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Search results

381 results found for “cadherin”

Name

Description

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  • View Data Sheet

    Name :

    GDI2 Human

    Description:

    GDP Dissociation Inhibitor 2 Human Recombinant

    GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.

    Product # :

    PRO-1948

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    Description

    GDI2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 468 amino acids (1-445) and having a molecular mass of 53.1 kDa.GDI2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDI2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Rab GDP dissociation inhibitor beta isoform 1 (GDI2) is a member of the GDP dissociation inhibitors (GDIs) family. GDI proteins can bind and release GDP-bound Rab proteins from membranes. GDI1 interacts with virtually all of the Rab proteins, whereas GDI2 interacts with Rabll but not Rab3A. GDI2 distributes ubiquitously, presenting a membrane bound location in perinuclear regions of cells.

    • Synonyms

      GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.

    • 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 MGSMNEEYDV IVLGTGLTEC ILSGIMSVNG KKVLHMDRNP YYGGESASIT PLEDLYKRFK IPGSPPESMG RGRDWNVDLI PKFLMANGQL VKMLLYTEVT RYLDFKVTEG SFVYKGGKIY KVPSTEAEAL ASSLMGLFEK RRFRKFLVYV ANFDEKDPRT FEGIDPKKTT MRDVYKKFDL GQDVIDFTGH ALALYRTDDY LDQPCYETIN RIKLYSESLA RYGKSPYLYP LYGLGELPQG FARLSAIYGG TYMLNKPIEE IIVQNGKVIG VKSEGEIARC KQLICDPSYV KDRVEKVGQV IRVICILSHP IKNTNDANSC QIIIPQNQVN RKSDIYVCMI SFAHNVAAQG KYIAIVSTTV ETKEPEKEIR PALELLEPIE QKFVSISDLL VPKDLGTESQ IFISRTYDAT THFETTCDDI KNIYKRMTGS EFDFEEMKRK KNDIYGED.

    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.

    Gdi2 Human
  • View Data Sheet

    Name :

    LBH Human

    Description:

    Limb Bud And Heart Development Human Recombinant

    Protein LBH, hLBH, Limb Bud And Heart Development Homolog.

    Product # :

    PRO-423

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    Description

    LBH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-105 a.a) and having a molecular mass of 14.6kDa.LBH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LBH protein solution (0.25mg/ml) containing 20mM Tris-HCl(pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Limb Bud And Heart Development, (LBH) belongs to the LBH family.LBH is highly expressed in the heart, and expressed at low levels in placenta, lung, skeletal muscle, kidney and liver. In addition, LBH protein is a transcriptional activator which may act in mitogen-activated protein kinase signaling pathway. Among the diseases associated with LBH are celiac disease, and rheumatoid arthritis.

    • Synonyms

      Protein LBH, hLBH, Limb Bud And Heart Development 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 MGSMSIYFPI HCPDYLRSAK MTEVMMNTQP MEEIGLSPRK DGLSYQIFPD PSDFDRCCKL KDRLPSIVVE PTEGEVESGE LRWPPEEFLV QEDEQDNCEE TAKENKEQ

    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.

    Lbh Human
  • View Data Sheet

    Name :

    TXN1 E.Coli

    Description:

    Thioredoxin E.Coli Recombinant

    Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    Product # :

    PRO-334

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    • description
    • source
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    • purity
    • biological activity
    • More Info

    Description

    Recombinant Thioredoxin was purified from E. coli harboring its gene.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 20mM phosphate buffer pH 7.4.

    Purity

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

    Biological Activity

    TRX activity is assayed by measuring the change in absorbance at 650 nm at 25°C using 0.13µM bovine insulin containing 0.33mM DTT (pH 6.5).
    The specific activity was found to be 3IU/mg.

    More Info

    • Introduction

      Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in refolding proteins expressed in E. coli. To this end, thioredoxin has been shown to act as a protein disulfide isomerase.Its Molecular Weight is 11.9kDa. and the pI is 4.67.

    • Synonyms

      Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    • Physical Appearance

      Sterile Lyophilized Powder.

    • Stability

      TRX although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TRX in sterile 18MΩ-cm H2O.

    • Amino Acid Sequence

      HMSDKIIHL TDDSFDTDVLKADGAIL VDFW AEWCGPCKMIAPILDEI GKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGAL DANLA.

    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.

    Thioredoxin 1
  • View Data Sheet

    Name :

    Borrelia Spielmanii DbpA

    Description:

    Borrelia Spielmanii Decorin Binding Protein A Recombinant

    Product # :

    BOR-026

    Price :

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    Description

    Recombinant Borrelia Spielmanii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 17kDa. Borrelia Spielmanii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Spielmanii DbpA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mostly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The Gram-negative bacterium Borreliella spielmanii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. DbpA, also known as p17 or Osp17, is a heterogeneous protein among the human pathogenic B. burgdorferi sensu lato species.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.

    • Applications

      Western blot with Lyme positive plasma.

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

    Borrelia Spielmanii Dbpa
  • View Data Sheet

    Name :

    Resistin Rat, His

    Description:

    Resistin Rat Recombinant, His Tag

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-458

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    Description

    Resistin Rat Recombinant is manufactured with N-terminal fusion of His tag. Resistin Rat Recombinant His-Tagged Fusion Protein is an 11.9 kDa protein containing 94 amino acid residues of the Resistin Rat and 16 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Mouse resistin is expressed as a 114 amino acid prepeptide; its hydrofobic Nterminal 20 amino acid signal peptide is cleaved before its secretion. Mouse resistin circulates in blood as a homodimeric protein consisting of two 94 amino acid polypeptides, which are disulfide-linked via Cys26.
      Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add 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 on cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMPSMS LCPMDEAISK KINQDFSSLL PAAMKNTVLH CWSVSSRGRL ASCPEGTTVT SCSCGSGCGS WDVREDTMCH CQCGSIDWTA ARCCTLRVGS.

    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.

    Resistin Rat
  • View Data Sheet

    Name :

    PPIH Human

    Description:

    Cyclophilin-H Human Recombinant

    Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    Product # :

    ENZ-379

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    Description

    PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-177) and having a molecular mass of 19.2 kDa. PPIH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml solution containing 1x PBS pH-7.4 10% glycerol.

    Purity

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

    Biological Activity

    Specific activity is > 220 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

      PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and increase protein folding. PPIH enzyme is a precise factor of the complex that comprises pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. PPIH possess PPIase activity and acts as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.

    • Synonyms

      Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    • 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

      MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGEFRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM.

    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.

    Ppih Human
  • View Data Sheet

    Name :

    RARRES2 Human, His

    Description:

    Retinoic Acid Receptor Responder 2 Human Recombinant, His Tag

    Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.

    Product # :

    PRO-1458

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    Description

    RARRES2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (21-157a.a) and having a total molecular mass of 18 kDa. RARRES2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RARRES2 protein solution (1mg/ml) containing 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

      RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in a vast variety of tissues. RARRES2 acts as an adipokine, and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23. RARRES2 signals via its receptor, ChemR23 (CMKLR1), as a positive regulator of adipocyte differentiation and metabolic function. The Chemerin receptor acts as a coreceptor for SIV and some primary HIV-1 strains. The Chemerin receptor has another ligand, called tazarotene-induced gene.

    • Synonyms

      Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.

    • 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 MELTEAQRRG LQVALEEFHK HPPVQWAFQE TSVESAVDTP FPAGIFVRLE FKLQQTSCRK RDWKKPECKV RPNGRKRKCL ACIKLGSEDK VLGRLVHCPI ETQVLREAEE HQETQCLRVQ RAGEDPHSFY FPGQFAFS.

    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.

    Rarres2 Human His
  • View Data Sheet

    Name :

    S100A10 Human

    Description:

    S100 Calcium Binding Protein A10 Human Recombinant

    Protein S100-A10, S100 calcium-binding protein A10, Calpactin-1 light chain, Calpactin I light chain, p10 protein, p11, Cellular ligand of annexin II, S100A10, ANX2LG, CAL1L, CLP11, 42C, p10, GP11, ANX2L, Ca[1], MGC111133.

    Product # :

    PRO-384

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    Description

    S100A10 Human Recombinant also called Calpactin light chain is expressed in E. coli having a molecular weight of 15.3kDa fused to an amino terminal hexahistidine tag.

    Source

    Escherichia Coli.

    Formulation

    S100-A10 is supplied in 1xPBS and 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    2 bands on Western blot at 15.3 and 30.6 kDa, respectively representing monomeric and dimeric form.

    More Info

    • Introduction

      S100A10 is a member of the S100 family of proteins contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A10 may function in exocytosis and endocytosis.

    • Synonyms

      Protein S100-A10, S100 calcium-binding protein A10, Calpactin-1 light chain, Calpactin I light chain, p10 protein, p11, Cellular ligand of annexin II, S100A10, ANX2LG, CAL1L, CLP11, 42C, p10, GP11, ANX2L, Ca[1], MGC111133.

    • 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.

    • Applications

      S100A10 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    S100A10 Human
  • View Data Sheet

    Name :

    S100A15 Mouse

    Description:

    S100 Calcium Binding Protein A15 Mouse Recombinant

    Protein S100-A7A, S100 calcium-binding protein A15A, S100 calcium-binding protein A7A.

    Product # :

    PRO-1145

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    Description

    S100A15 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (1-108) and having a molecular mass of 15.0 kDa.S100A15 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The S100A15 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mouse S100A15 is a protein of 104 amino acids with an expected molecular weight of 12,870 Dalton having 2 EF-hand calcium binding sites. The S100A15 expression is upregulated in cultured keratinocytes stimulated to differentiate by calcium or phorbol esters. S100A15 is expressed in the skin and keratinocytes.

    • Synonyms

      Protein S100-A7A, S100 calcium-binding protein A15A, S100 calcium-binding protein A7A.

    • 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 MGSHMPDTPV EDSLFQIIHC FHHYAAREGD KETLSLEELK ALLLDSVPRF MDTLGRRQPY YITELFRAAD KNKDNQICFD EFLYILGKLV KDYHLQFHRQ LCAHYCTEHS LY.

    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.

    S100A15 Mouse
  • View Data Sheet

    Name :

    CST3 Mouse

    Description:

    Cystatin-C Mouse Recombinant

    Post G-globulin, CST 3, CST3, Gamma-Trace, Cystatin 3, Amyloid Angiopathy and Cerebral Hemorrhage, Cystatin-C precursor, neuroendocrine basic polypeptide.

    Product # :

    PRO-597

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    Description

    Cystatin-C Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15kDa. The Mouse Cystatin-C is fused to His tag at N-Terminus.The Mouse Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Post G-globulin, CST 3, CST3, Gamma-Trace, Cystatin 3, Amyloid Angiopathy and Cerebral Hemorrhage, Cystatin-C precursor, neuroendocrine basic polypeptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MRGSHHHHHH GMASATPKQG PRMLGAPEEA DANEEGVRRA LDFAVSEYNK GSNDAYHSRA IQVVRARKQL VAGVNYFLDV EMGRTTCTKS QTNLTDCPFH DQPHLMRKAL CSFQIYSVPW KGTHSLTKFSCKNA.

    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.

    Cystatin C Mouse
  • View Data Sheet

    Name :

    CST3 Rat

    Description:

    Cystatin C Rat Recombinant

    Cystatin-C, Cystatin-3, CYSC, MGC105556.

    Product # :

    PRO-438

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    Description

    Total 134 AA, Mw: 14.93 kDa (calculated). N-terminal His-tag (14AA).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 micron) and lyophilized from 0.5 mg/ml in 0.03M Acetate buffer, pH 4.

    Purity

    Greater than 96% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, CYSC, MGC105556.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add 0.2 ml of 0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 0.1mg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MRGSHHHHHH GMASGTSRPP PRLLGAPQEA DASEEGVQRA LDFAVSEYNK GSNDAYHSRA IQVVRARKQLVAGINYYLDV EMGRTTCTKS QTNLTNCPFH DQPHLMRKAL CSFQIYSVPW KGTHTLTKSS.

    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.

    Cystatin C Rat
  • View Data Sheet

    Name :

    CST6 Human

    Description:

    Cystatin E/M Human Recombinant

    Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.

    Product # :

    PRO-892

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    Description

    CST6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (29-149) and having a molecular mass of 15.9 kDa.The CST6 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CST6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CST6 belongs to the type 2 cystatin family. Unlike other family members that act as active cysteine protease inhibitors, CST6 restrain the inhibition of cathepsin B but is not active against cathepsin C. CST6 are secretable proteins that influence osteogenesis and bone resorption, regulation of the hepatocyte growth factor receptors, and the response to systemic inflammation.

    • Synonyms

      Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.

    • 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 MRPQERMVGE LRDLSPDDPQ VQKAAQAAVA SYNMGSNSIY YFRDTHIIKA QSQLVAGIKY FLTMEMGSTD CRKTRVTGDH VDLTTCPLAA GAQQEKLRCD FEVLVVPWQN SSQLLKHNCV QM.

    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.

    Cst6 Human
  • View Data Sheet

    Name :

    Activin-A Rat

    Description:

    Activin-A Rat Recombinant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-147

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    Description

    Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). 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

      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

      Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 26.2 kDa.

      What is the source or expression system of Activin A Protein?
      Ecoli

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

      What is the Biological Activity of Activin A Protein?
      Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.

      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?
      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

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

    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.

    Inhba Rat
  • View Data Sheet

    Name :

    ALCAM (CD166) Mouse

    Description:

    Activated Leukocyte Cell Adhesion Molecule (CD166) Mouse Recombinant

    Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.

    Product # :

    PRO-2749

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    Description

    ALCAM mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 739 amino acids (28-527a.a.) and having a molecular mass of 83.1kDa. ALCAM is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ALCAM protein solution (0.25mg/ml) contains 50% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to block the adhesion of Jurkat human acute T cell leukemia cells to immobilized Recombinant Human CD6. When cells are added to 1 ug/ml of mouse ALCAM binded to CD6, this effect is more to 50%.

    More Info

    • Introduction

      CD166 antigen isoform 2 (ALCAM) is a type 1 membrane glycoprotein and belongs to the immunoglobulin superfamily. ALCAM is expressed on thymic epithelium, microvascular endothelium, activated lymphocytes and monocytes, and monocyte-derived dendritic cells. CD166 and CD6 interaction plays a role in T cell development and T cell regulation, as well as in the binding of T cells and B cells to activated leukocytes.

    • Synonyms

      Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.

    • 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

      WYTVNSAYGD TIVMPCRLDV PQNLMFGKWK YEKPDGSPVF IAFRSSTKKS VQYDDVPEYK DRLSLSENYT LSIANAKISD EKRFVCMLVT EDNVFEAPTL VKVFKQPSKP EIVNKAPFLE TDQLKKLGDC ISRDSYPDGN ITWYRNGKVL QPVEGEVAIL FKKEIDPGTQ LYTVTSSLEY KTTRSDIQMP FTCSVTYYGP SGQKTIYSEQ EIFDIYYPTE QVTIQVLPPK NAIKEGDNIT
      LQCLGNGNPP PEEFMFYLPG QPEGIRSSNT YTLTDVRRNA TGDYKCSLID KRNMAASTTI TVHYLDLSLN PSGEVTKQIG DTLPVSCTIS ASRNATVVWM KDNIRLRSSP SFSSLHYQDA GNYVCETALQ EVEGLKKRES LTLIVEGKPQ IKMTKKTDPS GLSKTIICHV EGFPKPAIHW TITGSGSVIN QTEESPYING RYYSKIIISP EENVTLTCTA ENQLERTVNS LNVSAISIPE
      HDEADDISDE NREKVNDQAK LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK 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.

    Cd166 Mouse
  • View Data Sheet

    Name :

    NECTIN2 Human

    Description:

    Nectin Cell Adhesion Molecule 2 Human Recombinant

    Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.

    Product # :

    PRO-2461

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    Description

    NECTIN2 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 337 amino acids (32-360a.a.) and having a molecular mass of 36.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN2 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    NECTIN2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nectin Cell Adhesion Molecule 2, also known as NECTIN2, is a Ca(2+)-independent cell-cell adhesion molecule which is one of the plasma membrane components of adherens junctions. NECTIN2 takes a vital part in the establishment of homotypic as well as heterotypic cell to cell contacts. NECTIN2 is essential for resisting herpes simplex virus type 2 infection in transfected cells. NECTIN2 is also a possible target for antibody therapy of breast & ovarian cancers. NECTIN2 might be related with human longevity. Two diseases which have been associated with NECTIN2 are Herpes Simplex and Ovarian Cystic Teratoma.

    • Synonyms

      Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.

    • 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

      QDVRVQVLPE VRGQLGGTVE LPCHLLPPVP GLYISLVTWQ RPDAPANHQN VAAFHPKMGP SFPSPKPGSE RLSFVSAKQS TGQDTEAELQ DATLALHGLT VEDEGNYTCE FATFPKGSVR GMTWLRVIAK PKNQAEAQKV TFSQDPTTVA LCISKEGRPP ARISWLSSLD WEAKETQVSG TLAGTVTVTS RFTLVPSGRA DGVTVTCKVE HESFEEPALI PVTLSVRYPP EVSISGYDDN WYLGRTDATL SCDVRSNPEP TGYDWSTTSG TFPTSAVAQG SQLVIHAVDS LFNTTFVCTV TNAVGMGRAE QVIFVRETPN TAGAGATGGL EHHHHHH.

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    Nectin2 Human
  • View Data Sheet

    Name :

    EFNB1 Human, Sf9

    Description:

    Ephrin-B1 Human Recombinant, Sf9

    Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2. 

    Product # :

    PRO-2543

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    Description

    EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EFNB1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.

    • Synonyms

      Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 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

      ADPLAKNLEP VSWSSLNPKF LSGKGLVIYP KIGDKLDIIC PRAEAGRPYE YYKLYLVRPE QAAACSTVLD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL EFKKHHDYYI TSTSNGSLEG LENREGGVCR TRTMKIIMKV GQDPNAVTPE QLTTSRPSKE ADNTVKMATQ APGSRGSLGD
      SDGKHETVNQ EEKSGPGASG GSSGDPDGFF NSKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN
      QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH 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.

    Ephrin B1
  • View Data Sheet

    Name :

    ENHO Human

    Description:

    Energy Homeostasis Associated Human Recombinant

    Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    Product # :

    PRO-1569

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    Description

    ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.

    • Synonyms

      Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.

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    Enho Human
  • View Data Sheet

    Name :

    Calumenin Human

    Description:

    Calumenin Human Recombinant

    CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.

    Product # :

    PRO-2465

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    Description

    Calumenin Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (20-315) and having a molecular mass of 35kDa. Calumenin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Calumenin solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The IC50 value is < 2.0nM. The inhibitory function of Cystatin 5 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.

    More Info

    • Introduction

      Calumenin is a calcium-binding protein located in the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin belongs to a family of multiple EF-hand proteins (CERC) that include reticulocalbin, ERC-55, and Cab45 and the product of this gene. Calumenin binds 7 calcium ions having low affinity and takes part in such ER functions as protein folding and sorting.

    • Synonyms

      CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.

    • 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

      MKPTEKKDRV HHEPQLSDKV HNDAQSFDYD HDAFLGAEEA KTFDQLTPEE SKERLGKIVS KIDGDKDGFV TVDELKDWIK FAQKRWIYED VERQWKGHDL NEDGLVSWEE YKNATYGYVL DDPDPDDGFN YKQMMVRDER RFKMADKDGD LIATKEEFTA FLHPEEYDYM KDIVVQETME DIDKNADGFI DLEEYIGDMY SHDGNTDEPE WVKTEREQFV EFRDKNRDGK MDKEETKDWI LPSDYDHAEA EARHLVYESD QNKDGKLTKE EIVDKYDLFV GSQATDFGEA LVRHDEF.

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    Calumenin Human 2
  • View Data Sheet

    Name :

    CX3CL1 Human, His

    Description:

    Fractalkine Human Recombinant (CX3CL1), His Tag

    Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    Product # :

    CHM-360

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    • SDS-PAGE

    Description

    Fractalkine Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 97 amino acids (25-100 a.a.) and having a molecular mass of 10.9kDa. The Fractalkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Fractalkine solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    CX3CL1 Human, His-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

      Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    • 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 MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.

    • Background

      What is the molecular weight/Mw of CX3CL1 HUMAN, HIS Protein?
      CX3CL1 HUMAN, HIS Protein has a total Mw of 10.9kDa.

      What is the source or expression system of CX3CL1 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CX3CL1 HUMAN, HIS Protein?
      CX3CL1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 HUMAN, HIS Protein?
      The biological functionality of CX3CL1 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CX3CL1 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.

      What applications can CX3CL1 HUMAN, HIS Protein be used in?
      CX3CL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 HUMAN, HIS Protein?
      The endotoxin level is minimal, CX3CL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.


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    Fractalkine Human His
  • View Data Sheet

    Name :

    PLDN Human

    Description:

    Pallidin Homolog Human Recombinant

    Pallidin protein homolog (mouse), PA, HPS9, PALLID, syntaxin 13-interacting protein pallid.

    Product # :

    PRO-1068

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    Description

    PLDN Human Recombinant produced in E. coli is a single polypeptide chain containing 192 amino acids (1-172) and having a molecular mass of 21.9kDa.PLDN is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PLDN solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pallidin is involved in intracellular vesicle trafficking. PLDN cooperates with Syntaxin 13 that facilitates intracellular membrane fusion. A Few alternatively spliced transcript variations of this gene have been discovered however the full-length nature of several of these variants has not been determined. PLDN takes part in the creation of lysosome-related organelles, for example melanosomes and platelet-dense granules. PLDN is known to cooperate with Dysbindin, BLOC1S1, STX12, CNO, MUTED, SNAPAP and BLOC1S2.

    • Synonyms

      Pallidin protein homolog (mouse), PA, HPS9, PALLID, syntaxin 13-interacting protein pallid.

    • 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 MSVPGPSSPD GALTRPPYCL EAGEPTPGLS DTSPDEGLIE DLTIEDKAVE QLAEGLLSHY LPDLQRSKQA LQELTQNQVV LLDTLEQEIS KFKECHSMLD INALFAEAKH YHAKLVNIRK EMLMLHEKTS KLKKRALKLQ QKRQKEELER EQQREKEFER EKQLTARPAK RM

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    Pldn Human
  • View Data Sheet

    Name :

    GADD45GIP1 Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant

    Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

    Product # :

    PRO-972

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    Description

    GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GADD45GIP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.

    • Synonyms

      Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

    • 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 MPRWQLGPRY AAKQFARYGA ASGVVPGSLW PSPEQLRELE AEEREWYPSL ATMQESLRVK QLAEEQKRRE REQHIAECMA KMPQMIVNWQ QQQRENWEKA QADKERRARL QAEAQELLGY QVDPRSARFQ ELLQDLEKKE RKRLKEEKQK RKKEARAAAL AAAVAQDPAA SGAPSS

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    Gadd45Gip1 Human
  • View Data Sheet

    Name :

    PPIH Human, His

    Description:

    Cyclophilin-H Human Recombinant, His Tag

    Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    Product # :

    ENZ-730

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    Description

    PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-177) containing 186 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 20.3kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in phosphate buffered saline pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and increase protein folding. PPIH enzyme is a precise factor of the complex that comprises pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. PPIH possess PPIase activity and acts as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.

    • Synonyms

      Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHASAVANSSPVNP VVFFDVSIGG QEVGRMKIEL FADVVPKTAE NFRQFCTGEF RKDGVPIGYK GSTFHRVIKD FMIQGGDFVN GDGTGVASIY RGPFADENFK LRHSAPGLLS MANSGPSTNG CQFFITCSKC DWLDGKHVVF GKIIDGLLVM RKIENVPTGP NNKPKLPVVI SQCGEM.

    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.

    Ppih Human His
  • View Data Sheet

    Name :

    CECR1 Human

    Description:

    Cat Eye Syndrome Chromosome Region Candidate 1 Human Recombinant

    Cat Eye Syndrome Chromosome Region, Candidate 1, Cat Eye Syndrome Critical Region Protein 1, IDGFL, ADA2, ADGF, Adenosine Deaminase 2, EC 3.5.4.4, SNEDS, PAN, CECR1.

    Product # :

    PRO-2323

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    Description

    CECR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 490 amino acids (30-511a.a.) and having a molecular mass of 56.9kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CECR1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Insect Cell.

    Formulation

    CECR1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adenosine deaminase CECR1 isoform (CECR1) belongs to a family of adenosine deaminase-related growth factors. Adenosine deaminase is a key enzyme of purine nucleotide metabolism. CECR1 is a secreted protein, which is expressed in various tissues, with the highest expression in the lymphoblasts, heart, lung, and the placenta.

    • Synonyms

      Cat Eye Syndrome Chromosome Region, Candidate 1, Cat Eye Syndrome Critical Region Protein 1, IDGFL, ADA2, ADGF, Adenosine Deaminase 2, EC 3.5.4.4, SNEDS, PAN, CECR1.

    • 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

      IDETRAHLLL KEKMMRLGGR LVLNTKEELA NERLMTLKIA EMKEAMRTLI FPPSMHFFQA KHLIERSQVF NILRMMPKGA ALHLHDIGIV TMDWLVRNVT YRPHCHICFT PRGIMQFRFA HPTPRPSEKC SKWILLEDYR KRVQNVTEFD DSLLRNFTLV TQHPEVIYTN QNVVWSKFET IFFTISGLIH YAPVFRDYVF RSMQEFYEDN VLYMEIRARL LPVYELSGEH HDEEWSVKTY QEVAQKFVET HPEFIGIKII YSDHRSKDVA VIAESIRMAM GLRIKFPTVV AGFDLVGHED TGHSLHDYKE ALMIPAKDGV KLPYFFHAGE TDWQGTSIDR NILDALMLNT TRIGHGFALS KHPAVRTYSW KKDIPIEVCP ISNQVLKLVS DLRNHPVATL MATGHPMVIS SDDPAMFGAK GLSYDFYEVF MGIGGMKADL RTLKQLAMNS IKYSTLLESE KNTFMEIWKK RWDKFIADVA TKLEHHHHHH

    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.

    Cecr1 Human
  • View Data Sheet

    Name :

    CETN1 Human

    Description:

    Centrin-1 Human Recombinant

    Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.

    Product # :

    PRO-1104

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CETN1 Human Recombinant produced E. coli is a single polypeptide chain containing 196 amino acids (1-172) and having a molecular mass of 22.1kDa.CETN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CETN1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.

    • Synonyms

      Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.

    • 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 MGSHMASGFK KPSAASTGQK RKVAPKPELT EDQKQEVREA FDLFDVDGSG TIDAKELKVA MRALGFEPRK EEMKKMISEV DREGTGKISF NDFLAVMTQK MSEKDTKEEI LKAFRLFDDD ETGKISFKNL KRVANELGEN LTDEELQEMI DEADRDGDGE VNEEEFLRIM KKTSLY

    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.

    Cetn1 Human
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