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Search results

1000 results found for “gluteradoxin”

Name

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  • View Data Sheet

    Name :

    Rhodanese Human

    Description:

    Thiosulfate Sulfurtransferase Human Recombinant

    EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.

    Product # :

    ENZ-459

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    Description

    Recombinant Human Rhodanese produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a) and having a molecular mass of 35.6 kDa. Rhodanese is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Rhodanese protein solution contains 20mM Tris-HCl, pH-8 and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Rhodanese is a mitochondrial matrix enzyme that is encoded by the nucleus. Rhodanese is involved in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes. Rhodanese catalyzes the chemical reaction of thiosulfate & cyanide to sulfite & thiocyanate (detoxification). Rhodanese is part of the transferase family of proteins. Rhodanese includes two highly conservative domains, identified as rhodanese homology domains. In mammals, the majority of cyanide is converted to thiocyanate. Rhodanese has weak mercaptopyruvate sulfurtransferase activity.

    • Synonyms

      EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.

    • 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 MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE RHVPGASFFD IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD GEHLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLDRS LLKTYEQVLE NLESKRFQLV DSRSQGRFLG TEPEPDAVGL DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL SQPLIATCRK GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA.

    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.

    Rhodanese Human
  • View Data Sheet

    Name :

    SORD Human, His

    Description:

    Sorbitol Dehydrogenase Human Recombinant, His Tag

    EC 1.1.1.14, SORD1,SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase.

    Product # :

    ENZ-520

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    Description

    SORD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 377 amino acids (1-357 a.a.) and having a molecular mass of 40.4 kDa. SORD protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SORD protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl pH-8, 0.2M NaCl, 5mM DTT & 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 0.2 units/mg, in which one unit will convert 1.0 umole of D-fructose to D-sorbitol per minute at pH 7.5 at 25°C.

    Citations

    More Info

    • Introduction

      SORD enzyme is part of of the zinc-containing alcohol dehydrogenase family that is broadly expressed in kidney and in the lens eye. SORD enzymatically catalyzes the zinc-dependent interconversion of polyols, such as sorbitol and xylitol, to their respective ketoses.

    • Synonyms

      EC 1.1.1.14, SORD1,SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase.

    • 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 MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP.

    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.

    Sord Human
  • View Data Sheet

    Name :

    GAPDH Antibody

    Description:

    Glyceraldehyde-3-Phosphate Dehydrogenase, Mouse Anti Human

    G3PD, GAPD, MGC88685, GAPDH, Glyceraldehyde-3-Phosphate Dehydrogenase.

    Product # :

    ANT-005

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    Citations

    More Info

    • Introduction

      GAPDH is a catalytic enzyme normally known to play a role in glycolysis. GAPDH exists as a tetramer composed of 36-kDa subunits and has a range of intracellular functions. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Besides functioning as a glycolytic enzyme in cytoplasm, GAPDH has function in intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and DNA repair. GAPDH catalyzes a vital energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains.

    • Synonyms

      G3PD, GAPD, MGC88685, GAPDH, Glyceraldehyde-3-Phosphate Dehydrogenase.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human GAPDH mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GAPDH amino acids 1-335 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT8G4AT.

    • Applications

      GAPDH antibody has been tested by ELISA, Western blot and Immunofluorescence analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis and Immunofluorescence is 1:500 ~ 10,000.
      Recommended starting dilution is 1:1,000.

    • 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

      GAPDH antibody was purified from mouse ascitic fluids by protein-G 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.

    Gapdh Antibody
  • View Data Sheet

    Name :

    CXCL7 95 a.a Human

    Description:

    Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-277

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    Description

    NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      NAP 2 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

      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

    • Background

      What is the molecular weight/Mw of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CXCL7 95 A.A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL7 95 A.A HUMAN Protein?
      The biological functionality of CXCL7 95 A.A HUMAN Protein will be determined in the future.

      What is the amino acid sequence of CXCL7 95 A.A HUMAN Protein?
      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

      What applications can CXCL7 95 A.A HUMAN Protein be used in?
      CXCL7 95 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL7 95 A.A HUMAN Protein?
      The endotoxin level is minimal, CXCL7 95 A.A HUMAN Protein was purified using conventional chromatography techniques.


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

    Nap 2 95 Aa Human
  • View Data Sheet

    Name :

    FHIT Human, GST

    Description:

    Fragile Histidine Triad Human Recombinant, GST Tag

    Bis(5'-adenosyl)-triphosphatase, EC 3.6.1.29, Diadenosine 5',5'''-P1,P3-triphosphate hydrolase, Dinucleosidetriphosphatase, AP3A hydrolase, AP3Aase, Fragile histidine triad protein, FHIT, FRA3B.

    Product # :

    PRO-297

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    Description

    FHIT Human Recombinant full length protein expressed in E.coli, shows a 43 kDa band on SDS-PAGE. The FHIT is fused to GST-Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FHIT in 50mM Tris-Acetate, pH7.5, 1mM EDTA and 20% Glycerol.

    Citations

    More Info

    • Introduction

      FHIT is a member of the histidine triad gene family. FHIT gene encodes a diadenosine 5',5'''-P1,P3-triphosphate hydrolase involved in purine metabolism. FHIT gene includes the common fragile site FRA3B on chromosome 3, where carcinogen-induced damage can lead to translocations and abnormal transcripts of this gene. The FHIT protein is a tumor suppressor with reduced or no expression in numerous types of cancer. FHIT may also act as a tumor suppressor in normal cells. Alterations and deletions of the FHIT (Fragile Histidine Triad) gene are strongly linked to the genesis and establishment of human tumors of the lung, cervix, breast, colon, stomach, and pancreas. The expression of FHIT is more often lost in cancers of individuals with familial mutations causing deficiency in DNA repair genes such as BRCA1, BRCA2 and MSH2. In vitro FHIT functions as a hydrolase that cleaves diadenosine triphosphate (Ap3A) to ADP and AMP. The FHIT -Ap3A enzyme-substrate complex seems to be the tumor suppressor signal. The restoration of FHIT expression in FHIT -deficient cancer cells leads to apoptosis, involving the intrinsic caspase pathway, in cancer-derived cells and in tumor xenografts.

    • Synonyms

      Bis(5'-adenosyl)-triphosphatase, EC 3.6.1.29, Diadenosine 5',5'''-P1,P3-triphosphate hydrolase, Dinucleosidetriphosphatase, AP3A hydrolase, AP3Aase, Fragile histidine triad protein, FHIT, FRA3B.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

    • Applications

      • ELISA
      • Inhibition Assays
      • Western Blotting.

    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.

    Fhit Human Gst
  • View Data Sheet

    Name :

    SDC2 Human

    Description:

    Syndecan-2 Human Recombinant

    Syndecan 2, Heparan Sulfate Proteoglycan 1 Cell Surface-Associated, Heparan Sulfate Proteoglycan Core Protein, Syndecan Proteoglycan 2, Fibroglycan, HSPG1, SYND2, HSPG, Cell Surface-Associated Heparan Sulfate Proteoglycan 1, CD362 Antigen, Syndecan-2, CD362, SDC2.

    Product # :

    PRO-2449

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    Description

    SDC2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 135 amino acids (19-144a.a.) and having a molecular mass of 15kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SDC2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SDC2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Syndecan 2 (SDC2) is a conserved family of heparan- and chondroitin-sulfate carrying transmembrane protein. Syndecan 2 is a cell membrane proteoglycan which modulates the activity and dynamics of some growth factor receptors and integrins. SDC2 is expressed in HSCs (hepatic stellate cells), a key cell type involved in matrix deposition in liver fibrotic disorders. SDC2 is implicated in the formation of specialized membrane domains and serves as a direct link between the extracellular environment and the organization of the cortical cytoplasm.

    • Synonyms

      Syndecan 2, Heparan Sulfate Proteoglycan 1 Cell Surface-Associated, Heparan Sulfate Proteoglycan Core Protein, Syndecan Proteoglycan 2, Fibroglycan, HSPG1, SYND2, HSPG, Cell Surface-Associated Heparan Sulfate Proteoglycan 1, CD362 Antigen, Syndecan-2, CD362, SDC2.

    • 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

      ADPESRAELT SDKDMYLDNS SIEEASGVYP IDDDDYASAS GSGADEDVES PELTTSRPLP KILLTSAAPK VETTTLNIQN KIPAQTKSPE ETDKEKVHLS DSERKMDPAE EDTNVYTEKH SDSLFKRTEH HHHHH.

    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.

    Sdc2 Human
  • View Data Sheet

    Name :

    CD105 Human, His

    Description:

    Endoglin Human Recombinant, His-Tag

    CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    Product # :

    CYT-823

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    • Citations

    Description

    Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The Endoglin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    CD105-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.

    • Synonyms

      CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    • 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 KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG

    • Background

      What is the molecular weight/Mw of CD105 Protein?
      CD105 Protein has a total Mw of 64.9kDa.

      What is the source or expression system of CD105 Protein?
      Escherichia Coli.

      What is the Purity of CD105 Protein?
      CD105 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD105 Protein?
      The biological functionality of CD105 Protein will be determined in the future.

      What is the amino acid sequence of CD105 Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG

      What applications can CD105 Protein be used in?
      CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD105 Protein?
      The endotoxin level is minimal, CD105 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.

    Endoglin Human His
  • View Data Sheet

    Name :

    BDH1 Human

    Description:

    3-Hydroxybutyrate Dehydrogenase, Type 1 Human Recombinant

    D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.

    Product # :

    ENZ-215

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    Description

    BDH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (47-343) and having a molecular mass of 35.3kDa.BDH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BDH1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BDH1 belongs to the short-chain dehydrogenase/reductase gene family. BDH1 forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific necessity for phosphatidylcholine for optimal enzymatic activity. BDH1 catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the 2 main ketone bodies formed during fatty acid catabolism.

    • Synonyms

      D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.

    • 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 MASAAEPVGS KAVLVTGCDS GFGFSLAKHL HSKGFLVFAG CLMKDKGHDG VKELDSLNSD RLRTVQLNVC SSEEVEKVVE IVRSSLKDPE KGMWGLVNNA GISTFGEVEF TSLETYKQVA EVNLWGTVRM TKSFLPLIRR AKGRVVNISS MLGRMANPAR SPYCITKFGV EAFSDCLRYE MYPLGVKVSV VEPGNFIAAT SLYSPESIQA IAKKMWEELP EVVRKDYGKK YFDEKIAKME TYCSSGSTDT SPVIDAVTHA LTATTPYTRY HPMDYYWWLR MQIMTHLPGA ISDMIYIR.

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    Bdh1 Human
  • View Data Sheet

    Name :

    BTN3A1 Human

    Description:

    Butyrophilin Subfamily 3 Member A1 Human Recombinant

    Butyrophilin Subfamily 3 Member A1, BTF5, DJ45P21.3 (Butyrophilin, Subfamily 3, Member A1), Butyrophilin, Subfamily 3, Member A1, CD277 Antigen, BTN3.1, BT3.1, CD277, Butyrophilin subfamily 3 member A1.

    Product # :

    PRO-2454

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    Description

    BTN3A1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 464 amino acids (30-254a.a.) and having a molecular mass of 51.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).BTN3A1 is expressed with a 239 amino acid hIgG-His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    BTN3A1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Butyrophilin sub family 3 member A1, also known as BTN3A1 is a member of the immunoglobulin superfamily. BTN3A1 is composed of an extracellular N-terminal IgV as well as a membrane proximal IgC domain followed by a transmembrane domain and also a cytoplasmic tail. BTN3A1 participates in T-cell activation and also in the adaptive immune response. Furthermore, BTN3A1 regulates the proliferation of activated T-cells & the release of cytokines and IFNG by activated T-cells. BTN3A1, Mediates the response of T-cells to infected as well as transformed cells which are categorized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate.

    • Synonyms

      Butyrophilin Subfamily 3 Member A1, BTF5, DJ45P21.3 (Butyrophilin, Subfamily 3, Member A1), Butyrophilin, Subfamily 3, Member A1, CD277 Antigen, BTN3.1, BT3.1, CD277, Butyrophilin subfamily 3 member A1.

    • 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

      QFSVLGPSGP ILAMVGEDAD LPCHLFPTMS AETMELKWVS SSLRQVVNVY ADGKEVEDRQ SAPYRGRTSI LRDGITAGKA ALRIHNVTAS DSGKYLCYFQ DGDFYEKALV ELKVAALGSD LHVDVKGYKD GGIHLECRST GWYPQPQIQW SNNKGENIPT VEAPVVADGV GLYAVAASVI MRGSSGEGVS CTIRSSLLGL EKTASISIAD PFFRSAQRWI AALAGLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH 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.

    Btn3A1 Human
  • View Data Sheet

    Name :

    PDCL Human

    Description:

    Phosducin-Like Human Recombinant

    Phosducin-like protein, PHLP, DKFZp564M1863.

    Product # :

    PRO-1141

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    Description

    PDCL Human Recombinant produced in E. coli is a single polypeptide chain containing 325 amino acids (1-301) and having a molecular mass of 36.8 kDa.PDCL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Phosducin-like protein (PDCL) is a member of the phosducin family. PDCL is a putative modulator of heterotrimeric G proteins. PDCL shares broad amino acid sequence homology with phosducin, a phosphoprotein expressed in the retina and pineal gland. Both PDCL and phosphoducin regulate G-protein signaling by binding to the beta-gamma subunits of G proteins.

    • Synonyms

      Phosducin-like protein, PHLP, DKFZp564M1863.

    • 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 MGSHMTTLDD KLLGEKLQYY YSSSEDEDSD HEDKDRGRCA PASSSVPAEA ELAGEGISVN TGPKGVINDW RRFKQLETEQ REEQCREMER LIKKLSMTCR SHLDEEEEQQ KQKDLQEKIS GKMTLKEFAI MNEDQDDEEF LQQYRKQRME EMRQQLHKGP QFKQVFEISS GEGFLDMIDK EQKSIVIMVH IYEDGIPGTE AMNGCMICLA AEYPAVKFCK VKSSVIGASS QFTRNALPAL LIYKGGELIG NFVRVTDQLG DDFFAVDLEA FLQEFGLLPE KEVLVLTSVR NSATCHSEDS DLEID

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    Pdcl Human
  • View Data Sheet

    Name :

    FUT7 Human

    Description:

    Fucosyltransferase 7 Human Recombinant

    Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.

    Product # :

    ENZ-784

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    Description

    FUT7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (37-342) and having a molecular mass of 37.9kDa.FUT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FUT7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fucosyltransferase 7 (FUT7) is a golgi stack membrane protein which is involved in the creation of sialyl-Lewis X antigens. The FUT7 protein leads the synthesis of the E-selectin-binding sialyl-Lewis X moiety. FUT7 catalyzes alpha-1,3 glycosidic linkages involved in the expression of sialyl Lewis X antigens.

    • Synonyms

      Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.

    • 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 MGSPRGTPAP QPTITILVWH WPFTDQPPEL PSDTCTRYGI ARCHLSANRS LLASADAVVF HHRELQTRRS HLPLAQRPRG QPWVWASMES PSHTHGLSHL RGIFNWVLSY RRDSDIFVPY GRLEPHWGPS PPLPAKSRVA AWVVSNFQER QLRARLYRQL APHLRVDVFG RANGRPLCAS CLVPTVAQYR FYLSFENSQH RDYITEKFWR NALVAGTVPV VLGPPRATYE AFVPADAFVH VDDFGSAREL AAFLTGMNES RYQRFFAWRD RLRVRLFTDW RERFCAICDR YPHLPRSQVY EDLEGWFQA.

    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.

    Fut7 Human
  • View Data Sheet

    Name :

    GFRA1 Rat

    Description:

    GDNF Family Receptor Alpha 1 Rat Recombinant

    GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

    Product # :

    CYT-1012

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    Description

    GFRA1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 645 amino acids (25-430a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GFRA1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.

    • Synonyms

      GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

    • 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

      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    • Background

      What is the molecular weight/Mw of GFRA1 RAT Protein?
      GFRA1 RAT Protein has a total Mw of 72.3kDa.

      What is the source or expression system of GFRA1 RAT Protein?
      Sf9, Baculovirus cells.

      What is the Purity of GFRA1 RAT Protein?
      GFRA1 RAT Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of GFRA1 RAT Protein?
      The biological functionality of GFRA1 RAT Protein will be determined in the future.

      What is the amino acid sequence of GFRA1 RAT Protein?
      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

      What applications can GFRA1 RAT Protein be used in?
      GFRA1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GFRA1 RAT Protein?
      The endotoxin level is minimal, GFRA1 RAT 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.

    Gfra1 Rat
  • View Data Sheet

    Name :

    LDHA Rat

    Description:

    Lactate Dehydrogenase A, Rat Recombinant

    L-lactate dehydrogenase A chain, LDH-A, LDH muscle subunit, LDH-M.

    Product # :

    ENZ-960

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    Description

    LDHA Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 340 amino acids (1-332 a.a) and having a molecular mass of 37.5kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). LDHA is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LDHA protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4), 1mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.

    • Synonyms

      L-lactate dehydrogenase A chain, LDH-A, LDH muscle subunit, LDH-M.

    • 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

      MAALKDQLIV NLLKEEQVPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG EMMDLQHGSL FLKTPKIVSS KDYSVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNVVKYSPQ CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWVL GEHGDSSVPV WSGVNVAGVS LKSLNPQLGT DADKEQWKDV HKQVVDSAYE VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI SDVVKVTLTP DEEARLKKSA DTLWGIQKEL QFLEHHHHHH.

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    Ldha Rat
  • View Data Sheet

    Name :

    CDC25A Human

    Description:

    Cell Division Cycle 25A Human Recombinant

    M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.

    Product # :

    ENZ-091

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    Description

    CDC25A Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 560 amino acids (1-524 a.a.) and having a molecular mass of 63.2kDa. The CDC25A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDC25A solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 20% glycerol, 0.2M NaCl and 1mM EDTA.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      M-phase inducer phosphatase 1 (CDC25A) belongs to the CDC25 family of phosphatases. CDC25A is essential for progression from G1 to the S phase of the cell cycle. CDC25A activates the cyclin-dependent kinase CDC2 by eliminating 2 phosphate groups. CDC25A is specifically degraded in reaction to DNA damage, which inhibits cells with chromosomal abnormalities from progressing in the course of cell division. CDC25A is an oncogene, though its exact function in oncogenesis has not been determined.

    • Synonyms

      M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMELG PEPPHRRRLL FACSPPPASQ PVVKALFGAS AAGGLSPVTN LTVTMDQLQG LGSDYEQPLE VKNNSNLQRM GSSESTDSGF CLDSPGPLDS KENLENPMRR IHSLPQKLLG CSPALKRSHS DSLDHDIFQL IDPDENKENE AFEFKKPVRP VSRGCLHSHG LQEGKDLFTQ RQNSAPARML SSNERDSSEP GNFIPLFTPQ SPVTATLSDE DDGFVDLLDG ENLKNEEETP SCMASLWTAP LVMRTTNLDN RCKLFDSPSL CSSSTRSVLK RPERSQEESP PGSTKRRKSM SGASPKESTN PEKAHETLHQ SLSLASSPKG TIENILDNDP RDLIGDFSKG YLFHTVAGKH QDLKYISPEI MASVLNGKFA NLIKEFVIID CRYPYEYEGG HIKGAVNLHM EEEVEDFLLK KPIVPTDGKR VIVVFHCEFS SERGPRMCRY VRERDRLGNE YPKLHYPELY VLKGGYKEFF MKCQSYCEPP SYRPMHHEDF KEDLKKFRTK SRTWAGEKSK REMYSRLKKL.

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    Cdc25A Human
  • View Data Sheet

    Name :

    Leptin Human, His

    Description:

    Leptin Human Recombinant, His Tag

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-287

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    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Leptin is a protein hormone with important effects in regulating body weight, metabolism and reproductive function. The protein is approximately~16 kDa in mass and encoded by the obese (ob)gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus known to be important in regulating body weight, as well as in T lymphocytes and vascular endothelial cells.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.Please avoid freeze-thaw cycles.

    • Solubility

      The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.

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

    Leptin Human His
  • View Data Sheet

    Name :

    Leptin N82K Human, PEG

    Description:

    Leptin N82K Human Recombinant, Pegylated

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1107

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    Citations

    More Info

    • Introduction

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

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Leptin Mutant Protein
  • View Data Sheet

    Name :

    RGS2 Human

    Description:

    Regulator of G-Protein Signaling 2 Human Recombinant

    Regulator of G-protein Signaling 2 24kDa, G0S8, G0/G1 switch regulatory protein 8, Cell growth-inhibiting gene 31 protein, RGS2.

    Product # :

    PRO-182

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    Description

    RGS2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-211a.a.) and having a molecular mass of 26.5 kDa. RGS2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RGS2 protein solution (0.25mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RGS2 belongs to the RGS family which are regulatory molecules that act as GTPase activating proteins for G alpha subunits of heterotrimeric G proteins. RGS2 inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits and as a result driving them into their inactive GDP-bound form.

    • Synonyms

      Regulator of G-protein Signaling 2 24kDa, G0S8, G0/G1 switch regulatory protein 8, Cell growth-inhibiting gene 31 protein, RGS2.

    • 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 MQSAMFLAVQ HDCRPMDKSA GSGHKSEEKR EKMKRTLLKD WKTRLSYFLQ NSSTPGKPKT GKKSKQQAFI KPSPEEAQLW SEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK KTKSPQKLSS KARKIYTDFI EKEAPKEINI DFQTKTLIAQ NIQEATSGCF TTAQKRVYSL MENNSYPRFL ESEFYQDLCK KPQITTEPHA T

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    Rgs2 Human
  • View Data Sheet

    Name :

    KLK2 Human, sf9

    Description:

    Kallikrein-2 Human Recombinant, sf9

    hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.

    Product # :

    ENZ-971

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    Description

    KLK2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 246 amino acids (25-261 aa) and having a molecular mass of 27.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).KLK2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      KLK2 is a part of the grandular kallikrein protein family whose Members are engaged in a diverse array of biological functions. Kallikreins are a subgroup of serine proteases which are clustered on chromosome 19. KLK2 is a highly active trypsin-like serine protease which selectively cleaves at arginine remains. KLK2 is mostly expressed in prostatic tissue and is accountable for cleaving pro-prostate-specific antigen into its enzymatically active form. KLK2 is greatly expressed in prostate tumor cells and may possibly be a prognostic maker for prostate cancer risk.

    • Synonyms

      hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.

    • 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

      ADPIVGGWEC EKHSQPWQVA VYSHGWAHCG GVLVHPQWVL TAAHCLKKNS QVWLGRHNLF EPEDTGQRVP VSHSFPHPLY NMSLLKHQSL RPDEDSSHDL MLLRLSEPAK ITDVVKVLGL PTQEPALGTT CYASGWGSIE PEEFLRPRSL QCVSLHLLSN DMCARAYSEK VTEFMLCAGL WTGGKDTCGG DSGGPLVCNG VLQGITSWGP EPCALPEKPA VYTKVVHYRK WIKDTIAANP HHHHHH

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    Klk2 Human Sf9
  • View Data Sheet

    Name :

    CRYAA Human

    Description:

    Crystallin Alpha A Human Recombinant

    CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein beta-4.

    Product # :

    HSP-002

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    Description

    Recombinant Human CRYAA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids and having a molecular mass of 19.9kDa.CRYAA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRYAA protein contains 20mM Tris-HCl buffer (pH 7.5), 50mM NaCl and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein(sHSP also known as the HSP20). They act as molecular chaperones and hold them in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. The expression of alpha-A is preferentially restricted to the lens cell.

    • Synonyms

      CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein beta-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

      MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSGISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRLPSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS.

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    Cryaa Human
  • View Data Sheet

    Name :

    MMP2 Mouse

    Description:

    Matrix Metalloproteinase-2 Mouse Recombinant

    72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    Product # :

    ENZ-1117

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    Description

    MMP2 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 644 amino acids (30-662 aa) and having a molecular mass of 72.4kDa.MMP2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The MMP2 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MMP-2 or gelatinase A, is secreted by fibroblasts, cardiomyocytes, and myofibroblasts. MMP-2 has a broad feild of substrates, that contain elastin, collagen, fibroblast growth factor, endothelin, MMP-9, plasminogen, MMP-13 and TGF-beta, pointing towards bread roles of MMP-2. MMP-2 activity boosts at day four post-MI and attains a maximum by day seven.

    • Synonyms

      72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    • 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

      ADPEFAPSPI IKFPGDVAPK TDKELAVQYL NTFYGCPKES CNLFVLKDTL KKMQKFFGLP QTGDLDQNTI ETMRKPRCGN PDVANYNFFP RKPKWDKNQI TYRIIGYTPD LDPETVDDAF ARALKVWSDV TPLRFSRIHD GEADIMINFG RWEHGDGYPF DGKDGLLAHA FAPGTGVGGD SHFDDDELWT LGEGQVVRVK YGNADGEYCK FPFLFNGREY SSCTDTGRSD GFLWCSTTYN FEKDGKYGFC PHEALFTMGG NADGQPCKFP FRFQGTSYNS CTTEGRTDGY RWCGTTEDYD RDKKYGFCPE TAMSTVGGNS EGAPCVFPFT FLGNKYESCT SAGRNDGKVW CATTTNYDDD RKWGFCPDQG YSLFLVAAHE FGHAMGLEHS QDPGALMAPI YTYTKNFRLS HDDIKGIQEL YGPSPDADTD TGTGPTPTLG PVTPEICKQD IVFDGIAQIR GEIFFFKDRF IWRTVTPRDK PTGPLLVATF WPELPEKIDA VYEAPQEEKA VFFAGNEYWV YSASTLERGY PKPLTSLGLP PDVQQVDAAF NWSKNKKTYI FAGDKFWRYN EVKKKMDPGF PKLIADSWNA IPDNLDAVVD LQGGGHSYFF KGAYYLKLEN QSLKSVKFGS IKSDWLGCHH 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.

    Mmp2 Mouse
  • View Data Sheet

    Name :

    CD105 Human, Sf9

    Description:

    Endoglin Human Recombinant, Sf9

    CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    Product # :

    CYT-389

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    Description

    CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

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

    Biological Activity

    Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

    Citations

    More Info

    • Introduction

      Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
      The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.

    • Synonyms

      CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 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 CD-105 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.

    • Background

      What is the molecular weight/Mw of CD105 Protein?
      CD105 Protein has a total Mw of 90kDa.

      What is the source or expression system of CD105 Protein?
      Sf9 Insect Cells.

      What is the Purity of CD105 Protein?
      CD105 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD105 Protein?
      Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

      What is the amino acid sequence of CD105 Protein?
      MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.

      What applications can CD105 Protein be used in?
      CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD105 Protein?
      The endotoxin level is minimal, CD105 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.

    Endoglin Human Sf9
  • View Data Sheet

    Name :

    PROK Tritirachium album

    Description:

    Tritirachium album Proteinase-K Recombinant

    Proteinase K (EC:3.4.21.64), Endopeptidase K, Tritirachium alkaline proteinase, PROK.

    Product # :

    ENZ-1015

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    • Citations

    Description

    Recombinant Tritirachium album Proteinase-K expressed in yeast containing 285 amino acids having a Mw of 29.3 kDa is purified by standard chromatography techniques.

    Source

    Yeast

    Formulation

    The Proteinase-K was lyophilized without any additives.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    36 Units/mg.
    One unit is defined as the amount of enzyme that will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 mol tyrosine per min at 37°C, pH 7.5 (color by Folin-Ciocalteu reagent).

    Citations

    More Info

    • Introduction

      The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.

    • Synonyms

      Proteinase K (EC:3.4.21.64), Endopeptidase K, Tritirachium alkaline proteinase, PROK.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Recombinant Proteinase-K although stable at room temperature, should be stored between 2-8°C. Do not freeze!

    • Solubility

      It is recommended to reconstitute the lyophilized Proteinase-K in 20mM Tris-HCl (pH 7.4~8.0), 1mM CaCl2, 50% glycerol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Note

      Bulk Proteinase-K recombinant is available 1,000 grams price is $100 per gram

    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.

    Prok Tritirachium Album
  • View Data Sheet

    Name :

    POGLUT1 Human

    Description:

    Protein O-Glucosyltransferase 1 Human Recombinant

    POGLUT1, C3orf9, CLP46, hCLP46, KDELCL1, KTELC1, Protein O-glucosyltransferase 1, CAP10-like 46 kDa protein, KTEL motif-containing protein 1, Myelodysplastic syndromes relative protein, O-glucosyltransferase Rumi homolog, hRumi, Protein O-xylosyltransferase, MDSRP.

    Product # :

    ENZ-956

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    Description

    POGLUT1 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 377 amino acids (24-392a.a) and having a molecular mass of 44.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). POGLUT1 is fused to a 8 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The POGLUT1 solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      POGLUT1 is a homologue of Rumi from Drosophila, an endoplasmic reticulum (ER)-retaining glucosyltransferase which catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to EGF repeats on the consensus sequence C-X-S-X-P-C. POGLUT1 positively regulates Notch signaling without affecting Notch ligand binding.

    • Synonyms

      POGLUT1, C3orf9, CLP46, hCLP46, KDELCL1, KTELC1, Protein O-glucosyltransferase 1, CAP10-like 46 kDa protein, KTEL motif-containing protein 1, Myelodysplastic syndromes relative protein, O-glucosyltransferase Rumi homolog, hRumi, Protein O-xylosyltransferase, MDSRP.

    • 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

      RQKESGSKWK VFIDQINRSL ENYEPCSSQN CSCYHGVIEE DLTPFRGGIS RKMMAEVVRR KLGTHYQITK NRLYRENDCM FPSRCSGVEH FILEVIGRLP DMEMVINVRD YPQVPKWMEP AIPVFSFSKT SEYHDIMYPA WTFWEGGPAV WPIYPTGLGR WDLFREDLVR SAAQWPWKKK NSTAYFRGSR TSPERDPLIL LSRKNPKLVD AEYTKNQAWK SMKDTLGKPA AKDVHLVDHC KYKYLFNFRG VAASFRFKHL FLCGSLVFHV GDEWLEFFYP QLKPWVHYIP VKTDLSNVQE LLQFVKANDD VAQEIAERGS QFIRNHLQMD DITCYWENLL SEYSKFLSYN VTRRKGYDQI IPKMLKTELL 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.

    Poglut1 Human
  • View Data Sheet

    Name :

    BETV4

    Description:

    Polcalcin Bet v 4 Recombinant

    Polcalcin Bet v 4, Calcium-binding pollen allergen Bet v 4, Bet v 4, BETV4.

    Product # :

    ALR-017

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    Description

    Recombinant BETV4 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 10,473 Dalton. BETV4 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    BETV4 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BETV4 is primarily expressed in mature birch (Betula verrucosa) pollen and Causes an allergic reaction in human. BETV4 is a calcium-binding protein of 2-EF-hand type, which is exists in pollen of various plant species. This cross-reactivity can serve as a marker allergen for plant polysensitization.

    • Synonyms

      Polcalcin Bet v 4, Calcium-binding pollen allergen Bet v 4, Bet v 4, BETV4.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Betv4
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