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Search results

1000 results found for “allergy”

Name

Description

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  • View Data Sheet

    Name :

    ABHD12B Human

    Description:

    Abhydrolase Domain Containing 12B Human Recombinant

    BEM46L3, c14_5314, Abhydrolase domain-containing protein 12B, ABHD12B, C14orf29.

    Product # :

    PRO-1998

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    Description

    ABHD12B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-255a.a) and having a molecular mass of 31.0kDa. ABHD12B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ABHD12B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Abhydrolase Domain Containing 12B, also known as ABHD12B is a part of the serine esterase family. ABHD12B is a protein coding gene.

    • Synonyms

      BEM46L3, c14_5314, Abhydrolase domain-containing protein 12B, ABHD12B, C14orf29.

    • 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 MGSMLGIWHT VPSCRGEDAK GKDCCWYEAA LRDGNPIIVY LHGSAEHRAA SHRLKLVKVL SDGGFHVLSV DYRGFGDSTG KPTEEGLTTD AICVYEWTKA RSGITPVCLW GHSLGTGVAT NAAKVLEEKG CPVDAIVLEA PFTNMWVASI NYPLLKIYRN IPGFLRTLMD ALRKDKIIFP NDENVKFLSS PLLILHGEDD RTVPLEYGKK LYEIARNAYR NKERVKMVIF PPGFQHNLLC KSPTLLITVR DFLSKQWS.

    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.

    Abhd12B Human
  • View Data Sheet

    Name :

    CSTA Human, Active

    Description:

    Cystatin-A Human Recombinant, Active

    Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.

    Product # :

    PRO-086

    Price :

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    Description

    Cystatin A Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 118 amino acids (1-98a.a.) and having a molecular mass of 13.1 kDa.The Cystatin A is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cystatin-A (1mg/ml) in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

    Purity

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

    Biological Activity

    The IC50 value is < 1.0nM. The inhibitory function of CSTA on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.

    Citations

    More Info

    • Introduction

      Human Cystatin A (CSTA or Stefin A) belongs to family 1 of the cystatin superfamily, which is characterized by the lack of disulphide bonds and carbohydrates. CSTA is an intracellular inhibitor regulating the activities of cysteine proteases of the papain family such as Cathepsins B, H and L. Cystatin A has also been implicated in several disease states. Because of altered proteolytic state in cancer progression, CSTA may have a role in the proteolitic pathways.

    • Synonyms

      Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.

    • 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 MIPGGLSEAK PATPEIQEIV DKVKPQLEEK TNETYGKLEA VQYKTQVVAG TNYYIKVRAG DNKYMHLKVF KSLPGQNEDL VLTGYQVDKN KDDELTGF.

    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.

    Csta Human
  • View Data Sheet

    Name :

    Batroxobin

    Description:

    Batroxobin

    Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.

    Product # :

    PRO-2146

    Price :

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    • description
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    • Citations

    Description

    Batroxobin, isolated from Bothrops atrox snake venom, has an Mw of approximately 43kDa.

    Formulation

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

    Citations

    More Info

    • Introduction

      Batroxobin is a serin protease that reduces fibronogen levels and is originally extracted from snake venom of Bothrops Atrox. Batroxobin is used in defibrinogenation and thrombolysis and also has an effect on c-fos gene and growth factor.
      Batroxobin can efficiently restrain proliferation of VSMCs, by blocking the release and uptake of Ca2+, thus influencing [Ca2+]i.
      Batroxobin converts fibrinogen to fibrin through the restricted release of fibrinopeptide-A from fibrinogen to promote blood to clot. Unlike thrombin, it is not affected by heparin and hirudin.

    • Synonyms

      Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Store the lyophilized Batroxobin between 2-8°C. Do not freeze!

    • Solubility

      It is recommended to reconstitute the lyophilized Batroxobin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.

    • Unit Definition

      100BU [Batroxobin Units]=1mg.

    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.

    Batroxobin Native
  • View Data Sheet

    Name :

    Epigen Human, His

    Description:

    Epigen Human Recombinant, His Tag

    EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

    Product # :

    CYT-794

    Price :

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    Description

    EPGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (23-110 a.a) and having a molecular mass of 12.1kDa.EPGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EPGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.

    • Synonyms

      EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

    • 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 MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

    • Background

      What is the molecular weight/Mw of EPIGEN Protein?
      EPIGEN Protein has a total Mw of 12.1kDa.

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

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

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

      What is the amino acid sequence of EPIGEN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

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

      What is the endotoxin level for EPIGEN Protein?
      The endotoxin level is minimal, EPIGEN 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.

    Epgn Human His
  • View Data Sheet

    Name :

    CALML3 Human

    Description:

    Calmodulin Like 3 Human Recombinant

    Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.

    Product # :

    PRO-1323

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    Description

    CALML3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-149 a.a.) and having a molecular mass of 19kDa.CALML3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CALML3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Calmodulin Like 3 (CALML3) is a member of the calmodulin family and contains 4 EF-hand domains. The CALML3 protein may be similar to that of genuine calmodulin and may in fact compete with calmodulin by binding, with different affinities, to cellular substrates. CALML3 protein is expressed in normal mammary, prostate, cervical, and epidermal tissues.

    • Synonyms

      Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.

    • 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 MGSHMADQLT EEQVTEFKEA FSLFDKDGDG CITTRELGTV MRSLGQNPTE AELRDMMSEI DRDGNGTVDF PEFLGMMARK MKDTDNEEEI REAFRVFDKD GNGFVSAAEL RHVMTRLGEK LSDEEVDEMI RAADTDGDGQ VNYEEFVRVL VSK.

    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.

    Calml3 Human
  • View Data Sheet

    Name :

    THRSP Human

    Description:

    Thyroid Hormone Responsive Human Recombinant

    Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 protein.

    Product # :

    PRO-1485

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    Description

    THRSP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146 a.a.) and having a molecular mass of 18.9kDa.THRSP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thyroid Hormone Responsive (THRSP) is a member of the SPOT14 family. THRSP is similar to the gene product of S14, a rat gene whose expression is limited to liver and adipose tissue and is controlled by nutritional and hormonal factors. THRSP is expressed in liver and adipocytes, specifically in lipomatous modules. In addition It is expressed in lipogenic breast cancers, which suggests a role in controlling tumor lipid metabolism.

    • Synonyms

      Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 protein.

    • 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 MGSMQVLTKR YPKNCLLTVM DRYAAEVHNM EQVVMIPSLL RDVQLSGPGG QAQAEAPDLY TYFTMLKAIC VDVDHGLLPR EEWQAKVAGS EENGTAETEE VEDESASGEL DLEAQFHLHF SSLHHILMHL TEKAQEVTRK YQEMTGQVW.

    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.

    Thrsp Human
  • View Data Sheet

    Name :

    Globular Adiponectin Human

    Description:

    Globular Adiponectin Human Recombinant

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

    Product # :

    CYT-615

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    Description

    gAcrp30 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 145 amino acids and having a molecular mass of 16.7kDa. The gAcrp30 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 10mM sodium phosphate & 0.5mM DTT, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.

    Citations

    More Info

    • Introduction

      gAcrp30 globular protein, exists as a result of proteolytic processing of adiponectin. Adiponectin is manufactured and secreted solely by adipocytes, and is a highly obtained plasma protein, accounting for up to 0.05% of total serum protein. Similar to Adiponectin, gAcrp30 is able of lowering hyperglycemia and reversing INS resistance. In addition, gAcrp30 is an significant protein that is involved in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids. AdipoR1 & AdipoR2 are the 2 signaling receptors for adiponectin and gAcrp30 that were recently been identified.

    • Synonyms

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

    • Stability

      For long term, store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time two weeks.

    • Solubility

      We recommended reconstituting gAcrp30 at a concentration of 0.1mg per ml with 10mM sodium phosphate & 0.5mM DTT, pH 7.5. which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

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

      What is the Biological Activity of ADIPONECTIN Protein?
      gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.

      What is the amino acid sequence of ADIPONECTIN Protein?
      MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.

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

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

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

    Globular Adiponectin Human
  • View Data Sheet

    Name :

    PVALB Human

    Description:

    Parvalbumin Human Recombinant

    Parvalbumin alpha, PVALB, D22S749, MGC116759.

    Product # :

    PRO-004

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    Description

    PVALB Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-110 a.a.) and having a molecular mass of 14.6kDa. The PVALB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PVALB solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Parvalbumin alpha (PVALB) is a member of a larger group of EF hand proteins. PVALB is a high affinity calcium ion-binding protein which is structurally and functionally similar to calmodulin and troponin C. Parvalbumin is expressed in a specific population of GABAergic interneurones which are believed to have a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus.

    • Synonyms

      Parvalbumin alpha, PVALB, D22S749, MGC116759.

    • 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 MGSHMSMTDL LNAEDIKKAV GAFSATDSFD HKKFFQMVGLKKKSADDVKK VFHMLDKDKS GFIEEDELGF ILKGFSPDAR DLSAKETKML MAAGDKDGDG KIGVDEFSTL VAES.

    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.

    Pvalb Human
  • View Data Sheet

    Name :

    REG3A Human

    Description:

    Regenerating Islet-Derived 3 Alpha Human Recombinant

    Regenerating islet-derived protein 3 alpha, Reg III-alpha, Pancreatitis-associated protein 1, REG3A, HIP, PAP, PAP1, REG3, INGAP, PAP-H, PBCGF, REG-III.

    Product # :

    PRO-421

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    Description

    The Recombinant Human REG3A protein is produced with N-terminal fusion of His Tag. The REG3A His -Tagged Fusion Protein is an 18.4 kDa protein containing 149 amino acid residues of the Human REG3A and 16 additional amino acid residues- His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Pancreatitis-associated protein (PAP) is a secretory protein not normally expressed in healthy pancreas but highly induced during acute pancreatitis. While PAP has been shown to be anti-bacterial and antiapoptotic in vitro, its definitive biological function in vivo is not clear. Using antisepse oligonucleotides, inhibition of PAP expression significantly worsened pancreatitis in a rat model. During pancreatitis, PAP released by the pancreas could mediate lung inflammation through induction of hepatic TNF- alpha expression and subsequent increase in circulating TNF-alpha.
      PAP is activated in primary liver cancers. In normal liver, the protein is undetectable in normal mature hepatocytes and found only in some ductular cells, representing potential hepatic progenitor cells. PAP can be considered hepatic cytokine that combines mitogenic and anti-apoptotic functions regarding hepatocytes, and consequently acts as a growth factor in vivo to enhance liver regeneration. In pancreatic cancor, PAP was overexpressed in 79% (30 of 38) of pancreatic ductal adenocarcinoma, 19% (7 of 36) of chronic pancreatitis, and 29% (2 of 7) of mucinous cystadenoma. PAP was found in malignant ductular structures in pancreatic carcinomas as well as in benign proliferating ductules and acinar cells in chronic pancreatitis. Elevation of PAP in patients with pancreatic cancer is not merely explainable by concomitant pancreatitis, but seems to be due to increased PAP production by the cancer cells and is also correlated to tumour load as expressed by the UICC stages.
      Epithelial expression of PAP was induced under intestinal mucosal inflammation initiated by exposure to commensal bacteria or DSS as well as inflamed IBD colon. Increased serum level of PAP diagnosed ileal location in active Crohn disease with a sensitivity of 60%, a specificity of 94%, a positive predictive value of 84% and a negative predictive value of 81%. Elevated serum PAP (> 50 ng/mL) is significantly associated with disease activity and ileal location of Crohn disease.

    • Synonyms

      Regenerating islet-derived protein 3 alpha, Reg III-alpha, Pancreatitis-associated protein 1, REG3A, HIP, PAP, PAP1, REG3, INGAP, PAP-H, PBCGF, REG-III.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMEEPQ RELPSARIRC PKGSKAYGSH CYALFLSPKS WTDADLACQK RPSGNLVSVL SGAEGSFVSS LVKSIGNSYS YVWIGLHDPT QGTEPNGEGW EWSSSDVMNY FAWERNPSTI SSPGHCASLS RSTAFLRWKD YNCNVRLPYV CKFTD.

    • Applications

      Western blotting, ELISA.

    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.

    Reg3A Human
  • View Data Sheet

    Name :

    Chitodextrinase

    Description:

    Chitodextrinase Clostridium Botulinum Recombinant

    Product # :

    ENZ-032

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    Description

    Chitodextrinase Clostridium Botulinum Recombinant fused with a 13 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 590 amino acids and having a molecular mass of 66.9kDa. The Chitodextrinase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Chitodextrinase lyophilized from a 0.2µm filtered concentrated solution in PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Chitodextrinase is a unique membrane-bound endoenzyme. The chitodextrinase enzyme cleaves soluble oligomers, but not chitin, to the di- and trisaccharides. Chitodextrinase is unable to solubilize chitin, but it can catalyze the hydrolysis of high to low molecular weight soluble chitin oligosaccharides.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Chitodextrinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Chitodextrinase 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 Chitodextrinase in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HMRGSGSHHHHHHKEKFKTTKIKNSSELNRKLVGYFPEWAYSSEAQGYFNVTD
      LQWDSLTHIQYSFAMVDPSTNKITLSNKHAAIEEDFSEFDLNYNGKKIELDPS
      LPYKGHFNVLQTMKKNYPDVSLLISVGGWTGTRCFYTMIDTDNRINTFADSCV
      DFIRKYGFDGVDIDFEYPSSTSQSGNPDDFDLSEPRRTKLNERYNILIKTLRE
      KIDMASKEDGKEYLLTAAVTASPWVLGGISDNTYAKYLDFLSIMSYDYHGGWN
      EYVEHLAGIYPNKEDRETVTQIMPTLCMDWAYRYYRGVLPAEKILMGIPYYTR
      GWENVQGGINGLHGSSKTPASGKYNILGDDLNNDGVLEPDGANPLWHVLNLME
      QDPNLKVYWDEISKVPYVWQNDKKVFVSFENEKSIDARLEYIQNKNLGGALIW
      VMNGDYGLNPNYVEGSNKINEGKYTFGDTLTKRLSQGLKKMGVCNKTPDDLNI
      SLEPINVDVKFNGKYDHPNYTYSIDITNYTDKEIKGGWNVSFDLPKSAVFKSS
      WGGTYSVTDNGDFNTITLTSGAWQNIAPNSTITVQGMIGLCFSGIRNVTFNGM
      NPIGNDK.

    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.

    Chitodextrinase
  • View Data Sheet

    Name :

    SAA1 Human, His

    Description:

    Serum Amyloid A Human Recombinant (APO-SAA1), His Tag

    Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.

    Product # :

    CYT-675

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    Description

    SAA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (19-122 a.a.) and having a total molecular mass of 13.9 kDa. SAA1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAA1 solution contains 20mM Tris buffer(pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SAA1 protein is an acute phase apolipoprotein reactant which is produced mostly by hepatocytes and under regulation of inflammatory cytokines. SAA1 (Serum amyloid A1) protein is produced mainly in the liver and circulates in low levels in the blood. The SAA1 seems to have a role in the immune system. SAA1 protein levels increase in the blood and other tissues under conditions of inflammation. SAA1 may facilitate the repair of injured tissues; it also acts as an antibacterial agent, and signals the migration of germ-fighting cells to sites of infection. SAA1 also functions as an apolipoprotein of the HDL complex.
      Elevated levels of SAA1 ultimately affect secondary amyloidosis, extracellular amassing of amyloid fibrils, resulting from a circulating precursor, in a variety of tissues and organs. The most widespread type of amyloidosis appears secondary to chronic inflammatory disease, mainly rheumatoid arthritis. The SAA1 cleavage product a designated amyloid protein A is deposited systemically as amyloid in vital organs such as the liver, spleen, and kidneys in chronic inflammatory diseases patients. These deposits are extremely insoluble and resistant to proteolysis; they disrupt tissue structure and compromise performance.

    • Synonyms

      Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.

    • 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 MRSFFSFLGE AFDGARDMWR AYSDMREANY IGSDKYFHAR GNYDAAKRGP GGVWAAEAIS DARENIQRFF GHGAEDSLAD QAANEWGRSG KDPNHFRPAG LPEKY.

    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.

    Saa1 Human
  • View Data Sheet

    Name :

    SORBS3 Human

    Description:

    Sorbin And SH3 Domain Containing 3 Human Recombinant

    Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.

    Product # :

    PRO-1829

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    Description

    SORBS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329) and having a molecular mass of 39.1 kDa. SORBS3 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The SORBS3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.

    • Synonyms

      Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.

    • 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 MGSMADGGSP FLGRRDFVYP SSTRDPSASN GGGSPARREE KKRKAARLKF DFQAQSPKEL TLQKGDIVYI HKEVDKNWLE GEHHGRLGIF PANYVEVLPA DEIPKPIKPP TYQVLEYGEA VAQYTFKGDL EVELSFRKGE HICLIRKVNE NWYEGRITGT GRQGIFPASY VQVSREPRLR LCDDGPQLPT SPRLTAAARS ARHPSSPSAL RSPADPIDLG GQTSPRRTGF SFPTQEPRPQ TQNLGTPGPA LSHSRGPSHP LDLGTSSPNT SQIHWTPYRA MYQYRPQNED ELELREGDRV DVMQQCDDGW FVGVSRRTQK FGTFPGNYVA PV

    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.

    Sorbs3 Human
  • View Data Sheet

    Name :

    EPYC Human

    Description:

    Epiphycan Human Recombinant

    Epiphycan, SLRR3B, DSPG3, EPYC Dermatan sulfate proteoglycan 3, Proteoglycan-Lb, PG-Lb, Small chondroitin/dermatan sulfate proteoglycan, PGLB, epiphycan proteoglycan.

    Product # :

    PRO-2778

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    Description

    EPYC Human Recombinant produced in HEK293 Cells.is a single, glycosylated polypeptide chain containing 309 amino acids (20-322 a.a.) and having a molecular mass of 35.5kDa. EPYC is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    EPYC protein solution (0.5mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    >60% and is measured by the ability of the immobilized protein to support the adhesion of Saos‑2 human osteosarcoma cells. When cells are added to human DSPG3 1.25 ug/ml and human fibronectin 0.5 ug/ml coated plates.

    Citations

    More Info

    • Synonyms

      Epiphycan, SLRR3B, DSPG3, EPYC Dermatan sulfate proteoglycan 3, Proteoglycan-Lb, PG-Lb, Small chondroitin/dermatan sulfate proteoglycan, PGLB, epiphycan proteoglycan.

    • 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

      APTLESINYD SETYDATLED LDNLYNYENI PVDKVEIEIA TVMPSGNREL LTPPPQPEKA QEEEEEEEST PRLIDGSSPQ EPEFTGVLGP HTNEDFPTCL LCTCISTTVY CDDHELDAIP PLPKNTAYFY SRFNRIKKIN KNDFASLSDL KRIDLTSNLI SEIDEDAFRK LPQLRELVLR DNKIRQLPEL PTTLTFIDIS NNRLGRKGIK QEAFKDMYDL HHLYLTDNNL DHIPLPLPEN LRALHLQNNN ILEMHEDTFC NVKNLTYIRK ALEDIRLDGN PINLSKTPQA YMCLPRLPVG SLVHHHHHH.

    • Background

      Epiphycan, a small leucine-rich proteoglycan, has gained recognition as a crucial player in tissue development, repair, and homeostasis. This research aims to explore the significance of epiphycan and its potential therapeutic applications in various physiological and pathological contexts. By investigating the properties and functions of epiphycan, we can uncover new insights into its role in tissue biology and its potential as a target for therapeutic interventions.

      Epiphycan is a proteoglycan primarily expressed in skeletal tissues, such as the growth plate of long bones, articular cartilage, and intervertebral discs. It is an extracellular matrix component that interacts with various growth factors, cytokines, and other matrix proteins, influencing cell behavior and tissue organization. The unique structure of epiphycan, comprising a core protein and attached glycosaminoglycan chains, endows it with diverse regulatory functions.

      The involvement of epiphycan in tissue development and repair has been highlighted in several studies. It plays a critical role in chondrogenesis, modulating the differentiation and proliferation of chondrocytes. Furthermore, epiphycan has been implicated in the maintenance of articular cartilage integrity and the prevention of osteoarthritis progression. Its ability to interact with growth factors, such as transforming growth factor-beta (TGF-β) and bone morphogenetic proteins (BMPs), suggests its potential as a modulator of tissue regeneration and repair.

      This research will delve into the molecular mechanisms underlying epiphycan's functions and its interactions with various signaling pathways. The paper will explore the regulatory effects of epiphycan on cell behavior, matrix remodeling, and tissue architecture. Additionally, it will examine the implications of epiphycan dysregulation in pathological conditions, such as osteoarthritis, and discuss its potential as a therapeutic target for promoting tissue regeneration and repair.

      The study will also investigate the diagnostic and prognostic value of epiphycan in various diseases and conditions. Understanding the expression patterns and alterations of epiphycan in different tissues and disease states may provide valuable insights into disease progression and aid in the development of personalized treatment strategies.

      By unraveling the multifaceted roles of epiphycan in tissue biology and its potential therapeutic applications, this research aims to contribute to our understanding of tissue development and repair mechanisms. Furthermore, it highlights the potential of epiphycan as a target for therapeutic interventions and emphasizes the importance of further investigations to harness its full therapeutic potential.

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    Epyc Protein
  • View Data Sheet

    Name :

    FCAR Human

    Description:

    Fc Fragment Of IgA Receptor Human Recombinant

    Fc Fragment Of IgA Receptor, Fc Fragment Of IgA, Receptor For, CD89, Immunoglobulin Alpha Fc Receptor, Fc Alpha Receptor, FCAR Variant 14, IgA Fc Receptor, CD89 Antigen, CTB-61M7.2, FcalphaRI, Immunoglobulin alpha Fc receptor, IgA Fc receptor.

    Product # :

    PRO-2471

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    Description

    FCAR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 215 amino acids (22-227a.a.) and having a molecular mass of 24.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).FCAR is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fc Fragment Of IgA Receptor, also known as FCAR, is part of the multichain immune recognition receptor family which is the most abundant immunoglobulin in mucosal areas however it is only the second most common antibody isotype in serum. FCAR participates in both pro-and anti-inflammatory responses depending on the state of IgA bound. FCAR is also a vital Fc receptor for neutrophil killing of tumor cells. Once FCAR expressing neutrophils interact with IgA-opsonized tumor cells, the neutrophils not only show antibody-dependent cell-mediated cytotoxicity, but also release the cytokines TNF-α and IL-1β which cause increased neutrophil migration to the site.

    • Synonyms

      Fc Fragment Of IgA Receptor, Fc Fragment Of IgA, Receptor For, CD89, Immunoglobulin Alpha Fc Receptor, Fc Alpha Receptor, FCAR Variant 14, IgA Fc Receptor, CD89 Antigen, CTB-61M7.2, FcalphaRI, Immunoglobulin alpha Fc receptor, IgA Fc receptor.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPQEGDFPM PFISAKSSPV IPLDGSVKIQ CQAIREAYLT QLMIIKNSTY REIGRRLKFW NETDPEFVID HMDANKAGRY QCQYRIGHYR FRYSDTLELV VTGLYGKPFL SADRGLVLMP GENISLTCSS AHIPFDRFSL AKEGELSLPQ HQSGEHPANF SLGPVDLNVS GIYRCYGWYN RSPYLWSFPS NALELVVTDS IHQDYTTQNH HHHHH.

    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.

    Fcar Human
  • View Data Sheet

    Name :

    ITGB4 Human

    Description:

    Integrin Beta 4 Human Recombinant

    Integrin beta-4, GP150, CD104, ITGB4, Integrin Subunit Beta 4, CD104 Antigen, Integrin, Beta 4, Integrin Beta-4.

    Product # :

    PRO-2528

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    Description

    ITGB4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 691 amino acids (28-710a.a.) and having a molecular mass of 77.5kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ITGB4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ITGB4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ITGB4 (integrin beta-4 isoform 1) belongs to the Integrin beta family. ITGB4 forms noncovalent heterodimers with Integrin alpha 6 and takes part in the formation of epithelial hemidesmosomes. ITGB4 has a vital structural role in the hemidesmosome of epithelial cells and is needed for the regulation of keratinocyte motility & polarity. ITGB4 leans towards the association with alpha 6 subunit and is expected to take a key role in the biology of invasive carcinoma.

    • Synonyms

      Integrin beta-4, GP150, CD104, ITGB4, Integrin Subunit Beta 4, CD104 Antigen, Integrin, Beta 4, Integrin Beta-4.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      NRCKKAPVKS CTECVRVDKD CAYCTDEMFR DRRCNTQAEL LAAGCQRESI VVMESSFQIT EETQIDTTLR RSQMSPQGLR VRLRPGEERH FELEVFEPLE SPVDLYILMD FSNSMSDDLD NLKKMGQNLA RVLSQLTSDY TIGFGKFVDK VSVPQTDMRP EKLKEPWPNS DPPFSFKNVI SLTEDVDEFR NKLQGERISG NLDAPEGGFD AILQTAVCTR DIGWRPDSTH LLVFSTESAF HYEADGANVL AGIMSRNDER CHLDTTGTYT QYRTQDYPSV PTLVRLLAKH NIIPIFAVTN YSYSYYEKLH TYFPVSSLGV LQEDSSNIVE LLEEAFNRIR SNLDIRALDS PRGLRTEVTS KMFQKTRTGS FHIRRGEVGI YQVQLRALEH VDGTHVCQLP EDQKGNIHLK PSFSDGLKMD AGIICDVCTC ELQKEVRSAR CSFNGDFVCG QCVCSEGWSG QTCNCSTGSL SDIQPCLREG EDKPCSGRGE CQCGHCVCYG EGRYEGQFCE YDNFQCPRTS GFLCNDRGRC SMGQCVCEPG WTGPSCDCPL SNATCIDSNG GICNGRGHCE CGRCHCHQQS LYTDTICEIN YSAIHPGLCE DLRSCVQCQA WGTGEKKGRT CEECNFKVKM VDELKRAEEV VVRCSFRDED DDCTYSYTME GDGAPGPNST VLVHKKKDCP PGSLEHHHHH H

    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.

    Itgb4 Human
  • View Data Sheet

    Name :

    VTCN1 Human, Sf9

    Description:

    V-Set Domain Containing T Cell Activation Inhibitor 1 Human Recombinant, Sf9

    V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.

    Product # :

    PRO-2439

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    Description

    VTCN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 244 amino acids (25-259a.a.) and having a molecular mass of 26.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). VTCN1 is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    VTCN1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      V-Set Domain Containing T Cell Activation Inhibitor 1, also known as VCTN1, is part of the B7 costimulatory protein family. Proteins in this family are located on the surface of antigen-presenting cells and interact with ligand bound to receptors on the surface of T cells. High level of the encoded protein has been associated with tumor progression. VCTN1 also takes part in promoting epithelial cell transformation.

    • Synonyms

      V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPLIIGFGI SGRHSITVTT VASAGNIGED GILSCTFEPD IKLSDIVIQW LKEGVLGLVH EFKEGKDELS EQDEMFRGRT AVFADQVIVG NASLRLKNVQ LTDAGTYKCY IITSKGKGNA NLEYKTGAFS MPEVNVDYNA SSETLRCEAP RWFPQPTVVW ASQVDQGANF SEVSNTSFEL NSENVTMKVV SVLYNVTINN TYSCMIENDI AKATGDIKVT ESEIKRRSHL QLLNSKASHH HHHH.

    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.

    Vtcn1 Protein
  • View Data Sheet

    Name :

    ACY3 Human

    Description:

    AminoAcylase-3 Human Recombinant

    Aspartoacylase-2, Acylase III, Aminoacylase-3, ACY-3, Hepatitis C virus core-binding protein 1, HCBP1, ACY3, ASPA2.

    Product # :

    ENZ-153

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    Description

    ACY3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-319 a.a.) and having a molecular mass of 37.6kDa.ACY3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACY3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Aspartoacylase 3 (ACY3) belongs to the Aspartoacylase subfamily. ACY3 has a vital role in deacetylating mercapturic acids in kidney proximal tubules. Aspartoacylase 3 localizes to the cytoplasm of S2 and S3 proximal tubules and also to the apical domain of S1 proximal tubules. In addition, ACY3 protein is expressed at low levels in the stomach, testis, heart, brain, lung and liver, and can function as an HCV (Hepatitis C virus) core binding protein.

    • Synonyms

      Aspartoacylase-2, Acylase III, Aminoacylase-3, ACY-3, Hepatitis C virus core-binding protein 1, HCBP1, ACY3, ASPA2.

    • 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 MGSMCSLPVP REPLRRVAVT GGTHGNEMSG VYLARHWLHA PAELQRASFS AVPVLANPAA TSGCRRYVDHDLNRTFTSSF LNSRPTPDDP YEVTRARELN QLLGPKASGQ AFDFVLDLHN TTANMGTCLI AKSSHEVFAM HLCRHLQLQY PELSCQVFLY QRSGEESYNL DSVAKNGLGL ELGPQPQGVL RADIFSRMRT LVATVLDFIE LFNQGTAFPA FEMEAYRPVG VVDFPRTEAG HLAGTVHPQL QDRDFQPLQP GAPIFQMFSG EDLLYEGEST VYPVFINEAA YYEKGVAFVQ TEKFTFTVPA MPALTPAPSP AS.

    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.

    Acy3 Human
  • View Data Sheet

    Name :

    EBI3 Mouse

    Description:

    Epstein Barr Virus Induced 3 Mouse Recombinant

    IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.

    Product # :

    CYT-621

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    Description

    EBI3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 22.9kDa. The Murine EBI3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EBI3 was lyophilized from 10mM Sodium Citrate pH-3.

    Purity

    Greater than 90% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.

    • Synonyms

      IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 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 EBI3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.

    • Background

      What is the molecular weight/Mw of EBI3 Protein?
      EBI3 Protein has a total Mw of 22.9kDa.

      What is the source or expression system of EBI3 Protein?
      Escherichia Coli.

      What is the Purity of EBI3 Protein?
      EBI3 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of EBI3 Protein?
      The biological functionality of EBI3 Protein will be determined in the future.

      What is the amino acid sequence of EBI3 Protein?
      MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.

      What applications can EBI3 Protein be used in?
      EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EBI3 Protein?
      The endotoxin level is minimal, EBI3 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.

    Ebi3 Mouse
  • View Data Sheet

    Name :

    IL 23 Human, His

    Description:

    Interleukin-23 Human Recombinant, His Tag

    Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.

    Product # :

    CYT-067

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    Description

    Recombinant Human Interleukin-23 produced in Sf9 Baculovirus cells is a glycosylated heterodimer composed of 2 disulfide-linked subunits. A p19 subunit which is unique to IL23 and a p40 subunit which is shared with IL12. The p19 subunit/IL23A (20-189aa, total of 176 aa, MW 19.5kDa) and p40 subunit /IL12B (23-328aa, total of 306 aa, MW 34.6kDa), the total predicted molecular mass of 54.1kDa (Molecular weight on SDS-PAGE will appear higher). IL23 is fused to a 6 aa His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL23 protein solution (1mg/ml) contains PBS (pH7.4) and 10% glycerol.

    Purity

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

    Citations

    More Info

    • Introduction

      IL23 is composed of a subunit of the heterodimeric cytokine IL23 and the p40 subunit of interleukin 12 (IL12B). Interleukin-23 (IL-23) belongs to the IL-12 family and is produced by antigen presenting cells. IL-23 using IL12RB1 and IL-23R (specific for IL-23) can activate STAT and NF-kB pathways and stimulate the production of interferon-gamma. ). IL-23 is known to take a vital part in the inflammation process and is associated with auto immune diseases. However, unlike IL12, which acts primarily on naive CD4(+) T cells, IL23 preferentially acts on memory CD4(+) T cells.

    • Synonyms

      Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.

    • 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

      IL12B: IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.

      IL23A: RAVPGGSSPA WTQCQQLSQK LCTLAWSAHP LVGHMDLREE GDEETTNDVP HIQCGDGCDP QGLRDNSQFC LQRIHQGLIF YEKLLGSDIF TGEPSLLPDS PVGQLHASLL GLSQLLQPEG HHWETQQIPS LSPSQPWQRL LLRFKILRSL QAFVAVAARV FAHGAATLSP HHHHHH.

    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.

    Il 23 Human His
  • View Data Sheet

    Name :

    Borrelia Spielmanii OspC

    Description:

    Borrelia Spielmanii Outer Surface Protein C Recombinant

    Product # :

    BOR-009

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    Description

    Recombinant Borrelia Spielmanii Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 24kDa. Borrelia Spielmanii OspC is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Spielmanii OspC is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma; suitable for LTT (lymphocyte transformation test).

    • Applications

      Western blot with patient sample.

    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.

    Borrelia Spielmanii Ospc
  • View Data Sheet

    Name :

    IL7 Human, His

    Description:

    Interleukin-7 Human Recombinant, His Tag

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-485

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    Description

    IL-7 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 152 amino acids fragment (26-177) and having a total molecular mass of 21.97 kDa with an amino-terminal hexahistidine tag. The IL-7 His-Tag protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin -7 His is supplied in 1x PBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Interleukin-7 is a potent lymphoid cell growth factor produced primarily by stromal cells.
      IL-7 has been shown to support the proliferation and differentiation of pre B- and early T cells as well as displaying a biological effect on cells of NK and myeloid lineages.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • 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

      What is the molecular weight/Mw of IL7 HUMAN, HIS Protein?
      IL7 HUMAN, HIS Protein has a total Mw of 21.97kDa.

      What is the source or expression system of IL7 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL7 HUMAN, HIS Protein?
      IL7 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of IL7 HUMAN, HIS Protein?
      IL7 HUMAN, HIS Protein is composed from 152 amino acids.

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

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

      Who supplies recombinant IL7 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 IL7 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.

    Il 7 Human His
  • View Data Sheet

    Name :

    IL10 Human

    Description:

    Interleukin-10 Human Recombinant

    B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

    Product # :

    CYT-500

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    Description

    Interleukin-10 Human Recombinant produced in E.coli is a single non-glycosylated polypeptide chains containing 161 amino acids each and having a molecular mass of 18.6kDa.The IL-10 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent co-stimulation (with murine IL-4) of MC/9 cells was found to be less than 2.0ng/ml, corresponding to a specific activity of 5.0×105 IU/mg.

    Citations

    More Info

    • Introduction

      Recombinant 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

      B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL10 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-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.

    • Background

      What is the molecular weight/Mw of IL10 HUMAN Protein?
      IL10 HUMAN Protein has a total Mw of 18.6kDa.

      What is the source or expression system of IL10 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL10 HUMAN Protein?
      IL10 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL10 HUMAN Protein?
      The ED50 as determined by the dose-dependent co-stimulation (with murine IL-4) of MC/9 cells was found to be less than 2.0ng/ml, corresponding to a specific activity of 5.0×105 IU/mg.

      What is the amino acid sequence of IL10 HUMAN Protein?
      MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.

      What applications can IL10 HUMAN Protein be used in?
      IL10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL10 HUMAN Protein?
      The endotoxin level is minimal, IL10 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL10 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 IL10 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.

    Il 10 Human
  • View Data Sheet

    Name :

    IL21R Mouse

    Description:

    Interleukin-21 Receptor Mouse Recombinant

    Interleukin-21 receptor, IL-21 receptor, IL-21R, Il21r, Lymphocyte receptor beta, LR-beta, Novel interleukin receptor, Novel cytokine receptor 8, NR8, Novel interleukin receptor, CD360, CD360 antigen, NILR, Nilr.

    Product # :

    CYT-1204

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    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
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    • More Info
    • Citations

    Description

    IL21R Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 457amino acids (20-237 a.a) and having a molecular mass of 52 kDa.IL21R is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The IL21R solution (0.25mg/1ml) contains PBS (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit IFN-g secretion using NK-92 human natural killer cells. The ED50 range ≤ 4 ug/ml with mouse IL-2.

    Citations

    More Info

    • Introduction

      IL-21 is produced by CD4+ T cells in response to antigenic stimulation. Its action enhances antigen-specific responses of immune cells. The biological effects of IL-21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation (in conjuction) with IL-4 of IgG production, and induction of apoptotic effects in na?ve B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the gamma chain (?c) found in other cytokine receptors including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.

    • Synonyms

      Interleukin-21 receptor, IL-21 receptor, IL-21R, Il21r, Lymphocyte receptor beta, LR-beta, Novel interleukin receptor, Novel cytokine receptor 8, NR8, Novel interleukin receptor, CD360, CD360 antigen, NILR, Nilr.

    • 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

      CLDLTCYTDY LWTITCVLET RSPNPSILSL TWQDEYEELQ DQETFCSLHR SGHNTTHIWY TCHMRLSQFL SDEVFIVNVT DQSGNNSQEC GSFVLAESIK PAPPLNVTVA FSGRYDISWD SAYDEPSNYV LRGKLQYELQ YRNLRDPYAV RPVTKLISVD SRNVSLLPEE FHKDSSYQLQ VRAAPQPGTS FRGTWSEWSD PVIFQTQAGE PEAGWDPHLE 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.

    Il21R Mouse
  • View Data Sheet

    Name :

    B2M Human

    Description:

    Beta-2 Microglobulin Human

    Beta-2-microglobulin, B2M.

    Product # :

    PRO-553

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    Shipped at Room temp

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    Description

    Human Beta-2 Microglobulin produced in Human urine from patients with tubular proteinuria having a molecular mass of 12KDa.

    Source

    Human urine from patients with tubular proteinuria.

    Formulation

    Lyophilized from 0.02M NH4HCO3 pH-7.2, 0.15M NaCl, 1mM EDTA, 2% mannitol and 0.09% NaN3.

    Purity

    Greater than 95%.

    Citations

    More Info

    • Introduction

      Beta 2 microglobulin is an 11 kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2 microglobulin associates with class I-like molecules such as CD1 and Qa as well as with the alpha chain of MHC class I molecules. Very limited amounts of MHC class I molecules can be found on the surface in the absence of Beta 2 microglobulin. CD8 T cells cannot develop in the absence of MHC class I.
      Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinaemia, renal failure, or kidney transplants. Human Beta 2 microglobulin levels can rise either because its rate of synthesis has increased (e.g. in AIDS, malignant monoclonal plasma cell dyscrasia, solid tumors and autoimmune disease) or because of impaired renal filtration (e.g. due to renal insufficiency, graft rejection or nephrotoxicity induced by post-transplantation immunosuppressive therapy). Beta-2 microglobulin levels might also be elevated in multiple myeloma and lymphoma cases. Dialysis-related amyloidosis develops after a long-term hemodialysis, it can aggregate into amyloid fibers that deposit in joint spaces.

    • Synonyms

      Beta-2-microglobulin, B2M.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Human B2M although stable at room temperature for 3 weeks, should be stored between 2-8°C.

    • Solubility

      It is recommended to reconstitute the lyophilized HuB2M in water at 1mg/ml.

    • Human Virus Test

      Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen and Hepatitis C 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.

    B2M Human
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