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1000 results found for “anti human enzyme”
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Name :
EPHX1 HumanDescription:
Epoxide Hydrolase 1 Microsomal Human Recombinant
Epoxide hydrolase 1, microsomal (xenobiotic), MEH, EPHX, EPOX, Epoxide hydratase, Microsomal epoxide hydrolase.
Product # :
ENZ-773Price :
Quantity :
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Shipped with Ice Packs
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Description
EPHX1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 451 amino acids (21-455a.a) and having a molecular mass of 52.2kDa. EPHX1 is fused to a 16 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EPHX1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Epoxide Hydrolase 1 Microsomal (EPHX1) is a vital biotransformation enzyme which transfers epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase plays a role in both activation and detoxification of epoxides. Mutations in EPHX1 trigger preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.
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Synonyms
Epoxide hydrolase 1, microsomal (xenobiotic), MEH, EPHX, EPOX, Epoxide hydratase, Microsomal epoxide hydrolase.
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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
MASMTGGQQM GRGSHMRDKE ETLPLEDGWW GPGTRSAARE DDSIRPFKVE TSDEEIHDLH QRIDKFRFTP PLEDSCFHYG FNSNYLKKVI SYWRNEFDWK KQVEILNRYP HFKTKIEGLD IHFIHVKPPQ LPAGHTPKPL LMVHGWPGSF YEFYKIIPLL TDPKNHGLSD EHVFEVICPS IPGYGFSEAS SKKGFNSVAT ARIFYKLMLR LGFQEFYIQG GDWGSLICTN MAQLVPSHVK GLHLNMALVL SNFSTLTLLL GQRFGRFLGL TERDVELLYP VKEKVFYSLM RESGYMHIQC TKPDTVGSAL NDSPVGLAAY ILEKFSTWTN TEFRYLEDGG LERKFSLDDL LTNVMLYWTT GTIISSQRFY KENLGQGWMT QKHERMKVYV PTGFSAFPFE LLHTPEKWVR FKYPKLISYS YMVRGGHFAA FEEPELLAQD IRKFLSVLER Q.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CNDP1 MouseDescription:
CNDP Dipeptidase 1 Mouse Recombinant
Beta-Ala-His dipeptidase, CNDP dipeptidase 1, Carnosine dipeptidase 1.
Product # :
ENZ-977Price :
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Description
CNDP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 500 amino acids (1-492 a.a.) and having a molecular mass of 56.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). CNDP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CNDP1 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
CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.
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Synonyms
Beta-Ala-His dipeptidase, CNDP dipeptidase 1, Carnosine dipeptidase 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
MFSSAHSGLL EKLFHYIDLH QDEFVQTLKE WVAIESDSVQ PVPRLRQKLF QMMALAADKL RNLGAGVESI DLGSQQMPDG QSLPIPPILL AELGSDPEKP TVCFYGHLDV QPAQKDDGWL TDPYTLTEVD GKLYGRGATD NKGPVLAWIN AVSTFRALQQ DLPVNIKLIL EGMEEAGSIA LEELVMREKD HFFSSVDYIV ISDNLWLSQR KPALTYGTRG NCYFTVEVKC RDQDFHSGTF GGILNEPMAD LVALLGSLVD SSGHILIPGI YDQMAPITEG EKTMYKNIDM DLEEYQNINQ VEKFLFDTKE ELLMHLWRYP SLSIHGIEGA FDEPGTKTVI PGRVLGKFSI RLVPTMSPSV VEKQVTQHLE AVFSKRNSFN KMAVSMVLGL HPWTANVNDT QYLAAQRTIK TVFGVNPDMI RDGSTIPIAK IFQAITQKSV MMLPLGAVDD GEHSQNEKIN RWNYIQGSKL FAAFFLELSK QHSGHQMPSS VYLEHHHHHH.
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 :
UBE2E3 HumanDescription:
Ubiquitin Conjugating Enzyme E2E3 Human Recombinant
UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.
Product # :
ENZ-906Price :
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Shipped with Ice Packs
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Description
UBE2E3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-207 a.a) and having a molecular mass of 25.3kDa.UBE2E3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2E3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
UBE2E3 or Ubiquitin-conjugating enzyme E2 E3 is part of the E2 ubiquitinconjugating enzyme family. UBE2E3 is needed for the destruction of mitotic cyclins and for cell cycle progression. The ubiquitination process covalently attaches to a short protein of 76 amino acids called ubiquitin, to a lysine residue on the target protein. When a protein has been tagged with one ubiquitin molecule, other rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein which grants passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.
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Synonyms
UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.
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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 MGSMSSDRQR SDDESPSTSS GSSDADQRDP AAPEPEEQEE RKPSATQQKK NTKLSSKTTA KLSTSAKRIQ KELAEITLDP PPNCSAGPKG DNIYEWRSTI LGPPGSVYEG GVFFLDITFS SDYPFKPPKV TFRTRIYHCN INSQGVICLD ILKDNWSPAL TISKVLLSIC SLLTDCNPAD PLVGSIATQY LTNRAEHDRI ARQWTKRYAT.
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 :
NUDT9 HumanDescription:
Nudix Type Motif 9 Human Recombinant
ADP-ribose pyrophosphatase mitochondrial, ADP-ribose diphosphatase, ADP-ribose phosphohydrolase, Adenosine diphosphoribose pyrophosphatase, ADPR-PPase, Nucleoside diphosphate-linked moiety X motif 9, Nudix motif 9, NUDT9, NUDT10, PSEC0099, UNQ3012/PRO9771.
Product # :
ENZ-137Price :
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Shipped with Ice Packs
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Description
NUDT9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (47-350 a.a.) and having a molecular mass of 36.5kDa (molecular weight on SDS-PAGE will appear higher).NUDT9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NUDT9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NUDT9 is a member of a superfamily of Nudix hydrolases. NUDT9 functions as a highly specific adenosine diphosphate ribose pyrophosphatase which hydrolyzes ADP ribose to AMP and ribose 5'-phosphate. In addition, NUDT9 may be involved in the regulation of the menstrual cycle and may be related to the proliferation of glandular cells in the human endometrium.
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Synonyms
ADP-ribose pyrophosphatase mitochondrial, ADP-ribose diphosphatase, ADP-ribose phosphohydrolase, Adenosine diphosphoribose pyrophosphatase, ADPR-PPase, Nucleoside diphosphate-linked moiety X motif 9, Nudix motif 9, NUDT9, NUDT10, PSEC0099, UNQ3012/PRO9771.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
NUDT9 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
MGSSHHHHHH SSGLVPRGSH MNTNVMSGSN GSKENSHNKA RTSPYPGSKV ERSQVPNEKV GWLVEWQDYK PVEYTAVSVL AGPRWADPQI SESNFSPKFN EKDGHVERKS KNGLYEIENG RPRNPAGRTG LVGRGLLGRW GPNHAADPII TRWKRDSSGN KIMHPVSGKH ILQFVAIKRK DCGEWAIPGG MVDPGEKISA TLKREFGEEA LNSLQKTSAE KREIEEKLHK LFSQDHLVIY KGYVDDPRNT DNAWMETEAV NYHDETGEIM DNLMLEAGDD AGKVKWVDIN DKLKLYASHS QFIKLVAEKR DAHWSEDSEA DCHAL.
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 :
CASP3 HumanDescription:
Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant
Caspase 3 Apoptosis-Related Cysteine Peptidase, CPP32 Caspase 3 Apoptosis-Related Cysteine Protease, Cysteine Protease CPP32, Protein Yama, CASP-3, CPP-32, SCA-1, SREBP Cleavage Activity 1, EC 3.4.22.56, CPP32B, caspase-3, PARP Cleavage Protease, procaspase3, Apopain, EC 3.4.22, CASP3.
Product # :
ENZ-791Price :
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Shipped with Ice Packs
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Description
CASP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 103 amino acids (176-277) and having a molecular mass of 12kDa.CASP3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CASP3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Caspase 3 Apoptosis-Related Cysteine Peptidase (CASP3) belongs to the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a key role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to generate 2 subunits, large and small, that dimerize to create the active enzyme. CASP3 protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. CASP3 is the leading caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is linked with neuronal death in Alzheimer's disease. In addition, CASP3 is involved in the cleavage of huntingtin. CASP3 also cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. CASP3 initiates cell adhesion in sympathetic neurons through RET cleavage.
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Synonyms
Caspase 3 Apoptosis-Related Cysteine Peptidase, CPP32 Caspase 3 Apoptosis-Related Cysteine Protease, Cysteine Protease CPP32, Protein Yama, CASP-3, CPP-32, SCA-1, SREBP Cleavage Activity 1, EC 3.4.22.56, CPP32B, caspase-3, PARP Cleavage Protease, procaspase3, Apopain, EC 3.4.22, CASP3.
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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
MSGVDDDMAC HKIPVEADFL YAYSTAPGYY SWRNSKDGSW FIQSLCAMLK QYADKLEFMH ILTRVNRKVA TEFESFSFDA TFHAKKQIPC IVSMLTKELY FYH.
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 :
GPX2 HumanDescription:
Glutathione Peroxidase 2 Human Recombinant
Glutathione peroxidase 2, GPx-2, GSHPx-2, Gastrointestinal glutathione peroxidase, Glutathione peroxidase-gastrointestinal, GPx-GI, GSHPx-GI, Glutathione peroxidase-related protein 2, GPRP-2, GPX2, GPRP, GI-GPx.
Product # :
ENZ-206Price :
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Shipped with Ice Packs
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Description
GPX2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-190) and having a molecular mass of 24.1kDa.GPX2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GPX2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Glutathione peroxidase 2 (GPX2) is a member of the glutathione peroxidase family, consisting of 8 known glutathione peroxidases (Gpx1-8) in humans. Glutathione peroxidase functions in the detoxification of hydrogen peroxide, and is one of the most important antioxidant enzymes in humans. GPX2 may have a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. GPX2 is one of only a few proteins known in higher vertebrates to contain selenocysteine, which appears at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA.
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Synonyms
Glutathione peroxidase 2, GPx-2, GSHPx-2, Gastrointestinal glutathione peroxidase, Glutathione peroxidase-gastrointestinal, GPx-GI, GSHPx-GI, Glutathione peroxidase-related protein 2, GPRP-2, GPX2, GPRP, GI-GPx.
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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 MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLC GTTTRDFTQL NELQCRFPRR LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT LVQKCEVNGQ NEHPVFAYLK DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV AWNFEKFLIG PEGEPFRRYS RTFPTINIEP DIKRLLKVAI.
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 :
CK2h HumanDescription:
Casein Kinase 2 Holoenzyme Human Recombinant
Casein Kinase 2 Holoenzyme, CK2h.
Product # :
PKA-211Price :
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Shipped with Ice Packs
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Description
Human recombinant casein kinase 2 holo enzyme containing alpha and beta subunits which were separately expressed in E. coli as non-fusion proteins and purified using several chromatographic steps. The holo enzyme has been reconstituted in the course of the purification and is highly active suitable for labelling CK2 substrates. CK2 holoenzyme is a non-glycosilated polypeptide having a molecular mass of 140 kDa.
Source
Escherichia Coli.
Formulation
CK2 Holoenzyme is supplied 0.5mg/1ml in 25mM Tris-HCl, 500mM NaCl, 1mM DTT, 500 µM PMSF, 5% glycerol, pH 8.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Synonyms
Casein Kinase 2 Holoenzyme, CK2h.
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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.Avoid multiple freeze-thaw cycles.
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Unit Definition
No protease activity detectable, specific activity > 1.3U/mg (1U = 1µmol/min at 37 degree C) using the synthetic peptide RRRDDDSDDD.
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 :
PI16 HumanDescription:
Peptidase Inhibitor 16 Human Recombinant
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
Product # :
ENZ-113Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.
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Synonyms
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized PI16 Human recombinant 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.
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 :
PTGES3 HumanDescription:
Prostaglandin E Synthase 3 Human Recombinant
TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.
Product # :
ENZ-458Price :
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Shipped with Ice Packs
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Description
Recombinant Human PTGES3 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 160 amino acids (1-160 a.a.) and having a molecular mass of 18.6 kDa.PTGES3 is purified by convential chromatogrpahy techniques.
Source
Escherichia Coli.
Formulation
The PTGES3 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT & 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PTGES3 takes part as a cochaperone and is involved in signal transduction.
PTGES3 is a molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexess. PTGES3 is necessary for appropriate functioning of the glucocorticoid and other steroid receptors.
PTGES3 localizes to genomic response elements in a hormone-dependent method and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. -
Synonyms
TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.
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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
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE.
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 :
HYKK HumanDescription:
Hydroxylysine Kinase Human Recombinant
Hydroxylysine kinase, AGPHD1, 5-hydroxy-L-lysine kinase, HYKK, Aminoglycoside phosphotransferase domain-containing protein 1.
Product # :
PKA-064Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HYKK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.3kDa.HYKK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
HYKK solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4), 40% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Hydroxylysine Kinase, also known as HYKK, is a Protein Coding gene. HYKK which is a part of the aminoglycoside phosphotransferase family catalyzes the GTPdependent phosphorylation of 5-hydroxy-L-lysine.
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Synonyms
Hydroxylysine kinase, AGPHD1, 5-hydroxy-L-lysine kinase, HYKK, Aminoglycoside phosphotransferase domain-containing protein 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 MGSMSSGNYQ QSEALSKPTF SEEQASALVE SVFGLKVSKV RPLPSYDDQN FHVYVSKTKD GPTEYVLKIS NTKASKNPDL IEVQNHIIMF LKAAGFPTAS VCHTKGDNTA SLVSVDSGSE IKSYLVRLLT YLPGRPIAEL PVSPQLLYEI GKLAAKLDKT LQRFHHPKLS SLHRENFIWN LKNVPLLEKY LYALGQNRNR EIVEHVIHLF KEEVMTKLSH FRECINHGDL NDHNILIESS KSASGNAEYQ VSGILDFGDM SYGYYVFEVA ITIMYMMIES KSPIQVGGHV LAGFESITPL TAVEKGALFL LVCSRFCQSL VMAAYSCQLY PENKDYLMVT AKTGWKHLQQ MFDMGQKAVE EIWFETAKSY ESGISM.
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 :
NDUFA4 HumanDescription:
NADH Dehydrogenase1 Alpha Subcomplex 4 Human Recombinant
NDUFA4, Mitochondrial Complex Associated, NADH-Ubiquinone Oxidoreductase MLRQ Subunit, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4, 9kDa, Complex I 9kDa Subunit, Complex I-MLRQ, CI-MLRQ, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4 (9kD, MLRQ), NADH Dehydrogenase [Ubiquinone] 1 Alpha Subcomplex Subunit 4, CI-9k, MLRQ, Cytochrome c oxidase subunit NDUFA4.
Product # :
ENZ-803Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NDUFA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 104 amino acids (1-81 a.a) and having a molecular mass of 11.8kDa. NDUFA4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NDUFA4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
NADH Dehydrogenase1 Alpha Subcomplex 4 (NDUFA4) is a member of the complex I 9kDa subunit family. Mammalian complex I of mitochondrial respiratory chain is comprised of 45 different subunits. NDUFA4 protein has NADH dehydrogenase activity and oxidoreductase activity. NDUFA4 transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the NDUFA4 enzyme is assumed to be ubiquinone.
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Synonyms
NDUFA4, Mitochondrial Complex Associated, NADH-Ubiquinone Oxidoreductase MLRQ Subunit, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4, 9kDa, Complex I 9kDa Subunit, Complex I-MLRQ, CI-MLRQ, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4 (9kD, MLRQ), NADH Dehydrogenase [Ubiquinone] 1 Alpha Subcomplex Subunit 4, CI-9k, MLRQ, Cytochrome c oxidase subunit NDUFA4.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLRQIIG QAKKHPSLIP LFVFIGTGAT GATLYLLRLA LFNPDVCWDR NNPEPWNKLG PNDQYKFYSV NVDYSKLKKE RPDF.
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 :
GSTT1 HumanDescription:
Glutathione S-Transferase Theta-1 Human Recombinant
Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.
Product # :
ENZ-429Price :
Quantity :
Shipping Method :
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Description
GSTT1 Human Recombinant fused with 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 277 amino acids (1-240 a.a.) and having a molecular mass of 31.5kDa.The GSTT1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTT1 solution contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GSTT1 belongs to a superfamily of proteins which catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. GSTT1 is one of the GSTs’ four main classes: alpha, mu, pi and theta (which includes GSTT1 and GSTT2). GSTT1 is involved in activation and detoxification reactions and catalyzes the conjugation of industrial chemicals, such as epoxybutane, ethylene oxides, halomethane with glutathione. GSTT1 is found in erythrocytes, at low levels in the liver as well as in Clara and ciliated cells at the alveolar/bronchiolar junction in the lung.
The GSTT1 gene is deficient in 38% of the population. The GSTTI enzyme deficiency might influence the individual risk for development of acquired aplastic anemia and acute myeloid leukemia. The presence or absence of the GSTT1 gene is concurrent with GSST1+ (the conjugator) and GSTT1- (the non-conjugator) phenotypes correspondingly. The GSTT1+ phenotype is able to catalyze the glutathione conjugation of dichloromethane. GSTT1-null genotypes are seen as having a higher risk of developing leukoplakia. Germline genetic polymorphism in GSTT1 is linked to breast cancer. -
Synonyms
Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMGL ELYLDLLSQP CRAVYIFAKK NDIPFELRIV DLIKGQHLSD ACAQVNPLKK VPALKDGDFT LTESVAILLY LTRKYKVPDY WYPQDLQARA RVDEYLAWQH TTLRRSCLRA LWHKVMFPVF LGEPVSPQTL AATLAELDVT LQLLEDKFLQ NKAFLTGPHI SLADLVAITE LMHPVGAGCQ VFEGRPKLAT WRQRVEAAVG EDLFQEAHEV ILKAKDFPPA DPTIKQKLMP WVLAMIR.
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 :
AKR1C3 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member C3 Human Recombinant, His Tag
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
Product # :
ENZ-406Price :
Quantity :
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Description
AKR1C3 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 39 kDa. The AKR1C3 is fused to a 20 amino acid His tag purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1C3 solution contains 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: approximately < 0.1 units/mg.
Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.More Info
-
Introduction
AKR1C3 is part of the aldo/keto reductase superfamily, which has at least 40 identified proteins. AKR1C3 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. AKR1C3 displays overlapping but distinct substrate specificity. AKR1C3 catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. AKR1C3 is involved in the pathogenesis of allergic diseases such as asthma. AKR1C3 controls cell growth and/or differentiation. AKR1C3 takes part in adrenal testosterone production. AKR1C3 expression is affected by metabolic disease, and its levels are considerably reduced in response to diet-induced weight loss and correlate with leptin levels.
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Synonyms
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
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Physical Appearance
Sterile Filtered clear colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKPGLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD RNLHYFNSDS FASHPNYPYS DEY.
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 :
LDHA MouseDescription:
Lactate Dehydrogenase A Mouse Recombinant
L-lactate dehydrogenase A chain, LDH-A, LDH muscle subunit, LDH-M.
Product # :
ENZ-952Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LDHA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 340 amino acids (1-332a.a.) and having a molecular mass of 37.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). LDHA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LDHA 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 > 250 units/mg, and is defined as the Amount of enzyme that convert 1.0 umole of pyruvate to L-lactate and per minute at pH 7.5 at 37C.More Info
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Introduction
LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.
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Synonyms
L-lactate dehydrogenase A chain, LDH-A, LDH muscle subunit, LDH-M.
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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.
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Amino Acid Sequence
MATLKDQLIV NLLKEEQAPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVMEDKLKG EMMDLQHGSL FLKTPKIVSS KDYCVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNIVKYSPH CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HALSCHGWVL GEHGDSSVPV WSGVNVAGVS LKSLNPELGT DADKEQWKEV HKQVVDSAYE VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGINEDVFLS VPCILGQNGI SDVVKVTLTP EEEARLKKSA DTLWGIQKEL QFLEHHHHHH.
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 :
UBE2L6 HumanDescription:
Ubiquitin Conjugating Enzyme E2L 6 Human Recombinant
RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.
Product # :
ENZ-347Price :
Quantity :
Shipping Method :
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Description
UBE2L6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-152 a.a.) & having a molecular mass of 21.7 kDa. The UBE2L6 is fused to a 36 amino acid His Tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris pH-8, 0.1mM PMSF, 1mM DTT, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UBE2L6 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2L6 enzyme is very similar in its primary structure to the enzyme encoded by UBE2L3 gene. UBE2L6 catalyzes the covalent attachment of ubiquitin to other proteins. UBE2L6 functions in the e6/e6-ap-induced ubiquitination of p53/tp53.
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Synonyms
RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASM RVVKELEDLQ KKPPPYLRNL SSDDANVLVW HALLLPDQPP YHLKAFNLRI SFPPEYPFKP PMIKFTTKIY HPNVDENGQI CLPIISSENW KPCTKTCQVL EALNVLVNRP NIREPLRMDL ADLLTQNPEL FRKNAEEFTL RFGVDRPS.
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 :
KLK15 Human, sf9Description:
Kallikrein-15 Human Recombinant, sf9
Kallikrein Related Peptidase 15, ACO Protease, Kallikrein-Like Serine Protease, Kallikrein 15, Kallikrein-15, Prostinogen, EC 3.4.21.4, EC 3.4.21.-, EC 3.4.21, HSRNASPH, ACO.
Product # :
ENZ-1047Price :
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Description
KLK15 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 249 amino acids (17-256a.a.) and having a molecular mass of 27.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).KLK15 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK15 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-15 (KLK15) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. KLK15 contains numerous polyadenylation sites and alternative splicing results in multiple transcript variants encoding different isoforms. KLK15 is over expressed in prostate cancer and therefore uses as a diagnostic or prognostic marker for prostate cancer.
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Synonyms
Kallikrein Related Peptidase 15, ACO Protease, Kallikrein-Like Serine Protease, Kallikrein 15, Kallikrein-15, Prostinogen, EC 3.4.21.4, EC 3.4.21.-, EC 3.4.21, HSRNASPH, ACO.
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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.
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Amino Acid Sequence
ADPQDGDKLL EGDECAPHSQ PWQVALYERG RFNCGASLIS PHWVLSAAHC QSRFMRVRLG EHNLRKRDGP EQLRTTSRVI PHPRYEARSH RNDIMLLRLV QPARLNPQVR PAVLPTRCPH PGEACVVSGW GLVSHNEPGT AGSPRSQVSL PDTLHCANIS IISDTSCDKS YPGRLTNTMV CAGAEGRGAE SCEGDSGGPL VCGGILQGIV SWGDVPCDNT TKPGVYTKVC HYLEWIRETM KRNHHHHHH.
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 :
POR Human, ActiveDescription:
P450 Oxidoreductase Human Recombinant, Active
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
Product # :
ENZ-1176Price :
Quantity :
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Description
POR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 686 amino acids (1-680a.a.) and having a molecular mass of 77.9kDa. POR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
POR protein solution (0.25mg/ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 4,000 pmol/min/mg. Defined by the amount of enzyme that reduction of 1 pmole cytochrome-C by NADPH/min. at pH-8 25C.
More Info
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Introduction
P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.
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Synonyms
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
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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
MINMGDSHVD TSSTVSEAVA EEVSLFSMTD MILFSLIVGL LTYWFLFRKK KEEVPEFTKI QTLTSSVRES SFVEKMKKTG RNIIVFYGSQ TGTAEEFANR LSKDAHRYGM RGMSADPEEY DLADLSSLPE IDNALVVFCM ATYGEGDPTD NAQDFYDWLQ ETDVDLSGVK FAVFGLGNKT YEHFNAMGKY VDKRLEQLGA QRIFELGLGD DDGNLEEDFI TWREQFWLAV CEHFGVEATG EESSIRQYEL VVHTDIDAAK VYMGEMGRLK SYENQKPPFD AKNPFLAAVT TNRKLNQGTE RHLMHLELDI SDSKIRYESG DHVAVYPAND SALVNQLGKI LGADLDVVMS LNNLDEESNK KHPFPCPTSY RTALTYYLDI TNPPRTNVLY ELAQYASEPS EQELLRKMAS SSGEGKELYL SWVVEARRHI LAILQDCPSL RPPIDHLCEL LPRLQARYYS IASSSKVHPN SVHICAVVVE YETKAGRINK GVATNWLRAK EPVGENGGRA LVPMFVRKSQ FRLPFKATTP VIMVGPGTGV APFIGFIQER AWLRQQGKEV GETLLYYGCR RSDEDYLYRE ELAQFHRDGA LTQLNVAFSR EQSHKVYVQH LLKQDREHLW KLIEGGAHIY VCGDARNMAR DVQNTFYDIV AELGAMEHAQ AVDYIKKLMT KGRYSLDVWS HHHHHH.
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 :
OLA1 HumanDescription:
Obg-Like ATPase 1 Human Recombinant
Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.
Product # :
ENZ-637Price :
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Description
OLA1 Human Recombinant produced in E. coli is a single polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 47.3kDa.OLA1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OLA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Obg-like ATPase 1 (OLA1) acts as a negative regulator of the cellular antioxidant response independent of transcriptional processes. OLA1 curbs the antioxidant response via nontranscriptional mechanisms. OLA1 hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. OLA1 is clearly down-regulated by DNA damage-inducing agents. OLA1 is expressed in all tissues; however it is more abundant in the testis, liver, lung, and brain. OLA1 is overexpressed in a number of malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.
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Synonyms
Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPPKKG GDGIKPPPII GRFGTSLKIG IVGLPNVGKS TFFNVLTNSQ ASAENFPFCT IDPNESRVPV PDERFDFLCQ YHKPASKIPA FLNVVDIAGL VKGAHNGQGL GNAFLSHISA CDGIFHLTRA FEDDDITHVE GSVDPIRDIE IIHEELQLKD EEMIGPIIDK LEKVAVRGGD KKLKPEYDIM CKVKSWVIDQ KKPVRFYHDW NDKEIEVLNK HLFLTSKPMV YLVNLSEKDY IRKKNKWLIK IKEWVDKYDP GALVIPFSGA LELKLQELSA EERQKYLEAN MTQSALPKII KAGFAALQLE YFFTAGPDEV RAWTIRKGTK APQAAGKIHT DFEKGFIMAE VMKYEDFKEE GSENAVKAAG KYRQQGRNYI VEDGDIIFFK FNTPQQPKKK.
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 :
NUDT1 HumanDescription:
Nudix Type Motif 1 Human Recombinant
7,8-dihydro-8-oxoguanine triphosphatase, 8-oxo-dGTPase, Nucleoside diphosphate-linked moiety X motif 1, Nudix motif 1, NUDT1, MTH1.
Product # :
ENZ-010Price :
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Description
NUDT1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 176 amino acids (1-156 a.a.) and having a molecular mass of 20.1kDa. The NUDT1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NUDT1 solution (1mg/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
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Introduction
NUDT1 is an enzyme that hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy rATP, to monophosphates, thereby preventing misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G transversions. NUDT1 is found mostly in the cytoplasm, with some in the mitochondria, suggesting that it is involved in the sanitization of nucleotide pools both for nuclear and mitochondrial genomes. Moreover, NUDT1 is expressed at much higher levels in proliferating cells than in resting cells. Misincorporation of oxidized nucleoside triphosphates into DNA/RNA during replication and transcription can cause mutations which may result in carcinogenesis or neurodegeneration.
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Synonyms
7,8-dihydro-8-oxoguanine triphosphatase, 8-oxo-dGTPase, Nucleoside diphosphate-linked moiety X motif 1, Nudix motif 1, NUDT1, MTH1.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGASRLYTLV LVLQPQRVLL GMKKRGFGAG RWNGFGGKVQ EGETIEDGAR RELQEESGLT VDALHKVGQI VFEFVGEPEL MDVHVFCTDS IQGTPVESDE MRPCWFQLDQ IPFKDMWPDD SYWFPLLLQK KKFHGYFKFQ GQDTILDYTL REVDTV.
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 :
TK1 HumanDescription:
Thymidine Kinase 1 Human Recombinant
Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.
Product # :
PKA-036Price :
Quantity :
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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
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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.
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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 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 :
DUSP26 HumanDescription:
Dual Specificity Phosphatase 26 Human Recombinant
Dual specificity protein phosphatase 26, Dual specificity phosphatase SKRP3, Low-molecular-mass dual-specificity phosphatase 4, DSP-4, LDP-4, Mitogen-activated protein kinase phosphatase 8, MAP kinase phosphatase 8, MKP-8, Novel amplified gene in thyroid anaplastic cancer, DUSP26, DUSP24, LDP4, MKP8, NATA1, SKRP3, Dual specificity phosphatase 26 (putative).
Product # :
ENZ-747Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
DUSP26 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-211a.a) and having a molecular mass of 26.3kDa.DUSP26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DUSP26 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Dual Specificity Phosphatase 26 (DUSP26) inhibits MAP kinase p38 by dephosphorylating it and inhibits p38-mediated apoptosis in anaplastic thyroid cancer cells. DUSP26 also induces activation of MAP kinase p38 and c-Jun N-terminal kinase. DUSP26 inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a decrease in its DNA-binding activity.
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Synonyms
Dual specificity protein phosphatase 26, Dual specificity phosphatase SKRP3, Low-molecular-mass dual-specificity phosphatase 4, DSP-4, LDP-4, Mitogen-activated protein kinase phosphatase 8, MAP kinase phosphatase 8, MKP-8, Novel amplified gene in thyroid anaplastic cancer, DUSP26, DUSP24, LDP4, MKP8, NATA1, SKRP3, Dual specificity phosphatase 26 (putative).
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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 MGSMCPGNWL WASMTFMARF SRSSSRSPVR TRGTLEEMPT VQHPFLNVFE LERLLYTGKT ACNHADEVWP GLYLGDQDMA NNRRELRRLG ITHVLNASHS RWRGTPEAYE GLGIRYLGVE AHDSPAFDMS IHFQTAADFI HRALSQPGGK ILVHCAVGVS RSATLVLAYL MLYHHLTLVE AIKKVKDHRG IIPNRGFLRQ LLALDRRLRQ GLEA.
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 :
CTSS HumanDescription:
Cathepsin-S Human Recombinant
Cathepsin S, MGC3886, CTSS, Cathepsin-S.
Product # :
ENZ-686Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
CTSS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (17-331) and having a molecular mass of 38.1kDa. CTSS is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTSS solution (1mg/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
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Introduction
Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.
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Synonyms
Cathepsin S, MGC3886, CTSS, Cathepsin-S.
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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 MQLHKDPTLD HHWHLWKKTY GKQYKEKNEE AVRRLIWEKN LKFVMLHNLE HSMGMHSYDL GMNHLGDMTS EEVMSLMSSL RVPSQWQRNI TYKSNPNWIL PDSVDWREKG CVTEVKYQGS CGACWAFSAV GALEAQLKLK TGKLVSLSAQ NLVDCSTEKY GNKGCNGGFM TTAFQYIIDN KGIDSDASYP YKAMDQKCQY DSKYRAATCS KYTELPYGRE DVLKEAVANK GPVSVGVDAR HPSFFLYRSG VYYEPSCTQN VNHGVLVVGY GDLNGKEYWL VKNSWGHNFG EEGYIRMARN KGNHCGIASF PSYPEI.
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 :
UBE2C HumanDescription:
Ubiquitin Conjugating enzyme E2C Human Recombinant
Ubiquitin-conjugating enzyme E2 C, EC 6.3.2.19, Ubiquitin-protein ligase C, Ubiquitin carrier protein C, Ubc10, UBCH10, dJ447F3.2.
Product # :
ENZ-346Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UBE2C Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-179) and having a molecular mass of 22.1 kDa.The UBE2C is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2C protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.15M NaCl, 1mM DTT and 10% Glycerol.
Purity
Greater than 90.0% as determined by Analysis by SDS-PAGE.
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Introduction
UbcH10 is an essential mediator of mitotic destruction events and cell cycle progression. It catalyzes the destruction of cyclins A and B in conjunction with the anaphase-promoting complex, and therefore, plays an important role in the control of the cell exit from mitosis This activity is essential at then end of mitosis for the inactivation of their partner kinase Cdc2 and exit from mitosis into G1 of the next cell cycle. In addition, UbcH10 bears homology to yeast PAS2, a gene that is essential for biogenesis of peroxisomes. UbcH10 is useful for in vitro ubiquitinylation reactions.
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Synonyms
Ubiquitin-conjugating enzyme E2 C, EC 6.3.2.19, Ubiquitin-protein ligase C, Ubiquitin carrier protein C, Ubc10, UBCH10, dJ447F3.2.
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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 MGSMASQNRD PAATSVAAAR KGAEPSGGAA RGPVGKRLQQ ELMTLMMSGD KGISAFPESD NLFKWVGTIH GAAGTVYEDL RYKLSLEFPS GYPYNAPTVK FLTPCYHPNV DTQGNICLDI LKEKWSALYD VRTILLSIQS LLGEPNIDSP LNTHAAELWK NPTAFKKYLQ ETYSKQVTSQ EP
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 :
AKR1D1 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member D1 Human Recombinant, His Tag
3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-keto reductase family 1 member D1, Delta(4)-3-ketosteroid 5-beta-reductase, Delta(4)-3-oxosteroid 5-beta-reductase, KR1D1, SRD5B1, CBAS2, 3o5bred.
Product # :
ENZ-098Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AKR1D1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 346 amino acids (1-326 a.a.) and having a molecular mass of 39.5kDa. The AKR1D1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1D1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Aldo-keto reductase family 1 member D1 (AKR1D1) belongs to the AKR superfamily. The AKR family proteins are soluble NADPH oxidoreductases, which have vital roles in the metabolism of drugs, carcinogens and reactive aldehydes. AKR1D1 is also responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones that carry a delta (4)-3-1 structure. AKR1D1 is highly expressed in the liver, colon and testis. Deficiency of the AKR1D1 enzyme may contribute to hepatic dysfunction.
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Synonyms
3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-keto reductase family 1 member D1, Delta(4)-3-ketosteroid 5-beta-reductase, Delta(4)-3-oxosteroid 5-beta-reductase, KR1D1, SRD5B1, CBAS2, 3o5bred.
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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 MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE ALNKNVRFVE LLMWRDHPEY PFHDEY.
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.