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1000 results found for “isomerase”
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Name :
CTSF HumanDescription:
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-738Price :
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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
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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.
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Synonyms
CATSF, CLN13, Cathepsin F, EC=3.4.22.41.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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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.
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Name :
NAA10 HumanDescription:
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-158Price :
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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
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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.
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Synonyms
N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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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.
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Name :
XPNPEP1 HumanDescription:
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-880Price :
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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
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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.
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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.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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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.
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Name :
LDHB Human, HisDescription:
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-539Price :
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Shipped with Ice Packs
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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
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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.
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Synonyms
LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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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.
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Name :
DHODH HumanDescription:
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-642Price :
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Shipped with Ice Packs
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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
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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.
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Synonyms
Dihydroorotate dehydrogenase (quinone), Dihydroorotate oxidase, human complement of yeast URA1, DHOdehase, POADS, EC 1.3.5.2, EC 1.3.3.1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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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.
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Name :
PGC HumanDescription:
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-966Price :
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Shipped with Ice Packs
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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
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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.
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Synonyms
Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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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.
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.
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Name :
LDHB MouseDescription:
Lactate Dehydrogenase B Mouse Recombinant
L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.
Product # :
ENZ-1052Price :
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Shipped with Ice Packs
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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
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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.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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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.
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.
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Name :
LIPG Human, HEKDescription:
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-810Price :
Quantity :
Shipping Method :
Shipped at Room temp
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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
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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.
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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.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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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.
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.
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Name :
HAGH HumanDescription:
Hydroxyacylglutathione Hydrolase Human Recombinant
GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.
Product # :
ENZ-034Price :
Quantity :
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Shipped with Ice Packs
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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
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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.
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Synonyms
GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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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.
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.
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Name :
TK1 HumanDescription:
Thymidine Kinase 1 Human Recombinant
Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.
Product # :
PKA-036Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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.
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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.
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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.
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.
- View Data Sheet
Name :
MDP1 HumanDescription:
Magnesium-Dependent Phosphatase 1 Human Recombinant
Magnesium-dependent phosphatase 1, MGC5987, MDP-1, FN6Pase, fructosamine-6-phosphatase, SFTB3, SFTPB, MDP1.
Product # :
ENZ-044Price :
Quantity :
Shipping Method :
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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.
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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.
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.
- View Data Sheet
Name :
AKR1A1 HumanDescription:
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-464Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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.
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Synonyms
Alcohol dehydrogenase, ALR, ARM, DD3, ALDR1, MGC1380, MGC12529, AKR1A1, Alcohol dehydrogenase [NADP+], Aldehyde reductase, Aldo-keto reductase family 1 member A1.
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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.
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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
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.
- View Data Sheet
Name :
DUSP18 Human, ActiveDescription:
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-1040Price :
Quantity :
Shipping Method :
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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.
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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
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.
- View Data Sheet
Name :
ACKA E.ColiDescription:
Acetate Kinase E.Coli Recombinant
Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.
Product # :
PKA-063Price :
Quantity :
Shipping Method :
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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.
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Synonyms
Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.
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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.
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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.
- View Data Sheet
Name :
HMGCL HumanDescription:
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-218Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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.
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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.
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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.
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.
- View Data Sheet
Name :
DUSP18 HumanDescription:
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-582Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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.
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.
- View Data Sheet
Name :
GLO1 MouseDescription:
Glyoxalase-I Mouse Recombinant
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
Product # :
ENZ-953Price :
Quantity :
Shipping Method :
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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
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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.
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Synonyms
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
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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.
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.
- View Data Sheet
Name :
M2 HumanDescription:
DLAT/DLST/BCOADC Recombinant Human
Product # :
ENZ-072Price :
Quantity :
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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.
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.
- View Data Sheet
Name :
DUSP22 HumanDescription:
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-800Price :
Quantity :
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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.
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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.
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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.
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.
- View Data Sheet
Name :
PHPT1 HumanDescription:
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-012Price :
Quantity :
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Shipped with Ice Packs
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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.
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Synonyms
PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.
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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.
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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.
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Name :
GSTM3 HumanDescription:
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-592Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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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
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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.
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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.
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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.
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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
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.
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Name :
SQSTM1 HumanDescription:
Sequestosome 1 Human Recombinant
A170, OSIL, p60, p62, p62B, PDB3, ZIP3, EBIAP, ORCA, OSIL, SQSTM1.
Product # :
PRO-806Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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
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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.
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Synonyms
A170, OSIL, p60, p62, p62B, PDB3, ZIP3, EBIAP, ORCA, OSIL, SQSTM1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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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.
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.
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Name :
ALAD HumanDescription:
Aminolevulinate Dehydratase Human Recombinant
Aminolevulinate delta-dehydratase, ALADH, PBGS, Porphobilinogen synthase, delta-aminolevulinic acid dehydratase, EC 4.2.1.24.
Product # :
ENZ-586Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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
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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.
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Synonyms
Aminolevulinate delta-dehydratase, ALADH, PBGS, Porphobilinogen synthase, delta-aminolevulinic acid dehydratase, EC 4.2.1.24.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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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.
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Name :
FUT3 HumanDescription:
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-745Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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
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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.
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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.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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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.