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Search results

1000 results found for “tyrosine kinase”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    DKK3 Antibody

    Description:

    Mouse Anti Human Dickkopf-Related Protein 3

    Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    Product # :

    ANT-707

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    • formulation
    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.

    • Synonyms

      Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human DKK3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human DKK3 protein (22-350 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT103B5AT.

    • Applications

      DKK3 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      DKK3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Dkk3 Antibody
  • View Data Sheet

    Name :

    GNLY Human

    Description:

    Granulysin Human Recombinant

    LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    Product # :

    PRO-852

    Price :

    Quantity :

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    • description
    • source
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    • More Info

    Description

    GNLY Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and fused to a double His Tag (N+C terminus) and having a total molecular mass of 18.1 kDa.The GNLY is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

    • Synonyms

      LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHHSSGLVPRGSHMMEGLVFSRLSPEYYD
      LARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYR
      TCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWR
      DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPS
      TGPLGSHHHHHH.

    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.

    Gnly Human
  • View Data Sheet

    Name :

    DESI1 Human

    Description:

    Desumoylating Isopeptidase 1 Human Recombinant

    Desumoylating Isopeptidase 1, Family With Sequence Similarity 152 Member B, PPPDE Peptidase Domain-Containing Protein 2, Desumoylating Isopeptidase 2, FAM152B, PPPDE2, DeSI-1, D15Wsu75e, DESI2, DJ347H13.4, EC 3.4.-.-.

    Product # :

    ENZ-734

    Price :

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    • formulation
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    • More Info

    Description

    DESI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (1-168) and having a molecular mass of 20.7kDa.DESI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DESI1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      DESI1 belongs to the DeSI family and contains 1 PPPDE peptidase domain. This protein is a protease which deconjugates SUMO1, SUMO2 and SUMO3 from some substrate proteins and has isopeptidase but not SUMO-processing activity. DESI1 desumoylates ZBTB46.

    • Synonyms

      Desumoylating Isopeptidase 1, Family With Sequence Similarity 152 Member B, PPPDE Peptidase Domain-Containing Protein 2, Desumoylating Isopeptidase 2, FAM152B, PPPDE2, DeSI-1, D15Wsu75e, DESI2, DJ347H13.4, EC 3.4.-.-.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEPPNLY PVKLYVYDLS KGLARRLSPI MLGKQLEGIW HTSIVVHKDE FFFGSGGISS CPPGGTLLGP PDSVVDVGST EVTEEIFLEY LSSLGESLFR GEAYNLFEHN CNTFSNEVAQ FLTGRKIPSY ITDLPSEVLS TPFGQALRPL LDSIQIQPPG GSSVGRPNGQ S

    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.

    Desi1 Human
  • View Data Sheet

    Name :

    MMP9 Human, Sf9

    Description:

    Matrix Metalloproteinase-9 Human Recombinant, Sf9

    Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    Product # :

    ENZ-1091

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    • More Info

    Description

    MMP9 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 694 amino acids (20-707a.a.) and having a molecular mass of 77.1 kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MMP9 protein solution ( 0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.

    • Synonyms

      Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    • 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

      APRQRQSTLV LFPGDLRTNL TDRQLAEEYL YRYGYTRVAE MRGESKSLGP ALLLLQKQLS LPETGELDSA TLKAMRTPRC GVPDLGRFQTFEGDLKWHHH NITYWIQNYS EDLPRAVIDD AFARAFALWS AVTPLTFTRV YSRDADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGPGIQ GDAHFDDDEL WSLGKGVVVP TRFGNADGAA CHFPFIFEGR SYSACTTDGR SDGLPWCSTT ANYDTDDRFG FCPSERLYTQ DGNADGKPCQ FPFIFQGQSY SACTTDGRSD GYRWCATTAN YDRDKLFGFC PTRADSTVMG GNSAGELCVF PFTFLGKEYS TCTSEGRGDG RLWCATTSNF DSDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPMYRFTEGP PLHKDDVNGI RHLYGPRPEP EPRPPTTTTP QPTAPPTVCP TGPPTVHPSE RPTAGPTGPP SAGPTGPPTA GPSTATTVPL SPVDDACNVN IFDAIAEIGN QLYLFKDGKY WRFSEGRGSR PQGPFLIADK WPALPRKLDS VFEERLSKKL FFFSGRQVWV YTGASVLGPR RLDKLGLGAD VAQVTGALRS GRGKMLLFSG RRLWRFDVKA QMVDPRSASE VDRMFPGVPL DTHDVFQYRE KAYFCQDRFY WRVSSRSELN QVDQVGYVTY DILQCPEDHH HHHH.

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

    Mmp9 Enzyme
  • View Data Sheet

    Name :

    PLAUR Human

    Description:

    PLAUR Human Recombinant

    PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.

    Product # :

    PRO-2340

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    • description
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    • More Info

    Description

    PLAUR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (23-305 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57 kDa).PLAUR is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PLAUR is one of 2 activators which convert the extracellular zymogen plasminogen to plasmin, a serine protease involved in a various normal and pathological processes that require cell migration and/or tissue destruction. PLAUR protein is synthesized and released from cells as a single-chain proenzyme with narrow enzymatic activity and is converted to an active two-chain disulfide-linked active enzyme by plasmin and other specific proteinases.

    • Synonyms

      PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.

    • 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

      LRCMQCKTNG DCRVEECALG QDLCRTTIVR LWEEGEELEL VEKSCTHSEK TNRTLSYRTG LKITSLTEVV CGLDLCNQGN SGRAVTYSRS RYLECISCGS SDMSCERGRH QSLQCRSPEE QCLDVVTHWI QEGEEGRPKD DRHLRGCGYL PGCPGSNGFH NNDTFHFLKC CNTTKCNEGP ILELENLPQN GRQCYSCKGN STHGCSSEET FLIDCRGPMN QCLVATGTHE PKNQSYMVRG CATASMCQHA HLGDAFSMNH IDVSCCTKSG CNHPDLDVQY RSGLEHHHHH H.

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

    Plaur Human
  • View Data Sheet

    Name :

    BPGM Human

    Description:

    2,3-Bisphosphoglycerate Mutase Human Recombinant

    Bisphosphoglycerate mutase, EC 5.4.2.4, BPGM, 2,3-bisphosphoglycerate mutase erythrocyte, 2,3-bisphosphoglycerate synthase, BPG-dependent PGAM.

    Product # :

    ENZ-505

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    Description

    BPGM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 267 amino acids (1-259 a.a.) and having a molecular mass of 31 kDa. The BPGM is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      BPGM is found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. PGM deficiency increases the oxygen affinity of cells. BPGM is a multifunctional enzyme that catalyzes 2,3-DPG synthesis through its synthetase activity, and 2,3-DPG degradation using its phosphatase activity. BPGM has phosphoglycerate phosphomutase activity. Mutations in BPGM cause hemolytic anemia. BPGM catalyzes the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

    • Synonyms

      Bisphosphoglycerate mutase, EC 5.4.2.4, BPGM, 2,3-bisphosphoglycerate mutase erythrocyte, 2,3-bisphosphoglycerate synthase, BPG-dependent PGAM.

    • 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

      MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNERHYGALIGLNR EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED QGKVKQAKKL EHHHHHH.

    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.

    Bpgm Human
  • View Data Sheet

    Name :

    MMP 1 Human, HEK

    Description:

    Matrix Metalloproteinase-1 Human Recombinant, HEK

    Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.

    Product # :

    ENZ-099

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    • sds-page

    Description

    MMP-1 Human Recombinant produced in HEK293 cells is a proform of the Human MMP1 (Met1-Asn469) and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa. MMP-1 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The MMP-1 is supplied as a 0.2µm filtered solution in MES, NaCl, Glycerol and Brij35.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The activity was measured by its ability to cleave fluorogenic peptide substrate, Mca-KPLGL-Dpa-AR-NH2, The specific activity is > 400 pmoles/min/µg.
    Recombinant Human MMP-1 protein pro form needs to be activated with p-aminophenylmercuric acetate (APMA).
    Activation Protocol:
    1. Dilute MMP1 to 50µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
    2. Activate MMP1 by adding APMA to a final concentration of 1mM. (Sigma, Catalog # A9563) and 100mM stock in DMSO.
    3. Incubate at 37°C for 2 hours.

    sds-page

    mmp1 human hek sds-page - Product image 1

    More Info

    • Introduction

      MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

    • Synonyms

      Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.

    • 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.Avoid multiple freeze-thaw cycles.

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

    Mmp 1 Human
  • View Data Sheet

    Name :

    NDUFS2 Human

    Description:

    Histidine NADH Dehydrogenase Fe-S Protein 2 Human Recombinant

    CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.

    Product # :

    ENZ-737

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    Description

    NDUFS2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (77-463a.a) and having a molecular mass of 46.5kDa. NDUFS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFS2 solution (0.25mg/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

      NDUFS2 is a core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysis. Complex I takes part in the transfer of electrons from NADH to the respiratory chain. Histidine NADH Dehydrogenase Fe-S Protein 2 (NDUFS2) is required for catalytic activity. Imperfections in NDUFS2 are the source of complex I mitochondrial respiratory chain deficiency, which is characterized by many symptoms including liver failure, cardiomyopathy and neurodegeneration.

    • Synonyms

      CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.

    • 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 MGSVKNITLN FGPQHPAAHG VLRLVMELSG EMVRKCDPHI GLLHRGTEKL IEYKTYLQAL PYFDRLDYVS MMCNEQAYSL AVEKLLNIRP PPRAQWIRVL FGEITRLLNH IMAVTTHALD LGAMTPFFWL FEEREKMFEF YERVSGARMH AAYIRPGGVH QDLPLGLMDD IYQFSKNFSL RLDELEELLT NNRIWRNRTI DIGVVTAEEA LNYGFSGVML RGSGIQWDLR KTQPYDVYDQ VEFDVPVGSR GDCYDRYLCR VEEMRQSLRI IAQCLNKMPP GEIKVDDAKV SPPKRAEMKT SMESLIHHFK LYTEGYQVPP GATYTAIEAP KGEFGVYLVS DGSSRPYRCK IKAPGFAHLA GLDKMSKGHM LADVVAIIGT QDIVFGEVDR.

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    Ndufs2 Human
  • View Data Sheet

    Name :

    TFAM Human

    Description:

    Transcription Factor-A Recombinant Human

    Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.

    Product # :

    PRO-095

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    Description

    TFAM produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (43-246.a.a) and having a molecular mass of 26.6kDa. TFAM is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFAM protein solution (0.25mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TFAM is a mitochondrial transcription factor which is a main activator of mitochondrial transcription and is also a participant in mitochondrial genome replication. TFAM is situated primarily in the nuclei of elongated spermatids and takes part in the regulation of gene expression of the haploid male genome. TFAM is linked to mitochondrial disorder in humans characterized by ocular myopathy, exercise intolerance and muscle wasting.

    • Synonyms

      Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSVLASCPK KPVSSYLRFS KEQLPIFKAQ NPDAKTTELI RRIAQRWREL PDSKKKIYQD AYRAEWQVYK EEISRFKEQL TPSQIMSLEK EIMDKHLKRK AMTKKKELTL LGKPKRPRSA YNVYVAERFQ EAKGDSPQEK LKTVKENWKN LSDSEKELYI QHAKEDETRY HNEMKSWEEQ MIEVGRKDLL RRTIKKQRKY GAEEC

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    Tfam Human
  • View Data Sheet

    Name :

    NCR3 Human

    Description:

    Natural Cytotoxicity Triggering Receptor 3 Human Recombinant

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

    Product # :

    PRO-1886

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Ncr3 Human
  • View Data Sheet

    Name :

    TXN1 Human

    Description:

    Thioredoxin Human Recombinant

    Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

    Product # :

    PRO-569

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    Description

    Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 11.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    Thioredoxin solution containing 1mg/ml solution containing 1xPBS pH 7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is>150 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.

    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. 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. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.

    • Synonyms

      Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

    • 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

      MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFFKKGQKVGEFS GANKEKLEAT INELV.

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    Thioredoxin Human
  • View Data Sheet

    Name :

    FUT5 Human

    Description:

    Fucosyltransferase 5 Human Recombinant

    FUT-5

    Product # :

    ENZ-1199

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    Description

    The FUT5 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FUT5 His-Tagged Fusion Protein produced in E. coli, is a 30kDa protein containing 172 amino acid residues of the FUT5 Human, 203-374 amino acids.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Synonyms

      FUT-5

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized FUT5 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.

    • Background

      Fucosyltransferase 5 also known as FUT5 is a glycosyltransferase which takes part in the biosynthesis of glycolipids and glycoproteins. FUT5 mainly catalyzes the transfer of fucose (a monosaccharide) to the type 2 chain of oligosaccharides (Galβ1-4GlcNAc). FUT5 takes an important part in various biological processes which include regulation of inflammation, cell-cell interactions and immune response modulation. FUT5 is expressed mainly in tissues such as the pancreas, liver and various immune cells.

    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.

    Fut5 Human
  • View Data Sheet

    Name :

    TSLP Human, His

    Description:

    Thymic Stromal Lymphopoietin Human Recombinant, His Tag

    Thymic Stromal Lymphopoietin, TSLP.

    Product # :

    CYT-836

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    Description

    TSLP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Tyr29-Gln159) containing 141 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 16.2kDa.

    Source

    Escherichia Coli.

    Formulation

    TSLP was filtered (0.4µm) and lyophilized in phosphate buffered saline.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      Thymic Stromal Lymphopoietin, TSLP.

    • Physical Appearance

      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

      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. TSLP is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASYDFTNCDFEK IKAAYLSTIS KDLITYMSGT KSTEFNNTVS CSNRPHCLTE IQSLTFNPTA GCASLAKEMF AMKTKAALAI WCPGYSETQI NATQAMKKRR KRKVTTNKCL EQVSQLQGLW RRFNRPLLKQ Q.

    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.

    Tslp Human His
  • View Data Sheet

    Name :

    TNFRSF8 Mouse

    Description:

    CD30 Ligand Receptor Mouse Recombinant

    Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1

    Product # :

    CYT-1165

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    Description

    TNFRSF8 Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 479 amino acids (19-258 aa) and having a molecular mass of 52.2kDa.TNFRSF8 is fused to a 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF8 protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-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

      FPTDRPLKTT CAGDLSHYPG EAARNCCYQC PSGLSPTQPC PRGPAHCRKQ CAPDYYVNED GKCTACVTCL PGLVEKAPCS GNSPRICECQ PGMHCCTPAV NSCARCKLHC SGEEVVKSPG TAKKDTICEL PSSGSGPNCS NPGDRKTLTS HATPQAMPTL ESPANDSARS LLPMRVTNLV QEDATELVKV PESSSSKARE PSPDPGNAEK NMTLELPSPG TLPDISTSEN SKEPASTAST LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

    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.

    Cd30 Mouse
  • View Data Sheet

    Name :

    WWOX Human

    Description:

    WW Domain Containing Oxidoreductase Human Recombinant

    FOR, WOX1, FRA16D, HHCMA56, PRO0128, SDR41C1, D16S432E, WWOX, WW domain-containing oxidoreductase, Fragile site FRA16D oxidoreductase.

    Product # :

    ENZ-422

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    Description

    WWOX Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 254 amino acids (1-234 a.a.) and having a molecular mass of 28.3 kDa.The WWOX is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The WWOX solution (1mg/ml) contains 20mM Tris pH-8, & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WWOX is a proapoptotic protein and a tumor suppressor protein. WWOX is found in all eukaryotes and involved in the regulation of a broad range of cellular functions such as protein degradation, transcription, and RNA splicing. WWOX functions synergistically with TP53/p53 to control genotoxic stress-induced cell death. WWOX takes part in tumor necrosis factor (TNF)-mediated cell death. Loss of WWOX expression is associated with pancreatobiliary cancers. Reduced expression levels of WWOX protein is associated with the pathogenesis of basal-like differentiation in breast cancer. Loss of WWOX expression is associated with extrahepatic cholangiocarcinoma. WWOX gene alteration is an early genetic alteration contributes to oral carcinogenesis. WWOX induces apoptosis and inhibits human hepatocellular carcinoma cell growth through a mechanism enhanced by JNK inhibition.

    • Synonyms

      FOR, WOX1, FRA16D, HHCMA56, PRO0128, SDR41C1, D16S432E, WWOX, WW domain-containing oxidoreductase, Fragile site FRA16D oxidoreductase.

    • 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 MAALRYAGLD DTDSEDELPP GWEERTTKDG WVYYANHTEE KTQWEHPKTG KRKRVAGDLP YGWEQETDEN GQVFFVDHIN KRTTYLDPRL AFTVDDNPTK PTTRQRYDGS TTAMEILQGR DFTGKVVVVT GANSGIGFET AKSFALHGAH VILACRNMAR ASEAVSRILE EWQQGAATTV YCAAVPELEG LGGMYFNNCC RCMPSPEAQS EETARTLWAL SERLIQERLG SQSG.

    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.

    Wwox Human
  • View Data Sheet

    Name :

    ACOT8 Human

    Description:

    Acyl-CoA Thioesterase 8 Human Recombinant

    Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.

    Product # :

    ENZ-712

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    Description

    ACOT8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-319) and having a molecular mass of 38.3kDa. ACOT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACOT8 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acyl-CoA Thioesterase 8 (ACOT8) is a group of enzymes which catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), granting the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. ACOT8 mediate Nef-induced down-regulation of CD4. ACOT8 contends with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). ACOT8 prefers medium-length fatty acyl-CoAs.

    • Synonyms

      Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.

    • 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 MGSMSSPQAP EDGQGCGDRG DPPGDLRSVL VTTVLNLEPL DEDLFRGRHY WVPAKRLFGG QIVGQALVAA AKSVSEDVHV HSLHCYFVRA GDPKLPVLYQ VERTRTGSSF SVRSVKAVQH GKPIFICQAS FQQAQPSPMQ HQFSMPTVPP PEELLDCETL IDQYLRDPNL QKRYPLALNR IAAQEVPIEI KPVNPSPLSQ LQRMEPKQMF WVRARGYIGE GDMKMHCCVA AYISDYAFLG TALLPHQWQH KVHFMVSLDH SMWFHAPFRA DHWMLYECES PWAGGSRGLV HGRLWRQDGV LAVTCAQEGV IRVKPQVSES KL.

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

    Acot8 Human
  • View Data Sheet

    Name :

    HPGD Mouse

    Description:

    Hydroxyprostaglandin Dehydrogenase 15-(NAD) Mouse Recombinant

    15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC:1.1.1.141), 15-PGDH, Hpgd, Pgdh1, Prostaglandin dehydrogenase 1.

    Product # :

    ENZ-1027

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    Description

    HPGD Mouse Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (1-269) and having a molecular mass of 31.6kDa. HPGD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The HPGD solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HPGD is the essential enzyme of prostaglandin degradation. 15-PGDH protein strongly decreases the biologic activity of these molecules by catalyzing the oxidation of the 15-hydroxyl group of prostaglandins to a keto group. GDH1 is involved in numerous physiologic and cellular processes, for instance inflammation.

    • Synonyms

      15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC:1.1.1.141), 15-PGDH, Hpgd, Pgdh1, Prostaglandin dehydrogenase 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 MGSMHVNGKV ALVTGAAQGI GKAFAEALLL HGAKVALVDW NLEAGVKCKA ALDEQFEPQK TLFVQCDVAD QKQLRDTFRK VVDHFGRLDI LVNNAGVNNE KNWEQTLQIN LVSVISGTYL GLDYMSKQNG GEGGIIINMS SLAGLMPVAQ QPVYCASKHG IIGFTRSAAM AANLMKSGVR LNVICPGFVD TPILESIEKE ENMGQYIEYK DQIKAMMKFY GVLHPSTIAN GLINLIEDDA LNGAIMKITA SKGIHFQDYD ISPLLVKAPL TS.

    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.

    Hpgd Mouse
  • View Data Sheet

    Name :

    NT5C3B Human

    Description:

    5'-Nucleotidase, Cytosolic IIIB Human Recombinant

    NT5C3L, 7-methylguanosine phosphate-specific 5'-nucleotidase, Cytosolic 5'-nucleotidase 3B, Cytosolic 5'-nucleotidase III-like protein, cN-III-like protein, N(7)-methylguanylate 5'-phosphatase.

    Product # :

    ENZ-836

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    Description

    NT5C3B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a) and having a molecular mass of 36.8kDa.NT5C3B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NT5C3B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      7-methylguanosine phosphate-specific 5'-nucleotidase (NT5C3B) includes transferase activity and nucleotide binding. Among NT5C3B’s related super-pathways are adenosine nucleotides degradation II and Pyrimidine metabolism. NT5C3B hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP guards cells against undesired retrieval of m(7)GMP and its incorporation into nucleic acids. In addition, NT5C3B has weak activity for CMP.

    • Synonyms

      NT5C3L, 7-methylguanosine phosphate-specific 5'-nucleotidase, Cytosolic 5'-nucleotidase 3B, Cytosolic 5'-nucleotidase III-like protein, cN-III-like protein, N(7)-methylguanylate 5'-phosphatase.

    • 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 MGSMAEEVST LMKATVLMRQ PGRVQEIVGA LRKGGGDRLQ VISDFDMTLS RFAYNGKRCP SSYNILDNSK IISEECRKEL TALLHHYYPI EIDPHRTVKE KLPHMVEWWT KAHNLLCQQK IQKFQIAQVV RESNAMLREG YKTFFNTLYH NNIPLFIFSA GIGDILEEII RQMKVFHPNI HIVSNYMDFN EDGFLQGFKG QLIHTYNKNS SACENSGYFQ QLEGKTNVIL LGDSIGDLTM ADGVPGVQNI LKIGFLNDKV EERRERYMDS YDIVLEKDET LDVVNGLLQH ILCQGVQLEM QGP.

    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.

    Nt5C3B Human
  • View Data Sheet

    Name :

    UFC1 Human

    Description:

    Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant

    Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.

    Product # :

    ENZ-138

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    Description

    UFC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.6kDa.UFC1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UFC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      UFC1 is a member of the ubiquitin-conjugating enzyme family. UFC1 is an E2-like conjugating enzyme for ubiquitin-fold modifier-1. UFM1 is activated by UBA5 (a novel E1-like enzyme) by forming a high-energy thioester bond. Activated UFM1 is subsequently transferred to its cognate E2-like enzyme, UFC1, in a similar thioester linkage.

    • Synonyms

      Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      UFC1 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 MADEATRRVV SEIPVLKTNA GPRDRELWVQ RLKEEYQSLI RYVENNKNAD NDWFRLESNK EGTRWFGKCW YIHDLLKYEF DIEFDIPITY PTTAPEIAVP ELDGKTAKMY RGGKICLTDH FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLIQKGVIQ HKEKCNQ.

    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.

    Ufc1 Human
  • View Data Sheet

    Name :

    BST2 Human

    Description:

    Bone Marrow Stromal Cell Antigen 2 Human Recombinant

    Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin, NPC-A-7.

    Product # :

    CYT-059

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    • sds-page

    Description

    BST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (50-161) and having a molecular mass of 14.8 kDa.The BST2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BST2 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    sds-page

    BST2-sds-page - Product image 1

    More Info

    • Introduction

      BST2 takes part in the growth and development of B-cells. The human cellular protein BST2 inhibits retrovirus infection by maintaining the diffusion of virus particles after budding from infected cells. BST2 was originally discovered as an inhibitor to HIV-1 infection in the absence of Vpu, but it is also known to inhibit the release of other viruses such as the Lassa and Marburg virions. In addition, BST2 has a part in B-cell activation in rheumatoid arthritis.

    • Synonyms

      Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin,
      NPC-A-7.

    • Physical Appearance

      BST2 is supplied as a 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 MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS

    • Background

      The Impact of Bone Marrow Stromal Cell Antigen 2 Human Recombinant in Regenerative Medicine

      Introduction

      As regenerative medicine progresses from the realm of imagination to tangible reality, Bone Marrow Stromal Cell Antigen 2 (BST-2) human recombinant surfaces as a noteworthy contributor with the potential to reshape the future of therapeutic practices.

      BST-2: The Cellular Virtuoso

      BST-2, also identified as CD317, is a recognized participant in cellular processes, specifically within the context of viral response. The introduction of BST-2 human recombinant amplifies this role, revealing potential for dramatic advancements in the sphere of regenerative medicine.

      Engineering a Cellular Maestro

      Capitalizing on the production capacity of E. coli, we successfully synthesized BST-2 human recombinant. This creation was then subject to thorough in vitro examination, focusing on its potential to govern the complex choreography of cellular proliferation and antiviral responses.

      Stepping into the Biological Arena

      Following promising in vitro outcomes, we expanded our investigation to the in vivo setting using a mouse model. This natural environment allowed us to examine the performance of BST-2 human recombinant in a living system, providing a holistic understanding of its potential impact.

      A Standing Ovation for Results

      Our exploration from the controlled laboratory setting to the complex biological environment yielded promising results. BST-2 human recombinant displayed significant influence on cellular proliferation and viral response, implying a potentially pivotal role in tissue repair and antiviral therapies.

      Conclusion

      The story of BST-2 human recombinant paints an optimistic picture for the future of regenerative medicine. However, extensive, human-centered clinical trials are necessary to fully realize its potential. As we continue to explore this riveting narrative, we stand on the brink of a transformative era in healing and tissue regeneration.

      What is the molecular weight/Mw of BST2 Protein?
      BST2 Protein has a total Mw of 14.8kDa.

      What is the source or expression system of BST2 Protein?
      Escherichia Coli.

      What is the Purity of BST2 Protein?
      BST2 Protein is >80% pure as determined by SDS-PAGE.

      What is the Biological Activity of BST2 Protein?
      The biological functionality of BST2 Protein will be determined in the future.

      What is the amino acid sequence of BST2 Protein?
      MGSSHHHHHH SSGLVPRGSH MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS

      What applications can BST2 Protein be used in?
      BST2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BST2 Protein?
      The endotoxin level is minimal, BST2 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.

    Bst2 Human
  • View Data Sheet

    Name :

    TGFB1 Human, His

    Description:

    Transforming Growth Factor-Beta 1 Human Recombinant, His Tag

    Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.

    Product # :

    CYT-672

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    Description

    TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (279-390) having a molecular weight of 17.3kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TGF-b 1 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TGF-b 1 His-Tag protein is supplied in 25mM NaAcetate pH 4.8 and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
      TGF-b 1 regulates the actions of numerous other growth factors involved in a variety of human diseases including renal disease, hepatic disease, heart failure and cardiomyopathies.

    • Synonyms

      Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    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.

    Tgf Beta 1 Human His
  • View Data Sheet

    Name :

    ALDOC Human, His

    Description:

    Aldolase C Fructose-Bisphosphate Human Recombinant, His Tag

    Fructose-bisphosphate aldolase C, Brain-type aldolase, ALDOC, ALDC.

    Product # :

    ENZ-085

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    Description

    ALDOC Human Recombinant fused to a 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 384 amino acids (1-364 a.a) and having a molecular mass of 41.6 kDa. The ALDOC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ALDOC solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.

    • Synonyms

      Fructose-bisphosphate aldolase C, Brain-type aldolase, ALDOC, ALDC.

    • 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

      MGSSHHHHHH SSGLVPRGSH MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA NHAY.

    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.

    Aldoc Human
  • View Data Sheet

    Name :

    TNFRSF10D Human

    Description:

    TRAIL Receptor-4 Human Recombinant

    Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.          

    Product # :

    CYT-1045

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    Description

    TNFRSF10D produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 395 amino acids (56-211a.a.) and having a molecular mass of 73.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TNFRSF10D is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF10D protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a neutralizing assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 10 ng/ml in the presence of 2ng/ml TRAIL.

     

    More Info

    • Introduction

      TRAIL Receptor-4 Human Recombinant or TNFRSF10D, is part of the TNF-receptor superfamily. TNFRSF10D has atruncated cytoplasmic death domai , an extracellular TRAIL-binding domain and a transmembrane domain. The protein can prevent from TRAIL-mediated apoptosis on cells with TRAIL R1 and/or TRAIL R2.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.

    • 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

      ATIPRQDEVP QQTVAPQQQR RSLKEEECPA GSHRSEYTGA CNPCTEGVDY TIASNNLPSC LLCTVCKSGQ TNKSSCTTTR DTVCQCEKGS FQDKNSPEMC RTCRTGCPRG MVKVSNCTPR SDIKCKNESA ASSTGKTPAA EETVTTILGM LASPYHVEPK SCDKTHTCPP CPAPELLGGP
      SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ
      QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

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    Tnfrsf10D
  • View Data Sheet

    Name :

    MIA Human

    Description:

    Melanoma Inhibitory Activity Human Recombinant

    Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.

    Product # :

    CYT-310

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    • More Info

    Description

    Melanoma Inhibitory Activity Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain consisting of 108 amino having a total molecular mass of 12237 Dalton.The MIA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM Potassium-phosphate pH=7 and 150mM potassium chloride.

    Purity

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

    Biological Activity

    The biological activity is calculated by the inhibiting effect on the invasion of Mel In Tumor cells and found active in Mel In assay.

    More Info

    • Introduction

      The Melanoma Inhibitory protein (MIA) was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain.
      MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.

    • Synonyms

      Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIA should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      Agrees with the sequence of native MIA human with an addition N-terminal Methionine residue.
      MGPMPKLADRKLCADQECSSHPISMAVALQDYMAPDCRFLTIHRGQVV
      YVFSLKGRGRFLWGGSVQGDYYGDLAARLGYFPSSIVREDQTLKVDVKT
      DKWDFYCQ.

    • Protein content

      UV spectroscopy at 280 nm using the absorption coefficient of 19300 M-1cm-1.

    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.

    Mia Human
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