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Search results

1000 results found for “isomerase”

Name

Description

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  • View Data Sheet

    Name :

    CTSF Human

    Description:

    Cathepsin-F Human Recombinant

    800x600 CATSF, CLN13, Cathepsin F, EC=3.4.22.41. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    ENZ-738

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    Description

    800x600 CTSF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (271-484) and having a molecular mass of 26kDa.CTSF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cathepsin F ( CTSF) is a member of the peptidase C1 family. Cathepsins are papain familycysteine proteinases which are a main component of the lysosomal proteolytic system. The CTSF gene isubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF plays a role in normal protein catabolism. CTSF involved in some degradative processes occurring in tumor progression since it is highly expressed in some cancer cell lines.

    • Synonyms

      CATSF, CLN13, Cathepsin F, EC=3.4.22.41.

    • 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 MGSAPPEWDW RSKGAVTKVK DQGMCGSCWA FSVTGNVEGQ WFLNQGTLLS LSEQELLDCD KMDKACMGGL PSNAYSAIKN LGGLETEDDY SYQGHMQSCN FSAEKAKVYI NDSVELSQNE QKLAAWLAKR GPISVAINAF GMQFYRHGIS RPLRPLCSPW LIDHAVLLVG YGNRSDVPFW AIKNSWGTDW GEKGYYYLHR GSGACGVNTM ASSAVVD.

    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.

    Ctsf Human
  • View Data Sheet

    Name :

    NAA10 Human

    Description:

    N Alpha-Acetyltransferase 10, NatA Catalytic Subunit Human Recombinant

    N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.

    Product # :

    ENZ-158

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    Description

    NAA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (1-235 a.a.) and having a molecular mass of 28.6kDa (the molecular weight on SDS-PAGE will appear higher).NAA10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAA10 is a member of the acetyltransferase family. NAA10 interacts with NAA15, HIF-1 and with the ribosome. In its binding to HIF-1, NAA10 functions as a protein acetyltransferase by regulating its stability. In various cell lines, NAA10 is downregulated in response to hypoxia. NAA10 is expressed during the course of the development of the brain.

    • Synonyms

      N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.

    • 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 MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS.

    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.

    Naa10 Human
  • View Data Sheet

    Name :

    XPNPEP1 Human

    Description:

    X-Prolyl Aminopeptidase-1 Human Recombinant

    X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 1.

    Product # :

    ENZ-880

    Price :

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    Description

    XPNPEP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 655 amino acids (1-623 a.a) and having a molecular mass of 73.4kDa. XPNPEP1 is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    XPNPEP1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      X-Prolyl Aminopeptidase-1, also known as XPNPEP1 is a member of the peptidase M24B family. XPNPEP1 encodes the cytosolic form of a metalloaminopeptidase which catalyzes the cleavage of the N-terminal amino acid adjacent to a proline residue. Furthermore, XPNPEP1 plays a role in degradation as well as maturation of tachykinins, neuropeptides and peptide hormones.

    • Synonyms

      X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 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 MGSEFELRRQ ASMPPKVTSE LLRQLRQAMR NSEYVTEPIQ AYIIPSGDAH QSEYIAPCDC RRAFVSGFDG SAGTAIITEE HAAMWTDGRY FLQAAKQMDS NWTLMKMGLK DTPTQEDWLV SVLPEGSRVG VDPLIIPTDY WKKMAKVLRS AGHHLIPVKE NLVDKIWTDR PERPCKPLLT LGLDYTGISW KDKVADLRLK MAERNVMWFV VTALDEIAWL FNLRGSDVEH NPVFFSYAII GLETIMLFID GDRIDAPSVK EHLLLDLGLE AEYRIQVHPY KSILSELKAL CADLSPREKV WVSDKASYAV SETIPKDHRC CMPYTPICIA KAVKNSAESE GMRRAHIKDA VALCELFNWL EKEVPKGGVT EISAADKAEE FRRQQADFVD LSFPTISSTG PNGAIIHYAP VPETNRTLSL DEVYLIDSGA QYKDGTTDVT RTMHFGTPTA YEKECFTYVL KGHIAVSAAV FPTGTKGHLL DSFARSALWD SGLDYLHGTG HGVGSFLNVH EGPCGISYKT FSDEPLEAGM IVTDEPGYYE DGAFGIRIEN VVLVVPVKTK YNFNNRGSLT FEPLTLVPIQ TKMIDVDSLT DKECDWLNNY HLTCRDVIGK ELQKQGRQEA LEWLIRETQP ISKQH.

    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.

    Xpnpep1 Human
  • View Data Sheet

    Name :

    LDHB Human, His

    Description:

    Lactate Dehydrogenase B Human Recombinant, His Tag

    LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.

    Product # :

    ENZ-539

    Price :

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    Description

    LDHB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-334 a.a.) and having a molecular mass of 38.8 kDa. The LDHB is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LDHB Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 6 units/mg. in which one unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C.

    More Info

    • Introduction

      LDHB is part of the lactate dehydrogenase family. LDHB is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LDHB catalyzes the oxidation of hydroxybutyrate, and frequently called Hydroxybutyrate Dehydrogenase (HBD). The LDH family consists of three members, LDH-A, LDH-B and LDH-C. LDHs function as powerful markers for germ cell tumors.

    • Synonyms

      LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.

    • 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 MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL.

    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.

    Ldhb Human
  • View Data Sheet

    Name :

    DHODH Human

    Description:

    Dihydroorotate Dehydrogenase Human Recombinant

    Dihydroorotate dehydrogenase (quinone), Dihydroorotate oxidase, human complement of yeast URA1, DHOdehase, POADS, EC 1.3.5.2, EC 1.3.3.1.

    Product # :

    ENZ-642

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    Description

    DHODH Human Recombinant produced in E. coli is a single polypeptide chain containing 390 amino acids (31-395) and having a molecular mass of 42.3 kDa.DHODH is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DHODH 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.

    More Info

    • Introduction

      Dihydroorotate dehydrogenase quinone (DHODH) is a member of the dihydroorotate dehydrogenase family. DHODH is a mitochondrial protein found on the outer surface of the inner mitochondrial membrane. DHODH catalyzes the 4th enzymatic step, the ubiquinone-mediated oxidation of dihydroorotate to orotate (with quinone as electron acceptor), in de novo pyrimidine biosynthesis. DHODH gene defects cause the postaxial acrofacial dysostosis (POADS), also known as Miller syndrome.

    • Synonyms

      Dihydroorotate dehydrogenase (quinone), Dihydroorotate oxidase, human complement of yeast URA1, DHOdehase, POADS, EC 1.3.5.2, EC 1.3.3.1.

    • 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

      GSSHHHHHH SSGLVPRGSH MGSHMTGDER FYAEHLMPTL QGLLDPESAH RLAVRFTSLG LLPRARFQDS DMLEVRVLGH KFRNPVGIAA GFDKHGEAVD GLYKMGFGFV EIGSVTPKPQ EGNPRPRVFR LPEDQAVINR YGFNSHGLSV VEHRLRARQQ KQAKLTEDGL PLGVNLGKNK TSVDAAEDYA EGVRVLGPLA DYLVVNVSSP NTAGLRSLQG KAELRRLLTK VLQERDGLRR VHRPAVLVKI APDLTSQDKE DIASVVKELG IDGLIVTNTT VSRPAGLQGA LRSETGGLSG KPLRDLSTQT IREMYALTQG RVPIIGVGGV SSGQDALEKI RAGASLVQLY TALTFWGPPV VGKVKRELEA LLKEQGFGGV TDAIGADHRR.

    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.

    Dhodh Human
  • View Data Sheet

    Name :

    PGC Human

    Description:

    Progastricsin-C Human Recombinant

    Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.

    Product # :

    ENZ-966

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    Description

    PGC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (17-388 a.a.) and having a molecular mass of 41.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PGC is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Progastricsin-C (PGC) is an aspartic proteinase which is synthesized in the gastric mucosa as inactive precursors. PGC is a part of the peptidase family A1 and contains a prosegment which is responsible for stabilizing the inactive form and preventing the entrance of the substrate to the active site. PGC is used as a biomarker for various gastric diseases including Helicobacter pylori related gastritis. PGC is also hydrolyzes various proteins.

    • Synonyms

      Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.

    • 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

      AVVKVPLKKF KSIRETMKEK GLLGEFLRTH KYDPAWKYRF GDLSVTYEPM AYMDAAYFGE ISIGTPPQNF LVLFDTGSSN LWVPSVYCQS QACTSHSRFN PSESSTYSTN GQTFSLQYGS GSLTGFFGYD TLTVQSIQVP NQEFGLSENE PGTNFVYAQF DGIMGLAYPA LSVDEATTAM QGMVQEGALT SPVFSVYLSN QQGSSGGAVV FGGVDSSLYT GQIYWAPVTQ ELYWQIGIEE FLIGGQASGW CSEGCQAIVD TGTSLLTVPQ QYMSALLQAT GAQEDEYGQF LVNCNSIQNL PSLTFIINGV EFPLPPSSYI LSNNGYCTVG VEPTYLSSQN GQPLWILGDV FLRSYYSVYD LGNNRVGFAT AALEHHHHHH.

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    Pgc Human
  • View Data Sheet

    Name :

    LDHB Mouse

    Description:

    Lactate Dehydrogenase B Mouse Recombinant

    L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.

    Product # :

    ENZ-1052

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    Description

    LDHB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-334 a.a) and having a molecular mass of 39kDa.LDHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 150 units/mg, in which one unit will 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5.

    More Info

    • Introduction

      Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
      A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

    • Synonyms

      L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.

    • 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 MGSMATLKEK LIASVADDEA AVPNNKITVV GVGQVGMACA ISILGKSLAD ELALVDVLED KLKGEMMDLQ HGSLFLQTPK IVADKDYSVT ANSKIVVVTA GVRQQEGESR LNLVQRNVNV FKFIIPQIVK YSPDCTIIVV SNPVDILTYV TWKLSGLPKH RVIGSGCNLD SARFRYLMAE KLGIHPSSCH GWILGEHGDS SVAVWSGVNV AGVSLQELNP EMGTDNDSEN WKEVHKMVVD SAYEVIKLKG YTNWAIGLSV ADLIESMLKN LSRIHPVSTM VKGMYGIENE VFLSLPCILN ARGLTSVINQ KLKDDEVAQL RKSADTLWDI QKDLKDL.

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    Ldhb Mouse
  • View Data Sheet

    Name :

    LIPG Human, HEK

    Description:

    Lipase Endothelial Human Recombinant, HEK

    LIPG, Lipase Endothelial, EDL, EL, Endothelial Cell-Derived Lipase, EC 3.1.1.3, PRO719, Endothelial Lipase, Lipoprotein Lipase H, EC 3.1.1.

    Product # :

    ENZ-810

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    Description

    LIPG Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser21-Pro500) containing a total of 490 amino acids, having a calculated molecular mass of 55.8kDa. LIPG is fused to a 2 aa N-terminal linker, a 2 aa C-terminal linker and a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    LIPG was filtered (0.4 µm) and lyophilized from a solution in phosphate buffered saline pH 7.5 (PBS), 1% (w/v) Sucrose and 4% (w/v) Mannitol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lipase Endothelial (LIPG) has extensive phospholipase activity and may be involved in lipoprotein metabolism and vascular biology. The LIPG protein is considered a member of the TG lipase family through its sequence and characteristic lid region which provides substrate specificity for enzymes of the TG lipase family. In addition, the LIPG has triglyceride lipase activities. LIPG hydrolyzes HDLs more efficiently than other lipoproteins. LIPG also binds heparin.

    • Synonyms

      LIPG, Lipase Endothelial, EDL, EL, Endothelial Cell-Derived Lipase, EC 3.1.1.3, PRO719, Endothelial Lipase, Lipoprotein Lipase H, EC 3.1.1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      ASSPVPFGPE GRLEDKLHKP KATQTEVKPS VRFNLRTSKD PEHEGCYLSV GHSQPLEDCS FNMTAKTFFI IHGWTMSGIF ENWLHKLVSA LHTREKDANV VVVDWLPLAH QLYTDAVNNT RVVGHSIARM LDWLQEKDDF SLGNVHLIGY SLGAHVAGYA GNFVKGTVGR ITGLDPAGPM FEGADIHKRL SPDDADFVDV LHTYTRSFGL SIGIQMPVGH IDIYPNGGDF QPGCGLNDVL GSIAYGTITE VVKCEHERAV HLFVDSLVNQ DKPSFAFQCT DSNRFKKGIC LSCRKNRCNS IGYNAKKMRN KRNSKMYLKT RAGMPFRVYH YQMKIHVFSY KNMGEIEPTF YVTLYGTNAD SQTLPLEIVE RIEQNATNTF LVYTEEDLGD LLKIQLTWEG ASQSWYNLWK EFRSYLSQPR NPGRELNIRR IRVKSGETQR KLTFCTEDPE NTSISPGREL WFRKCRDGWR MKNETSPTVE LP KLHHHHHH.

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    Lipg Human Hek
  • View Data Sheet

    Name :

    HAGH Human

    Description:

    Hydroxyacylglutathione Hydrolase Human Recombinant

    GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.

    Product # :

    ENZ-034

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    Description

    HAGH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-260a.a.) and having a molecular mass of 31.4kDa.HAGH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HAGH protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl Buffer (pH 8.5) and 10% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      HAGH is a part of the glyoxalase family and a thiolesterase which hydrolyses S-lactoyl-glutathione to reduced glutathione and D-lactate. HAGH protein is a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73 and serves as a pro-survival factor of the p53 family. HAGH appears only as a monomer and binds two zinc ions per subunit.

    • Synonyms

      GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.

    • 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 MGSHMKVEVL PALTDNYMYL VIDDETKEAA IVDPVQPQKV VDAARKHGVK LTTVLTTHHH WDHAGGNEKL VKLESGLKVY GGDDRIGALT HKITHLSTLQ VGSLNVKCLA TPCHTSGHIC YFVSKPGGSE PPAVFTGDTL FVAGCGKFYE GTADEMCKAL LEVLGRLPPD TRVYCGHEYT INNLKFARHV EPGNAAIREK LAWAKEKYSI GEPTVPSTLA EEFTYNPFMR VREKTVQQHA GETDPVTTMR AVRREKDQFK MPRD.

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    Hagh Human
  • View Data Sheet

    Name :

    TK1 Human

    Description:

    Thymidine Kinase 1 Human Recombinant

    Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    Product # :

    PKA-036

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    Description

    TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TK1 solution (1mg/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.

    More Info

    • Introduction

      Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.

    • Synonyms

      Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    • 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 MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.

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    Tk1 Human
  • View Data Sheet

    Name :

    MDP1 Human

    Description:

    Magnesium-Dependent Phosphatase 1 Human Recombinant

    Magnesium-dependent phosphatase 1, MGC5987, MDP-1, FN6Pase, fructosamine-6-phosphatase, SFTB3, SFTPB, MDP1.

    Product # :

    ENZ-044

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    Description

    MDP1 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 200 amino acids (1-176 a.a.) and having a molecular mass of 22.6kDa. The MDP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MDP1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Magnesium-dependent phosphatase 1 (MDP1) is a memeber of the HAD-like hydrolase superfamily. MDP1 is a magnesium-dependent phosphatase which may act as a tyrosine phosphatase. MDP1 is inhibited by vanadate and zinc, and slightly by calcium.

    • Synonyms

      Magnesium-dependent phosphatase 1, MGC5987, MDP-1, FN6Pase, fructosamine-6-phosphatase, SFTB3, SFTPB, MDP1.

    • 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 MGSHMARLPK LAVFDLDYTL WPFWVDTHVD PPFHKSSDGT VRDRRGQDVR LYPEVPEVLK RLQSLGVPGA AASRTSEIEG ANQLLELFDL FRYFVHREIY PGSKITHFER LQQKTGIPFS QMIFFDDERR NIVDVSKLGV TCIHIQNGMN LQTLSQGLET FAKAQTGPLR SSLEESPFEA.

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    Mdp1 Human
  • View Data Sheet

    Name :

    AKR1A1 Human

    Description:

    Aldo-Keto Reductase Family 1 Member A1 Human Recombinant

    Alcohol dehydrogenase, ALR, ARM, DD3, ALDR1, MGC1380, MGC12529, AKR1A1, Alcohol dehydrogenase [NADP+], Aldehyde reductase, Aldo-keto reductase family 1 member A1.

    Product # :

    ENZ-464

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    Description

    AKR1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 325 amino acids (1-325 a.a.) and having a molecular mass of 36.5 kDa. AKR1A1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AKR1A1 solution containing 20mM Tris pH-8, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      AKR1A1 is part of the aldo/keto reductase superfamily, it catalyzes the NADPH-dependent reduction from a range of aromatic and aliphatic aldehydes to their related alcohols. AKR1A1 corresponds (65% identity) to aldose reductase, an enzyme that takes part in the pathogenesis of some diabetic and galactosemic complications. AKR1A1 is involved in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs.

    • Synonyms

      Alcohol dehydrogenase, ALR, ARM, DD3, ALDR1, MGC1380, MGC12529, AKR1A1, Alcohol dehydrogenase [NADP+], Aldehyde reductase, Aldo-keto reductase family 1 member A1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      AKR1A1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAVKYALSVG YRHIDCAAIY GNEPEIGEAL KEDVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTICYDSTHY KETWKALEAL VAKGLVQALG LSNFNSRQID DILSVASVRP AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RDPDEPVLLE EPVVLALAEKYGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIKVFDFT FSPEEMKQLN ALNKNWRYIV PMLTVDGKRV PRDAGHPLYP FNDPY

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    Akr1A1 Human
  • View Data Sheet

    Name :

    DUSP18 Human, Active

    Description:

    Dual Specificity Phosphatase 18 Human Recombinant, Active

    Dual specificity protein phosphatase 18, Low molecular weight dual specificity phosphatase 20, LMW-DSP20, DUSP18, LMWDSP20, VHP, DUSP26.

    Product # :

    ENZ-1040

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    Description

    DUSP18 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-188a.a.) and having a molecular mass of 23.6kDa.DUSP18 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DUSP18 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF, 1mM DTT, 40% glycerol and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37°C.

    More Info

    • Introduction

      Dual specificity phosphatase 18 (DUSP18) belongs to the dual-specificity phosphatase (DSP) family, which catalyzes dephosphorylation of phosphotyrosine and phosphothreonine residues. DUSP18 has a preferential enzymatic activity for phosphorylated tyrosine residues over threonine residues, in addition DUSP18 dephosphorylates p-nitrophenyl phosphate (pNPP) in vitro. Furthermore, DUSP18 is inhibited by iodoarectic acid and is activated by manganese ions. DUSP18 is extensively expressed with the highest levels in the liver, brain, ovary and testis.

    • Synonyms

      Dual specificity protein phosphatase 18, Low molecular weight dual specificity phosphatase 20, LMW-DSP20, DUSP18, LMWDSP20, VHP, DUSP26.

    • 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 MGSHMTAPSC AFPVQFRQPS VSGLSQITKS LYISNGVAAN NKLMLSSNQI TMVINVSVEV VNTLYEDIQY MQVPVADSPN SRLCDFFDPI ADHIHSVEMK QGRTLLHCAA GVSRSAALCL AYLMKYHAMS LLDAHTWTKS CRPIIRPNSG FWEQLIHYEF QLFGKNTVHM VSSPVGMIPD IYEKEVRLMI PL

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    Dusp18 Human Active
  • View Data Sheet

    Name :

    ACKA E.Coli

    Description:

    Acetate Kinase E.Coli Recombinant

    Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.

    Product # :

    PKA-063

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    Description

    Recombinant ACKA produced in E.coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400) and having a molecular mass of 45.7 kDa.The ACKA is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      E.Coli Acetate Kinase, also knowns as ACKA, catalyzes the formation of acetyl phosphate from acetate and ATP and also catalyzes the reverse reaction. ACKA takes part in synthesis of various ATP formed catabolically during anaerobic growth of the organism.

    • Synonyms

      Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.

    • 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 MGSMSSKLVL VLNCGSSSLK FAIIDAVNGE EYLSGLAECF HLPEARIKWK MDGNKQEAAL GAGAAHSEAL NFIVNTILAQ KPELSAQLTA IGHRIVHGGE KYTSSVVIDE SVIQGIKDAA SFAPLHNPAH LIGIEEALKS FPQLKDKNVA VFDTAFHQTM PEESYLYALP YNLYKEHGIR RYGAHGTSHF YVTQEAAKML NKPVEELNII TCHLGNGGSV SAIRNGKCVD TSMGLTPLEG LVMGTRSGDI DPAIIFHLHD TLGMSVDAIN KLLTKESGLL GLTEVTSDCR YVEDNYATKE DAKRAMDVYC HRLAKYIGAY TALMDGRLDA VVFTGGIGEN AAMVRELSLG KLGVLGFEVD HERNLAARFG KSGFINKEGT RPAVVIPTNE ELVIAQDASR LTA.

    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.

    Acka Ecoli
  • View Data Sheet

    Name :

    HMGCL Human

    Description:

    3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant

    Hydroxymethylglutaryl-CoA lyase mitochondrial, HL, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase, HMGCL.

    Product # :

    ENZ-218

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    Description

    HMGCL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (28-325) and having a molecular mass of 34.2kDa.HMGCL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HMGCL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hydroxymethylglutaryl-CoA lyase (HMGCL) is a mitochondrial matrix protein which is a member of the HMG-CoA lyase family. HMGCL is a homodimer and participates in leucine catabolism and ketogenesis, the hepatic synthesis of ketone bodies which, during fasting, provides a major source of energy for the heart, brain and kidney. More precisely, HMGCL catalyzes the final step of these processes, the cleavage of 3-hydroxy-3-methylglutaryl-CoA to acetoacetic acid and acetyl-CoA.

    • Synonyms

      Hydroxymethylglutaryl-CoA lyase mitochondrial, HL, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase, HMGCL.

    • 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 MGSHMTLPKR VKIVEVGPRD GLQNEKNIVS TPVKIKLIDM LSEAGLSVIE TTSFVSPKWV PQMGDHTEVL KGIQKFPGIN YPVLTPNLKG FEAAVAAGAK EVVIFGAASE LFTKKNINCS IEESFQRFDA ILKAAQSANI SVRGYVSCAL GCPYEGKISP AKVAEVTKKF YSMGCYEISL GDTIGVGTPG IMKDMLSAVM QEVPLAALAV HCHDTYGQAL ANTLMALQMG VSVVDSSVAG LGGCPYAQGA SGNLATEDLV YMLEGLGIHT GVNLQKLLEA GNFICQALNR KTSSKVAQAT CKL.

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    Hmgcl Human
  • View Data Sheet

    Name :

    DUSP18 Human

    Description:

    Dual Specificity Phosphatase 18 Human Recombinant

    Dual specificity protein phosphatase 18, Low molecular weight dual specificity phosphatase 20, LMW-DSP20, DUSP18, LMWDSP20, VHP, DUSP26.

    Product # :

    ENZ-582

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    Description

    DUSP18 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-188) and having a molecular mass of 23.6kDa.DUSP18 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DUSP18 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol, 0.1mM PMSF and 1mM EDTA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dual specificity phosphatase 18 (DUSP18) belongs to the dual-specificity phosphatase (DSP) family, which catalyzes dephosphorylation of phosphotyrosine and phosphothreonine residues. DUSP18 has a preferential enzymatic activity for phosphorylated tyrosine residues over threonine residues, in addition DUSP18 dephosphorylates p-nitrophenyl phosphate (pNPP) in vitro. Furthermore, DUSP18 is inhibited by iodoarectic acid and is activated by manganese ions. DUSP18 is extensively expressed with the highest levels in the liver, brain, ovary and testis.

    • Synonyms

      Dual specificity protein phosphatase 18, Low molecular weight dual specificity phosphatase 20, LMW-DSP20, DUSP18, LMWDSP20, VHP, DUSP26.

    • 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 MGSHMTAPSC AFPVQFRQPS VSGLSQITKS LYISNGVAAN NKLMLSSNQI TMVINVSVEV VNTLYEDIQY MQVPVADSPN SRLCDFFDPI ADHIHSVEMK QGRTLLHCAA GVSRSAALCL AYLMKYHAMS LLDAHTWTKS CRPIIRPNSG FWEQLIHYEF
      QLFGKNTVHM VSSPVGMIPD IYEKEVRLMI PL.

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    Dusp18 Human
  • View Data Sheet

    Name :

    GLO1 Mouse

    Description:

    Glyoxalase-I Mouse Recombinant

    Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.

    Product # :

    ENZ-953

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    Description

    GLO1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 192 amino acids (1-184a.a.) and having a molecular mass of 21.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GLO1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GLO1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 210 units/mg, and is defined as the amount of enzyme that will form 1.0 µmol of S-lactoylglutathione from methylglyoxal and reduced glutathione per minute at pH 6.5 at 25C.

    More Info

    • Introduction

      GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

    • Synonyms

      Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.

    • 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

      MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATIILEHHHH HH.

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    Glo1 Mouse
  • View Data Sheet

    Name :

    M2 Human

    Description:

    DLAT/DLST/BCOADC Recombinant Human

    Product # :

    ENZ-072

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    Description

    Recombinant antigen for solid (ELISA) and fluid phase diagnostic assays. Mixture of E2/dihydrolipamide acyltransferase-subunits from 3 mitochondrial protein complexes: pyruvate dehydrogenase complex (PDC-E2) having a molecular mass of 60,630 Dalton (pI 5.8); 2-oxo-glutarate dehydrogenase complex (OGDC-E2) having a molecular mass of 42,301 Dalton (pI 6.3); branched chain 2-oxo-acid dehydrogenase complex (BCOADCE2) having a molecular mass of 47,321 Dalton (pI 6.5). Mixture contains equal mass of each protein component. cDNAs coding for the mature forms of the human PDC-E2, OGDC-E2 and BCOADC-E2 proteins individually fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    M2 is supplied in 16mM HEPES buffer pH-8.0, 400mM NaCl, and 20% glycerol.

    Purity

    Greater than 75% as determined by SDS-PAGE.

    More Info

    • Introduction

      M2 autoantigen is a key mark of antimitochondrial autoantibodies (AMA), a typical serological feature in patients suffering from primary biliary cirrhosis (PBC) which is a serious autoimmune liver disease accompanied by damage to intrahepatic bile ducts. Molecular definition of the M2 antigen has displayed it as no less than 3 separate target proteins. The M2 role is like the so-called E2 subunits (or dihydrolipoamide transferases) of different mitochondrial dehydrogenase complexes:
      *pyruvate dehydrogenase complex.
      *branched chain 2-oxo-acid dehydrogenase complex.
      *2-oxoglutarate dehydrogenase complex.
      Biochemically, these complexes catalyze the oxidative decarboxylation of various alpha-keto-acid substrates and systematically engage with a prosthetic lipoamide group; they are situated in the mitochondrial matrix in association with the inner membrane. The most well-known reactivity of AMA positive PBC sera is against PDC-E2. Some patients have AMA which reacts with PDC-E2 alone (95%), but most patients also show reactivity against OGDC-E2 (39-88%) and/or BCOADC-E2 (53-55%). Actually, patients can be found with reactivity only against OGDC-E2 and/or BCOADC-E2 and no PDC-E2 autoantibodies. These patients will be overlooked in assays based on natural source-derived, predominantly PDC-E2-containing M2 antigen preparations.

    • Stability

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

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.

    • coating concentration

      0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with anti-M2-Antigen autoantibody-positive patient sera or monoclonal
      anti-hexa-His-tag antibody.

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    M2 Human
  • View Data Sheet

    Name :

    DUSP22 Human

    Description:

    Dual Specificity Phosphatase 22 Human Recombinant

    Dual specificity protein phosphatase 22, DUSP22, JNK-stimulatory phosphatase-1, JSP-1, Low molecular weight dual specificity phosphatase 2, LMW-DSP2, Mitogen-activated protein kinase phosphatase x, MAP kinase phosphatase x, MKP-x, LMWDSP2, MKPX, JKAP, JSP1, LMWDSP2, MKPX, VHX.

    Product # :

    ENZ-800

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    Description

    DUSP22 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-184 a.a.) and having a molecular mass of 23.3kDa.DUSP22 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DUSP22 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dual Specificity Phosphatase 22, also known as DUSP22, is a part of the protein-tyrosine phosphatase family which holds 1 tyrosine-protein phosphatase domain. DUSP22 activates the Jnk signaling pathway and dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK). DUSP22 interacts with MAPK1 and MAPK8.

    • Synonyms

      Dual specificity protein phosphatase 22, DUSP22, JNK-stimulatory phosphatase-1, JSP-1, Low molecular weight dual specificity phosphatase 2, LMW-DSP2, Mitogen-activated protein kinase phosphatase x, MAP kinase phosphatase x, MKP-x, LMWDSP2, MKPX, JKAP, JSP1, LMWDSP2, MKPX, VHX.

    • 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 MGSMGNGMNK ILPGLYIGNF KDARDAEQLS KNKVTHILSV HDSARPMLEG VKYLCIPAAD SPSQNLTRHF KESIKFIHEC RLRGESCLVH CLAGVSRSVT LVIAYIMTVT DFGWEDALHT VRAGRSCANP NVGFQRQLQE FEKHEVHQYR QWLKEEYGES PLQDAEEAKN ILAAPGILKF WAFLRRL.

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    Dusp22 Human
  • View Data Sheet

    Name :

    PHPT1 Human

    Description:

    Phosphohistidine Phosphatase 1 Human Recombinant

    PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    Product # :

    ENZ-012

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    Description

    PHPT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-125a.a.) and having a molecular mass of 15.9kDa.PHPT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHPT1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0) 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PHPT1 is a member of the Janus protein familyand is 125 amino acid long. PHPT1 appears as a monomer in the cytoplasm and is an EDTA-insensitive phosphohistidine phosphatase. Overexpression of PHPT1 resolts in specific phosphohistidine phosphatase activity towards phosphopeptide I, with no activity detected towards phosphotyrosine, phosphothreonine and phosphoserine peptides.

    • Synonyms

      PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    • 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 MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW ANDGY

    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.

    Phpt1 Human
  • View Data Sheet

    Name :

    GSTM3 Human

    Description:

    Glutathione S-Transferase MU 3 Human Recombinant

    Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.

    Product # :

    ENZ-592

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    • More Info

    Description

    GSTM3 Recombinant produced in E. coli is a single polypeptide chain containing 249 amino acids (1-225) and having a molecular mass of 29.1kDa.GSTM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GSTM3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl,
    1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GSTM3 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The mu type of enzymes takes part in the detoxification of electrophilic compounds, including therapeutic drugs, carcinogens, environmental toxins and products of oxidative stress, by conjugation with glutathione.

    • Synonyms

      Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione
      S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.

    • 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 MGSHMSCESS MVLGYWDIRG LAHAIRLLLE FTDTSYEEKR YTCGEAPDYD RSQWLDVKFK LDLDFPNLPY LLDGKNKITQ SNAILRYIAR KHNMCGETEE EKIRVDIIEN QVMDFRTQLI RLCYSSDHEK LKPQYLEELP GQLKQFSMFL GKFSWFAGEK LTFVDFLTYD ILDQNRIFDP KCLDEFPNLK AFMCRFEALE KIAAYLQSDQ FCKMPINNKM AQWGNKPVC

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    Gstm3 Human
  • View Data Sheet

    Name :

    SQSTM1 Human

    Description:

    Sequestosome 1 Human Recombinant

    A170, OSIL, p60, p62, p62B, PDB3, ZIP3, EBIAP, ORCA, OSIL, SQSTM1.

    Product # :

    PRO-806

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    Description

    SQSTM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 364 amino acids (1-356 a.a.) and having a molecular mass of 39.7 kDa. SQSTM1 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SQSTM1 Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SQSTM1 is an adapter protein which binds ubiquitin and mediates the activation of NFKB1 by TNF-a, NGF and IL-1. SQSTM1 is involved in titin/TTN downstream signaling in muscle cells. SQSTM1 controls signaling cascades through ubiquitination. SQSTM1 participates in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Mutations in UBA domain of the SQSTM1 protein cause Paget’s disease because the UBA is essential for aggregate sequestration and cell survival.

    • Synonyms

      A170, OSIL, p60, p62, p62B, PDB3, ZIP3, EBIAP, ORCA, OSIL, SQSTM1.

    • 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

      MAMSYVKDDI FRIYIKEKKE CRRDHRPPCA QEAPRNMVHP NVICDGCNGP VVGTRYKCSV CPDYDLCSVC EGKGLHRGHT KLAFPSPFGH LSEGFSHSRW LRKVKHGHFG WPGWEMGPPG NWSPRPPRAG EARPGPTAES ASGPSEDPSV NFLKNVGESV AAALSPLGIE VDIDVEHGGK RSRLTPVSPE SSSTEEKSSS QPSSCCSDPS KPGGNVEGAT QSLAEQMRKI ALESEGRPEE QMESDNCSGG DDDWTHLSSK EVDPSTGELQ SLQMPESEGP SSLDPSQEGP TGLKEAALYP HLPPEADPRL IESLSQMLSM GFSDEGGWLT RLLQTKNYDI GAALDTIQYS KHPPPLLEHH HHHH.

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    Sqstm1 Human
  • View Data Sheet

    Name :

    ALAD Human

    Description:

    Aminolevulinate Dehydratase Human Recombinant

    Aminolevulinate delta-dehydratase, ALADH, PBGS, Porphobilinogen synthase, delta-aminolevulinic acid dehydratase, EC 4.2.1.24.

    Product # :

    ENZ-586

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    • More Info

    Description

    ALAD Human Recombinant produced in E. coli is a single polypeptide chain containing 354 amino acids (1-330) and having a molecular mass of 38.8kDa.ALAD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ALAD form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins) by catalyzing the compression of 2 molecules of delta-aminolevulinate. ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is vital for enzymatic activity. ALAD has 8 identical subunits and its enzymatic activity is inhibited by lead. Mutations in the ALAD structural gene are the source for high sensitivity to lead poisoning and acute hepatic porphyria.

    • Synonyms

      Aminolevulinate delta-dehydratase, ALADH, PBGS, Porphobilinogen synthase, delta-aminolevulinic acid dehydratase, EC 4.2.1.24.

    • 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 MGSHMQPQSV LHSGYFHPLL RAWQTATTTL NASNLIYPIF VTDVPDDIQP ITSLPGVARY GVKRLEEMLR PLVEEGLRCV LIFGVPSRVP KDERGSAADS EESPAIEAIH LLRKTFPNLL VACDVCLCPY TSHGHCGLLS ENGAFRAEES RQRLAEVALA YAKAGCQVVA PSDMMDGRVE AIKEALMAHG LGNRVSVMSY SAKFASCFYG PFRDAAKSSP AFGDRRCYQL PPGARGLALR AVDRDVREGA DMLMVKPGMP YLDIVREVKD KHPDLPLAVY HVSGEFAMLW HGAQAGAFDL KAAVLEAMTA FRRAGADIII TYYTPQLLQW LKEE.

    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.

    Alad Human
  • View Data Sheet

    Name :

    FUT3 Human

    Description:

    Fucosyltransferase 3 Human Recombinant

    Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.

    Product # :

    ENZ-745

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    FUT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (35-361 a.a) and having a molecular mass of 40.6kDa.FUT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FUT3 solution (1mg/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

      Fucosyltransferase 3 (FUT3) catalyzes alpha-1, 3 and alpha-1, 4 glycosidic linkages which take part in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. FUT3 takes part in blood group Lewis determination; Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme. FUT3 also operates on the corresponding 1, 4-galactosyl derivative, creating1, 3-L-fucosyl links.

    • Synonyms

      Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.

    • 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 MGSRVSRDDA TGSPRAPSGS SRQDTTPTRP TLLILLWTWP FHIPVALSRC SEMVPGTADC HITADRKVYP QADTVIVHHW DIMSNPKSRL PPSPRPQGQR WIWFNLEPPP NCQHLEALDR YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH PPLNLSAKTE LVAWAVSNWK PDSARVRYYQ SLQAHLKVDV YGRSHKPLPK GTMMETLSRY KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD LARYLQELDK DHARYLSYFR WRETLRPRSF SWALDFCKAC WKLQQESRYQ TVRSIAAWFT.

    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.

    Fut3 Human
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