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Search results

1000 results found for “Prothymosin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    TPT1 Human

    Description:

    Tumor Protein Translationally-Controlled 1 Human Recombinant

    TCTP, Fortilin, Histamine-Releasing Factor, Translationally-controlled tumor protein, p23, HRF, Fortilin, p02, FLJ27337, TPT1.

    Product # :

    PRO-776

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    Description

    TPT1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 210 amino acids (1-172 a.a.) and having a molecular mass of 23.9 kDa. TPT1 is fused to a 38 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPT1 solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TPT1 takes part in calcium binding and microtubule stabilization. TPT1 is an immunoglobulin E dependent histamine-releasing factor produced by lymphocytes of atopic children and present in biologic fluids of allergic patients. TPT1 protein is similar to p23, a protein of Ehrlich ascites tumor cells, synthesized in the exponentially growing tumor. TPT1 is similar with IgE-dependent histamine releasing factor. TPT1 has a cell housekeeping function. TPT1 is involved in spermatogenesis and acts as a calcium binding protein of the human placenta that regulates calcium handling in trophoblast cells.

    • Synonyms

      TCTP, Fortilin, Histamine-Releasing Factor, Translationally-controlled tumor protein, p23, HRF, Fortilin, p02, FLJ27337, TPT1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMMI IYRDLISHDE MFSDIYKIRE IADGLCLEVE GKMVSRTEGN IDDSLIGGNA SAEGPEGEGT ESTVITGVDI VMNHHLQETS FTKEAYKKYI KDYMKSIKGK LEEQRPERVK PFMTGAAEQI KHILANFKNY QFFIGENMNP DGMVALLDYR EDGVTPYMIF FKDGLEMEKC.

    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.

    Tpt1 Human
  • View Data Sheet

    Name :

    PPM1G Human

    Description:

    Protein Phosphatase 1G Human Recombinant

    Protein Phosphatase 1G, PP2CG, PPP2CG, MGC1675, MGC2870, PP2C GAMMA, EC 3.1.3.16, Protein phosphatase 2C isoform gamma, PP2C-gamma, Protein phosphatase magnesium-dependent 1 gamma, Protein phosphatase 1C, PPM1G, PPM1C.

    Product # :

    ENZ-368

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    Description

    PPM1G Human Recombinant fused with His-tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids and having a molecular mass of 27 kDa.The PPM1G is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPM1G solution (1mg/ml) contains 25mM Tris pH-7.5, 1mM DTT, 1mM EDTA, 2mM b-ME and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PPM1G is part of the PP2C family of Ser/Thr protein phosphatases which are known to be negative regulators of cell stress response pathways. PPM1G is accountable for the dephosphorylation of Pre-mRNA splicing factors, an important factor for the formation of functional spliceosome. PPM1G regulates cell cycle progression.
      PPM1G mediates histone dephosphorylation/exchange in response to DNA damage or checkpoint recovery in higher eukaryotes.
      The degradation of p21/WAF1 induced by PPM1G is mediated in a proteasome-dependent manner.
      Protein phosphatase 1G regulates assembly and function of the beta-catenin degradation complex.

    • Synonyms

      Protein Phosphatase 1G, PP2CG, PPP2CG, MGC1675, MGC2870, PP2C GAMMA, EC 3.1.3.16, Protein phosphatase 2C isoform gamma, PP2C-gamma, Protein phosphatase magnesium-dependent 1 gamma, Protein phosphatase 1C, PPM1G, PPM1C.

    • 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 MEGKEEPGSD SGTTAVVALI RGKQLIVANA GDSRCVVSEA GKALDMSYDH KPEDEVELAR IKNAGGKVTM DGRVNGGLNL SRAIGDHFYK RNKNLPPEEQ MISALPDIKV LTLTDDHEFM VIACDGIWNV MSSQEVVDFI QSKISQRDEN GELRLLSSIV EELLDQCLAP DTSGDGTGCD NMTCIIICFK PRNTAELQPE SGKRKLEEVL STEGAEENGN SDKKKKAKRD.

    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.

    Ppm1G Human
  • View Data Sheet

    Name :

    PRPSAP2 Human

    Description:

    Phosphoribosyl Pyrophosphate Synthetase-Associated Protein 2 Human Recombinant

    PAP41, Phosphoribosyl pyrophosphate synthase-associated protein 2, PRPP synthase-associated protein 2, 41 kDa phosphoribosypyrophosphate synthetase-associated protein, PRPSAP2.

    Product # :

    PRO-1801

    Price :

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    • More Info

    Description

    PRPSAP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 392 amino acids (1-369) and having a molecular mass of 43.3kDa. PRPSAP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRPSAP2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoribosyl Pyrophosphate Synthetase-Associated Protein 2 (PRPSAP2) is a protein which relates with the enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes the formation of phosphoribosylpyrophosphate which is a substrate for synthesis of purine, pyrimidine, histidine, tryptophan and NAD. PRS is a complex with 2 catalytic subunits and 2 associated subunits. PRPSAP2 encodes a non-catalytic associated subunit of PRS.

    • Synonyms

      PAP41, Phosphoribosyl pyrophosphate synthase-associated protein 2, PRPP synthase-associated protein 2, 41 kDa phosphoribosypyrophosphate synthetase-associated protein, PRPSAP2.

    • 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 MGSMFCVTPP ELETKMNITK GGLVLFSANS NSSCMELSKK IAERLGVEMG KVQVYQEPNR ETRVQIQESV RGKDVFIIQT VSKDVNTTIM ELLIMVYACK TSCAKSIIGV IPYFPYSKQC KMRKRGSIVS KLLASMMCKA GLTHLITMDL HQKEIQGFFN IPVDNLRASP FLLQYIQEEI PDYRNAVIVA KSPASAKRAQ SFAERLRLGI AVIHGEAQDA ESDLVDGRHS PPMVRSVAAI HPSLEIPMLI PKEKPPITVV GDVGGRIAII VDDIIDDVDS FLAAAETLKE RGAYKIFVMA THGLLSSDAP RRIEESAIDE VVVTNTIPHE VQKLQCPKIK TVDISMILSE AIRRIHNGES MSYLFRNIGL DD.

    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.

    Prpsap2 Human
  • View Data Sheet

    Name :

    LXN Mouse

    Description:

    Latexin Mouse Recombinant

    Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.

    Product # :

    PRO-2218

    Price :

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    Description

    LXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222 a.a) and having a molecular mass of 27.9kDa. LXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LXN protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lxn also known as Latexin is a member of the protease inhibitor I47 (latexin) family. Lxn's function is hardly reversible, non-competitive, as well as potent inhibitor of CPA1, CPA2 and CPA4. Furthermore, Lxn plays a role in inflammation. Among the diseases associated with LXN are endocervicitis and listeriosis.

    • Synonyms

      Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.

    • 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 MGSMEIPPTH YAASRAASVA ENCINYQQGT PHKLFLVQTV QQASKEDIPG RGHKYHLKFS VEEIIQKQVT VNCTAEVLYP QMGQGSAPEV NFTFEGEIGK NPDEEDNTFY QSLMSLKRPL EAQDIPDNFG NVSPQMKPVQ HLAWVACGYV MWQNSTEDTW YKMLKIQTVK QVQRNDDFIE LDYTILLHDI ASQEIIPWQM QVLWHPQYGT KVKHNSRLPK EGQAE.

    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.

    Lxn Mouse
  • View Data Sheet

    Name :

    CXCL1 Human, His

    Description:

    GRO-Alpha/MGSA Human Recombinant (CXCL1), His Tag

    Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha(1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    Product # :

    CHM-242

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    Description

    CXCL1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 94 amino acids (35-107) and having a molecular mass of 10.1 kDa. The CXCL1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL1 in 20mM Tris-HCL pH-8 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-?). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.

    • Synonyms

      Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha(1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Liquid CXCL1 although stable at 10°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASVATELRC QCLQTLQGIH PKNIQSVNVK SPGPHCAQTE VIATLKNGRK ACLNPASPIV KKIIEKMLNS DKSN.

    • Background

      What is the molecular weight/Mw of CXCL1 HUMAN, HIS Protein?
      CXCL1 HUMAN, HIS Protein has a total Mw of 10.1kDa.

      What is the source or expression system of CXCL1 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL1 HUMAN, HIS Protein?
      CXCL1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL1 HUMAN, HIS Protein?
      The biological functionality of CXCL1 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL1 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MASVATELRC QCLQTLQGIH PKNIQSVNVK SPGPHCAQTE VIATLKNGRK ACLNPASPIV KKIIEKMLNS DKSN.

      What applications can CXCL1 HUMAN, HIS Protein be used in?
      CXCL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL1 HUMAN, HIS Protein?
      The endotoxin level is minimal, CXCL1 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.

    Gro A Human His
  • View Data Sheet

    Name :

    Haptoglobin

    Description:

    Haptoglobin Human Recombinant

    Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.

    Product # :

    PRO-567

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    Description

    Haptoglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing fusion protein with His tag and having a total Mw of 33 kDa (4 kDa His-tag).

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Haptoglobin is a glycoprotein which is synthesized in the liver and circulates in the blood. Haptoglobin is produced typically by hepatocytes but also by other tissues: e.g. skin, lung, and kidney. It is a positive acute phase protein that binds free hemoglobin and removes it from the circulation to prevent kidney injury, and iron loss following hemolysis. The haptoglobin-hemoglobin complex is subsequently removed by the reticuloendothelial system (generally the spleen). As the reticuloendothelial system removes the haptoglobin-hemoglobin complex from the body, haptoglobin levels are reduced in hemolytic anaemias. In the course of binding hemoglobin, haptoglobin sequesters the iron inside hemoglobin, preventing iron-utilizing bacteria from benefitting from hemolysis.
      Haptoglobin consists of two A- and two B-chains, connected by disulfide bonds. Three major haptoglobin phenotypes are known to exist (Hp 1-1, Hp 2-1, and Hp 2-2). Hp 1-1 is biologically the most effective in binding free hemoglobin and suppressing inflammatory responses associated with free hemoglobin. Hp 2-2 is biologically the least active, and Hp 2-1 is moderately active. Haptoglobin’s molecular mass ranges from 8-200 kDa.
      Reduced levels can be seen in haemolysis and impaired liver function. High levels are a marker for acute or chronic inflammation. Ahaptoglobinemia or hypohaptoglobinemia are caused by mutations in the haptoglobin gene and/or its regulatory regions. Haptoglobin is also linked to diabetic nephropathy, the incidence of coronary artery disease in type 1 diabetes, Crohn's disease, inflammatory disease behavior, primary sclerosing cholangitis, susceptibility to idiopathic Parkinson's disease, and a reduced incidence of Plasmodium falciparum malaria.

    • Synonyms

      Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      L ILGGHLDAKG SFPWQAKMVS HHNLTTGATL INEQWLLTTA KNLFLNHSEN ATAKDIAPTL TLYVGKKQLV EIEKVVLHPN YSQVDIGLIK LKQKVSVNER VMPICLPSKD YAEVGRVGYV SGWGRNANFK FTDHLKYVML PVADQDQCIR HYEGSTVPEK KTPKSPVGVQ PILNEHTFCA GMSKYQEDTC YGDAGSAFAV HDLEEDTWYA TGILSFDKSC AVAEYGVYVK VTSIQDWVQK TIAEN

    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.

    Haptoglobin Human Recombinant
  • View Data Sheet

    Name :

    RAC1 Human, His

    Description:

    Ras-Related C3 Botulinum Toxin substrate 1 Human Recombinant, His Tag

    P21-RAC1, RAC-1, RAC1, RAS-like protein TC25, MIG5, Cell-migration-inducing gene 5 protein,Ras-related C3 botulinum toxin substrate 1, rho family small GTP binding protein Rac1, TC-25, MGC111543.

    Product # :

    PRO-731

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    Description

    Ras-Related C3 Botulinum Toxin substrate 1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 23.6 kDa. RAC1 contains a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RAC1 His Tag protein solution contains 20mM Tris-HCl pH7.5, 1mM EDTA, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAC1 is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. RAC-1 regulates the actin cytoskeleton but also other cellular processes. RAC1 have been shown to be involved in the regulation of cell-cell adhesion.

    • Synonyms

      P21-RAC1, RAC-1, RAC1, RAS-like protein TC25, MIG5, Cell-migration-inducing gene 5 protein,Ras-related C3 botulinum toxin substrate 1, rho family small GTP binding protein Rac1, TC-25, MGC111543.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG QEDYDRLRPLSYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSALTQRGLKTVFD EAIRAVLCPP PVKKRKRKCL LL.

    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.

    Rac1 Human His
  • View Data Sheet

    Name :

    p38a/SAPK2 Human

    Description:

    p38a/SAPK2 Human Recombinant

    Mitogen-activated protein kinase 14, EC 2.7.11.24, Mitogen-activated protein kinase p38 alpha, MAP kinase p38 alpha, Cytokine suppressive anti-inflammatory drug-binding protein, CSAID-binding protein, CSBP, MAX-interacting protein 2, MAP kinase MXI2, SAPK2A, RK, p38, EXIP, Mxi2, CSBP1, CSBP2, CSPB1, PRKM14, PRKM15, p38ALPHA.

    Product # :

    PKA-217

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    Description

    p38/SAPK2 is a non-glycosilated polypeptide produced by phosphorylation of the purified p38 alpha with MKK6 having a molecular mass of 42.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    p38/SAPK2 is supplied in 25mM Tris-HCl, 150mM NaCl, 1mM DTT, 50% glycerol, pH 8.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      p38a/SAPK2 is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various environmental stresses and proinflammatory cytokines. The activation requires its phosphorylation by MAP kinase kinases (MKKs), or its autophosphorylation triggered by the interaction of MAP3K7IP1/TAB1 protein with this kinase. The substrates of this kinase include transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which suggest the roles of this kinase in stress related transcription and cell cycle regulation, as well as in genotoxic stress response. Four alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.

    • Synonyms

      Mitogen-activated protein kinase 14, EC 2.7.11.24, Mitogen-activated protein kinase p38 alpha, MAP kinase p38 alpha, Cytokine suppressive anti-inflammatory drug-binding protein, CSAID-binding protein, CSBP, MAX-interacting protein 2, MAP kinase MXI2, SAPK2A, RK, p38, EXIP, Mxi2, CSBP1, CSBP2, CSPB1, PRKM14, PRKM15, p38ALPHA.

    • 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.

    • Unit Definition

      No protease activity detectable, specific activity is 2.357.900 U*/mg (*1 U = 1 pmol/min transferred to myelin basic protein at 30°C).

    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.

    P38Alpha Human
  • View Data Sheet

    Name :

    CoV-2 Spike (318-542)

    Description:

    Coronavirus 2019 Spike Receptor Binding Domain (318-542 a.a.) Recombinant

    Product # :

    SARS-057

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    Description

    Recombinant Coronavirus 2019 Spike Receptor Binding Domain (318-542 aa) having a Mw of 25.7kDa was purified from E. coli.The CoV-2 Spike is fused to a 6xHis tag at its C terminal and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    CoV-2 Spike protein solution contains PBS and 25mM K2CO3.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • 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

      HMRVQPTESI VRFPNITNLC PFGEVFNATR FASVYAWNRK RISNCVADYS VLYNSASFS TFKCYGVSPT KLNDLCFTNV YADSFVIRGD EVRQIAPGQT GKIADYNYKL PDDFTGCVI AWNSNNLDSKV GGNYNYLYRL FRKSNLKPFE RDISTEIYQA GSTPCNGVEG FNCYFPLQSY GFQPTNGVGY QPYRVVVLSF ELLHAPATVC GPKKSTNLVK NKCVNFNLE

    • Applications

      ELISA, Western blot and lateral flow immunoassay.

    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.

    product_image.jpg
  • View Data Sheet

    Name :

    EREG Human

    Description:

    Epiregulin Human Recombinant

    EREG, Epiregulin, ER.

    Product # :

    CYT-609

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    Description

    Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

    More Info

    • Introduction

      Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

    • Synonyms

      EREG, Epiregulin, ER.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 5.6kDa.

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

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

      What is the Biological Activity of EREG Protein?
      The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

      What is the amino acid sequence of EREG Protein?
      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

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

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

    Epiregulin Human
  • View Data Sheet

    Name :

    Leptin N82K Human, PEG

    Description:

    Leptin N82K Human Recombinant, Pegylated

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1107

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    Description

    Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.

    More Info

    • Introduction

      Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K 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 Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Leptin Mutant Protein
  • View Data Sheet

    Name :

    Leptin tA Human

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant

    Product # :

    CYT-352

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    Description

    Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Ta Human
  • View Data Sheet

    Name :

    Tamm Horsfall

    Description:

    Recombinant Human Tamm Horsfall Glycoprotein

    Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.


    Product # :

    ENZ-1206

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    • SDS-PAGE

    Description

    Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.

    Source

    HEK293

    Formulation

    The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE analysis.

    SDS-PAGE

    Tamm Horsfall-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
      Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
      Reduced Uromodulin levels is associated with chronic kidney disease.
      UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.

    • Synonyms

      Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD should be stored at 4C between 2-7 days and for future use below -18C.
      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
      Please prevent freeze-thaw cycles.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH

    • Background

      Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

      What is the molecular weight/Mw of UMOD Protein?
      UMOD Protein has a total Mw of 65kDa.

      What is the source or expression system of UMOD Protein?
      HEK293.

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

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

      What is the amino acid sequence of UMOD Protein?
      UMOD Protein is composed from 595 amino acids.

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

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

    Tamm Horsfall
  • View Data Sheet

    Name :

    Activin A Human Plant

    Description:

    Activin A Human Recombinant, Plant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-052

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    Description

    Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Activin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin A should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Activin A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 27.4 kDa.
      What is the source or expression system of Activin A Protein?
      Nicotinia

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

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

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

      What is the amino acid sequence of ACTIVIN A Protein?
      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

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

    • Serological Identification

      The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin A.

    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.

    Activin A Human Plant
  • View Data Sheet

    Name :

    Cyclophilin B Mouse

    Description:

    Cyclophilin-B Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.

    Product # :

    ENZ-1039

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    Description

    Cyclophilin B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (34-216 a.a) and having a molecular mass of 22.7kDa.Cyclophilin B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cyclophilin B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.

    More Info

    • Introduction

      Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.

    • 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 MGSMNDKKKG PKVTVKVYFD LQIGDESVGR VVFGLFGKTV PKTVDNFVAL ATGEKGFGYK NSKFHRVIKD FMIQGGDFTR GDGTGGKSIY GERFPDENFK LKHYGPGWVS MANAGKDTNG SQFFITTVKT SWLDGKHVVF GKVLEGMDVV RKVESTKTDS
      RDKPLKDVII VDSGKIEVEK PFAIAKE.

    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.

    Cyclophilin B Mouse
  • View Data Sheet

    Name :

    NECTIN1 Human

    Description:

    Nectin Cell Adhesion Molecule 1 Human Recombinant

    PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.

    Product # :

    PRO-2648

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    Description

    NECTIN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 334amino acids (31-355a.a) and having a molecular mass of 37.3kDa.NECTIN1 is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The NECTIN1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.

    • Synonyms

      PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.

    • 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

      ADPQVVQVND SMYGFIGTDV VLHCSFANPL PSVKITQVTW QKSTNGSKQN VAIYNPSMGV SVLAPYRERV EFLRPSFTDG TIRLSRLELE DEGVYICEFA TFPTGNRESQ LNLTVMAKPT NWIEGTQAVL RAKKGQDDKV LVATCTSANG KPPSVVSWET RLKGEAEYQE IRNPNGTVTV ISRYRLVPSR EAHQQSLACI VNYHMDRFKE SLTLNVQYEP EVTIEGFDGN WYLQRMDVKL
      TCKADANPPA TEYHWTTLNG SLPKGVEAQN RTLFFKGPIN YSLAGTYICE ATNPIGTRSG QVEVNITEFP YTPSPPEHGR RAGPVPTAHH 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.

    Nectin1 Human
  • View Data Sheet

    Name :

    ICAM1 Mouse

    Description:

    Intercellular Adhesion Molecule-1 Mouse Recombinant

    Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58

    Product # :

    PRO-2636

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    Description

    ICAM1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 466 amino acids (28-485 a.a) and having a molecular mass of 51.2kDa.ICAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The ICAM1 solution (0.5mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The Biological Activity is measured by the ability of the immobilized protein to support the adhesion of HSB2 human peripheral blood acute lymphoblastic leukemia cells. ICAM-1/CD54 coated plates 5ug/ml when cells are added to. This effect is more to 60%.

    More Info

    • Introduction

      Intercellular adhesion molecule 1 or ICAM1 is a protein, part of the ICAM family of proteins. ICAM1 acts as ligand for integrin alpha-L/beta-2 which is a leukocyte adhesion peptide. Amid migration of leukocytes ICAM1 promotes endothelial apical assembly cups via activation of ARHGEF26/SGEF & RHOG.

    • Synonyms

      Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58

    • 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

      QVSIHPREAF LPQGGSVQVN CSSSCKEDLS LGLETQWLKD ELESGPNWKL FELSEIGEDS SPLCFENCGT VQSSASATIT VYSFPESVEL RPLPAWQQVG KDLTLRCHVD GGAPRTQLSA VLLRGEEILS RQPVGGHPKD PKEITFTVLA SRGDHGANFS CRTELDLRPQ GLALFSNVSE ARSLRTFDLP ATIPKLDTPD LLEVGTQQKL FCSLEGLFPA SEARIYLELG GQMPTQESTN SSDSVSATAL VEVTEEFDRT LPLRCVLELA DQILETQRTL TVYNFSAPVL TLSQLEVSEG SQVTVKCEAH SGSKVVLLSG VEPRPPTPQV QFTLNASSED HKRSFFCSAA LEVAGKFLFK NQTLELHVLY GPRLDETDCL GNWTWQEGSQ QTLKCQAWGN PSPKMTCRRK ADGALLPIGV VKSVKQEMNG TYVCHAFSSH GNVTRNVYLT VLYHSQNNVE 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.

    Icam1 Mouse
  • View Data Sheet

    Name :

    E Selectin Human

    Description:

    E-selectin Human Recombinant

    E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    Product # :

    PRO-380

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    Description

    E-Selectin Human Recombinant is expressed in E. coli containing amino acids 179-557 fused to an amino terminal hexahistidine tag, having a total molecular weight of 45.22 kDa.

    Source

    Escherichia Coli.

    Formulation

    E-Selectin is supplied in 1x PBS and 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    More Info

    • Introduction

      E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.

    • Synonyms

      E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    • Physical Appearance

      Sterile Filtered liquid formulation.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    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.

    E Selectin Human
  • View Data Sheet

    Name :

    SOST Mouse

    Description:

    Sclerostin Mouse Recombinant

    SOST, Sclerostin, 5430411E23Rik.

    Product # :

    PRO-2670

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    Description

    SOST Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (24-211 a.a) containing 194 amino acids and having a molecular mass of 21.9 kDa.SOST is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is expressed mainly in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

    • Synonyms

      SOST, Sclerostin, 5430411E23Rik.

    • 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

      QGWQAFRNDA TEVIPGLGEY PEPPPENNQT MNRAENGGRP PHHPYDAKDV SEYSCRELHY TRFLTDGPCR SAKPVTELVC SGQCGPARLL PNAIGRVKWW RPNGPDFRCI PDRYRAQRVQ LLCPGGAAPR SRKVRLVASC KCKRLTRFHN QSELKDFGPE TARPQKGRKP RPGARGAKAN QAELENAYHH 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.

    Sclerostin Mouse
  • View Data Sheet

    Name :

    SPSB1 Human

    Description:

    SPRY Domain-Containing SOCS Cox Protein 1 Human Recombinant

    SPRY domain-containing SOCS box protein 1, SSB-1, SPSB1, SSB1.

    Product # :

    PRO-223

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    Description

    SPSB1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (24-223 a.a.) and having a molecular mass of 26.1kDa.SPSB1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SPSB1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SPRY domain-containing SOCS box protein 1 (SPSB1) belongs to the SOCS box protein subfamily. SPSB1 includes a central SPRY domain and a C-terminal SOCS box. Even though, some of the SOCS protein subfamilies function as adaptors for a large family of ubiquitin-protein isopeptide ligases to regulate certain signaling pathways, the function of the SSB subfamily remains to be determined. SPSB1 may have an imperative role in enhancing the HGF-induced Erk-Elk-1-SRE pathway. SPSB1 overexpression exhibited no effect on the basal level or epidermal growth factor-induced SRE-luciferase activity.

    • Synonyms

      SPRY domain-containing SOCS box protein 1, SSB-1, SPSB1, SSB1.

    • 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 MQELQGLDYC KPTRLDLLLD MPPVSYDVQL LHSWNNNDRS LNVFVKEDDK LIFHRHPVAQ STDAIRGKVG YTRGLHVWQI TWAMRQRGTH AVVGVATADA PLHSVGYTTL VGNNHESWGW DLGRNRLYHD GKNQPSKTYP AFLEPDETFI VPDSFLVALD
      MDDGTLSFIV DGQYMGVAFR GLKGKKLYPV VSAVWGHCEI RMRYLNGLDP E.

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    Spsb1 Human
  • View Data Sheet

    Name :

    Epoetin Human, His

    Description:

    Erythropoietin-alpha Human Recombinant, His Tag

    800x600 Erythropoietin, EP, INN=Epoetin, EPO a, Erythropoietin-alpha, EPO. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    CYT-791

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    • sds-page

    Description

    800x600 EPO a Human Recombinant produced in Baculovirus is a single, glycosylated polypeptide chain containing 174 amino acids (28-193a.a.) and having a molecular mass of 19.5kDa.EPO a is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤0.5ng/ml and measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

    sds-page

    Epoetin-sds-page - Product image 1

    More Info

    • Introduction

      EPO a is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. EPO a is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO a also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

    • Synonyms

      Erythropoietin, EP, INN=Epoetin, EPO a, Erythropoietin-alpha, EPO.

    • 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

      APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

    • Background

      What is the molecular weight/Mw of EPOETIN Protein?
      EPOETIN Protein has a total Mw of 19.5kDa.

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

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

      What is the Biological Activity of EPOETIN Protein?
      The ED50 range is ≤0.5ng/ml and measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

      What is the amino acid sequence of EPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

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

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

    Epo A His Human
  • View Data Sheet

    Name :

    Epoetin Human, Sf9

    Description:

    Erythropoietin-alpha Human Recombinant, Sf9

    Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.

    Product # :

    CYT-934

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    • sds-page

    Description

    Erythropoietin-alpha Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 174 amino acids (28-193a.a.) and having a molecular mass of 19.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPO-a is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    EPO a protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is ≤ 0.5 ng/ml.

    sds-page

    Epoetin-sds-page - Product image 1

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    • Introduction

      This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

    • Synonyms

      Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.

    • 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

      APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

    • Background

      What is the molecular weight/Mw of EPOETIN Protein?
      EPOETIN Protein has a total Mw of 19.5kDa.

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

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

      What is the Biological Activity of EPOETIN Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is ≤ 0.5 ng/ml.

      What is the amino acid sequence of EPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

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

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

    Epo A Human Sf9
  • View Data Sheet

    Name :

    IL 22 Mouse

    Description:

    Interleukin-22 Mouse Recombinant

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

    Product # :

    CYT-539

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    Shipped at Room temp

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    • description
    • source
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    • More Info

    Description

    Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids and having a molecular mass of 16.7 kDa. The Murine IL-22 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 1X PBS.

    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 its ability to induce IL-10 secretion in Colo205 cells is less than 0.5ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.

    More Info

    • Introduction

      Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10R? (previously known as CRF2-4), belonging to the class II cytokine receptor family.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 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 Interleukin -22 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-Leu-Pro-Val-Asn.

    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 22 Mouse
  • View Data Sheet

    Name :

    STX17 Human

    Description:

    Syntaxin-17 Human Recombinant

    Syntaxin 17

    Product # :

    PRO-1712

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    Description

    STX17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229) and having a molecular mass of 28.6kDa.STX17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STX17 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STX17 is a member of to the syntaxin family and contains 1 t-SNARE coiled-coil homology domain. STX17 is involved in vesicle trafficking to lysosomes and takes part in procedures associated with cell division.

    • Synonyms

      Syntaxin 17

    • 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 MGSMSEDEEK VKLRRLEPAI QKFIKIVIPT DLERLRKHQI NIEKYQRCRI WDKLHEEHIN AGRTVQQLRS NIREIEKLCL KVRKDDLVLL KRMIDPVKEE ASAATAEFLQ LHLESVEELK KQFNDEETLL QPPLTRSMTV GGAFHTTEAE ASSQSLTQIY ALPEIPQDQN AAESWETLEA DLIELSQLVT DFSLLVNSQQ EKIDSIADHV NSAAVNVEEG TKNLGKAAKY KL

    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.

    Stx17 Human
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