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Search results

1000 results found for “glycophorin”

Name

Description

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  • View Data Sheet

    Name :

    FGFBP Human

    Description:

    Fibroblast Growth Factor Binding Protein 1 Human Recombinant

    Fibroblast Growth Factor Binding Protein 1, FGFBP, HBP17, 17 KDa Heparin-Binding Growth Factor-Binding Protein, 17 KDa HBGF-Binding Protein, FGF-Binding Protein 1, FGF-BP1, FGFBP-1, FGF-BP, Heparin-Binding Growth Factor Binding Protein, Fibroblast Growth Factor-Binding Protein 1, Fibroblast growth factor-binding protein 1.

    Product # :

    CYT-860

    Price :

    Quantity :

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    • sds-page

    Description

    FGFBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (24-234 a.a) and having a molecular mass of 26.2kDa. FGFBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGFBP protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    FGFBP Human - Product image 1

    More Info

    • Introduction

      Fibroblast Growth Factor Binding Protein 1, also known as FGFBP1 is a secreted fibroblast growth factor carrier protein. FGFBP1 plays a vital part in cell proliferation, differentiation and migration by binding to fibroblast growth factors and potentiating their biological effects on target cells. In addition, FGFBP1 also takes part in tumor growth as an angiogenic switch molecule, furthermore an expression of FGFBP1 has been associated with more than a few types of cancer as well as pancreatic and colorectal adenocarcinoma.

    • Synonyms

      Fibroblast Growth Factor Binding Protein 1, FGFBP, HBP17, 17 KDa Heparin-Binding Growth Factor-Binding Protein, 17 KDa HBGF-Binding Protein, FGF-Binding Protein 1, FGF-BP1, FGFBP-1, FGF-BP, Heparin-Binding Growth Factor Binding Protein, Fibroblast Growth Factor-Binding Protein 1, Fibroblast growth factor-binding protein 1.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC.

    • Background

      What is the molecular weight/Mw of CYT-860 Protein?
      CYT-860 Protein has a total Mw of 26.2kDa.

      What is the source or expression system of CYT-860 Protein?
      Escherichia Coli.

      What is the Purity of CYT-860 Protein?
      CYT-860 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CYT-860 Protein?
      The biological functionality of CYT-860 Protein will be determined in the future.

      What is the amino acid sequence of CYT-860 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC.

      What applications can CYT-860 Protein be used in?
      CYT-860 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CYT-860 Protein?
      The endotoxin level is minimal, CYT-860 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.

    Fgfbp Human
  • View Data Sheet

    Name :

    FSBP Human

    Description:

    Fibrinogen Silencer Binding Protein Human Recombinant

    Fibrinogen silencer-binding protein, FSBP.

    Product # :

    PRO-1493

    Price :

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    Description

    FSBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 37.2kDa.FSBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FSBP protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 1M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fibrinogen silencer-binding protein (FSBP), interacts with X11alpha. The X11alpha/FSBP complex send signals to the nucleus in order to repress glycogen synthase kinase-3beta promoter activity. X11alpha is a neuronal adaptor protein that interacts with the amyloid precursor protein (APP) via a centrally located phosphotyrosine binding domain to inhibit the production of Abeta peptide that is deposited in Alzheimer's diseased brains.

    • Synonyms

      Fibrinogen silencer-binding protein, FSBP.

    • 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 MGSMVGKARS SNFTLSEKLD LLKLVKPYVK ILEEHTNKHS VIVEKNRCWD IIAVNYNAIG VDRPPRTAQG LRTLYKRLKE YAKQELLQQK ETQSDFKSNI SEPTKKVMEM IPQISSFCLV RDRNHIQSAN LDEEAQAGTS SLQVMLDHHP VAITVEVKQE EDIKPPPPLV LNSQQSDTLE QREEHELVHV MERSLSPSLS SVDMRMTSSP SSIPRRDDFF RHESGEHFRS LLGYDPQILQ MLKEEHQIIL ENQKNFGLYV QEKRDGLKRR QQLEEELLRA KIEVEKLKAI RLRHDLPEYN SL.

    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.

    Fsbp Human
  • View Data Sheet

    Name :

    TNFA Mouse, Sf9

    Description:

    Tumor Necrosis Factor-alpha Mouse Recombinant, Sf9

    Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2.

    Product # :

    CYT-912

    Price :

    Quantity :

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    Description

    TNFA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 162 amino acids (80-235 a.a.) and having a molecular mass of 18kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).TNFA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFA protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      LRSSSQNSSD KPVAHVVANH QVEEQLEWLS QRANALLANG MDLKDNQLVV PADGLYLVYS QVLFKGQGCP DYVLLTHTVS RFAISYQEKV NLLSAVKSPC PKDTPEGAEL KPWYEPIYLG GVFQLEKGDQ LSAEVNLPKY LDFAESGQVY FGVIALHHHH HH

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

    Tnfa Mouse Sf9
  • View Data Sheet

    Name :

    TPM3 Human

    Description:

    Tropomyosin-3 Human Recombinant

    Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.

    Product # :

    PRO-1020

    Price :

    Quantity :

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    • description
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    Description

    TPM3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a.) and having a molecular mass of 31.6kDa. TPM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPM3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tropomyosin alpha-3 chain (TPM3) belongs to the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins which polymerize end-to-end along the major groove in most actin filaments. Tropomyosins give stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, tropomyosins regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.

    • Synonyms

      Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.

    • 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 MGSHMAGITT IEAVKRKIQV LQQQADDAEE RAERLQREVE GERRAREQAE AEVASLNRRI QLVEEELDRA QERLATALQK LEEAEKAADE SERGMKVIEN RALKDEEKME LQEIQLKEAK HIAEEADRKY EEVARKLVII EGDLERTEER AELAESRCRE MDEQIRLMDQ NLKCLSAAEE KYSQKEDKYE EEIKILTDKL KEAETRAEFA ERSVAKLEKT IDDLEDKLKC TKEEHLCTQR MLDQTLLDLN EM.

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    Tpm3 Human
  • View Data Sheet

    Name :

    TSLP Human

    Description:

    Thymic Stromal Lymphopoietin Human Recombinant

    Thymic Stromal Lymphopoietin, TSLP.

    Product # :

    CYT-572

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    Description

    TSLP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 15 kDa.The TSLP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated solution (1mg/ml) contains 130mM NaCl, and 20mM sodium phosphate, 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 is determined by the ability to induce proliferation of human Interleukin-7 receptor alpha & human TSLP Receptor co-transfected with mouse BaF3 cells which was found to be less than 0.3ng/ml.

    More Info

    • Introduction

      TSLP protein is a hemopoietic cytokine which signals throughout a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor & the Interleukin-7 receptor alpha chain. TSLP impacts myeloid cells thus induces the discharge of T cell-attracting chemokines from monocytes & increases the growth of CD11c(+) dendritic cells. TSLP is mainly expressed in the heart, liver and prostate. TSLP is related in its biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the Interleukin-7 receptor alpha chain & the TSLPR. Similar to IL-7, TSLP enhances phosphorylation of STAT3 and STAT5, though uses kinases excluding JAKs for its activation. TSLP induces the release of T cell-attracting chemokines such asTARC & MDC from monocytes & triggers CD11c(+) dendritic cells. TSLP activated dendritic cells primes naive T cells to manufacture pro-allergic cytokines such as Iinterleukin-4, Interleukin-5, Interleukin-13 and TNF-alpha whereas down-regulating Interleukin-10 and IFN-gamma play a role in the initiation of allergic inflammation.

    • Synonyms

      Thymic Stromal Lymphopoietin, TSLP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MYDFTNCDFE KIKAAYLSTI SKDLITYMSG TKSTEFNNTV SCSNRPHCLT EIQSLTFNPT AGCASLAKEM FAMKTKAALA IWCPGYSETQ INATQAMKKR RKRKVTTNKC LEQVSQLQGL WRRFNRPLLK QQ.

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    Tslp Human
  • View Data Sheet

    Name :

    GNB1 Human

    Description:

    Guanine Nucleotide Binding Protein Beta Polypeptide 1 Human Recombinant

    Guanine Nucleotide Binding Protein (G Protein) Beta Polypeptide 1, Transducin Beta Chain 1, GNB1.

    Product # :

    PRO-1955

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    Description

    GNB1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 363 amino acids (1-340) and having a molecular mass of 39.8 kDa.GNB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GNB1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Heterotrimeric guanine nucleotide-binding proteins (G proteins) which integrate signals between receptors and effector proteins, are comprised of an alpha, a beta and a gamma subunit. The alpha, beta and gamma subunits are encoded by families of related genes. GNB1 encodes a beta subunit. Beta subunits are vital regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. G proteins are involved as a modulator or transducer in numerous transmembrane signaling systems. The beta and gamma chains are necessary for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

    • Synonyms

      Guanine Nucleotide Binding Protein (G Protein) Beta Polypeptide 1, Transducin Beta Chain 1, GNB1.

    • 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 MGSMSELDQL RQEAEQLKNQ IRDARKACAD ATLSQITNNI DPVGRIQMRT RRTLRGHLAK IYAMHWGTDS RLLVSASQDG KLIIWDSYTT NKVHAIPLRS SWVMTCAYAP SGNYVACGGL DNICSIYNLK TREGNVRVSR ELAGHTGYLS CCRFLDDNQI VTSSGDTTCA LWDIETGQQT TTFTGHTGDV MSLSLAPDTR LFVSGACDAS AKLWDVREGM CRQTFTGHES DINAICFFPN GNAFATGSDD ATCRLFDLRA DQELMTYSHD NIICGITSVS FSKSGRLLLA GYDDFNCNVW DALKADRAGV LAGHDNRVSC LGVTDDGMAV ATGSWDSFLK IWN.

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    Gnb1 Human
  • View Data Sheet

    Name :

    UBLCP1 Human

    Description:

    Ubiquitin-Like Domain Containing CTD Phosphatase 1 Human Recombinant

    CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.

    Product # :

    PRO-151

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    Description

    UBLCP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 39.2kDa.UBLCP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBLCP1 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation averts assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.

    • Synonyms

      CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.

    • 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 MGSMALPIIV KWGGQEYSVT TLSEDDTVLD LKQFLKTLTG VLPERQKLLG LKVKGKPAEN DVKLGALKLK PNTKIMMMGT REESLEDVLG PPPDNDDVVN DFDIEDEVVE VENREENLLK ISRRVKEYKV EILNPPREGK KLLVLDVDYT LFDHRSCAET GVELMRPYLH EFLTSAYEDY DIVIWSATNM KWIEAKMKEL GVSTNANYKI TFMLDSAAMI TVHTPRRGLI DVKPLGVIWG KFSEFYSKKN TIMFDDIGRN FLMNPQNGLK IRPFMKAHLN RDKDKELLKL TQYLKEIAKL DDFLDLNHKY WERYLSKKQG Q.

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    Ublcp1 Human
  • View Data Sheet

    Name :

    MED27 Human

    Description:

    Mediator Complex Subunit 27 Human Recombinant

    Mediator Complex Subunit 27, MED27, CRSP8, Cofactor Required For Sp1 Transcriptional Activation, Subunit 8 34kDa, P37 TRAP/SMCC/PC2 Subunit, Transcriptional Coactivator CRSP34, CRSP34, CRSP Complex Subunit 8, CRAP34, TRAP37, Mediator of RNA Polymerase II Transcription Subunit 27, Cofactor Required For Sp1 Transcriptional Activation Subunit 8.

    Product # :

    PRO-1946

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    Description

    MED27 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-311) and having a molecular mass of 37.8 kDa.MED27 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MED27 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mediator Complex Subunit 27 (MED27) is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, together with TFIID, is necessary for efficient activation by SP1. MED27 is a component of the Mediator complex, a coactivator involved in the regulated transcription of virtually all RNA polymerase II-dependent genes. MED27 protein is also a component of other multisubunit complexes such as the thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. The activation of MED27 gene transcription is a multistep process, which is triggered by factors that identify transcriptional enhancer sites in DNA.

    • Synonyms

      Mediator Complex Subunit 27, MED27, CRSP8, Cofactor Required For Sp1 Transcriptional Activation, Subunit 8 34kDa, P37 TRAP/SMCC/PC2 Subunit, Transcriptional Coactivator CRSP34, CRSP34, CRSP Complex Subunit 8, CRAP34, TRAP37, Mediator of RNA Polymerase II Transcription Subunit 27, Cofactor Required For Sp1 Transcriptional Activation Subunit 8.

    • 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 MGSMADVINV SVNLEAFSQA ISAIQALRSS VSRVFDCLKD GMRNKETLEG REKAFIAHFQ DNLHSVNRDL NELERLSNLV GKPSENHPLH NSGLLSLDPV QDKTPLYSQL LQAYKWSNKL QYHAGLASGL LNQQSLKRSA NQMGVSAKRR PKAQPTTLVL PPQYVDDVIS RIDRMFPEMS IHLSRPNGTS AMLLVTLGKV LKVIVVMRSL FIDRTIVKGY NENVYTEDGK LDIWSKSNYQ VFQKVTDHAT TALLHYQLPQ MPDVVVRSFM TWLRSYIKLF QAPCQRCGKF LQDGLPPTWR DFRTLEAFHD TCRQ.

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    Med27 Human
  • View Data Sheet

    Name :

    LGALS4 Mouse

    Description:

    Galectin-4 Mouse Recombinant

    gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 4.

    Product # :

    CYT-187

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    • SDS-PAGE

    Description

    LGALS4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-326a.a) and having a molecular mass of 38.8kDa.LGALS4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LGALS4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.

    SDS-PAGE

    LGALS4 Mouse-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 & IL-17.

    • Synonyms

      gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 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

      MGSSHHHHHH SSGLVPRGSH MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.

    • Background

      What is the molecular weight/Mw of LGALS4 MOUSE Protein?
      LGALS4 MOUSE Protein has a total Mw of 38.8kDa.

      What is the source or expression system of LGALS4 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of LGALS4 MOUSE Protein?
      LGALS4 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS4 MOUSE Protein?
      The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.

      What is the amino acid sequence of LGALS4 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.

      What applications can LGALS4 MOUSE Protein be used in?
      LGALS4 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS4 MOUSE Protein?
      The endotoxin level is minimal, LGALS4 MOUSE Protein was purified using conventional chromatography techniques.


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

    Lgals4 Mouse
  • View Data Sheet

    Name :

    CCL15 68 a.a Human

    Description:

    Macrophage Inflammatory Protein-5 (68 a.a) Human Recombinant (CCL15)

    Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.

    Product # :

    CHM-011

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    Description

    Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7.4kDa. The MIP5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIP5 was lyophilized from a 0.2µm filtered concentrated solution containing PBS, pH-7.4.

    Purity

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

    Biological Activity

    Measured by its ability to chemoattract THP-1 human acute monocytic leukemia cells. The ED50 for this effect is typically 2-4ng/ml.

    More Info

    • Introduction

      CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.

    • Synonyms

      Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL15 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 MIP5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM KKLKPYSI.

    • Background

      What is the molecular weight/Mw of CCL15 68 A.A HUMAN Protein?
      CCL15 68 A.A HUMAN Protein has a total Mw of 7.4kDa.

      What is the source or expression system of CCL15 68 A.A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL15 68 A.A HUMAN Protein?
      CCL15 68 A.A HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL15 68 A.A HUMAN Protein?
      Measured by its ability to chemoattract THP-1 human acute monocytic leukemia cells. The ED50 for this effect is typically 2-4ng/ml.

      What is the amino acid sequence of CCL15 68 A.A HUMAN Protein?
      SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM KKLKPYSI.

      What applications can CCL15 68 A.A HUMAN Protein be used in?
      CCL15 68 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL15 68 A.A HUMAN Protein?
      The endotoxin level is minimal, CCL15 68 A.A HUMAN 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.

    Mip 5 68 Aa Human
  • View Data Sheet

    Name :

    GM- CSF Human

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant

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

    Product # :

    CYT-221

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14477 Dalton. GM-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GM-CSF was lyophilized after extensive dialysis against 2mM sodium phosphate buffer pH= 7.4±0.1.

    Purity

    Greater than 98.0% as determined by:
    1. Analysis by RP-HPLC.
    2. Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 11,100,000 IU/mg.

    More Info

    • Introduction

      Granulocyte Macrophage Colony Stimulating Factor (GM-CSF) was first characterized as a growth factor that supports the in-vitro colony formation of granulocytes-macrophages progenitor cells. It is a pleiotropic cytokine and a member of a family of endogenous cytokines of the hematopoietic system. GM-CSF is produced as a response to immune or inflammatory stimuli by activated cells of the hematopoietic system such as T cells, B cells, macrophages, mast cells and also fibroblasts and alveolar epithelial cells. It plays an important role in regulating the proliferation, differentiation, survival and activation of hematopoietic cells such as granulocytes and monocytes ,neutrophiles, basophiles and eosonophoiles, erythroid cells, megakaryocytes and T cells.
      Human and mouse GM-CSF have about 56% homology and are species specific. Human GM-CSF is not active on mouse cells and vice versa. It is active on canine and feline cells.
      GMCSF is 144 amino acids, 22kDa glycoprotein. It is composed of four bundles alpha helices. Its receptor is heterodimers with a ligand-specific alpha subunit and a betac subunit that is shared with the interleukin IL-3 and IL-5 receptors. This unusual form of receptor assembly likely applies also to IL-3 and IL-5 receptors. Cross-linking the two receptor subunits is required for receptor activation and signaling .
      GMCSF has been shown to be involved in maturation, mobilization and antigen presentation of myeloid dentritic cells (DCs) in-vivo or ex-vivo. This function promotes Th1 immune responses, cytotoxcity, anti-angiogenesis as well as allergic inflammation, and the development of autoimmunity. Therefore GMCSF can be used in immunotherapy for the treatment of immune suppressed and immune-compromised patients as well as in veterinary medicine for the same purpose. GM-CSF is also important in regulation of embryo development and pregnancy and specifically in embryo implantation and subsequent development .

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor 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 Ala-Pro-Ala-Arg-Ser.
      N-terminal methionine has been completely removed enzymatically.

    • Background

      What is the molecular weight/Mw of GM CSF HUMAN Protein?
      GM CSF HUMAN Protein has a total Mw of 14.47kDa.

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

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

      What is the Biological Activity of GM CSF HUMAN Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 11,100,000 IU/mg.

      What is the amino acid sequence of GM CSF HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
      N-terminal methionine has been completely removed enzymatically.

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

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


    • Protein content

      GM-CSF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.963 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GEN computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of GM-CSF as a Reference Standard.

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    Gm Csf Human
  • View Data Sheet

    Name :

    LIF Mouse

    Description:

    Leukemia Inhibitory Factor Mouse Recombinant

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

    Product # :

    CYT-645

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    Description

    Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.02% Tween-20.

    Purity

    Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Activity of murine LIF was determined by the M1 cell differentiation assay which was found to be < 0.01 ng/ml, corresponding to a specific activity of 100,000,000 IU/mg.
    A standard of 50 Units is defined as the concentration of mouse LIF in 1.0 mL of tissue culture medium that induces the differentiation of 50% of M1 colonies.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPLPITPVNATCAIRHPCHGNLMNQIKNQLAQLNGSANALFISYYTAQGEPFP NNVEKLCAPNMTDFPSFHGNGTEKTKLVELYRMVAYLSASLTNITRDQKVLNP TAVSLQVKLNATIDVMRGLLSNVLCRLCNKYRVGHVDVPPVPDHSDKEAFQR KKLGCQLLGTYKQVISVVVQAF.

    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.

    Lif Mouse
  • View Data Sheet

    Name :

    MEMO1 Human

    Description:

    Mediator of Cell Motility 1 Human Recombinant

    Protein MEMO1, C21orf19-like protein, Hepatitis C virus NS5A-transactivated protein 7, HCV NS5A-transactivated protein 7, Mediator of ErbB2-driven cell motility 1, Mediator of cell motility 1, Memo-1, MEMO1, C2orf4, MEMO, NS5ATP7, CGI-27.

    Product # :

    PRO-1148

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    Description

    MEMO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-297 a.a) and having a molecular mass of 36.4kDa.MEMO1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MEMO1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 50% glycerol, 5mM DTT, 300mM NaCl and 2mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mediator of ErbB2-driven cell motility 1 (MEMO1) is a member of the UPF0103 family. MEMO1 regulates cell migration by transmitting extracellular chemotactic signals to the microtubule cytoskeleton. Furthermore, MEMO1 controls the localization of APC and CLASP2 to the cell membrane, using the regulation of GSK3B activity. MEMO1 is essential for breast carcinoma cell migration, suggesting a key role in tumorigenesis. MEMO1 is also a mediator of ERBB2 signaling.

    • Synonyms

      Protein MEMO1, C21orf19-like protein, Hepatitis C virus NS5A-transactivated protein 7, HCV NS5A-transactivated protein 7, Mediator of ErbB2-driven cell motility 1, Mediator of cell motility 1, Memo-1, MEMO1, C2orf4, MEMO, NS5ATP7, CGI-27.

    • 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 MGSHMMSNRV VCREASHAGS WYTASGPQLN AQLEGWLSQV QSTKRPARAI IAPHAGYTYC GSCAAHAYKQ VDPSITRRIF ILGPSHHVPL SRCALSSVDI YRTPLYDLRI DQKIYGELWK TGMFERMSLQ TDEDEHSIEM HLPYTAKAME SHKDEFTIIP VLVGALSESK EQEFGKLFSK YLADPSNLFV VSSDFCHWGQ RFRYSYYDES QGEIYRSIEH LDKMGMSIIE QLDPVSFSNY LKKYHNTICG RHPIGVLLNA ITELQKNGMN MSFSFLNYAQ SSQCRNWQDS SVSYAAGALT VH.

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    MEMO1 Human
  • View Data Sheet

    Name :

    S100A6 Mouse

    Description:

    S100 Calcium Binding Protein A6 Mouse Recombinant

    Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.

    Product # :

    PRO-240

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    Description

    S100A6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89 a.a) and having a molecular mass of 12.2kDa.S100A6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.
      S100A6 may function in stimulation prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

    • Synonyms

      Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.

    • 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 MACPLDQAIG LLVAIFHKYS GKEGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMDDL DRNKDQEVNF QEYVAFLGAL ALIYNEALK.

    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.

    S100A6 Mouse
  • View Data Sheet

    Name :

    CTACK Mouse

    Description:

    CTACK Mouse Recombinant (CCL27)

    C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    Product # :

    CHM-013

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    Description

    CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM NaCl.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

    More Info

    • Introduction

      CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.

    • Synonyms

      C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

    • Background

      What is the molecular weight/Mw of CTACK MOUSE Protein?
      CTACK MOUSE Protein has a total Mw of 10.9kDa.

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

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

      What is the Biological Activity of CTACK MOUSE Protein?
      The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

      What is the amino acid sequence of CTACK MOUSE Protein?
      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

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

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


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

    Ctack Mouse
  • View Data Sheet

    Name :

    NCR3 Human

    Description:

    Natural Cytotoxicity Triggering Receptor 3 Human Recombinant

    Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    Product # :

    PRO-1886

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    Description

    NCR3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (19-138 a.a) and having a molecular mass of 15.3kDa.NCR3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NCR3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytotoxicity Triggering Receptor 3 also known as NCR3 is a natural cytotoxicity receptor (NCR) which assists NK cells in the lysis of tumor cells. Moreover, NCR3 interacts with CD3-zeta (CD247), a T-cell receptor. A single nucleotide polymorphism in the 5' untranslated region of NCR3 has been related with mild malaria suceptibility. Three transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLWVSQPPEI RTLEGSSAFL PCSFNASQGR LAIGSVTWFR DEVVPGKEVR NGTPEFRGRL APLASSRFLH DHQAELHIRD VRGHDASIYV CRVEVLGLGV GTGNGTRLVV EKEHPQLGAG T

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    Ncr3 Human
  • View Data Sheet

    Name :

    TAGLN3 Human

    Description:

    Transgelin-3 Human Recombinant

    Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.

    Product # :

    PRO-946

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    Description

    TAGLN3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.6 kDa.The TAGLN3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TAGLN3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.

    • Synonyms

      Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.

    • 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 MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS NKGASQAGMT GYGMPRQIM

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    Tagln3 Human
  • View Data Sheet

    Name :

    PIN1 Human

    Description:

    Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Human Recombinant

    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, EC 5.2.1.8, Rotamase Pin1, PPIase Pin1, DOD, UBL5, PIN1, PPIase.

    Product # :

    ENZ-331

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    Description

    PPIase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids & having a molecular mass of 18.2 kDa. The PIN1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PIN1 protein solution (1 mg/ml) containing 20mM Tris-HCl buffer (pH7.5) 0.1M NaCl, 5mM DTT & 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 330 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-HCl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, EC 5.2.1.8, Rotamase Pin1, PPIase Pin1, DOD, UBL5, PIN1, PPIase.

    • 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

      MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE.

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    Pin1 Human
  • View Data Sheet

    Name :

    TNNI1 Human

    Description:

    Troponin I Type 1 Human Recombinant

    DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.

    Product # :

    PRO-1269

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    Description

    TNNI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.8kDa.TNNI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNNI1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.

    • Synonyms

      DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.

    • 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 MPEVERKPKI TASRKLLLKS LMLAKAKECW EQEHEEREAE KVRYLAERIP TLQTRGLSLS ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK VMDLRGKFKR PPLRRVRVSA DAMLRALLGS KHKVSMDLRA NLKSVKKEDT EKERPVEVGD WRKNVEAMSG MEGRKKMFDA AKSPTSQ

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    Tnni1 Human
  • View Data Sheet

    Name :

    CHP Human

    Description:

    Calcium Binding Protein P22 Human Recombinant

    CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.

    Product # :

    PRO-847

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    Description

    CHP Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-195 a.a.) and having a molecular mass of 24.7 kDa. The CHP is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHP Human solution containing 20mM Tris-HCl pH-7.5 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calcium-binding protein P22 is a phosphoprotein that binds to the sodium-hydrogen exchangers (NHEs). CHP is an essential cofactor which maintains the physiological activity of NHE family members. CHP has protein sequence resemblance to calcineurin B and it is also identified to be an endogenous inhibitor of calcineurin activity.CHP is necessary for constitutive membrane traffic. CHP Inhibits GTPase-stimulated Na(+)/H(+) exchange. CHP inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1.

    • Synonyms

      CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.

    • 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 MMGSRASTLL RDEELEEIKK ETGFSHSQIT RLYSRFTSLD KGENGTLSRE DFQRIPELAI NPLGDRIINA FFPEGEDQVN FRGFMRTLAH FRPIEDNEKS KDVNGPEPLN SRSNKLHFAF RLYDLDKDEK ISRDELLQVL RMMVGVNISD EQLGSIADRT IQEADQDGDS AISFTEFVKV LEKVDVEQKM SIRFLH.

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    Chp Human
  • View Data Sheet

    Name :

    CXCL1 Mouse

    Description:

    GRO1/KC Mouse Recombinant (CXCL1)

    Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

    Product # :

    CHM-335

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    Description

    KC Mouse Recombinant also known as N51 and GRO-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of approximately 7.8 kDa. The GRO-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer pH-7.4 and 0.1M NaCl.

    Purity

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

    Biological Activity

    The biological activity was determined by measuring the ability to chemoattrat human neutrophilsat a concentration of 10ng/ml-100ng/ml.

    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-a). 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 alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KC Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 GRO1 Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APIANELRCQ CLQTMAGIHL KNIQSLKVLP SGPHCTQTEV IATLKNGREA CLDPEAPLVQ KIVQKMLKGV PK.

    • Background

      What is the molecular weight/Mw of CXCL1 MOUSE Protein?
      CXCL1 MOUSE Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CXCL1 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL1 MOUSE Protein?
      CXCL1 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL1 MOUSE Protein?
      The biological activity was determined by measuring the ability to chemoattrat human neutrophilsat a concentration of 10ng/ml-100ng/ml.

      What is the amino acid sequence of CXCL1 MOUSE Protein?
      APIANELRCQ CLQTMAGIHL KNIQSLKVLP SGPHCTQTEV IATLKNGREA CLDPEAPLVQ KIVQKMLKGV PK.

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

      What is the endotoxin level for CXCL1 MOUSE Protein?
      The endotoxin level is minimal, CXCL1 MOUSE Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.03 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of KC as a Reference Standard.

    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 Mouse
  • View Data Sheet

    Name :

    CMC1 Human

    Description:

    COX Assembly Mitochondrial Protein 1 Human Recombinant

    C3orf68, Cmc1p, COX assembly mitochondrial protein homolog.

    Product # :

    PRO-1651

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    Description

    CMC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106 a.a.) and having a molecular mass of 14.9kDa.CMC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CMC1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COX Assembly Mitochondrial Protein 1(CMC1) is a member of the CMC family. CMC1 is required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. CMC1 attaches copper and might be involved in copper trafficking and distribution to COX and SOD1.

    • Synonyms

      C3orf68, Cmc1p, COX assembly mitochondrial protein homolog.

    • 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 MGSMALDPAD QHLRHVEKDV LIPKIMREKA KERCSEQVQD FTKCCKNSGV LMVVKCRKEN SALKECLTAY YNDPAFYEEC KMEYLKEREE FRKTGIPTKK RLQKLPTSM.

    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.

    Cmc1 Human
  • View Data Sheet

    Name :

    VBP1 Human

    Description:

    Von Hippel-Lindau Binding Protein 1 Human Recombinant

    Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.

    Product # :

    PRO-1325

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    Description

    VBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a) and having a molecular mass of 25kDa.VBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    VBP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prefoldin subunit 3 (VBP1) is a member of the prefoldin subunit alpha family. VBP1 interacts with the Von Hippel-Lindau protein in order to create an intracellular complex. Since VBP1 serves as a chaperone protein, it is assumed to have a role in the transport of the Von Hippel-Lindau protein from the perinuclear granules to the nucleus or cytoplasm. VBP1 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. VBP1 also binds to nascent polypeptide chain and stimulates folding in an environment in which there are numerous competing pathways for nonnative proteins.

    • Synonyms

      Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.

    • 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 MGSMAAVKDS CGKGEMATGN GRRLHLGIPE AVFVEDVDSF MKQPGNETAD TVLKKLDEQY QKYKFMELNL AQKKRRLKGQ IPEIKQTLEI LKYMQKKKES TNSMETRFLL ADNLYCKASV PPTDKVCLWL GANVMLEYDI DEAQALLEKN LSTATKNLDS LEEDLDFLRD QFTTTEVNMA RVYNWDVKRR NKDDSTKNKA.

    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.

    Vbp1 Human
  • View Data Sheet

    Name :

    GZMK Human

    Description:

    Granzyme-K Human Recombinant

    Granzyme K, Fragmentin-3, Granzyme-3, NK-tryptase-2, NK-Tryp-2, GZMK, TRYP2, Granzyme-K.

    Product # :

    ENZ-741

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    Description

    GZMK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 amino acids (27-264 a.a.) and having a molecular mass of 28.2kDa.GZMK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GZMK protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      GZMK is a part of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes and natural killer cells have the outstanding ability to bind, recognize and lyse specific target cells. They defend their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens.

    • Synonyms

      Granzyme K, Fragmentin-3, Granzyme-3, NK-tryptase-2, NK-Tryp-2, GZMK, TRYP2, Granzyme-K.

    • 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 MGSIIGGKEV SPHSRPFMAS IQYGGHHVCG GVLIDPQWVL TAAHCQYRFT KGQSPTVVLG AHSLSKNEAS KQTLEIKKFI PFSRVTSDPQ SNDIMLVKLQ TAAKLNKHVK MLHIRSKTSL RSGTKCKVTG WGATDPDSLR PSDTLREVTV TVLSRKLCNS QSYYNGDPFI TKDMVCAGDA KGQKDSCKGD SGGPLICKGV FHAIVSGGHE CGVATKPGIY TLLTKKYQTW IKSNLVPPHT N.

    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.

    Gzmk Human
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