Search: 886 results found for "tumor necrosis factor"

Description:

Glial-Derived Neurotrophic Factor Mouse Recombinant

ATF1, ATF2, HFB1-GDNF, GDNF.

Product # :

CYT-243

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Description

Glial derived Neurotrophic Factor Mouse Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2 x 135 amino acids and having a total molecular mass of 30.2kDa. GDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDNF was lyophilized with no additives.

Purity

Greater than 98.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

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Introduction
GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.
Synonyms
ATF1, ATF2, HFB1-GDNF, GDNF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF 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 Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.
Background
What is the molecular weight/Mw of GDNF MOUSE Protein?
GDNF MOUSE Protein has a total Mw of 30.2kDa.

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

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

What is the Biological Activity of GDNF MOUSE Protein?
The ED50 as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

What is the amino acid sequence of GDNF MOUSE Protein?
MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.
What applications can GDNF MOUSE Protein be used in?
GDNF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

Fibroblast Growth Factor-23 Human Recombinant, His Tag

Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

Product # :

CYT-374

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Description

Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain expressed with a -6xHis tag containing a total of 257 amino acids (251 a.a. FGF23+ 6 a.a. His tag) and having a molecular mass of 28629.5 Dalton. The FGF-23 is and purified by chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (0.5mg/ml) was lyophilized from 25mM Tris pH7.5 and 0.6M NaCl solution.

Purity

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

Biological Activity

Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

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Introduction
FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. Mutations FGF23 have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.
Synonyms
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized Fibroblast Growth Factor 23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 Fibroblast Growth Factor-23 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
FAKFIHHHHHH.
Background
What is the molecular weight/Mw of FGF23 HUMAN, HIS Protein?
FGF23 HUMAN, HIS Protein has a total Mw of 28.6kDa.

What is the source or expression system of FGF23 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of FGF23 HUMAN, HIS Protein?
FGF23 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF23 HUMAN, HIS Protein?
Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

What is the amino acid sequence of FGF23 HUMAN, HIS Protein?
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
FAKFIHHHHHH.

What applications can FGF23 HUMAN, HIS Protein be used in?
FGF23 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF23 HUMAN, HIS Protein?
The endotoxin level is minimal, FGF23 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:

Granulocyte Macrophage Colony Stimulating Factor, Mouse Anti-Human

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

Product # :

ANT-129

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Shipped at Room temp

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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human GM-CSF.
Ig Subclass
Mouse IgG.
Clone
NYRhGMCSF.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.4 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 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion exchange Protein concentration1mg/ml in PBS (after reconstitution).

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 Receptor Alpha Human Recombinant

Leukemia Inhibitory Factor Receptor Alpha, CD118 Antigen, LIF Receptor, LIF-R, Leukemia Inhibitory Factor Receptor, CD118, SJS2, STWS, SWS, Leukemia inhibitory factor receptor, LIF receptor, LIF-R.

Product # :

CYT-949

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Shipped with Ice Packs

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Description

LIFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 798 amino acids (45-833a.a.) and having a molecular mass of 90.5kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa). LIFR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

LIFR 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.

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Introduction
Leukemia inhibitory factor receptor (LIFR) is the receptor for leukemia inhibitory factor, a pleiotropic cytokine affecting the differentiation, survival, and proliferation of various cells in the adult and the embryo. LIFR plays an imperative role in a number of aspects of early pregnancy such as blastocyst implantation in the uterus.
Synonyms
Leukemia Inhibitory Factor Receptor Alpha, CD118 Antigen, LIF Receptor, LIF-R, Leukemia Inhibitory Factor Receptor, CD118, SJS2, STWS, SWS, Leukemia inhibitory factor receptor, LIF receptor, LIF-R.
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
ADPQKKGAPH DLKCVTNNLQ VWNCSWKAPS GTGRGTDYEV CIENRSRSCY QLEKTSIKIP ALSHGDYEIT INSLHDFGSS TSKFTLNEQN VSLIPDTPEI LNLSADFSTS TLYLKWNDRG SVFPHRSNVI WEIKVLRKES MELVKLVTHN TTLNGKDTLH HWSWASDMPL ECAIHFVEIR CYIDNLHFSG LEEWSDWSPV KNISWIPDSQ TKVFPQDKVI LVGSDITFCC VSQEKVLSAL IGHTNCPLIH LDGENVAIKI RNISVSASSG TNVVFTTEDN IFGTVIFAGY PPDTPQQLNC ETHDLKEIIC SWNPGRVTAL VGPRATSYTL VESFSGKYVR LKRAEAPTNE SYQLLFQMLP NQEIYNFTLN AHNPLGRSQS TILVNITEKV YPHTPTSFKV KDINSTAVKL SWHLPGNFAK INFLCEIEIK KSNSVQEQRN VTIKGVENSS YLVALDKLNP YTLYTFRIRC STETFWKWSK WSNKKQHLTT EASPSKGPDT WREWSSDGKN LIIYWKPLPI NEANGKILSY NVSCSSDEET QSLSEIPDPQ HKAEIRLDKN DYIISVVAKN SVGSSPPSKI ASMEIPNDDL KIEQVVGMGK GILLTWHYDP NMTCDYVIKW CNSSRSEPCL MDWRKVPSNS TETVIESDEF RPGIRYNFFL YGCRNQGYQL LRSMIGYIEE LAPIVAPNFT VEDTSADSIL VKWEDIPVEE LRGFLRGYLF YFGKGERDTS KMRVLESGRS DIKVKNITDI SQKTLRIADL QGKTSYHLVL RAYTDGGVGP EKSMYVVTKE NSHHHHHH.

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:

Thioredoxin Human Recombinant

Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

Product # :

PRO-569

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Description

Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 11.7 kDa.

Source

Escherichia Coli.

Formulation

Thioredoxin solution containing 1mg/ml solution containing 1xPBS pH 7.4.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is>150 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.

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Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.
Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
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
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFFKKGQKVGEFS GANKEKLEAT INELV.

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, BioActive

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-1142

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Shipped with Ice Packs

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Description

IL10RA Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 220 amino acids (22-235 aa) and having a molecular mass of 25.2kDa.IL10RA is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL10RA solution (0.2mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Determined by its ability to inhibit proliferation using MC/9 mouse mast cells. ED50 for this effect is ≤ 300 ng/ml with Human IL-10.

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Introduction
Interleukin 10 receptor, alpha subunit or CDW210A, is a part of the IL-10 receptor. This protein is encoded by the IL10RA gene in humans. IL10RA is a receptor for IL-10 (interleukin 10), it is part of the interferon receptors family. This protein is responsible for the inhibition of interferon receptors synthesis by taking part in the immunosuppressive signal of interleukin 10. Among its other roles are the insulin receptor substrate-2/PI 3-kinase/AKT pathway and phosphorylation of JAK1 and TYK2 kinases.
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 CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH
Background
What is the molecular weight/Mw of IL10RA HUMAN, ACTIVE Protein?
IL10RA HUMAN, ACTIVE Protein has a total Mw of 25.2kDa.

What is the source or expression system of IL10RA HUMAN, ACTIVE Protein?
Sf9, Baculovirus cells.
What is the Purity of IL10RA HUMAN, ACTIVE Protein?
IL10RA HUMAN, ACTIVE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10RA HUMAN, ACTIVE Protein?
Determined by its ability to inhibit proliferation using MC/9 mouse mast cells. ED50 for this effect is ≤ 300 ng/ml with Human IL-10.

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

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

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

Who supplies recombinant IL10RA HUMAN, ACTIVE 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, ACTIVE?
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:

Interferon Regulatory Factor-5, Mouse Anti Human

Interferon regulatory factor 5, IRF-5, IRF5, SLEB10.

Product # :

ANT-407

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Shipped with Ice Packs

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Formulation

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

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Introduction
IRF5 belongs to the interferon regulatory factor (IRF) family, which is a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats.
Synonyms
Interferon regulatory factor 5, IRF-5, IRF5, SLEB10.
Immunogen
Anti-human IRF5 mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human IRF5 amino acids 176-240 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P10T1AT.
Applications
IRF5 antibody has been tested by ELISA, Western blot, ICC/IF, FACS and IHC analysis
to assure specificity and reactivity. Since application varies, however, each
investigation should be titrated by the reagent to obtain optimal results.
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
IRF5 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-6 Rhesus Macaque Recombinant

IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, IFN beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

Product # :

CYT-174

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Shipping Method :

Shipped at Room temp

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Description

IL 6 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 186 amino acids and having a molecular mass of 21.1kDa.The IL 6 Rhesus Macaque 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 SDS-PAGE and HPLC analyses.

Biological Activity

Fully biologically active when compared to standard. The ED50 determined by a cell proliferation assay using IL-6-dependent murine 7TD1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.

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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
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, IFN beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-6 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 IL-6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPVLPGEDS KNVAAPHSQP LTSSERIDKH IRYILDGISA LRKETCNRSN MCESSKEALA ENNLNLPKMA EKDGCFQSGF NEDTCLVKII TGLLEFEVYL EYLQNRFESS EEQARAVQMS TKVLIQFLQK KAKNLDAITT PEPTTNASLL TKLQAQNQWL QDMTTHLILR SFKEFLQSNL RALRQM
Background
Research Paper on Interleukin-6 Rhesus Macaque Recombinant
Abstract:
Interleukin-6 (IL-6) Rhesus Macaque Recombinant holds a significant role in the realm of immunological exploration. This research paper delves into the molecular intricacies and implications of IL-6 Rhesus Macaque Recombinant in immune modulation. Through an investigation of its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its contribution to understanding immune responses.
Introduction:
IL-6 Rhesus Macaque Recombinant is a key player in immunological studies. This paper aims to provide a comprehensive understanding of its molecular attributes and its impact on immune mechanisms.
Molecular Structure and Insights:
Examining the molecular composition of IL-6 Rhesus Macaque Recombinant, we uncover its role in immune signaling. Its interactions and functions contribute to the fine-tuning of immune responses.
Exploring Immune Dynamics:
IL-6's influence on immune cell activation and inflammation is well-acknowledged. IL-6 Rhesus Macaque Recombinant provides a tool to delve deeper into these immune processes, enriching our comprehension of cytokine-mediated functions.
Synonyms and Network Connections:
Understanding IL-6's synonyms, such as DIF, TNFA, and TNFSF2, adds depth to our understanding of immune signaling networks. IL-6 Rhesus Macaque Recombinant helps uncover the complexity of these interconnected pathways.
Potential Applications in Research and Beyond:
Beyond research settings, IL-6 Rhesus Macaque Recombinant holds potential in deciphering immune-related diseases. Its significance extends to possible therapeutic interventions and diagnostic applications.
Clinical Implications and Future Prospects:
The clinical relevance of IL-6 Rhesus Macaque Recombinant is underlined by its role in diseases characterized by altered IL-6 signaling. Exploring its therapeutic potential paves the way for novel strategies in disease management.
Conclusion:
In the realm of immunology, IL-6 Rhesus Macaque Recombinant stands as a pivotal tool. Its molecular insights, pivotal functions, and potential implications position it as a valuable asset for advancing our understanding of immune regulation.
What is the molecular weight/Mw of IL6 RHESUS MACAQUE Protein?
IL6 RHESUS MACAQUE Protein has a total Mw of 21.1kDa.

What is the source or expression system of IL6 RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of IL6 RHESUS MACAQUE Protein?
IL6 RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6 RHESUS MACAQUE Protein?
Fully biologically active when compared to standard. The ED50 determined by a cell proliferation assay using IL-6-dependent murine 7TD1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.

What is the amino acid sequence of IL6 RHESUS MACAQUE Protein?
MAPVLPGEDS KNVAAPHSQP LTSSERIDKH IRYILDGISA LRKETCNRSN MCESSKEALA ENNLNLPKMA EKDGCFQSGF NEDTCLVKII TGLLEFEVYL EYLQNRFESS EEQARAVQMS TKVLIQFLQK KAKNLDAITT PEPTTNASLL TKLQAQNQWL QDMTTHLILR SFKEFLQSNL RALRQM.
What applications can IL6 RHESUS MACAQUE Protein be used in?
IL6 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

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

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

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

Description:

Growth and Differentiation factor 5 Mouse Recombinant

Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5, Growth/differentiation factor 5.

Product # :

CYT-941

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
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biological activity
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Description

GDF5 Mouse Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.2kDa.The GDF-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF-5 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

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 inducing alkaline phosphatase production of murine ATDC5 cells is less than 1.0µg/ml, corresponding to a specific activity of > 1000IU/mg.

More Info

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, Growth/differentiation factor 5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-5 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 GDF5 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APLANRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.
Background
What is the molecular weight/Mw of GDF5 MOUSE Protein?
GDF5 MOUSE Protein has a total Mw of 27.2kDa.

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 >96% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF5 MOUSE Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 1.0µg/ml, corresponding to a specific activity of > 1000IU/mg.

What is the amino acid sequence of GDF5 MOUSE Protein?
APLANRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.

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:

Interleukin-5 Rat Recombinant

EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.

Product # :

CYT-387

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Interleukin-5 Rat Recombinant produced in E.Coli is a dimeric, non-glycosylated polypeptide chain containing 113 amino acids and having a molecular mass of 13074 Dalton.The IL-5 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 ED₅₀ range=0.3-1.0 ng/ml as determined by the dose-dependant stimulation of the proliferation of BCL-1 cells.

More Info

Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
Synonyms
EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-5 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL5 Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please avoid freeze thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleikin-5 Rat in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Ile-Pro-Met.
Background
What is the molecular weight/Mw of IL 5 RAT Protein?
IL 5 RAT Protein has a total Mw of 13kDa.

What is the source or expression system of IL 5 RAT Protein?
Escherichia Coli.

What is the Purity of IL 5 RAT Protein?
IL 5 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 RAT Protein?
The ED50 range=0.3-1.0 ng/ml as determined by the dose-dependant stimulation of the proliferation of BCL-1 cells.

What is the amino acid sequence of IL 5 RAT Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Ile-Pro-Met.

What applications can IL 5 RAT Protein be used in?
IL 5 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 5 RAT Protein?
The endotoxin level is minimal, IL 5 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 5 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 IL 5 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:

Interleukin-6 Soluble Receptor Human Recombinant

IL6R-alpha, CD126, IL-6R 1, CD126 antigen, IL6RA, Interleukin 6 receptor, Interleukin 6 receptor alpha subunit, Interleukin-6 receptor alpha chain precursor, B cell stimulatory factor-2,Membrane glycoprotein 80, gp80, IL-6R, MGC104991.

Product # :

CYT-286

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

sIL-6R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (20-357) corresponding to the mature IL-6R protein, having a molecular weight of 42.25 kDa, with an aminoterminal hexahistidine tag.The sIL6R is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CD126 His-Tag protein is supplied in 20mM Tris-HCl, pH 8.0, 0.8M Urea & 50% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
The IL-6 receptor complex is composed of two membrane glycoproteins: the low affinity receptor and the signaltransducing component. The soluble form of IL6R is found in the urine of healthy adult humans and the serum of HIV positive individuals, as well as in the cell culture supernatants of stimulated PBMC’s. This soluble form of IL6R results from either proteolytic cleavage from the membrane, or an isoform derived splice variant.
Synonyms
IL6R-alpha, CD126, IL-6R 1, CD126 antigen, IL6RA, Interleukin 6 receptor, Interleukin 6 receptor alpha subunit, Interleukin-6 receptor alpha chain precursor, B cell stimulatory factor-2,Membrane glycoprotein 80, gp80, IL-6R, MGC104991.
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.
Background
Research Paper on Interleukin-6 Soluble Receptor Human Recombinant
Abstract:
Interleukin-6 (IL-6) Soluble Receptor Human Recombinant holds a critical place in immunological research, offering a unique lens into the intricate world of immune signaling. This research paper explores the molecular intricacies and the profound implications of IL-6 Soluble Receptor Human Recombinant in the context of immune responses. As we unravel its functions, synonyms, including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into the multifaceted role of immune regulation.
Introduction:
IL-6 Soluble Receptor Human Recombinant has emerged as a focal point of interest in the field of immunology. This paper aims to provide a comprehensive overview of its molecular characteristics and its role in shaping immune responses.
Molecular Insights and Receptor Specificity:
Delving into the molecular structure of IL-6 Soluble Receptor Human Recombinant, we uncover its pivotal role in binding IL-6. Its high affinity and specificity contribute to precise modulation of IL-6-mediated signaling pathways.
Mediating Immune Responses:
IL-6 exerts profound effects on immune cell activation, inflammation, and homeostasis. IL-6 Soluble Receptor Human Recombinant acts as a strategic player in fine-tuning these responses by sequestering IL-6, thereby influencing immune balance.
Synonyms and Complex Interactions:
Understanding the synonyms linked to IL-6, such as DIF, TNFA, and TNFSF2, enriches our comprehension of immune signaling networks. The interplay between IL-6 Soluble Receptor Human Recombinant and these molecules intricately shapes immune outcomes.
Potential Therapeutic and Diagnostic Applications:
The implications of IL-6 Soluble Receptor Human Recombinant extend beyond research settings. Its potential as a therapeutic candidate for immune-related disorders and its diagnostic utility in disease monitoring highlight its translational significance.
Clinical Relevance and Future Prospects:
IL-6 Soluble Receptor Human Recombinant's clinical potential is underscored by its role in diseases characterized by dysregulated IL-6 signaling. Investigating its role as a therapeutic intervention paves the way for innovative treatment strategies.
Conclusion:
In the realm of immunology, IL-6 Soluble Receptor Human Recombinant emerges as a key regulator of immune equilibrium. Its molecular intricacies, vital functions, and potential therapeutic implications position it as a cornerstone in unraveling immune responses and disease pathogenesis.
What is the molecular weight/Mw of SIL 6R HUMAN Protein?
SIL 6R HUMAN Protein has a total Mw of 42.25kDa.

What is the source or expression system of SIL 6R HUMAN Protein?
Escherichia Coli.

What is the Purity of SIL 6R HUMAN Protein?
SIL 6R HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of SIL 6R HUMAN Protein?
The biological functionality of SIL 6R HUMAN Protein will be determined in the future.

What is the amino acid sequence of SIL 6R HUMAN Protein?
SIL 6R HUMAN Protein is composed from 338 amino acids.

What applications can SIL 6R HUMAN Protein be used in?
SIL 6R HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for SIL 6R HUMAN Protein?
The endotoxin level is minimal, SIL 6R HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant SIL 6R 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 SIL 6R 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-12 p40 Human Recombinant, Baculovirus

NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.

Product # :

CYT-134

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Citations

Description

IL 12 p40 Human Recombinant produced in Hi-5 cell using Baculovirus is a single polypeptide chain containing 315 amino acids (23-328) and having a molecular mass of 35.8kDa.IL 12 p40 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Baculovirus

Formulation

The IL 12 p40 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT, 100mM PMSF and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
Synonyms
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPIWELKKD VYVVELDWYP DAPGEMVVLT CDTPEEDGIT WTLDQSSEVL GSGKTLTIQV KEFGDAGQYT CHKGGEVLSH SLLLLHKKED GIWSTDILKD QKEPKNKTFL RCEAKNYSGR FTCWWLTTIS TDLTFSVKSS RGSSDPQGVT CGAATLSAER VRGDNKEYEY SVECQEDSAC PAAEESLPIE VMVDAVHKLK YENYTSSFFI RDIIKPDPPK NLQLKPLKNS RQVEVSWEYP DTWSTPHSYF SLTFCVQVQG KSKREKKDRV FTDKTSATVI CRKNASISVR AQDRYYSSSW SEWASVPCSH HHHHH
Background
What is the molecular weight/Mw of IL12P40 HUMAN BACULOVIRUS Protein?
IL12P40 HUMAN BACULOVIRUS Protein has a total Mw of 35.8kDa.

What is the source or expression system of IL12P40 HUMAN BACULOVIRUS Protein?
Baculovirus.
What is the Purity of IL12P40 HUMAN BACULOVIRUS Protein?
IL12P40 HUMAN BACULOVIRUS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12P40 HUMAN BACULOVIRUS Protein?
The biological functionality of IL12P40 HUMAN BACULOVIRUS Protein will be determined in the future.

What is the amino acid sequence of IL12P40 HUMAN BACULOVIRUS Protein?
ADPIWELKKD VYVVELDWYP DAPGEMVVLT CDTPEEDGIT WTLDQSSEVL GSGKTLTIQV KEFGDAGQYT CHKGGEVLSH SLLLLHKKED GIWSTDILKD QKEPKNKTFL RCEAKNYSGR FTCWWLTTIS TDLTFSVKSS RGSSDPQGVT CGAATLSAER VRGDNKEYEY SVECQEDSAC PAAEESLPIE VMVDAVHKLK YENYTSSFFI RDIIKPDPPK NLQLKPLKNS RQVEVSWEYP DTWSTPHSYF SLTFCVQVQG KSKREKKDRV FTDKTSATVI CRKNASISVR AQDRYYSSSW SEWASVPCSH HHHHH.
What applications can IL12P40 HUMAN BACULOVIRUS Protein be used in?
IL12P40 HUMAN BACULOVIRUS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12P40 HUMAN BACULOVIRUS Protein?
The endotoxin level is minimal, IL12P40 HUMAN BACULOVIRUS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12P40 HUMAN BACULOVIRUS 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 IL12P40 HUMAN BACULOVIRUS?
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-9 Human Recombinant, Sf9

Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.

Product # :

CYT-866

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

IL-9 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-144 a.a.) including an 18 aa signal peptide (1-18 aa) and fused to a 6 aa His Tag at C-terminus containing a total of 150 amino acids and having a molecular mass of 14.5kDa.IL9 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL-9 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
IL-9 is a factor which is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
Synonyms
Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.
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
MLLAMVLTSA LLLCSVAGQG CPTLAGILDI NFLINKMQED PASKCHCSAN VTSCLCLGIP SDNCTRPCFS ERLSQMTNTT MQTRYPLIFS RVKKSVEVLK NNKCPYFSCE QPCNQTTAGN ALTFLKSLLE IFQKEKMRGM RGKIHHHHHH.
Background
What is the molecular weight/Mw of IL9 HUMAN, SF9 Protein?
IL9 HUMAN, SF9 Protein has a total Mw of 23kDa.

What is the source or expression system of IL9 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL9 HUMAN, SF9 Protein?
IL9 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL9 HUMAN, SF9 Protein?
The biological functionality of IL9 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of IL9 HUMAN, SF9 Protein?
MLLAMVLTSA LLLCSVAGQG CPTLAGILDI NFLINKMQED PASKCHCSAN VTSCLCLGIP SDNCTRPCFS ERLSQMTNTT MQTRYPLIFS RVKKSVEVLK NNKCPYFSCE QPCNQTTAGN ALTFLKSLLE IFQKEKMRGM RGKIHHHHHH.

What applications can IL9 HUMAN, SF9 Protein be used in?
IL9 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL9 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL9 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL9 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 IL9 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 alpha Human Recombinant, His Tag

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.

Product # :

CHM-241

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

Stromal Cell-Derived Factor-1 alpha Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 78 amino acids, having a molecular mass of 9.2 kDa. The SDF-1a is fused to 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was filtered (0.4µm) and lyophilized from a concentrated (0.5mg/ml) solution containing 20mM Tris buffer pH-7.5 and 20mM sodium chloride.

Purity

Greater than 95.0% as determined SDS-PAGE.

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, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF1A 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 add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK.
Background
What is the molecular weight/Mw of CXCL12 HUMAN ALPHA, HIS Protein?
CXCL12 HUMAN ALPHA, HIS Protein has a total Mw of 9.2kDa.

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

What is the Purity of CXCL12 HUMAN ALPHA, HIS Protein?
CXCL12 HUMAN ALPHA, HIS Protein is > 95% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of CXCL12 HUMAN ALPHA, HIS Protein?
MKHHHHHHAS KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK.

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

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

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

Where can I order bulk mg quantities of CXCL12 HUMAN ALPHA, 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:

Thymidylate Synthetase, Mouse Anti Human

TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.

Product # :

ANT-002

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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Citations

Formulation

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

More Info

Introduction
Thymidylate synthase catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5,10-methylenetetrahydrofolate as a cofactor which maintains the dTMP (thymidine-5-prime monophosphate) pool vital for DNA replication and repair. Thymidylate synthase plays an important role as a cancer chemotherapeutic agent. Thymidylate synthase is the primary site of action for 5-fluorouracil, 5-fluoro-2-prime-deoxyuridine, and several folate analogs.
Synonyms
TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.
Immunogen
Anti-human TYMS mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human TYMS amino acids 1-313 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT1S5AT.
Applications
TYMS antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot and Immunofluorescence analysis is 1:500 ~ 1000. Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
TYMS 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:

Gametocyte Specific Factor 1 Human Recombinant

Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.

Product # :

PRO-561

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Description

GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.
Synonyms
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
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 MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.

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:

Proteinase-3 Human

AGP7, P29, PR-3, ACPA, C-ANCA, MBT, MBN, Leukocyte proteinase 3, Neutrophil proteinase 4, Wegener granulomatosis autoantigen, Azurophil granule protein 7, myeloblastin, Serine proteinase neutrophil.

Product # :

ENZ-075

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Description

PRTN3 is a natural antigen having a molecular mass of 25kDa. PRTN3 is isolated from human peripheral blood leukocytes.

Source

Native.

Formulation

PRTN3 is supplied in 20mM Sodium Phosphate pH-6.2, 300mM NaCl, and 0.02% Lubrol.

Purity

Greater than 95% in the sum of different glycosylation isoforms according to following section as determined by SDS-PAGE and capillary electrophoresis.

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Introduction
PRTN3 is a polymorphonuclear leukocyte serine protease which degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) and causes emphysema once managed by tracheal insufflation to hamsters.
Synonyms
AGP7, P29, PR-3, ACPA, C-ANCA, MBT, MBN, Leukocyte proteinase 3, Neutrophil proteinase 4, Wegener granulomatosis autoantigen, Azurophil granule protein 7, myeloblastin, Serine proteinase neutrophil.
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. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG-type human auto-antibodies. Auto-antibodies to PR3 recognize conformation-dependent epitopes. 2. Standard ELISA test (checker-board analysis of positive/negative samples), immunodot analysis with positive/negative samples.
coating concentration
0.5-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
Applications
Western blot with rabbit anti-PR3 antisera and mouse anti-PR3 monoclonal antibodies.

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-17B Human Recombinant, Sf9

Interleukin-17B, IL-17B, Cytokine Zcyto7, Interleukin-20, Neuronal interleukin-17-related factor, IL20, NIRF, ZCYTO7.

Product # :

CYT-1004

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Description

IL17B Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 169 amino acids (21-180a.a.) and having a molecular mass of 19.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL17B is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL17B protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL-17 family members are glycoproteins secreted as dimers which induce local cytokine production and recruit granulocytes to sites of inflammation. The IL-17 family is comprised of at least six pro-inflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 is induced by IL-15 and IL-23, mostly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL17B Diseases associated with IL17B include spondyloarthropathy, and neuronitis, and among its related super-pathways are Mucin expression in CF via IL-6, IL-17 signaling pathways and STAT3 Pathway.
Synonyms
Interleukin-17B, IL-17B, Cytokine Zcyto7, Interleukin-20, Neuronal interleukin-17-related factor, IL20, NIRF, ZCYTO7.
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
ADPQPRSPKS KRKGQGRPGP LAPGPHQVPL DLVSRMKPYA RMEEYERNIE EMVAQLRNSS ELAQRKCEVN LQLWMSNKRS LSPWGYSINH DPSRIPVDLP EARCLCLGCV NPFTMQEDRS MVSVPVFSQV PVRRRLCPPP PRTGPCRQRA VMETIAVGCT CIFHHHHHH.

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:

Transcription Factor B2, Mitochondrial Human Recombinant

Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.

Product # :

PRO-1259

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Description

TFB2M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (20-396 a.a) and having a molecular mass of 45.8kDa.TFB2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TFB2M protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Transcription Factor B2, Mitochondrial (TFB2M) is an S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. In addition, TFB2M is essential for basal transcription of mitochondrial DNA, most likely via its interaction with POLRMT and TFAM. TFB2M promotes transcription independently of the methyltransferase activity. TFB2M like TFB1M, activates transcription of mitochondrial DNA more effectively, whilst having less methyltransferase activity.
Synonyms
Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.
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 MGSMAGRFCI LGSEAATRKH LPARNHCGLS DSSPQLWPEP DFRNPPRKAS KASLDFKRYV TDRRLAETLA QIYLGKPSRP PHLLLECNPG PGILTQALLE AGAKVVALES DKTFIPHLES LGKNLDGKLR VIHCDFFKLD PRSGGVIKPP AMSSRGLFKN LGIEAVPWTA DIPLKVVGMF PSRGEKRALW KLAYDLYSCT SIYKFGRIEV NMFIGEKEFQ KLMADPGNPD LYHVLSVIWQ LACEIKVLHM EPWSSFDIYT RKGPLENPKR RELLDQLQQK LYLIQMIPRQ NLFTKNLTPM NYNIFFHLLK HCFGRRSATV IDHLRSLTPL DARDILMQIG KQEDEKVVNM HPQDFKTLFE TIERSKDCAY KWLYDETLED R.

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-5 Human Recombinant, Sf9

EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.

Product # :

CYT-999

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Description

Interleukin-5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 124 amino acids (20-134a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).IL5 is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL5 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.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED₅₀ for this effect is less or equal to 1.5 ng/ml.

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Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
Synonyms
EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.
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
ADPIPTEIPT SALVKETLAL LSTHRTLLIA NETLRIPVPV HKNHQLCTEE IFQGIGTLES QTVQGGTVER LFKNLSLIKK YIDGQKKKCG EERRRVNQFL DYLQEFLGVM NTEWIIESHH HHHH.
Background
What is the molecular weight/Mw of IL 5 HUMAN, SF9 Protein?
IL 5 HUMAN, SF9 Protein has a total Mw of 14.2kDa.

What is the source or expression system of IL 5 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 5 HUMAN, SF9 Protein?
IL 5 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 HUMAN, SF9 Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effect is less or equal to 1.5 ng/ml.

What is the amino acid sequence of IL 5 HUMAN, SF9 Protein?
ADPIPTEIPT SALVKETLAL LSTHRTLLIA NETLRIPVPV HKNHQLCTEE IFQGIGTLES QTVQGGTVER LFKNLSLIKK YIDGQKKKCG EERRRVNQFL DYLQEFLGVM NTEWIIESHH HHHH.

What applications can IL 5 HUMAN, SF9 Protein be used in?
IL 5 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 5 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL 5 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 5 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 IL 5 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:

Granulocyte-Colony Stimulating Factor Human Recombinant, HEK

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-088

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Shipped at Room temp

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Description

G-CSF Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 21-25kDa due to glycosylation.The G-CSF is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The G-CSF was lyophilized from 1mg/ml in 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells (Mouse Myeloid Leukemia indicator cell line), the ED₅₀ is <0.01ng/ml.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution G-CSF 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 G-CSF in sterile 1xPBS containing 0.1% endotoxin-free recombinant HSA.
Background
What is the molecular weight/Mw of G CSF HUMAN, HEK Protein?
G CSF HUMAN, HEK Protein has a total Mw of 23kDa.

What is the source or expression system of G CSF HUMAN, HEK Protein?
HEK.

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

What is the Biological Activity of G CSF HUMAN, HEK Protein?
The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells (Mouse Myeloid Leukemia indicator cell line), the ED50 is <0.01ng/ml.

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

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

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

Description:

Monocyte Chemotactic Protein-1 Human Recombinant (CCL2), His Tag

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.

Product # :

CHM-246

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Description

MCP-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids (24-99) and having a molecular mass of 10.9 kDa. The MCP-1 is fused to 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The His Tag MCP-1 protein (1mg/ml) solution contains 20mM Tris-HCL pH-8.0, 1mM DTT and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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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 weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
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 MQPDAINAPV TCCYNFTNRK ISVQRLASYR RITSSKCPKE AVIFKTIVAK EICADPKQKW VQDSMDHLDK QTQTPKT.
Background
What is the molecular weight/Mw of CCL2 HUMAN, HIS Protein?
CCL2 HUMAN, HIS Protein has a total Mw of 10.9kDa.

What is the source or expression system of CCL2 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL2 HUMAN, HIS Protein?
CCL2 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 HUMAN, HIS Protein?
The biological functionality of CCL2 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL2 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQPDAINAPV TCCYNFTNRK ISVQRLASYR RITSSKCPKE AVIFKTIVAK EICADPKQKW VQDSMDHLDK QTQTPKT.

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

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

Who supplies recombinant CCL2 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 CCL2 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:

Fas-Associated Death Domain, Mouse Anti Human

GIG3, MORT1, MGC8528, FADD, Fas (TNFRSF6)-associated via death domain, Protein FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity, Growth-inhibiting gene 3 protein.

Product # :

ANT-344

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Formulation

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

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Introduction
FADD is an adaptor protein that cooperates with a variety of cell surface receptors and mediates cell apoptotic signals. Using its C-terminal death domain, FADD is recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and consequently it take parts in the death signaling initiated by these receptors. FADD interaction with the receptors reviels the N-terminal effector domain of, which allows it to recruit caspase-8, and thus initiate the cysteine protease cascade. Knockout studies in mice furthermore propose the significance of FADD in premature T cell development. FADD plays a role in survival/proliferation and cell cycle development. FADD also takes part in cellular sublocalization, protein phosphorylation, and inhibitory molecules.
Synonyms
GIG3, MORT1, MGC8528, FADD, Fas (TNFRSF6)-associated via death domain, Protein FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity, Growth-inhibiting gene 3 protein.
Immunogen
Anti-human FADD mAb is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human FADD amino acids 1-208 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PJ1D2AT.
Applications
FADD antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot is 1:1,000~1:2,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:1,000 and Immunohistochemistry is 1:50.
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
FADD 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:

Podoplanin clone P56F7AT, Mouse Anti Human

Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.

Product # :

ANT-641

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Formulation

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

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Introduction
Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors.
Synonyms
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human PDPN mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PDPN amino acids 99-207 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
P56F7AT.
Applications
PDPN antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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
PDPN antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

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Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Formulation

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info