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Search results

1000 results found for “hemopexin”

Name

Description

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  • View Data Sheet

    Name :

    PLAC8 Human

    Description:

    Placenta-Specific 8 Human Recombinant

     Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.

    Product # :

    PRO-1725

    Price :

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    Description

    PLAC8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa.PLAC8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PLAC8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0),0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Placenta-Specific 8 (PLAC8) is a member of the cornifelin family. The PLAC8 protein is expressed at high levels in the plasmacytoid dendritic cells, spleen, lymph nodes, peripheral blood leukocytes, and bone marrow.

    • Synonyms

      Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.

    • 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 MGSMQAQAPV VVVTQPGVGP GPAPQNSNWQ TGMCDCFSDC GVCLCGTFCF PCLGCQVAAD MNECCLCGTS VAMRTLYRTR YGIPGSICDD YMATLCCPHC TLCQIKRDIN RRRAMRTF.

    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.

    Plac8 Human
  • View Data Sheet

    Name :

    Pleiotrophin Human

    Description:

    Pleiotrophin Human Recombinant

    PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.

    Product # :

    CYT-749

    Price :

    Quantity :

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    • sds-page

    Description

    Pleiotrophin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids and having a molecular mass of 15.3kDa.The Pleiotrophin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Pleiotrophin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    sds-page

    Pleiotrophin Human SDS-PAGE - Product image 1

    More Info

    • Introduction

      Pleiotrophin (Osteoblast-Specific Factor-1, OSF-1) contains 136 amino acid residues. The sequence is very rich in cationic amino acids (24% of the residues); lysine cluster sequences are found in the N-terminal and C-terminal ends of the structure.
      The OSF-1 gene was shown by Northern blotting analysis to be expressed in mouse calvarial osteoblast-enriched cells and in mouse brain tissues, but not in thymus, spleen, kidney, liver, lung, testis or heart. Pleiotrophin has the ability to promote adhesion, migration, expansion, and differentiation of human osteoprogenitor cells. In addition to certain types of cancer, the embryonic growth and differentiation factor pleiotrophin is found also in adults in inflammatory diseases. In osteoarthritis, pleiotrophin is especially expressed in early stages, and its concentrations in the synovial fluid could serve as a marker for the progress of the disease. Pleitrophin might be involved in cartilage repair in osteoarthritis, in particular, in earlier stages.

    • Synonyms

      PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD.

    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.

    Pleiotrophin
  • View Data Sheet

    Name :

    FURIN Human

    Description:

    Furin Human Recombinant

    Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    Product # :

    PRO-2199

    Price :

    Quantity :

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    • description
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    • formulation
    • purity
    • More Info

    Description

    FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.

    • Synonyms

      Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.

    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.

    Furin Human
  • View Data Sheet

    Name :

    GH Human, HEK

    Description:

    Growth Hormone Human Recombinant, HEK

    GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-091

    Price :

    Quantity :

    Shipping Method :

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

    Description

    Growth Hormone Human Recombinant produced in HEK cells is a non-glycosylated monomer, having a total molecular weight of 22kDa.The GH is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The GH was lyophilized from 1.13mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The activity was determined by the dose dependent stimulation of the proliferation of rat lymphoma line Nb2-11 cells (prolactin indicator cell line), the ED50 is 0.1ng/ml.

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH 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 GH in sterile 1xPBS containing 0.1% endotoxin-free recombinant HSA.

    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.

    Gh Human Hek
  • View Data Sheet

    Name :

    PRDX2 Rat

    Description:

    Peroxiredoxin-2 Rat Recombinant

    Peroxiredoxin-2, Prdx2, Prdx, Thiol-specific antioxidant protein, TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1.

    Product # :

    ENZ-910

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    Description

    PRDX2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-198 a.a) and having a molecular mass of 24.3kDa. PRDX2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRDX2 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
      If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer.

    • Synonyms

      Peroxiredoxin-2, Prdx2, Prdx, Thiol-specific antioxidant protein, TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1.

    • 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 MGSHMASGNA HIGKPAPDFT GTAVVDGAFK EIKLSDYRGK YVVLFFYPLD FTFVCPTEII AFSDHAEDFR KLGCEVLGVS VDSQFTHLAW INTPRKEGGL GPLNIPLLAD VTKSLSQNYG VLKNDEGIAY RGLFIIDAKG VLRQITVNDL PVGRSVDEAL RLVQAFQYTD EHGEVCPAGW KPGSDTIKPN VDDSKEYFSK HN.

    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.

    Prdx2 Rat
  • View Data Sheet

    Name :

    GLRX1 Human

    Description:

    Glutaredoxin 1 Human Recombinant

    Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin-1, Thioltransferase-1, TTase-1, GLRX, MGC117407.

    Product # :

    ENZ-391

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    Description

    Glutaredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 106 amino acids having a molecular mass of 11.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    Glutaredoxin solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

    • Synonyms

      Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin-1, Thioltransferase-1, TTase-1, GLRX, MGC117407.

    • Physical Appearance

      Sterile Filtered clear 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

      MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ.

    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.

    Glrx1 Human
  • View Data Sheet

    Name :

    TSNAX Human

    Description:

    Translin-Associated Factor X Human Recombinant

    TRAX, Translin-associated protein X, Translin-associated factor X.

    Product # :

    PRO-1292

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    Description

    TSNAX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (1-290 a.a.) and having a molecular mass of 35kDa.TSNAX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TSNAX protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TSNAX is a member of translin family. TSNAX particularly interacts with translin, a DNA-binding protein that binds consensus sequences at breakpoint junctions of chromosomal translocations. TSNAX works in combination with TSN as an endonuclease involves in the activation of the RNA-induced silencing complex (RISC). TSNAX has bipartite nuclear targeting sequences that afford nuclear transport for translin, which lacks any nuclear targeting motifs.

    • Synonyms

      TRAX, Translin-associated protein X, Translin-associated factor X.

    • 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 MGSMSNKEGS GGFRKRKHDN FPHNQRREGK DVNSSSPVML AFKSFQQELD ARHDKYERLV KLSRDITVES KRTIFLLHRI TSAPDMEDIL TESEIKLDGV RQKIFQVAQE LSGEDMHQFH RAITTGLQEY VEAVSFQHFI KTRSLISMDE INKQLIFTTE DNGKENKTPS SDAQDKQFGT WRLRVTPVDY LLGVADLTGE LMRMCINSVG NGDIDTPFEV SQFLRQVYDG FSFIGNTGPY EVSKKLYTLK QSLAKVENAC YALKVRGSEI PKHMLADVFS VKTEMIDQEE GIS.

    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.

    Tsnax Human
  • View Data Sheet

    Name :

    CLMP Human

    Description:

    CXADR-Like Membrane Protein Human Recombinant

    CXADR-Like Membrane Protein, CLMP, Adipocyte Adhesion Molecule, Coxsackie- And Adenovirus Receptor-Like Membrane Protein, ACAM, ASAM, Adipocyte-Specific Adhesion Molecule, CAR-Like Membrane Protein, CSBS, CSBM.

    Product # :

    PRO-1941

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    Description

    CLMP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (19-235) and having a molecular mass of 26.1 kDa.CLMP is fused to a 16 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CLMP solution (0.5mg/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

      The CTX family of proteins (including ASAM) are type I transmembrane proteins within the Ig superfamily, which localize to junctional complexes between endothelial and epithelial cells and may play a role in cell-cell adhesion. CLMP has a role in adipocyte differentiation and development of obesity. CLMP is required for normal small intestine development.

    • Synonyms

      CXADR-Like Membrane Protein, CLMP, Adipocyte Adhesion Molecule, Coxsackie- And Adenovirus Receptor-Like Membrane Protein, ACAM, ASAM, Adipocyte-Specific Adhesion Molecule, CAR-Like Membrane Protein, CSBS, CSBM.

    • 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

      MASMTGGQQM GRGSHMTHTE IKRVAEEKVT LPCHHQLGLP EKDTLDIEWL LTDNEGNQKV VITYSSRHVY NNLTEEQKGR VAFASNFLAG DASLQIEPLK PSDEGRYTCK VKNSGRYVWS HVILKVLVRP SKPKCELEGE LTEGSDLTLQ CESSSGTEPI VYYWQRIREK EGEDERLPPK SRIDYNHPGR VLLQNLTMSY SGLYQCTAGN EAGKESCVVR VTVQYVQSIG MVA.

    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.

    Clmp Human
  • View Data Sheet

    Name :

    UROS Human

    Description:

    Uroporphyrinogen III Synthase Human Recombinant

    Uroporphyrinogen-III synthase, UROIIIS, UROS, Hydroxymethylbilane hydrolyase [cyclizing], Uroporphyrinogen-III cosynthase.

    Product # :

    ENZ-140

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    Description

    UROS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-265 a.a.) and having a molecular mass of 30.7kDa.UROS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UROS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Uroporphyrinogen III synthase (UROS) is an enzyme involved in the 4th step of porphyrin metabolism and in the conversion of hydroxymethyl bilane into uroporphyrinogen III. Defects in the UROS protein can cause molecular lesions which lead to the autosomal recessive Gunther disease, otherwise known as congenital erythropoietic porphyria (CEP).

    • Synonyms

      Uroporphyrinogen-III synthase, UROIIIS, UROS, Hydroxymethylbilane hydrolyase [cyclizing], Uroporphyrinogen-III cosynthase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      UROS Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKVLLLKDAK EDDCGQDPYI RELGLYGLEA TLIPVLSFEF LSLPSFSEKL SHPEDYGGLI FTSPRAVEAA ELCLEQNNKT EVWERSLKEK WNAKSVYVVG NATASLVSKI GLDTEGETCG NAEKLAEYIC SRESSALPLL FPCGNLKREI LPKALKDKGI AMESITVYQT VAHPGIQGNL NSYYSQQGVP ASITFFSPSG LTYSLKHIQE LSGDNIDQIK FAAIGPTTAR ALAAQGLPVS CTAESPTPQA LATGIRKALQ PHGCC.

    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.

    Uros Human
  • View Data Sheet

    Name :

    UXT Human

    Description:

    Ubiquitously-Expressed, Prefoldin-Like Chaperone Human Recombinant

    Protein UXT, Androgen receptor trapped clone 27 protein, ART-27, Ubiquitously expressed transcript protein, UXT, HSPC024, STAP1.

    Product # :

    PRO-1312

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    Description

    UXT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (1-157 a.a.) and having a molecular mass of 20.4kDa.UXT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitously-expressed transcript (UXT) is a member of the UXT family. UXT serves as a cofactor which modulates androgen receptor-dependent transcription, and also has a crucial role in tumor necrosis factor-induced apoptosis. UXT gene expression has a role in tumorigenesis. UXT is ubiquitous expressed: it is expressed in prostate epithelial cells, overexpressed in a number of tumor tissues. The highest levels are found in the heart, skeletal muscle, pancreas, kidney, liver, adrenal gland, peripheral blood leukocytes, lymph node, prostate, and thyroid and the lowest levels in bladder and uterus.

    • Synonyms

      Protein UXT, Androgen receptor trapped clone 27 protein, ART-27, Ubiquitously expressed transcript protein, UXT, HSPC024, STAP1.

    • 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 MATPPKRRAV EATGEKVLRY ETFISDVLQR DLRKVLDHRD KVYEQLAKYL QLRNVIERLQ EAKHSELYMQ VDLGCNFFVD TVVPDTSRIY VALGYGFFLE LTLAEALKFI DRKSSLLTEL SNSLTKDSMN IKAHIHMLLE GLRELQGLQN FPEKPHH.

    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.

    Uxt Human
  • View Data Sheet

    Name :

    MANF Human, His

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant, His Tag

    Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    Product # :

    CYT-133

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    Description

    MANF Human Recombinant produced in E. coli is a single polypeptide chain containing 183 amino acids (25-182) and having a molecular mass of 20.8kDa.MANF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MANF solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    • 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 MGSHMLRPGD CEVCISYLGR FYQDLKDRDV TFSPATIENE LIKFCREARG KENRLCYYIG ATDDAATKII NEVSKPLAHH IPVEKICEKL KKKDSQICEL KYDKQIDLST VDLKKLRVKE LKKILDDWGE TCKGCAEKSD YIRKINELMP KYAPKAASAR TDL

    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.

    Manf Human
  • View Data Sheet

    Name :

    Resistin Human, His

    Description:

    Resistin Human 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-256

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    Description

    Resistin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing a 92 amino acids fragment (17-108) of the mature Human Resistin, having a total molecular mass of 14.23kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Resistin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Resistin protein solution is supplied in 20mM Tris-HCl pH 8.0, 5mM EDTA and 50% glycerol.

    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 which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
      Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
      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

      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.Please avoid freeze thaw cycles.

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

    Resistin Human His
  • View Data Sheet

    Name :

    DCN Human

    Description:

    Decorin Human Recombinant

    Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

    Product # :

    PRO-1583

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    Description

    DCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (31-359 a.a) and having a molecular mass of 38.6kDa.DCN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCN protein solution (0.25mg/ml) containing 20mM Tris pH 8.0 and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.

    • Synonyms

      Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

    • 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 MDEASGIGPE VPDDRDFEPS LGPVCPFRCQ CHLRVVQCSDLGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK VSPGAFTPLVKLERLYLSKN QLKELPEKMP KTLQELRAHE NEITKVRKVT FNGLNQMIVI ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD GNKISRVDAA SLKGLNNLAKLGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA EHKYIQVVYL HNNNISVVGSSDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK.

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    Dcn Human
  • View Data Sheet

    Name :

    NCF1 Human

    Description:

    Neutrophil Cytosolic Factor 1 Human Recombinant

    NCF1A, NOXO2, p47phox, SH3PXD1A .

    Product # :

    PRO-488

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    Description

    NCF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-390 a.a.) and having a molecular mass of 45.7 kDa. The NCF1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NCF1 is a cytosolic subunit protein of neutrophil NADPH oxidase which a
      Multi-component enzyme that is activates production of superoxide anion. NCF1, along with NCF2 and a membrane bound cytochrome b558, is necessary for activation of the latent NADPH oxidase necessary for superoxide production. Mutations in this NCF1 have been related with chronic granulomatous disease.

    • Synonyms

      NCF1A, NOXO2, p47phox, SH3PXD1A .

    • 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

      MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDDVTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV VEHHHHHH.

    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.

    Ncf1 Human
  • View Data Sheet

    Name :

    HSPBP1 Human

    Description:

    Heat Shock Protein-Binding Protein 1 Human Recombinant

    Hsp70-binding protein 1, Heat shock protein-binding protein 1, Hsp70-interacting protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 2, HspBP1, HspBP2, HSPBP1, HSPBP, FES1.

    Product # :

    HSP-030

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    Description

    HSPBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 382 amino acids (1-362 a.a.) and having a molecular mass of 41.6kDa. HSPBP1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HSPBP1 solution containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 30% glycerol, 2mM EDTA and 0.1M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hsp70-binding protein 1 (HSPBP1) is a member of a family of eukaryotic proteins identified as nucleotide exchange factors for HSP 70 that exhibit varying degrees of compartment and species specificity. HSPBP1 is localized mainly in cytoplasm and nucleus but is also found extracellularly. HSPBP1 is mostly expressed in heart and skeletal muscle .HSPBP1 binds to HSP 70, inhibits its activity and promotes dissociation of nucleotides from the HSP 70 ATPase domain. In addition, HSPBP1 inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and obstructing the ATP binding. HSPBP1 may also have a role in tumor (dys)regulation of chaperone proteins. Furthermore, HSPBP1 hinders ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.

    • Synonyms

      Hsp70-binding protein 1, Heat shock protein-binding protein 1, Hsp70-interacting protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 2, HspBP1, HspBP2, HSPBP1, HSPBP, FES1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      HSPBP1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR AMQQQVQKLK VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT CFSSPADDSM DR.

    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.

    Hspbp1 Human
  • View Data Sheet

    Name :

    ARMC10 Human

    Description:

    Armadillo Repeat Containing 10 Human Recombinant

    Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    Product # :

    PRO-1453

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    Description

    ARMC10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (28-308 a.a) and having a molecular mass of 33.6 kDa.ARMC10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARMC10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.

    • Synonyms

      Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    • 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 MGSTRGRRRG DRELGIRSSK SAEDLTDGSY DDVLNAEQLQ KLLYLLESTE DPVIIERALI TLGNNAAFSV NQAIIRELGG IPIVANKINH SNQSIKEKAL NALNNLSVNV ENQIKIKIYI SQVCEDVFSG PLNSAVQLAG LTLLTNMTVT NDHQHMLHSY ITDLFQVLLT GNGNTKVQVL KLLLNLSENP AMTEGLLRAQ VDSSFLSLYD SHVAKEILLR VLTLFQNIKN CLKIEGHLAV QPTFTEGSLF FLLHGEECAQ KIRALVDHHD AEVKEKVVTI IPKI.

    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.

    Armc10 Human
  • View Data Sheet

    Name :

    Bcl 2 Human (1-206 a.a.)

    Description:

    B-Cell Leukemia/Lymphoma 2, (1-206 a.a.) Human Recombinant

    Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    Product # :

    PRO-630

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    Description

    Bcl-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-206. The wild type Bcl-2 is missing 12 amino acids from C-terminus. C-terminus is fused to His-Tag. C-terminus his-tag, mimics the deleted C-terminus membrane domain thus maintaining its biological activity. Bcl-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 10mM Tris-HCl pH-8, 1mM EDTA and 250mM NaCl.

    Purity

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

    More Info

    • Introduction

      BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.

    • Synonyms

      Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bcl-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-2 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

      Suspend Bcl-2 in 100ul of 0.5M Acetic acid, over night at 4°C. Dilute 10 fold into selected buffer system. BCL-2 has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.

    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.

    Bcl2 Human 1 206 Aa
  • View Data Sheet

    Name :

    OSM Human, 195 a.a

    Description:

    Oncostatin-M Human Recombinant (195 a.a.)

    OSM, MGC20461, Oncostatin M.

    Product # :

    CYT-735

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    Description

    Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids and having a molecular mass of 22kDa. The OSM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 1xPBS pH-7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of human TF-1 cells is < 0.2ng/ml, corresponding to a specific activity of > 5.0x106 units/mg.

    More Info

    • Introduction

      Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

    • Synonyms

      OSM, MGC20461, Oncostatin M.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSR.

    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.

    Oncostatin M Human 195 Aa
  • View Data Sheet

    Name :

    THAP11 Human

    Description:

    THAP Domain Containing, Apoptosis Associated Protein 11 Human Recombinant

    THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.

    Product # :

    PRO-2009

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    Description

    THAP11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 36.8kDa.THAP11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The THAP11 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

      THAP Domain Containing, Apoptosis Associated Protein 11 (THAP11) is a part of the thanatos-associated protein family. THAP11 plays a role as a transcriptional repressor and interacts with HCF1 through a coiled coil domain. THAP11 which is localized to the nucleus and cytoplasm takes part in embryogenesis and pluripotency of embryonic stem cells by recruiting epigenetic modifiers.

    • Synonyms

      THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.

    • 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 MGSMPGFTCC VPGCYNNSHR DKALHFYTFP KDAELRRLWL KNVSRAGVSG CFSTFQPTTG HRLCSVHFQG GRKTYTVRVP TIFPLRGVNE RKVARRPAGA AAARRRQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQSSPSA STAQTAQLQP NLVSASAAVL LTLQATVDSS QAPGSVQPAP ITPTGEDVKP IDLTVQVEFA AAEGAAAAAA ASELQAATAG LEAAECPMGP QLVVVGEEGF PDTGSDHSYS LSSGTTEEEL LRKLNEQRDI LALMEVKMKE MKGSIRHLRL TEAKLREELR EKDRLLAMAV IRKKHGM.

    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.

    Thap11 Human
  • View Data Sheet

    Name :

    L Selectin Human

    Description:

    L-selectin Human Recombinant

    L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.

    Product # :

    PRO-381

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    Description

    L-Selectin Human Recombinant is expressed in E. coli containing 294 amino acids 39-332 fused to an amino terminal hexahistidine tag, having a total molecular weight of 37.55kDa.

    Source

    Escherichia Coli.

    Formulation

    L-Sel is supplied in 1x PBS and 50% Glycerol.

    Purity

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

    More Info

    • Introduction

      L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
      L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
      L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.

    • Synonyms

      L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.

    • Physical Appearance

      Sterile filtered colorless solution.

    • 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

      L-Selectin 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.

    L Selectin Human
  • View Data Sheet

    Name :

    HSA Protein

    Description:

    HSA Human Protein

    HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    Product # :

    PRO-354

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    Description

    HSA contains 584 amino acid residues derived from the prototypicalHSA sequence.

    Source

    Human Serum.

    Formulation

    0.2gr/ml solution containing no additives.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSA is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted HSA. HSA is a soluble, monomeric protein which comprises about one-half of the blood serum protein. HSA functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. HSA is a globular unglycosylated serum protein of molecular weight 65,000. The human HSA gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
      Suitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications.

    • Synonyms

      HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    • Physical Appearance

      Sterile Filtered clear yellowish solution.

    • Stability

      HSA although stable at room temperature for 2 weeks should be stored at 4°C.

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

    Human Serum Albumin
  • View Data Sheet

    Name :

    HBZ Human

    Description:

    Hemoglobin-Zeta Human Recombinant

    Zeta-globin, HBAZ, HBZ2, Hemoglobin subunit zeta, Hemoglobin zeta chain, HBZ.

    Product # :

    PRO-803

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    Description

    HBZ Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 150 amino acids (1-142 a.a.) and having a molecular mass of 16.7 kDa. The HBZ is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HBZ solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hemoglobin subunit zeta (HBZ) is part of the globin family. Hemoglobin Zeta is alpha-like hemoglobin. The HBZ polypeptide is synthesized in the yolk sac of the early embryo, while alpha-globin is produced throughout fetal and adult life.

    • Synonyms

      Zeta-globin, HBAZ, HBZ2, Hemoglobin subunit zeta, Hemoglobin zeta chain, HBZ.

    • Physical Appearance

      Sterile Filtered clear 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

      MSLTKTERTI IVSMWAKIST QADTIGTETL ERLFLSHPQT KTYFPHFDLH PGSAQLRAHG SKVVAAVGDA VKSIDDIGGA LSKLSELHAY ILRVDPVNFK LLSHCLLVTL AARFPADFTA EAHAAWDKFL SVVSSVLTEK YRLEHHHHHH.

    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.

    Hbz Human
  • View Data Sheet

    Name :

    SIRPG Human

    Description:

    Signal-Regulatory Protein Gamma Human Recombinant

    signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.

    Product # :

    PRO-2013

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    Description

    SIRPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (29-360 a.a.) and having a molecular mass of 39.1kDa.SIRPG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Signal-Regulatory Protein Gamma (SIRPG) belongs to the signal-regulatory protein (SIRP) family whose members are receptor-type transmembrane glycoproteins which negatively regulate the receptor tyrosine kinase-coupled signaling processes. SIRPG is also a part of the immunoglobulin superfamily.

    • Synonyms

      signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.

    • 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 MGSEEELQMI QPEKLLLVTV GKTATLHCTV TSLLPVGPVL WFRGVGPGRE LIYNQKEGHF PRVTTVSDLT KRNNMDFSIR ISSITPADVG TYYCVKFRKG SPENVEFKSG PGTEMALGAK PSAPVVLGPA ARTTPEHTVS FTCESHGFSP RDITLKWFKN GNELSDFQTN VDPTGQSVAY SIRSTARVVL DPWDVRSQVI CEVAHVTLQG DPLRGTANLS EAIRVPPTLE VTQQPMRVGN QVNVTCQVRK FYPQSLQLTW SENGNVCQRE TASTLTENKD GTYNWTSWFL VNISDQRDDV VLTCQVKHDG QLAVSKRLAL EVTVHQKDQS SDATP.

    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.

    Sirpg Human
  • View Data Sheet

    Name :

    IHH Human

    Description:

    Indian Hedgehog Human Recombinant

    Indian hedgehog protein, IHH, HHG-2, BDA1.

    Product # :

    CYT-195

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    Description

    IHH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.

    More Info

    • Introduction

      IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.

    • Synonyms

      Indian hedgehog protein, IHH, HHG-2, BDA1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.

    • Background

      What is the molecular weight/Mw of IHH HUMAN Protein?
      IHH HUMAN Protein has a total Mw of 19.8kDa.

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

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

      What is the Biological Activity of IHH HUMAN Protein?
      Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.

      What is the amino acid sequence of IHH HUMAN Protein?
      IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.

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

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

    Ihh Human
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