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1000 results found for “Mutase”
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Name :
FOLH1 HumanDescription:
Folate Hydrolase 1 Human Recombinant
Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA
Product # :
ENZ-1170Price :
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Description
FOLH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 717 amino acids (44-750 a.a) and having a molecular mass of 80.7kDa.FOLH1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FOLH1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
FOLH1, also known as glutamate carboxypeptidase 2 (GCPII), is a single pass type 2 membrane protein which belongs to the peptidase M28 family. FOLH1 is highly produced in prostate epithelium. FOLH1 is also found in ovary, live, stomach, small intestine colon, urinary bladder, kidney, testis, and the capillary endothelium of a variety of tumours. Therefore, it plays a role in directed imaging and therapy of recurrent of metastatic disease. FOLH1 is a zinc metalloenzyme that resides in membranes and catalyses the hydrolysis of N-acetylaspartylglutamate to glutamate and N-acetylaspartate.
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Synonyms
Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA
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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
ADPMKSSNEA TNITPKHNMK AFLDELKAEN IKKFLYNFTQ IPHLAGTEQN FQLAKQIQSQ WKEFGLDSVE LAHYDVLLSY PNKTHPNYIS IINEDGNEIF NTSLFEPPPP GYENVSDIVP PFSAFSPQGM PEGDLVYVNY ARTEDFFKLE RDMKINCSGK IVIARYGKVF RGNKVKNAQL AGAKGVILYS DPADYFAPGV KSYPDGWNLP GGGVQRGNIL NLNGAGDPLT PGYPANEYAY RRGIAEAVGL PSIPVHPIGY YDAQKLLEKM GGSAPPDSSW RGSLKVPYNV GPGFTGNFST QKVKMHIHST NEVTRIYNVI GTLRGAVEPD RYVILGGHRD SWVFGGIDPQ SGAAVVHEIV RSFGTLKKEG WRPRRTILFA SWDAEEFGLL GSTEWAEENS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVHNLTK ELKSPDEGFE GKSLYESWTK KSPSPEFSGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWETNKFSGY PLYHSVYETY ELVEKFYDPM FKYHLTVAQV RGGMVFELAN SIVLPFDCRD YAVVLRKYAD KIYSISMKHP QEMKTYSVSF DSLFSAVKNF TEIASKFSER LQDFDKSNPI VLRMMNDQLM FLERAFIDPL GLPDRPFYRH VIYAPSSHNK YAGESFPGIY DALFDIESKV DPSKAWGEVK RQIYVAAFTV QAAAETLSEV AHHHHHH
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 :
PRCP HumanDescription:
Prolylcarboxypeptidase Human Recombinant
Angiotensinase-C, PRCP, Proline Carboxypeptidase.
Product # :
ENZ-1178Price :
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Description
PRCP Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-496 a.a) containing a total of 481 amino acids, having a molecular mass of 54.3 kDa. PRCP is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The PRCP solution (0.25mg/ml) contains 30% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3,000 pmol/min/μg, and is defined as the amount of enzyme that converts 1pmole of Z-ProAla-OH/min. at pH-4 at 25˚C.
More Info
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Introduction
PRCP is a plasma protein which takes part in the cleavage of C-terminal amino acids linked to proline in proteinfor example angiotensin-2 & 3 at acidic pHenvironment rather than at neutral pHwhich exhibit less activity. This cleavage is important since Angiotensin-2 takes part in regulation of blood pressure & electrolyte balance which is essential to hypertension.
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Synonyms
Angiotensinase-C, PRCP, Proline Carboxypeptidase.
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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
LRPALRALGS LHLPTNPTSL PAVAKNYSVL YFQQKVDHFG FNTVKTFNQR YLVADKYWKK NGGSILFYTG NEGDIIWFCN NTGFMWDVAE ELKAMLVFAE HRYYGESLPF GDNSFKDSRH LNFLTSEQAL ADFAELIKHL KRTIPGAENQ PVIAIGGSYG GMLAAWFRMK YPHMVVGALA ASAPIWQFED LVPCGVFMKI VTTDFRKSGP HCSESIHRSW DAINRLSNTG SGLQWLTGALHLCSPLTSQD IQHLKDWISE TWVNLAMVDY PYASNFLQPL PAWPIKVVCQ YLKNPNVSDS LLLQNIFQAL NVYYNYSGQV KCLNISETAT SSLGTLGWSY QACTEVVMPF CTNGVDDMFE PHSWNLKELS DDCFQQWGVR PRPSWITTMY GGKNISSHTN IVFSNGELDP WSGGGVTKDI TDTLVAVTIS EGAHHLDLRT KNALDPMSVL LARSLEVRHM KNWIRDFYDS AGKQ 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.
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Name :
CKMT3 HumanDescription:
Creatine Kinase Muscle Type-3 Human Recombinant
Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.
Product # :
CKI-272Price :
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Description
CKMT3 Human Recombinant produced in Pichia Pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to MM Isoenzyme in ELISA.The CKMT3 is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
Each mg of protein contains 20mM Tris pH-8, 1mM EDTA and 1mM DTT.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 500 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 2,000ng/ml.More Info
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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
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Synonyms
Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBA3 HumanDescription:
Ubiquitin-Like Modifier Activating Enzyme 3 Human Recombinant
NEDD8-activating enzyme E1 catalytic subunit, NEDD8-activating enzyme E1C, Ubiquitin-activating enzyme E1C, Ubiquitin-like modifier-activating enzyme 3, Ubiquitin-activating enzyme 3, UBA3, UBE1C, hUBA3.
Product # :
ENZ-576Price :
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Description
UBA3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 487 amino acids (1-463) and having a molecular mass of 54.4kDa.UBA3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBA3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NEDD8-activating enzyme E1 catalytic subunit (UBA3) is the catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme, which belongs to the E1 ubiquitin-activating enzyme family. E1 activates NEDD8 by initially adenylating its C-terminal glycine residue with ATP, afterwards linking this residue to the side chain of the catalytic cysteine, generating a NEDD8-UBA3 thioester and free AMP. E1 at last transfers NEDD8 to the catalytic cysteine of UBE2M. The UBA3 enzyme connects with AppBp1, an amyloid beta precursor protein binding protein, to form a heterodimer, and at that point the enzyme complex activates NEDD8, a ubiquitin-like protein, which controls cell division, signaling and embryogenesis.
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Synonyms
NEDD8-activating enzyme E1 catalytic subunit, NEDD8-activating enzyme E1C, Ubiquitin-activating enzyme E1C, Ubiquitin-like modifier-activating enzyme 3, Ubiquitin-activating enzyme 3, UBA3, UBE1C, hUBA3.
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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 MGSHMADGEE PERKRRRIEE LLAEKMAVDG GCGDTGDWEG RWNHVKKFLE RSGPFTHPDF EPSTESLQFL LDTCKVLVIG AGGLGCELLK NLALSGFRQI HVIDMDTIDV SNLNRQFLFR PKDIGRPKAE VAAEFLNDRV PNCNVVPHFN KIQDFNDTFY RQFHIIVCGL DSIIARRWIN GMLISLLNYE DGVLDPSSIV PLIDGGTEGF KGNARVILPG MTACIECTLE LYPPQVNFPM CTIASMPRLP EHCIEYVRML QWPKEQPFGE GVPLDGDDPE HIQWIFQKSL ERASQYNIRG VTYRLTQGVV KRIIPAVAST NAVIAAVCAT EVFKIATSAY IPLNNYLVFN DVDGLYTYTF EAERKENCPA CSQLPQNIQF SPSAKLQEVL DYLTNSASLQ MKSPAITATL EGKNRTLYLQ SVTSIEERTR PNLSKTLKEL GLVDGQELAV ADVTTPQTVL FKLHFTS.
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 :
PLA2G7 Human, HEKDescription:
Secreted Phospholipase A2-VII Human Recombinant, HEK
Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.
Product # :
ENZ-736Price :
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Description
Recombinant Human PLA2G7 produced in HEK293 cells is a polypeptide chain (22-441 a.a), fused to an 8 amino acid His-tag at C-terminus, containing a total of 428 amino acids. PLA2G7 is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
The PLA2G7 is supplied as a 0.2µm filtered solution in 20mM HAc-NaCl, 150mM NaCl and 10% Glycerol, pH 4.5.
Purity
Greater than 95% as determined by SEC-HPLC and SDS-PAGE.
More Info
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Introduction
PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population. -
Synonyms
Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.
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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.Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
FDWQYINPVAHMKSSAWVNKIQVLMAAASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPS
QDNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNILRLLFGSMTTPANWNSPLRPGEKYPLVVFSHGL
GAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWLYLRTLKQEEETHIRN
EQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLSE
DQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVH
QNFADFTFATGKIIGHMLKLKGDIDSNAAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENLI
PGTNINTTNQHIMLQNSSGIEKYNVDHHHHHH.
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 :
EPHX1 Human, Sf9Description:
Epoxide Hydrolase 1 Microsomal Human Recombinant, sf9
Epoxide hydrolase 1, Epoxide hydratase, Microsomal epoxide hydrolase, Meh, EPHX1, EPHX, EPOX, Epoxide Hydrolase 1 Microsomal, Microsomal Epoxide Hydrolase, EC 3.3.2.9, HYL1
Product # :
ENZ-1076Price :
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Description
EPHX1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 442 amino acids (21-455 a.a.) and having a molecular mass of 51.5kDaEPHX1 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
EPHX1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 50% glycerol,1mM DTT and 0.1M NaCl.
Purity
Greater than 85% 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, Epoxide hydratase, Microsomal epoxide hydrolase, Meh, EPHX1, EPHX, EPOX, Epoxide Hydrolase 1 Microsomal, Microsomal Epoxide Hydrolase,
EC 3.3.2.9, HYL1 -
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
MRDKEETLPL EDGWWGPGTR SAAREDDSIR PFKVETSDEE IHDLHQRIDK FRFTPPLEDS CFHYGFNSNY LKKVISYWRN EFDWKKQVEI LNRYPHFKTK IEGLDIHFIH VKPPQLPAGH TPKPLLMVHG WPGSFYEFYK IIPLLTDPKN HGLSDEHVFE VICPSIPGYG FSEASSKKGF NSVATARIFY KLMLRLGFQE FYIQGGDWGS LICTNMAQLV PSHVKGLHLN MALVLSNFST LTLLLGQRFG RFLGLTERDV ELLYPVKEKV FYSLMRESGY MHIQCTKPDT VGSALNDSPV GLAAYILEKF STWTNTEFRY LEDGGLERKF SLDDLLTNVM LYWTTGTIIS SQRFYKENLG QGWMTQKHER MKVYVPTGFS AFPFELLHTP EKWVRFKYPK LISYSYMVRG GHFAAFEEPE LLAQDIRKFL SVLERQHHHH 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.
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Name :
CA10 HumanDescription:
Carbonic Anhydrase X Human Recombinant
Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.
Product # :
ENZ-1189Price :
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Description
CA10 Human Recombinant is a single, glycosylated polypeptide chain containing 317 amino acids (22-328a.a) and having a molecular mass of 36.3kDa (calculated). CA10 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
CA10 protein solution (0.5mg/ml) is filtered in Phosphate-Buffered Saline pH 7.4 and 10% (w/v) glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH8.0 at 37℃.
More Info
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Synonyms
Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.
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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. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
DGSMQQNSPK IHEGWWAYKE VVQGSFVPVP SFWGLVNSAW NLCSVGKRQS PVNIETSHMI FDPFLTPLRI NTGGRKVSGT MYNTGRHVSL RLDKEHLVNI SGGPMTYSHR LEEIRLHFGS EDSQGSEHLL NGQAFSGEVQ LIHYNHELYT NVTEAAKSPN GLVVVSIFIK VSDSSNPFLN RMLNRDTITR ITYKNDAYLL QGLNIEELYP ETSSFITYDG SMTIPPCYET ASWIIMNKPV YITRMQMHSL RLLSQNQPSQ IFLSMSDNFR PVQPLNNRCI RTNINFSLQG KDCPNNRAQK LQYRVNEWLL KHHHHHH
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Background
Carbonic anhydrases (CAs) are a family of enzymes that play a crucial role in regulating pH balance and carbon dioxide transport in various tissues and organs. Carbonic anhydrase X (CA10) is a less-studied member of this family, and this research aims to explore its structure, function, and implications in metabolism and disease. Understanding the molecular mechanisms and regulatory roles of CA10 can provide valuable insights into its potential as a therapeutic target for various disorders.
Structure and Expression of Carbonic Anhydrase X:
CA10, also known as mitochondrial carbonic anhydrase, is a membrane-associated protein predominantly found in the mitochondria of various tissues, including the liver, kidney, and brain. It possesses the characteristic zinc-binding catalytic domain found in other CAs. However, CA10 has distinct features, including a unique N-terminal mitochondrial targeting sequence, suggesting its specific role within mitochondria.
Role of Carbonic Anhydrase X in Metabolism:
CA10 is involved in the regulation of pH and bicarbonate concentrations within the mitochondrial matrix, impacting mitochondrial metabolism. It catalyzes the reversible hydration of carbon dioxide to bicarbonate, facilitating the exchange of carbon dioxide between the mitochondria and the cytoplasm. This process is vital for maintaining acid-base homeostasis and efficient energy production through oxidative phosphorylation.
Implications of Carbonic Anhydrase X in Disease:
Emerging evidence suggests that CA10 may be implicated in various pathological conditions. Alterations in CA10 expression or activity have been associated with metabolic disorders, including obesity and diabetes. Furthermore, dysregulation of mitochondrial function and pH homeostasis, in which CA10 plays a role, have been linked to neurodegenerative diseases, cancer, and cardiovascular disorders. Elucidating the precise contributions of CA10 in these pathologies is an area of active investigation.
Therapeutic Potential of Carbonic Anhydrase X:
The unique properties and expression patterns of CA10 make it an intriguing target for therapeutic interventions. Modulating CA10 activity or expression could have implications in metabolic disorders, where the manipulation of mitochondrial function and pH regulation could offer therapeutic benefits. Developing selective inhibitors or activators of CA10 could be explored to regulate its enzymatic activity and modulate mitochondrial metabolism.
Challenges and Future Directions:
Although CA10 shows promise as a therapeutic target, several challenges remain. The elucidation of the precise regulatory mechanisms and signaling pathways involving CA10 within mitochondria is necessary for a comprehensive understanding of its function. Additionally, the development of specific modulators that selectively target CA10 without affecting other CAs or disrupting physiological processes is a critical consideration.
Conclusion:
The study of CA10 protein provides valuable insights into its distinct role in mitochondrial metabolism and disease pathogenesis. Understanding the molecular mechanisms and functional implications of CA10 opens avenues for the development of targeted therapies for metabolic disorders, neurodegenerative diseases, cancer, and cardiovascular disorders. Further research on CA10, its interactions, and its modulation in pathological conditions will contribute to the development of novel therapeutic interventions to improve patient outcomes.
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 :
LCAT Human, HEKDescription:
Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Product # :
ENZ-254Price :
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Shipping Method :
Shipped at Room temp
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Description
LCAT Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 429 amino acids (25-440) which includes a 13 amino acid Flag Tag fused at N-terminus and having a total molecular mass of 48.5 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.
Source
Human Embryonic Kidney 293 cells
Formulation
The LCAT protein was lyophilized from 0.4um filtered solution at a concentration of 0.5mg/ml containing 20mM Tris buffer, and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
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Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LCAT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCAT should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. LCAT HEK 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
HVDYKDDDDK PAGFWLLNVL FPPHTTPKAE LSNHTRPVIL VPGCLGNQLE AKLDKPDVVN WMCYRKTEDF FTIWLDLNMF LPLGVDCWID NTRVVYNRSS GLVSNAPGVQ IRVPGFGKTY SVEYLDSSKL AGYLHTLVQN LVNNGYVRDE TVRAAPYDWR LEPGQQEEYY RKLAGLVEEM HAAYGKPVFL IGHSLGCLHL LYFLLRQPQA WKDRFIDGFI SLGAPWGGSI KPMLVLASGD NQGIPIMSSI KLKEEQRITT TSPWMFPSRM AWPEDHVFIS TPSFNYTGRD FQRFFADLHF EEGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPRTYIY DHGFPYTDPV GVLYEDGDDT VATRSTELCG LWQGRQPQPV HLLPLHGIQH LNMVFSNLTL EHINAILLGA YRQGPPASPT ASPEPPPPE
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 :
IDO1 Human, ActiveDescription:
Indoleamine 2,3-Dioxygenase 1 Human Recombinant, Active
IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.
Product # :
ENZ-1012Price :
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Description
IDO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403a.a) and having a molecular mass of 47.7kDa. IDO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDO1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 300 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of L-Tryptophan to N-formyl-Lkynurenine per minute at pH 6.5 at 25C.More Info
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Introduction
Indoleamine 2,3-Dioxygenase 1 (IDO1) catalyzes the primary and rate-limiting stage in tryptophan catabolism to N-formyl-kynurenine. IDO1 affects on various tryptophan substrates including D-tryptophan, and serotonin and is expressed in dendritic cells, monocytes, and macrophages. IDO1 takes part in a range of pathophysiological processes like neuropathology, antimicrobial and antitumor defense, immunoregulation, and antioxidant activity. IDO1 regulates T-cell behavior by its pericellular catabolization of the necessary amino acid tryptophan.
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Synonyms
IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.
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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 MGSMAHAMEN SWTISKEYHI DEEVGFALPN PQENLPDFYN DWMFIAKHLP DLIESGQLRE RVEKLNMLSI DHLTDHKSQR LARLVLGCIT MAYVWGKGHG DVRKVLPRNI AVPYCQLSKK LELPPILVYA DCVLANWKKK DPNKPLTYEN MDVLFSFRDG DCSKGFFLVS LLVEIAAASA IKVIPTVFKA MQMQERDTLL KALLEIASCL EKALQVFHQI HDHVNPKAFF SVLRIYLSGW KGNPQLSDGL VYEGFWEDPK EFAGGSAGQS SVFQCFDVLL GIQQTAGGGH AAQFLQDMRR YMPPAHRNFL CSLESNPSVR EFVLSKGDAG LREAYDACVK ALVSLRSYHL QIVTKYILIP ASQQPKENKT SEDPSKLEAK GTGGTDLMNF LKTVRSTTEK SLLKEG.
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 :
GSTA1 MouseDescription:
Glutathione S-Transferase Alpha 1 Mouse Recombinant
Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.
Product # :
ENZ-873Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GSTA1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.a) and having a molecular mass of 28kDa.GSTA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GSTA1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity is defined as the amount of enzyme that conjugate 1.0 pmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C and is > 4,000 pmol/min/ug.
More Info
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Introduction
Membrane-bound & Cytosolic forms of GST are encoded by 2 separate supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. There are 8 different classes of soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTA1 is found in a cluster mapped to chromosome 6, and is highly expressed in the liver. GSTA1 protects the cells from reactive oxygen species.
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Synonyms
Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.
-
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 MGSMAGKPVL HYFNARGRME CIRWLLAAAG VEFEEKFIQS PEDLEKLKKD GNLMFDQVPM VEIDGMKLAQ TRAILNYIAT KYDLYGKDMK ERALIDMYSE GILDLTEMIG QLVLCPPDQR EAKTALAKDR TKNRYLPAFE KVLKSHGQDY LVGNRLTRVD IHLLEVLLYV EEFDASLLTP FPLLKAFKSR ISSLPNVKKF LQPGSQRKPP MDAKQIQEAR KAFKIQ.
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 :
KLK2 Human, sf9Description:
Kallikrein-2 Human Recombinant, sf9
hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.
Product # :
ENZ-971Price :
Quantity :
Shipping Method :
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Description
KLK2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 246 amino acids (25-261 aa) and having a molecular mass of 27.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).KLK2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
KLK2 is a part of the grandular kallikrein protein family whose Members are engaged in a diverse array of biological functions. Kallikreins are a subgroup of serine proteases which are clustered on chromosome 19. KLK2 is a highly active trypsin-like serine protease which selectively cleaves at arginine remains. KLK2 is mostly expressed in prostatic tissue and is accountable for cleaving pro-prostate-specific antigen into its enzymatically active form. KLK2 is greatly expressed in prostate tumor cells and may possibly be a prognostic maker for prostate cancer risk.
-
Synonyms
hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADPIVGGWEC EKHSQPWQVA VYSHGWAHCG GVLVHPQWVL TAAHCLKKNS QVWLGRHNLF EPEDTGQRVP VSHSFPHPLY NMSLLKHQSL RPDEDSSHDL MLLRLSEPAK ITDVVKVLGL PTQEPALGTT CYASGWGSIE PEEFLRPRSL QCVSLHLLSN DMCARAYSEK VTEFMLCAGL WTGGKDTCGG DSGGPLVCNG VLQGITSWGP EPCALPEKPA VYTKVVHYRK WIKDTIAANP HHHHHH
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 :
ADH1A Human, sf9Description:
Alcohol Dehydrogenase 1A, Human Recombinant, sf9
ADH1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1.
Product # :
ENZ-1009Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ADH1A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 381 amino acids (1-375) and having a molecular mass of 40.6kDa. ADH1A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ADH1A protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
-
Introduction
Alcohol dehydrogenase 1A (ADH1A) is a member of the alcohol dehydrogenase family. ADH1A has a key role in ethanol metabolism. ADH1A along with coenzyme NAD catalyzes the reversible conversion of organic alcohols to ketones or aldehydes. The physiologic function of ADH1A in the liver is the elimination of ethanol formed by microorganisms in the intestinal tract. ADH1A is monomorphic and predominant in fetal and infant livers, growing to be less active in gestation and only weakly active during adulthood.
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Synonyms
ADH1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1.
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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.
-
Amino Acid Sequence
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV LPFEKINEGF DLLHSGKSIR TILMFHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EOGT MouseDescription:
EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase Mouse Recombinant
EGF domain-specific O-linked N-acetylglucosamine transferase, Extracellular O-linked N-acetylglucosamine transferase.
Product # :
ENZ-946Price :
Quantity :
Shipping Method :
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Description
EOGT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 516 amino acids (20-527 a.a.) and having a molecular mass of 60.4kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). EOGT is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EOGT protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase (EOGT) takes part in the regulation of Notch receptor. EOGT catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine/ threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). EOGT mainly glycosylates the Thr residue positioned between the fifth and sixth conserved cysteines of folded EGF-like domains.
-
Synonyms
EGF domain-specific O-linked N-acetylglucosamine transferase, Extracellular O-linked N-acetylglucosamine transferase.
-
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
DKAHSEADDA PGKALYDYSS LRLPAEHIPF FLHNNRHVAS VCREDSHCPY KKHLENLNYC WGYEKSCAPE FRFGSPVCSY VDLGWTDTLE SAQDMFWRQA DFGYARERLG EIRTICQPER ASDSSLVCSR YLQYCRATGL YLDLRNIKRN HDRFKEDFLQ GGEIGGYCKL DSHALVSEGQ RKSPLQSWFA ELQGYTQLNF RPIEDAKCDI VVEKPTYFMK LDAGINMYHH FCDFLNLYLT QHVNNSFSTD VYIVMWDTST YGYGDLFSDT WKAFTDYDVI HLKTYDSKKV CFKEAVFSLL PRMRYGLFYN TPLISGCQNT GLFRAFSQHV LHRLNITQEG PKDGKVRVTI LARSTEYRKI LNQDELVNAL KTVSTFEVRV VDYKYRELGF LDQLRITHNT DIFIGMHGAG LTHLLFLPDW AAVFELYNCE DERCYLDLAR LRGIHYITWR KPSKVFPQDK GHHPTLGEHP KFTNYSFDVE EFMYLVLQAA EHVLQHPQWP FKKKHDELLE 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 :
FDFT1 HumanDescription:
Farnesyl-Diphosphate Farnesyltransferase 1 Human Recombinant
Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.
Product # :
ENZ-820Price :
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Description
FDFT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-283 a.a) and having a molecular mass of 35.4 kDa. FDFT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FDFT1 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Farnesyl-Diphosphate Farnesyltransferase 1, also known as FDFT1 is a membrane-associated enzyme sited at a branch point in the mevalonate pathway. FDFT1belongs to the phytoene/squalene synthase family. FDFT1 is the 1st specific enzyme in cholesterol biosynthesis, which catalyzes the dimerization of 2 molecules of farnesyl diphosphate in a two-step reaction to form squalene.
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Synonyms
Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.
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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 MGSMEFVKCL GHPEEFYNLV RFRIGGKRKV MPKMDQDSLS SSLKTCYKYL NQTSRSFAAV IQALDGEMRN AVCIFYLVLR ALDTLEDDMT ISVEKKVPLL HNFHSFLYQP DWRFMESKEK DRQVLEDFPT ISLEFRNLAE KYQTVIADIC RRMGIGMAEF LDKHVTSEQE WDKYCHYVAG LVGIGLSRLF SASEFEDPLV GEDTERANSM GLFLQKTNII RDYLEDQQGG REFWPQEVWS RYVKKLGDFA KPENIDLAVQ CLNELITNAL HHIPDVITYL SRLRNQ.
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 :
GPBB HumanDescription:
Glycogen Phosphorylase Human Recombinant
Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.
Product # :
ENZ-282Price :
Quantity :
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Description
Glycogen Phosphorylase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain. The Human GPBB mature chain: 2 - 843 aa; that is a total of 842 aa having a molecular mass of 96695.96 Dalton. The theoretical pI is 6.40.The GPBB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of protein contains 50% glycerol.
Purity
Greater than 85.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Glycogen phosphorylase is one of the phosphorylaseenzymes(EC2.4.1.1). It breaks up glycogeninto glucosesubunits. Glycogenis left with one less glucosemolecule, and the free glucosemolecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphateby the enzyme phosphoglucomutase.
Glycogen phosphorylase can only act on linearchainsof glycogen(a 1-4 glycosidic linkage). Its work will immediately come to a halt four residues away from a 1-6 branch(which are exceedingly common in glycogen). In these situations, a debranching enzymeis necessary, which will straighten out the chain in that area. Additionally, an alpha 1-6 glucosidaseenzymeis required to break the remaining 1-6 residue that remains in the new linear chain. After all this is done, glycogen phosphorylase can continue.
An insulinstimulated enzyme known as phosphoprotein phosphatase(PP-1) inactivates glycogen phosphorylase to prevent glycogen break up.
GPBB - a sensitive marker for the AMI diagnosis within 4 hours after the onset of chest pain. It has also been shown that GPBB is increased in a considerable proportion of AMI patients within 2-3 hours from chest pain onset. GPBB is increased early in patients with unstable angina. GPBB can also be a sensitive marker for the detection of peri-operative myocardial ischaemia and infarction in patients undergoing coronary artery bypass grafting. -
Synonyms
Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.
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Physical Appearance
Sterile Filtered colourless liquid formualtion.
-
Stability
GPBB although stable at 10°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.
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Applications
Immunoassays and western blot.
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 :
AK1 MouseDescription:
Adenylate Kinase 1 Mouse Recombinant
Adenylate kinase Isoenzyme 1 isoform 1, Ak-1, B430205N08Rik, ATP-AMP transphosphorylase 1, ATP:AMP phosphotransferase, Adenylate monophosphate kinase, Myokinase.
Product # :
PKA-106Price :
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Description
AK1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 25.5kDa.AK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AK1 protein solution (0.5mg/ml) containing 20mM Tris-Hcl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 units/mg. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 37C.
More Info
-
Introduction
AK1 is a small ubiquitous enzyme which is essential for maintenance and cell growth. It is involved in the regulation of adenine nucleotide composition within a cell by catalyzing the reversible transfer of the terminal phosphate group between ATP and AMP. The AK1 protein is found in the cytosol of skeletal muscle, brain and erythrocytes. Defects in the AK1 gene are the cause of a form of hemolytic anemia.
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Synonyms
Adenylate kinase Isoenzyme 1 isoform 1, Ak-1, B430205N08Rik, ATP-AMP transphosphorylase 1, ATP:AMP phosphotransferase, Adenylate monophosphate kinase, Myokinase.
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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 MGSMGCCVSS EPQEEGGRKT GEKLKKAKII FVVGGPGSGK GTQCEKIVQK YGYTHLSTGD LLRAEVSSGS ERGKKLSAIM EKGELVPLDT VLDMLRDAML AKVDSSNGFL IDGYPREVKQ GEEFEQKIGQ PTLLLYVDAG AETMTQRLLK RGETSGRVDD
NEETIKKRLE TYYNATEPVI SFYDKRGIVR KVNAEGTVDT VFSEVCTYLD SLK.
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 :
APEX1 HumanDescription:
APEX Nuclease-1 Human Recombinant
APEX nuclease (multifunctional DNA repair enzyme) 1, APE, REF1, HAP1, APX, APEN, APEX, Apurinic-apyrimidinic endonuclease 1, Protein REF-1, AP endonuclease 1, APEX nuclease (multifunctional DNA repair enzyme), APE-1, deoxyribonuclease (apurinic or apyrimidinic), apurinic/apyrimidinic exonuclease, AP endonuclease class I, multifunctional DNA repair enzyme, redox factor 1, EC 4.2.99.18.
Product # :
ENZ-059Price :
Quantity :
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Description
APEX1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 332 amino acids (1-318a.a.) and having a molecular mass of 36.9kDa.APEX1 protein is fused to a 14 amino acid T7-tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
APEX1 Human solution (1mg/ml) containing 20mM Tris-HCl pH-8, 2mM DTT, 0.2M NaCl, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
APEX1 is in charge of the incision of DNA basic sites during base excision repair. APEX1 also stimulates the DNA binding activity of numerous transcription factors which take part in cancer promotion and progression. APEX1 is part of the cellular response to oxidative stress and protects cells from the genotoxic and cytotoxic effect of oxidizing agents.
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Synonyms
APEX nuclease (multifunctional DNA repair enzyme) 1, APE, REF1, HAP1, APX, APEN, APEX, Apurinic-apyrimidinic endonuclease 1, Protein REF-1, AP endonuclease 1, APEX nuclease (multifunctional DNA repair enzyme), APE-1, deoxyribonuclease (apurinic or apyrimidinic), apurinic/apyrimidinic exonuclease, AP endonuclease class I, multifunctional DNA repair enzyme, redox factor 1, EC 4.2.99.18.
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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.Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MASMTGGQQM GRGSMPKRGK KGAVAEDGDE LRTEPEAKKS KTAAKKNDKE AAGEGPALYE DPPDQKTSPS GKPATLKICS WNVDGLRAWI KKKGLDWVKE EAPDILCLQE TKCSENKLPA ELQELPGLSH QYWSAPSDKE GYSGVGLLSR QCPLKVSYGI GEEEHDQEGR VIVAEFDSFV LVTAYVPNAG RGLVRLEYRQ RWDEAFRKFL KGLASRKPLV LCGDLNVAHE EIDLRNPKGN KKNAGFTPQE RQGFGELLQA VPLADSFRHL YPNTPYAYTF WTYMMNARSK NVGWRLDYFL LSHSLLPALC DSKIRSKALG SDHCPITLYL AL.
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 :
GLK E.Coli, ActiveDescription:
Glucokinase E.coli Recombinant, BioActive
Glucokinase, ECK2384, JW2385.
Product # :
PKA-121Price :
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Description
GLK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321) and having a molecular mass of 37.1kDa.GLK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLK protein solution (1mg/ml) contains 0.15M NaCl, 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 70unit/mg obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. One unit will oxidize 1.0 umole of Glucose to D-glucose 6-phosphate per minute in the presence of Beta-NADP at pH 9.0 at 37C.
More Info
-
Introduction
Glucokinase or GLK, is a protein, part of the bacterial glucokinase superfamily. In the bacteria E. coli, glucose can be transported to the inner cell through a system called PTS as glucose 6-phosphate, therefore, GLK is less crucial to the bacteria.
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Synonyms
Glucokinase, ECK2384, JW2385.
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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 MGSMTKYALV GDVGGTNARL ALCDIASGEI SQAKTYSGLD YPSLEAVIRV YLEEHKVEVK DGCIAIACPI TGDWVAMTNH TWAFSIAEMK KNLGFSHLEI INDFTAVSMA IPMLKKEHLI QFGGAEPVEG KPIAVYGAGT GLGVAHLVHV DKRWVSLPGE GGHVDFAPNS EEEAIILEIL RAEIGHVSAE RVLSGPGLVN LYRAIVKADN RLPENLKPKD ITERALADSC TDCRRALSLF CVIMGRFGGN LALNLGTFGG VFIAGGIVPR FLEFFKASGF RAAFEDKGRF KEYVHDIPVY LIVHDNPGLL GSGAHLRQTL GHIL
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 :
CKMB Human S.ChainDescription:
Creatine Kinase MB Single Chain Human Recombinant
Product # :
CKI-285Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Human Creatine Kinase MB Single Chain produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.The CKMB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
CKMB although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HYAL1Description:
Hyaluronidase
Hyaluronidase-1, EC 3.2.1.35, Hyal-1, Hyaluronoglucosaminidase-1, LUCA-1.
Product # :
ENZ-323Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Hyaluronidase is an enzyme that temporarily and reversibly breaks down the polysaccharide, hyaluronic acid, which is found between the cells of connective tissue. Hyaluronic acid may be thought of as the "glue" that holds cells together. Hyaluronic acid is a mucopolysaccharide that exists in the human tissue matrix. It can constrain the diffusion of the extracellular fluid. Hyaluronidase makes the glucoseamine of the hyaluronic acid molecules hydrolyzed and depolymerized, thus decreases the viscosity of the body fluids and increases the flow and diffusion of the intercellular fluids. In this way the physic liquor, exudates or blood in local areas can be more easily diffused, and the drug can be more easily absorbed. Thus the local tissue tension and pains can be relieved. And it will also be easier for the edema and inflammatory exudates to be absorbed and dissolved. This product is a basic component of the articular cartilage. It can nourish, protect and maintain the functions of the joints.
Source
Bovine Testis.
Formulation
The enzyme was lyophilized 1xPBS and 2% sucrose.
More Info
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Synonyms
Hyaluronidase-1, EC 3.2.1.35, Hyal-1, Hyaluronoglucosaminidase-1, LUCA-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Hyaluronidase although although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hyaluronidase should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Hyaluronidase in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Specific Activity
300 IU/mg.
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 :
HSD17B1 HumanDescription:
Hydroxysteroid (17-beta) Dehydrogenase 1 Human Recombinant
E2 17-beta-dehydrogenase 1, EC 1.1.1.62, 17-beta-hydroxysteroid dehydrogenase type 1, 17-beta-HSD 1, 20 alpha-hydroxysteroid dehydrogenase, 20-alpha-HSD, E2DH, Placental 17-beta-hydroxysteroid dehydrogenase, HSD17B1, E17KSR, EDH17B1, EDH17B2, EDHB17, HSD17, SDR28C1.
Product # :
ENZ-709Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HSD17B1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-328 a.a) and having a molecular mass of 37.5kDa.HSD17B1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HSD17B1 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
E2 17-beta-dehydrogenase 1 (HSD17B1) is a member of the short-chain dehydrogenases/reductases (SDR) family. The HSD17B1 protein advances the reduction of estrogens and androgens. In addition, the HSD17B1 has a 20-alpha-HSD activity. HSD17B1 preferentially uses NADH.
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Synonyms
E2 17-beta-dehydrogenase 1, EC 1.1.1.62, 17-beta-hydroxysteroid dehydrogenase type 1, 17-beta-HSD 1, 20 alpha-hydroxysteroid dehydrogenase, 20-alpha-HSD, E2DH, Placental 17-beta-hydroxysteroid dehydrogenase, HSD17B1, E17KSR, EDH17B1, EDH17B2, EDHB17, HSD17, SDR28C1.
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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 MGSHMARTVV LITGCSSGIG LHLAVRLASD PSQSFKVYAT LRDLKTQGRL WEAARALACP PGSLETLQLD VRDSKSVAAA RERVTEGRVD VLVCNAGLGL LGPLEALGED AVASVLDVNV VGTVRMLQAF LPDMKRRGSG RVLVTGSVGG LMGLPFNDVY CASKFALEGL CESLAVLLLP FGVHLSLIEC GPVHTAFMEK VLGSPEEVLD RTDIHTFHRF YQYLAHSKQV FREAAQNPEE VAEVFLTALR APKPTLRYFT TERFLPLLRM RLDDPSGSNY VTAMHREVFG DVPAKAEAGA EAGGGAGPGA EDEAGRGAVG DPELGDPPAA PQ.
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 :
OXSM HumanDescription:
3-Oxoacyl-ACP Synthase, Mitochondrial Human Recombinant
3-Oxoacyl-ACP Synthase Mitochondrial, Type II Mitochondrial Beta-Ketoacyl Synthase, 3-Ketoacyl-Acyl Carrier Protein Synthase, FASN2D, KASI, EC 2.3.1, Beta-Ketoacyl-ACP Synthase.
Product # :
ENZ-751Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OXSM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (28-459) and having a molecular mass of 48.1kDa.OXSM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OXSM solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
OXSM, a beta-ketoacyl synthetase, is essential for elongation of fatty acid chains in the mitochondria. Alternatively spliced transcript variants were found.
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Synonyms
3-Oxoacyl-ACP Synthase Mitochondrial, Type II Mitochondrial Beta-Ketoacyl Synthase, 3-Ketoacyl-Acyl Carrier Protein Synthase, FASN2D, KASI, EC 2.3.1, Beta-Ketoacyl-ACP Synthase.
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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 MGSKRKFFGT VPISRLHRRV VITGIGLVTP LGVGTHLVWD RLIGGESGIV SLVGEEYKSI PCSVAAYVPR GSDEGQFNEQ NFVSKSDIKS MSSPTIMAIG AAELAMKDSG WHPQSEADQV ATGVAIGMGM IPLEVVSETA LNFQTKGYNK VSPFFVPKIL VNMAAGQVSI RYKLKGPNHA VSTACTTGAH AVGDSFRFIA HGDADVMVAG GTDSCISPLS LAGFSRARAL STNSDPKLAC RPFHPKRDGF VMGEGAAVLV LEEYEHAVQR RARIYAEVLG YGLSGDAGHI TAPDPEGEGA LRCMAAALKD AGVQPEEISY INAHATSTPL GDAAENKAIK HLFKDHAYAL AVSSTKGATG HLLGAAGAVE AAFTTLACYY QKLPPTLNLD CSEPEFDLNY VPLKAQEWKT EKRFIGLTNS FGFGGTNATL CIAGL.
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 :
PON2 HumanDescription:
Paraoxonase-2 Human Recombinant
Serum paraoxonase, arylesterase 2, EC 3.1.1.2, EC 3.1.8.1, PON 2, Serum aryldialkylphosphatase 2, A-esterase 2, Aromatic esterase 2.
Product # :
ENZ-300Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Paraoxonase-2 Human Recombinant is expressed in E. coli having a molecular weight of 43.5 kDa and fused to an amino terminal hexahistidine tag.The PON2 purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PON2 is supplied in PBS and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.More Info
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Introduction
Paraoxonase 2 (PON2) is a member of a multigene family whose genes share 65% identity at the amino acid level, and is expressed in a variety of tissues, including the pancreas. PON2 overexpression has been shown to lower the intracellular oxidative state and reduce the cells ability to oxidize LDL. PON2 is therefore implicated in the modulation of oxidative stress.
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Synonyms
Serum paraoxonase, arylesterase 2, EC 3.1.1.2, EC 3.1.8.1, PON 2, Serum aryldialkylphosphatase 2, A-esterase 2, Aromatic esterase 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 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGRLVAVGLLGIALALLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDID ILPNGLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNP HGISTFIDNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDIT AVGPAHFYATNDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSAN GINISPDDKYIYVADILAHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIW VGCHPNGQKLFVYDPNNPPSSEVLRIQNILSEKPTVTTVYANNGSVLQGSSVASVY DGKLLIGTLYHRALYCELZ.
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Applications
Arylesterase 2 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.
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 :
ACP6 HumanDescription:
Acid Phosphatase-6 Human Recombinant
Acid Phosphatase 6, Lysophosphatidic, Acid Phosphatase-Like Protein 1, PACPL1, ACPL1, LPAP, Lysophosphatidic Acid Phosphatase Type 6, Lysophosphatidic Acid Phosphatase 6, Acid Phosphatase Like 1, EC 3.1.3.2, Lysophosphatidic acid phosphatase type 6.
Product # :
ENZ-865Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (33-428a.a) and having a molecular mass of 47.7kDa. ACP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACP6 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1000 units/mg, and is defined as the amount of enzyme which hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at PH 5.0 at 37C.More Info
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Introduction
Acid Phosphatase-6, also known as ACP6 is Hydrolyzes lysophosphatidic acid (LPA) which contains a medium length fatty acid chain to the corresponding monoacylglycerol. ACP6 shows highest activity with lysophosphatidic acid which contains myristate (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower activity with C18:0 as well as C6:0 lysophosphatidic acid.
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Synonyms
Acid Phosphatase 6, Lysophosphatidic, Acid Phosphatase-Like Protein 1, PACPL1, ACPL1, LPAP, Lysophosphatidic Acid Phosphatase Type 6, Lysophosphatidic Acid Phosphatase 6, Acid Phosphatase Like 1, EC 3.1.3.2, Lysophosphatidic acid phosphatase type 6.
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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 MGSELQEADG QCPVDRSLLK LKMVQVVFRH GARSPLKPLP LEEQVEWNPQ LLEVPPQTQF DYTVTNLAGG PKPYSPYDSQ YHETTLKGGM FAGQLTKVGM QQMFALGERL RKNYVEDIPF LSPTFNPQEV FIRSTNIFRN LESTRCLLAG LFQCQKEGPI IIHTDEADSE VLYPNYQSCW SLRQRTRGRR QTASLQPGIS EDLKKVKDRM GIDSSDKVDF FILLDNVAAE QAHNLPSCPM LKRFARMIEQ RAVDTSLYIL PKEDRESLQM AVGPFLHILE SNLLKAMDSA TAPDKIRKLY LYAAHDVTFI PLLMTLGIFD HKWPPFAVDL TMELYQHLES KEWFVQLYYH GKEQVPRGCP DGLCPLDMFL NAMSVYTLSP EKYHALCSQT QVMEVGNEE.
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.