functionality and stability.
Storage and Stability
The stability of IL 2 is dependent on its storage conditions. When lyophilized, it can remain stable at room temperature for up to three weeks, but for long-term storage, it should be kept desiccated below -18°C.
Once reconstituted, IL 2 should be used within a week if kept at 4°C, or it can be stored at below -18°C for future use. It's important to avoid freeze-thaw cycles, which can degrade the protein.
Purity and Biological Activity
IL 2 HUMAN's purity is generally greater than 97%, confirmed by reverse-phase high-performance liquid chromatography (RP-HPLC) and SDS-PAGE analyses.
Its biological activity is evaluated by its ability to stimulate the proliferation of murine CTLL-2 cells, with an effective dose (ED50) typically less than 0.1 ng/ml. This indicates a very high specific activity, making it highly potent and effective in research settings.
Applications in Research
IL 2 is used extensively in research, particularly in studies focusing on the immune system, autoimmune diseases, and cancer. Furthermore, its role in T-cell growth and function makes it invaluable for developing new therapeutic strategies and understanding immune response mechanisms.
Important Considerations
It is important to remember that IL 2, like all cytokines used in research, is intended for laboratory use only. This protein is not suitable for drug, food, or cosmetic applications. Proper handling and usage instructions must be followed to ensure safety and efficacy in research environments.
Essentially, IL 2 HUMAN is a vital tool in immunological research, offering insights into the complex workings of the immune system and providing avenues for potential therapeutic developments. The careful production, handling, and storage of IL 2 are crucial for its effective use in laboratory settings.
What is the molecular weight/Mw of IL 2 HUMAN Protein?
IL 2 HUMAN Protein has a total Mw of 15.4kDa.

What is the source or expression system of IL 2 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL 2 HUMAN Protein?
IL 2 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 HUMAN Protein?
The ED50 as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x107IU/mg.

What is the amino acid sequence of IL 2 HUMAN Protein?
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.

What applications can IL 2 HUMAN Protein be used in?
IL 2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 HUMAN Protein?
The endotoxin level is minimal, IL 2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 HUMAN 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 IL 2 HUMAN?
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-21 Canine Recombinant

Interleukin-21.

Product # :

CYT-1181

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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biological activity
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Description

IL21 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (18-146a.a.) and having a molecular mass of 15kDa.

Source

Escherichia Coli.

Formulation

IL21 protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the IFN-g ELISA in a using NK-92 human natural killer cells. The ED50 range ≤ 2ng/ml.

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Introduction
Interleukin-21 isoform 1 or IL21, categorized as a T helper cytokine. IL21 is part of the regulation of immune responses, haematopoiesis and cell-mediated responses. IL21 takes a main part in haematopoiesis and immune responses regulation, therefore can affect lymphocyte development. Activation of T cells leads to production of the IL21 which has an important role in the viral infections persistence.
Synonyms
Interleukin-21.
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
MHKSSFQEQD LLLIRMRQLI DIVDQLKNYV NDLDPESLPA PEDVKRHCER SAFSCFQKVQ LKAANTGGNE QIINVLTKQL KRKLPPTNAG RRQKHRPACP SCDSYEKAPP KEFLERLKSL IQKMIHQHLS

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-31 Canine Recombinant, His Tag

IL-31, Interleukin 31, IL31.

Product # :

CYT-1016

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL31 Canine Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (24-159a.a.) and having a molecular mass of 16.1kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL31 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL31 Canine protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis.
Synonyms
IL-31, Interleukin 31, IL31.
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. Please avoid freeze thaw cycles.
Amino Acid Sequence
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQHHHH HH.

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:

Thymus & Activation Regulated Chemokine Human Recombinant (CCL17)

C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

Product # :

CHM-240

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

CCL17 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 8 kDa. The TARC is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (0.5mg/ml) solution containing 20mM PBS & 150mM NaCl 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 T-Lymphocytes using a concentration range of 1.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

More Info

Introduction
TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.
Synonyms
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TARC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TARC 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 CCL17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ARGTNVGRECCLEYFKGAIPLRKLKTWYQTSEDCSRD
AIVFVTVQGRAICSDPNNK RVKNAVKYLQSLERS.
Background
What is the molecular weight/Mw of CCL17 HUMAN Protein?
CCL17 HUMAN Protein has a total Mw of 8kDa.

What is the source or expression system of CCL17 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL17 HUMAN Protein?
CCL17 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL17 HUMAN Protein?
Determined by its ability to chemoattract human T-Lymphocytes using a concentration range of 1.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of CCL17 HUMAN Protein?
ARGTNVGRECCLEYFKGAIPLRKLKTWYQTSEDCSRD
AIVFVTVQGRAICSDPNNK RVKNAVKYLQSLERS.

What applications can CCL17 HUMAN Protein be used in?
CCL17 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL17 HUMAN Protein?
The endotoxin level is minimal, CCL17 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL17 HUMAN 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 CCL17 HUMAN?
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:

Monocyte Chemotactic Protein-1 Rat Recombinant (CCL2)

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

Product # :

CHM-315

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Quantity :

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Shipped at Room temp

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Description

Monocyte Chemotactic Protein-1 Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 125 amino acids and having a molecular mass of 14.1 kDa. The MCP-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

ED50 =1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg. The biological activity was determined by measuring the dose dependent chemotaxis with human THP-1 cells. The optimal concentration should be determined for each specific application by an initial dose-response assay.

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Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weightof approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11, Immediate-early serum-responsive JE protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Monocyte Chemotactic Protein-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPDAVNAPLT CCYSFTGKMI PMSRLENYKR ITSSRCPKEA VVFVTKLKRE ICADPNKEWV QKYIRKLDQN QVRSETTVFY KIASTLRTSA PLNVNLTHKS EANASTLFST TTSSTSVEVT SMTEN.
Background
What is the molecular weight/Mw of CCL2 RAT Protein?
CCL2 RAT Protein has a total Mw of 14.1kDa.

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

What is the Purity of CCL2 RAT Protein?
CCL2 RAT Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 RAT Protein?
ED50 =1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg. The biological activity was determined by measuring the dose dependent chemotaxis with human THP-1 cells. The optimal concentration should be determined for each specific application by an initial dose-response assay.

What is the amino acid sequence of CCL2 RAT Protein?
QPDAVNAPLT CCYSFTGKMI PMSRLENYKR ITSSRCPKEA VVFVTKLKRE ICADPNKEWV QKYIRKLDQN QVRSETTVFY KIASTLRTSA PLNVNLTHKS EANASTLFST TTSSTSVEVT SMTEN.

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

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

Who supplies recombinant CCL2 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 CCL2 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:

Natural anti-proliferative protein, Mouse-Anti Human

Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

Product # :

ANT-170

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Shipping Method :

Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human NAP-2.
Ig Subclass
Mouse IgG1.
Clone
NYRhNAP-2.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Note
This antibody will bind very well to protein A in a buffer (PBS) containing high salt concentration (3M Nacl).
Titer
In direct ELISA, using alkaline phosphatase goat anti-mouse Ig (Jackson Laboratories) 1:10,000 dilution will yield 0.5 O.D within 10 minutes.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
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:

Thymus and Activation Regulated Chemokine Human Recombinant (CCL17), His Tag

C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

Product # :

CHM-359

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Shipped with Ice Packs

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Description

TARC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 92 amino acids (24-94 a.a.) and having a molecular mass of 10.3 kDa. The TARC is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TARC protein (0.5mg/ml) contains 1xPBS (pH7.4) and 10% glycerol.

Purity

Greater than 95% as determined by Analysis by SDS-PAGE.

SDS-PAGE

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Introduction
TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.
Synonyms
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
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 MARGTNVGRE CCLEYFKGAI PLRKLKTWYQ TSEDCSRDAI VFVTVQGRAI CSDPNNKRVK NAVKYLQSLE RS.
Background
What is the molecular weight/Mw of CCL17 HUMAN, HIS Protein?
CCL17 HUMAN, HIS Protein has a total Mw of 10.3kDa.

What is the source or expression system of CCL17 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL17 HUMAN, HIS Protein?
CCL17 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL17 HUMAN, HIS Protein?
The biological functionality of CCL17 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL17 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MARGTNVGRE CCLEYFKGAI PLRKLKTWYQ TSEDCSRDAI VFVTVQGRAI CSDPNNKRVK NAVKYLQSLE RS.

What applications can CCL17 HUMAN, HIS Protein be used in?
CCL17 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL17 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL17 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL17 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL17 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

CX9C Motif Containing 4 Human Recombinant

C-X(9)-C Motif Containing 4, C-X(9)-C Motif Containing 4 Homolog, Mature T-Cell Proliferation 1 Neighbor Protein, MTCP1NB, MTCP1, Mature T-Cell Proliferation-1 Type A, Protein P8 MTCP-1, p8MTCP1, MTCP-1 Type A, C6.1B.

Product # :

PRO-1769

Price :

Quantity :

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Shipped with Ice Packs

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Description

CMC4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (1-68 a.a) and having a molecular mass of 10.4kDa.CMC4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CMC4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
CMC4 is a downstream 8kDa protein restricts to mitochondria which was identified by participation in some t(X;14) translocations related with mature T-cell proliferations. This region has a compound gene structure, with a common promoter and 5’ exon spliced to two different groups of 3’ exons which encode 2 separate proteins.
Synonyms
C-X(9)-C Motif Containing 4, C-X(9)-C Motif Containing 4 Homolog, Mature T-Cell Proliferation 1 Neighbor Protein, MTCP1NB, MTCP1, Mature T-Cell Proliferation-1 Type A, Protein P8 MTCP-1, p8MTCP1, MTCP-1 Type A, C6.1B.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMPQKD PCQKQACEIQ KCLQANSYME SKCQAVIQEL RKCCAQYPKG RSVVCSGFEK EEEENLTRKS ASK

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

Description:

Stromal Cell-Derived Factor-1 gamma Human Recombinant (CXCL12)

Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.

Product # :

CHM-020

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

SDF-1 gamma Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 99 amino acids and having a molecular mass of 11.6kDa.The SDF-1g is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SDF-1g protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1a/CXCL12a and SDF-1b/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SDF-1 gamma 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 SDF-1g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.
Background
What is the molecular weight/Mw of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein has a total Mw of 11.6kDa.

What is the source or expression system of CXCL12 HUMAN GAMMA Protein?
Escherichia Coli.

What is the Purity of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein is > 96% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 HUMAN GAMMA Protein?
The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.

What is the amino acid sequence of CXCL12 HUMAN GAMMA Protein?
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.

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

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

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

Where can I order bulk mg quantities of CXCL12 HUMAN GAMMA?
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-1b, Mouse Anti-Human

Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

Product # :

ANT-248

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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Formulation

1 mg/ml in PBS (after reconstitution).

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Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human IL-1b.
Ig Subclass
Mouse IgG2b.
Clone
NYR-hIL1b.
Applications
Direct ELISA, Western Blot, Immuneprecipitation, immunohistochemistry.
Note
The antibody was produced in BALB/c mice.
Titer
By direct ELISA, 1:20,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories). 1:2,000 dilution will completely inhibit a thymocyte co-stimulation assay using suboptimal doses of concanavalin A.
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:

Annexin A8 Human Recombinant

ANX8, Annexin-8, Annexin VII, Vascular anticoagulant-beta, VAC-beta.

Product # :

PRO-548

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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Description

ANXA8 Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 347 amino acids (1-327 a.a.)and having a total molecular mass of 39 kDa. ANXA8 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ANXA8 1mg/ml protein solution contains 20mM Tris-HCL pH-8, 1mM DTT,1mM EDTA, 0.1M NaCl and 10% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
ANXA8 is part of the annexin family of evolutionarily conserved Ca2+ and phospholipid binding proteins. ANXA8 is an anticoagulant protein that functions as an indirect inhibitor of the thromboplastin-specific complex, which takes part in the blood coagulation cascade. Where co-expressed in the same tissues, ANXA8 is expressed at a 100-fold lower level than Annexin A5. Though, ANXA8 is preferentially expressed in acute promyelocytic leukemia (APL) cells which suggests its involvement in hematopoietic cell differentiation.
Synonyms
ANX8, Annexin-8, Annexin VII, Vascular anticoagulant-beta, VAC-beta.
Physical Appearance
Sterile Filtered colorless 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
MGSSHHHHHH SSGLVPRGSH MAWWKSWIEQ EGVTVKSSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNTQRQQIA KSFKAQFGKD
LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKGLG TKEGVIIEIL ASRTKNQLRE IMKAYEEDYG SSLEEDIQAD TSGYLERILV
CLLQGSRDDV SSFVDPGLAL QDAQDLYAAG EKIRGTDEMK FITILCTRSA THLLRVFEEY EKIANKSIED SIKSETHGSL EEAMLTVVKC
TQNLHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKCHFKKMYG KTLSSMIMED TSGDYKNALL SLVGSDP.

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-17A/F Heterodimer Human Recombinant

IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.

Product # :

CYT-623

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL-17A/F Human Recombinant produced in E.Coli is a heterodimeric, non-glycosylated polypeptide chain containing 1 monomeric subunit of each IL-17A & IL-17F. The active dimer contains 271 amino acids and having a total molecular mass of 30.7 kDa. The IL-17A/F Human is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-17A/F was lyophilized from a (0.2µm) filtered protein solution containing 0.1% TFA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity as determined by production of IL-6 from mouse 3T3 cells is 3.2ng/ml (3.1x10⁵units/mg).

More Info

Introduction
Human IL-17A/F is a 40kDa glycoprotein which is secreted as a disulfide-linked heterodimer. IL-17A/F consists of two proteins of the IL-17 family, IL-17A and IL17F. Proteins of the 6 homodimeric IL17 family show a cysteine knot motif that contains two disulfide-bonds. Human IL17A is produced as a 155 a.a precursor that includes a 23 amino acids signal sequence and a 132 amino acid chain that includes an N-linked glycosylation site. Human IL17F is produced as a 153 amino acid precursor with a 20 amino acid signal sequence and a 133 amino acid region. Similar to IL17A, IL17F also has an N-linked glycosylation site. Both proteins (IL17A & IL17F) share 50% amino acid sequence identity. Human IL17A & IL17F show approximately 60% homology in their amino acid sequence to mouse IL-17A and IL-17F. Interleukin-17A/F and IL17A, IL17F homodimers are manufactured by activted CD4+ T cells, called Th17. IL-23 causes Th17 lymphocytes to manufacture IL-17A/F. IL17RA and IL17RC form a heterodimer for the binding of IL17A and IL17F. IL-17A/F binds IL-17RA. Interleukin-17A/F induces chemokine production and airway neutrophilia with intermediate potency between IL17A (most potent) and IL17F (least potent).
Synonyms
IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human IL-17A/F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human IL-17A/F 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 Human IL-17A/F in sterile water at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MIVKAGITIP RNPGCPNSED KNFPRTVMVN LNIHNRNTNT NPKRSSDYYN RSTSPWNLHR NEDPERYPSV IWEAKCRHLG CINADGNVDY HMNSVPIQQE ILVLRREPPH CPNSFRLEKI LVSVGCTCVT PIVHHVA.
MRKIPKVGHT FFQKPESCPP VPGGSMKLDI GIINENQRVS MSRNIESRST SPWNYTVTWD PNRYPSEVVQ AQCRNLGCIN AQGKEDISMN SVPIQQETLV VRRKHQGCSV SFQLEKVLVT VGCTCVTPVI HHVQ.

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-17 Receptor Alpha Human Recombinant

Interleukin 17 Receptor A, IL-17 Receptor A, IL-17RA, CDw217, IL17R, Interleukin-17 Receptor A, Interleukin 17 Receptor, CD217 Antigen, HIL-17R, CANDF5, CD217, IMD51.

Product # :

CYT-1023

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Shipping Method :

Shipped with Ice Packs

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Description

IL17RA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 527 amino acids (33-320) and having a molecular mass of 60.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). IL17RA is fused to a 239 amino acids hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL17RA protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Interleukin-17 receptor A isoform 1 (IL17RA) is a cytokine receptor which binds interleukin 17. IL17RA is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL17RA is a type 1 membrane glycoprotein which binds with low affinity to interleukin 17A. The IL17RA protein and Interleukin 17A has a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis.
Synonyms
Interleukin 17 Receptor A, IL-17 Receptor A, IL-17RA, CDw217, IL17R, Interleukin-17 Receptor A, Interleukin 17 Receptor, CD217 Antigen, HIL-17R, CANDF5, CD217, IMD51.
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
LRLLDHRALV CSQPGLNCTV KNSTCLDDSW IHPRNLTPSS PKDLQIQLHF AHTQQGDLFP VAHIEWTLQT DASILYLEGA ELSVLQLNTN ERLCVRFEFL SKLRHHHRRW RFTFSHFVVD PDQEYEVTVH HLPKPIPDGD PNHQSKNFLV PDCEHARMKV TTPCMSSGSL WDPNITVETL EAHQLRVSFT LWNESTHYQI LLTSFPHMEN HSCFEHMHHI PAPRPEEFHQ RSNVTLTLRN LKGCCRHQVQ IQPFFSSCLN DCLRHSATVS CPEMPDTPEP IPDYMPLWVE 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.

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