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1000 results found for “Epimerase”
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Name :
UFC1 HumanDescription:
Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant
Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.
Product # :
ENZ-138Price :
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Shipped with Ice Packs
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Description
UFC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.6kDa.UFC1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UFC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UFC1 is a member of the ubiquitin-conjugating enzyme family. UFC1 is an E2-like conjugating enzyme for ubiquitin-fold modifier-1. UFM1 is activated by UBA5 (a novel E1-like enzyme) by forming a high-energy thioester bond. Activated UFM1 is subsequently transferred to its cognate E2-like enzyme, UFC1, in a similar thioester linkage.
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Synonyms
Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
UFC1 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 MADEATRRVV SEIPVLKTNA GPRDRELWVQ RLKEEYQSLI RYVENNKNAD NDWFRLESNK EGTRWFGKCW YIHDLLKYEF DIEFDIPITY PTTAPEIAVP ELDGKTAKMY RGGKICLTDH FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLIQKGVIQ HKEKCNQ.
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 :
UBE2F HumanDescription:
Ubiquitin-Conjugating Enzyme E2F Human Recombinant
Ubiquitin-conjugating enzyme E2F (putative), NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, NEDD8-conjugating enzyme UBE2F, NCE2, EC 6.3.2.-.
Product # :
ENZ-625Price :
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Description
UBE2F Human Recombinant produced in E. coli is a single polypeptide chain containing 209 amino acids (1-185) and having a molecular mass of 23.7 kDa.UBE2F is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The UBE2F solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquitin-conjugating enzyme E2 F (UBE2F) is a member of the ubiquitin-conjugating enzyme family and UBE2F subfamily. Ubiquitin-conjugating enzymes or sometimes as ubiquitin-carrier enzymes, run the second step in the ubiquitination reaction which targets a protein for degradation using the proteasome. The UBE2F receives the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins.
RBX2-UBE2F complex neddylates specific target proteins, for example CUL5 as can be seen from the specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1. -
Synonyms
Ubiquitin-conjugating enzyme E2F (putative), NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, NEDD8-conjugating enzyme UBE2F, NCE2, EC 6.3.2.-.
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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 MGSHMLTLAS KLKRDDGLKG SRTAATASDS TRRVSVRDKL LVKEVAELEA NLPCTCKVHF PDPNKLHCFQ LTVTPDEGYY QGGKFQFETE VPDAYNMVPP KVKCLTKIWH PNITETGEIC LSLLREHSID GTGWAPTRTL KDVVWGLNSL FTDLLNFDDP LNIEAAEHHL RDKEDFRNKV DDYIKRYAR
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 :
SUOX HumanDescription:
Sulfite Oxidase Human Recombinant
Sulfite Oxidase, EC 1.8.3.1, Sulfite oxidase, mitochondrial.
Product # :
ENZ-887Price :
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Description
SUOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 489 amino acids (80-545 a.a) and having a molecular mass of 53.9kDa. SUOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SUOX protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Sulfite oxidase, also known as SUOX is a homodimeric protein localized to the intermembrane space of mitochondria. Each subunit includes a heme domain as well as a molybdopterin-binding domain. The SUOX enzyme catalyzes the oxidation of sulfite to sulfate, the last reaction in the oxidative degradation of the sulfur amino acids cysteine and methionine. In addition, the deficiency of SUOX results in neurological abnormalities which are often fatal at an early age.
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Synonyms
Sulfite Oxidase, EC 1.8.3.1, Sulfite oxidase, mitochondrial.
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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 MGSESTHIYT KEEVSSHTSP ETGIWVTLGS EVFDVTEFVD LHPGGPSKLM LAAGGPLEPF WALYAVHNQS HVRELLAQYK IGELNPEDKV APTVETSDPY ADDPVRHPAL KVNSQRPFNA EPPPELLTEN YITPNPIFFT RNHLPVPNLD PDTYRLHVVG APGGQSLSLS LDDLHNFPRY EITVTLQCAG NRRSEMTQVK EVKGLEWRTG AISTARWAGA RLCDVLAQAG HQLCETEAHV CFEGLDSDPT GTAYGASIPL ARAMDPEAEV LLAYEMNGQP LPRDHGFPVR VVVPGVVGAR HVKWLGRVSV QPEESYSHWQ RRDYKGFSPS VDWETVDFDS APSIQELPVQ SAITEPRDGE TVESGEVTIK GYAWSGGGRA VIRVDVSLDG GLTWQVAKLD GEEQRPRKAW AWRLWQLKAP VPAGQKELNI VCKAVDDGYN VQPDTVAPIW NLRGVLSNAW HRVHVYVSP.
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 :
AKR1B10 HumanDescription:
Aldo-Keto Reductase Family 1 Member B10 Human Recombinant
HIS, HSI, ARL1, ARL-1, ALDRLn, AKR1B11, AKR1B12, MGC14103, AKR1B10, Aldo-keto reductase family 1 member B10, Aldose reductase-like, Aldose reductase-related protein, ARP, hARP, Small intestine reductase, SI reductase.
Product # :
ENZ-416Price :
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Shipped with Ice Packs
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Description
AKR1B10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 316 amino acids (1-316 a.a) and having a molecular mass of 36 kDa. The AKR1B10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1B10 solution contains 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
AKR1B10 efficiently reduces aliphatic and aromatic aldehydes, and it is less active on hexoses. AKR1B10 is highly expressed in adrenal gland, small intestine, and colon, and may play an important role in liver carcinogenesis. AKR1B10 is a monomeric protein that competently catalyzes the reduction of aromatic and aliphatic aldehydes and ketones. AKR1B10 is widely expressed in numerous human tissues, small intestine, colon and adrenal gland. AKR1B10 is pathogenically involved in diabetic complications and is overexpressed in human tumors, such as liver, breast, and lung cancer, AKR1B10 is involved in the development and progression of cancer.
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Synonyms
HIS, HSI, ARL1, ARL-1, ALDRLn, AKR1B11, AKR1B12, MGC14103, AKR1B10, Aldo-keto reductase family 1 member B10, Aldose reductase-like, Aldose reductase-related protein, ARP, hARP, Small intestine reductase, SI reductase.
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Physical Appearance
Sterile Filtered clear 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
MATFVELSTK AKMPIVGLGT WKSPLGKVKE AVKVAIDAGY RHIDCAYVYQ NEHEVGEAIQ EKIQEKAVKR EDLFIVSKLW PTFFERPLVRKAFEKTLKDL KLSYLDVYLI HWPQGFKSGD DLFPKDDKGN AIGGKATFLD AWEAMEELVD EGLVKALGVS NFSHFQIEKL LNKPGLKYKP VTNQVECHPY LTQEKLIQYC HSKGITVTAY SPLGSPDRPW AKPEDPSLLE DPKIKEIAAK HKKTAAQVLI RFHIQRNVIV IPKSVTPARIVENIQVFDFK LSDEEMATIL SFNRNWRACN VLQSSHLEDY PFDAEY.
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 :
CTRB1 HumanDescription:
Chymotrypsinogen-B1, Human Recombinant
Product # :
ENZ-1016Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human CTRB1 expressed in E.coli containing 245 amino acids having a Mw of 27kDa is purified by standard chromatography techniques.
Source
E.coli
Formulation
The Human CTRB1 was lyophilized without any additives.
Purity
Greater than 95% as determined by HPLC.
Biological Activity
1100 units/mg protein.
One unit is defined as the amount of enzyme that will hydrolyze 1.0 μmole of N-alpha-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 7.0 at 25°C.More Info
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Introduction
Chymotrypsinogen-B1 (CTRB1) belongs to the serine protease family of enzymes and forms a main precursor of the pancreatic proteolytic enzymes. CTRB1 is located next to a related chymotrypsinogen gene. CTRB1 is a protein coding gene which encodes different isoforms which may undergo similar processing to generate the mature protein.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Recombinant Human CTRB1 although stable at room temp for 1 week, should be stored desiccated 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 Human CTRB1 in 1ml 50mM HAc which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND ITLLKLATPA RFSQTVSAVC LPSADDDFPAGTLCATTGWG KTKYNANKTP DKLQQAALPL LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSDTCST SSPGVYARVTKLIPWVQKIL AAN.
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 :
NQO2 HumanDescription:
NAD(P)H Dehydrogenase Quinone 2 Human Recombinant
DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].
Product # :
ENZ-515Price :
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Shipped with Ice Packs
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Description
NQO2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 251amino acids (1-231 a.a.) and having a molecular mass of 28.1 kDa. NQO2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
NQO2 Human solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
NQO2 is a flavoprotein that catalyzes the 2-electron reduction of diverse quinones, redox dyes, and the vitamin K menadione. NQO2 mainly uses dihydronicotinamide riboside (NRH) as the electron donor. NQO2 catalyzes the metabolic detoxification of quinones and their derivatives to hydroquinones. This detoxification process protects cells against quinone-induced oxidative stress, cytotoxicity and mutagenicity.
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Synonyms
DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].
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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 MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNFEPR ATDKDITGTL SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF QFPLYWFSVP AILKGWMDRV LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG 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 :
PCK1 HumanDescription:
Phosphoenolpyruvate Carboxykinase 1 Human Recombinant
Phosphoenolpyruvate carboxykinase 1 (soluble), PEPCK-C, PEPCK1, PEP carboxykinase, phosphoenolpyruvate carboxykinase cytosolic [GTP], EC 4.1.1.32.
Product # :
PKA-018Price :
Quantity :
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Shipped with Ice Packs
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Description
PCK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 646 amino acids (1-622) and having a molecular mass of 71.7kDa.PCK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PCK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
PCK1 is a central regulating point for the regulation of gluconeogenesis. PCK1 has a vital part in this process by stimulating hepatic glucose production. The expression of PCK1 is controlled by cAMP, glucocorticoids, diet etc. Modulation of the signals controlling PCK1 levels offers a possible therapeutic tactic to the treatment of Diabetes and subsequently obesity.
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Synonyms
Phosphoenolpyruvate carboxykinase 1 (soluble), PEPCK-C, PEPCK1, PEP carboxykinase, phosphoenolpyruvate carboxykinase cytosolic [GTP], EC 4.1.1.32.
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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 MGSHMPPQLQ NGLNLSAKVV QGSLDSLPQA VREFLENNAE LCQPDHIHIC DGSEEENGRL LGQMEEEGIL RRLKKYDNCW LALTDPRDVA RIESKTVIVT QEQRDTVPIP KTGLSQLGRW MSEEDFEKAF NARFPGCMKG RTMYVIPFSM GPLGSPLSKI GIELTDSPYV VASMRIMTRM GTPVLEALGD GEFVKCLHSV GCPLPLQKPL VNNWPCNPEL TLIAHLPDRR EIISFGSGYG GNSLLGKKCF ALRMASRLAK EEGWLAEHML VLGITNPEGE KKYLAAAFPS ACGKTNLAMM NPSLPGWKVE CVGDDIAWMK FDAQGHLRAI NPENGFFGVA PGTSVKTNPN AIKTIQKNTI FTNVAETSDG GVYWEGIDEP LASGVTITSW KNKEWSSEDG EPCAHPNSRF CTPASQCPII DAAWESPEGV PIEGIIFGGR RPAGVPLVYE ALSWQHGVFV GAAMRSEATA AAEHKGKIIM HDPFAMRPFF GYNFGKYLAH WLSMAQHPAA KLPKIFHVNW FRKDKEGKFL WPGFGENSRV LEWMFNRIDG KASTKLTPIG YIPKEDALNL KGLGHINMME LFSISKEFWE KEVEDIEKYL EDQVNADLPC EIEREILALK QRISQM.
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 :
TH MouseDescription:
Tyrosine Hydroxylase Mouse Recombinant
Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.
Product # :
ENZ-988Price :
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Shipped with Ice Packs
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Description
TH Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 507 amino acids (1-498a.a.) and having a molecular mass of 57.0kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). TH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TH 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
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Introduction
Tyrosine 3-monooxygenase (Th), is a rate-limiting enzyme in catecholamine synthesis. Th utilizes tetrahydrobiopterin as well as molecular oxygen to convert tyrosine to DOPA. Th regulates dopamine (DA) neurotransmission at the biosynthesis and reuptake steps. Th takes a vital part in the physiology of adrenergic neurons. Furthermore, Th effects overexpression in lymphocytes on the differentiation as well as function of T helper cells.
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Synonyms
Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.
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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
ADPMPTPSAS SPQPKGFRRA VSEQDTKQAE AVTSPRFIGR RQSLIEDARK EREAAAAAAA AAVASAEPGN PLEAVVFEER DGNAVLNLLF SLRGTKPSSL SRALKVFETF EAKIHHLETR PAQRPLAGSP HLEYFVRFEV PSGDLAALLS SVRRVSDDVR SAREDKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD QAYRQRRKLI AEIAFQYKQG EPIPHVEYTK EEIATWKEVY ATLKGLYATH ACREHLEAFQ LLERYCGYRE DSIPQLEDVS HFLKERTGFQ LRPVAGLLSA RDFLASLAFR VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADRTFAQ FSQDIGLASL GASDEEIEKL STVYWFTVEF GLCKQNGELK AYGAGLLSSY GELLHSLSEE PEVRAFDPDT AAVQPYQDQT YQPVYFVSES FSDAKDKLRN YASRIQRPFS VKFDPYTLAI DVLDSPHTIR RSLEGVQDEL HTLTQALSAI SHHHHHH.
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 :
CK2a Zea MaysDescription:
Casein Kinase 2 alpha Zea Mays Recombinant
Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2-alpha, CK2?.
Product # :
PKA-210Price :
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Shipped with Ice Packs
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Description
Casein Kinase 2 alpha Zea Mays Recombinant is a non-glycosylated polypeptide having a molecular mass of 39.2 kDa. Casein Kinase 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CK2a is supplied in 50% glycerol.
Purity
Greater than 99% as determined by SDS-PAGE.
More Info
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Introduction
The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes.
Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2. -
Synonyms
Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2-alpha, CK2?.
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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 > 1U/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 :
DUSP23 HumanDescription:
Dual Specificity Phosphatase 23 Human Recombinant
Dual specificity protein phosphatase 23, DUSP25, Low molecular mass dual specificity phosphatase 3, LDP-3, VHZ, VH1-like phosphatase Z, MOSP, RP11-190A12.1, FLJ20442, EC 3.1.3.16, EC 3.1.3.48.
Product # :
ENZ-195Price :
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Shipped with Ice Packs
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Description
DUSP23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150 a.a.) and having a molecular mass of 18.8kDa.DUSP23 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DUSP23 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 2mM DTT, and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE analysis.
More Info
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Introduction
DUSP23 is a member of the protein-tyrosine phosphatase family. DUSP23 is a protein phosphatase which facilitates dephosphorylation of phosphorylated proteins on Tyr and Ser/Thr residues. In vitro, DUSP23 dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10). In addition, DUSP23 enhances activation of JNK and p38(MAPK14).
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Synonyms
Dual specificity protein phosphatase 23, DUSP25, Low molecular mass dual specificity phosphatase 3, LDP-3, VHZ, VH1-like phosphatase Z, MOSP, RP11-190A12.1, FLJ20442, EC 3.1.3.16, EC 3.1.3.48.
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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 MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD AIAEIRRLRP GSIETYEQEK AVFQFYQRTK
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 :
BDH1 HumanDescription:
3-Hydroxybutyrate Dehydrogenase, Type 1 Human Recombinant
D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.
Product # :
ENZ-215Price :
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Shipped with Ice Packs
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Description
BDH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (47-343) and having a molecular mass of 35.3kDa.BDH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The BDH1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
BDH1 belongs to the short-chain dehydrogenase/reductase gene family. BDH1 forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific necessity for phosphatidylcholine for optimal enzymatic activity. BDH1 catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the 2 main ketone bodies formed during fatty acid catabolism.
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Synonyms
D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.
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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 MASAAEPVGS KAVLVTGCDS GFGFSLAKHL HSKGFLVFAG CLMKDKGHDG VKELDSLNSD RLRTVQLNVC SSEEVEKVVE IVRSSLKDPE KGMWGLVNNA GISTFGEVEF TSLETYKQVA EVNLWGTVRM TKSFLPLIRR AKGRVVNISS MLGRMANPAR SPYCITKFGV EAFSDCLRYE MYPLGVKVSV VEPGNFIAAT SLYSPESIQA IAKKMWEELP EVVRKDYGKK YFDEKIAKME TYCSSGSTDT SPVIDAVTHA LTATTPYTRY HPMDYYWWLR MQIMTHLPGA ISDMIYIR.
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 :
NAA30 HumanDescription:
N Alpha-Acetyltransferase 30, NatC Catalytic Subunit Human Recombinant
N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.
Product # :
ENZ-720Price :
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Description
NAA30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362 a.a) and having a molecular mass of 41.7kDa.NAA30 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAA30 protein solution (0.25mg/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
-
Introduction
N-alpha-acetyltransferase 30 (NAA30) is catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. NAA30 catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. In addition, NAA30 is essential for the lysosomal localization and function of ARL8B. The disease Eastern equine encephalitis has been associated with NAA30.
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Synonyms
N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAEVPPG PSSLLPPPAP PAPAAVEPRC PFPAGAALAC CSEDEEDDEE HEGGGSRSPA GGESATVAAK GHPCLRCPQP PQEQQQLNGL ISPELRHLRA AASLKSKVLS VAEVAATTAT PDGGPRATAT KGAGVHSGER PPHSLSSNAR TAVPSPVEAA AASDPAAARN GLAEGTEQEE EEEDEQVRLL SSSLTADCSL RSPSGREVEP GEDRTIRYVR YESELQMPDI MRLITKDLSE PYSIYTYRYF IHNWPQLCFL AMVGEECVGA IVCKLDMHKK MFRRGYIAML AVDSKYRRNG IGTNLVKKAI YAMVEGDCDE VVLETEITNK SALKLYENLG FVRDKRLFRY YLNGVDALRL KLWLR
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 :
LTA4H HumanDescription:
Leukotriene A4 Hydrolase Human Recombinant
Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.
Product # :
ENZ-869Price :
Quantity :
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Description
LTA4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 634 amino acids (1-611 a.a) and having a molecular mass of 71.7kDa.LTA4H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LTA4H protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Leukotriene A-4 hydrolase (LTA4H) is a bifunctional enzyme that converts leukotriene A4 to leukotriene B4 and functions as an aminopeptidase. The LTA4H enzyme is a member of the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). LTA4H participates in arachidonic acid metabolism.
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Synonyms
Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.
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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 MGSMPEIVDT CSLASPASVC RTKHLHLRCS VDFTRRTLTG TAALTVQSQE DNLRSLVLDT KDLTIEKVVI NGQEVKYALG ERQSYKGSPM EISLPIALSK NQEIVIEISF ETSPKSSALQ WLTPEQTSGK EHPYLFSQCQ AIHCRAILPC QDTPSVKLTY TAEVSVPKEL VALMSAIRDG ETPDPEDPSR KIYKFIQKVP IPCYLIALVV GALESRQIGP RTLVWSEKEQ VEKSAYEFSE TESMLKIAED LGGPYVWGQY DLLVLPPSFP YGGMENPCLT FVTPTLLAGD KSLSNVIAHE ISHSWTGNLV TNKTWDHFWL NEGHTVYLER HICGRLFGEK FRHFNALGGW GELQNSVKTF GETHPFTKLV VDLTDIDPDV AYSSVPYEKG FALLFYLEQL LGGPEIFLGF LKAYVEKFSY KSITTDDWKD FLYSYFKDKV DVLNQVDWNA WLYSPGLPPI KPNYDMTLTN ACIALSQRWI TAKEDDLNSF NATDLKDLSS HQLNEFLAQT LQRAPLPLGH IKRMQEVYNF NAINNSEIRF RWLRLCIQSK WEDAIPLALK MATEQGRMKF TRPLFKDLAA FDKSHDQAVR TYQEHKASMH PVTAMLVGKD LKVD.
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 :
CCBL1 HumanDescription:
Cysteine Conjugate-Beta Lyase Cytoplasmic Human Recombinant
Cysteine Conjugate-Beta Lyase, Cytoplasmic, Glutamine Transaminase K, Cysteine Conjugate-Beta Lyase; Cytoplasmic (Glutamine Transaminase K, Kyneurenine Aminotransferase), Kynurenine--Oxoglutarate Transaminase I, Glutamine--Phenylpyruvate Transaminase, Cysteine-S-Conjugate Beta-Lyase, Kynurenine Aminotransferase I, Kyneurenine Aminotransferase, KATI, GTK, Glutamine-Phenylpyruvate Aminotransferase, Kynurenine--Oxoglutarate Transaminase 1, Beta-Lysase, Kidney, EC 4.4.1.13, EC 2.6.1.64, EC 2.6.1.7, KAT1, Kynurenine--oxoglutarate transaminase 1.
Product # :
ENZ-878Price :
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Description
CCBL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 445 amino acids (1-422 a.a) and having a molecular mass of 50.3kDa. CCBL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCBL1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cysteine Conjugate-Beta Lyase Cytoplasmic also known as CCBL1 is a member of the class-I pyridoxal-phosphate-dependent aminotransferase family. CCBL1 catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) it also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Furthermore, CCBL1 catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno) cysteine, resulting in the cleavage of the C-S or C-Se bond.
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Synonyms
Cysteine Conjugate-Beta Lyase, Cytoplasmic, Glutamine Transaminase K, Cysteine Conjugate-Beta Lyase; Cytoplasmic (Glutamine Transaminase K, Kyneurenine Aminotransferase), Kynurenine--Oxoglutarate Transaminase I, Glutamine--Phenylpyruvate Transaminase, Cysteine-S-Conjugate Beta-Lyase, Kynurenine Aminotransferase I, Kyneurenine Aminotransferase, KATI, GTK, Glutamine-Phenylpyruvate Aminotransferase, Kynurenine--Oxoglutarate Transaminase 1, Beta-Lysase, Kidney, EC 4.4.1.13, EC 2.6.1.64, EC 2.6.1.7, KAT1, Kynurenine--oxoglutarate transaminase 1.
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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 MGSMAKQLQA RRLDGIDYNP WVEFVKLASE HDVVNLGQGF PDFPPPDFAV EAFQHAVSGD FMLNQYTKTF GYPPLTKILA SFFGELLGQE IDPLRNVLVT VGGYGALFTA FQALVDEGDE VIIIEPFFDC YEPMTMMAGG RPVFVSLKPG PIQNGELGSS SNWQLDPMEL AGKFTSRTKA LVLNTPNNPL GKVFSREELE LVASLCQQHD VVCITDEVYQ WMVYDGHQHI SIASLPGMWE RTLTIGSAGK TFSATGWKVG WVLGPDHIMK HLRTVHQNSV FHCPTQSQAA VAESFEREQL LFRQPSSYFV QFPQAMQRCR DHMIRSLQSV GLKPIIPQGS YFLITDISDF KRKMPDLPGA VDEPYDRRFV KWMIKNKGLV AIPVSIFYSV PHQKHFDHYI RFCFVKDEAT LQAMDEKLRK WKVEL.
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 :
PI3Ka BovineDescription:
Phosphoinositide 3-kinase alpha p110a/p85a Bovine Recombinant
Phosphoinositide 3-kinase alpha p110a/p85a, PI3Ka, 2.7.1.137, Phosphatidylinositol 3-kinase, 1-phosphatidylinositol 3-kinase, PI3-kinase, PtdIns-3-kinase, Type I phosphatidylinositol kinase, Type III phosphoinositide 3-kinase.
Product # :
PKA-327Price :
Quantity :
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Description
The PI3Ka catalytic and regulatory subunits are coexpressed in Sf9 insect cells. Phosphoinositide 3-kinase alpha Bovine Recombinant is a glycosilated protein having a molecular weight as follows: p85a chain 83.5 kDa, p110 chain 124.3 kDa.
Source
Sf9 insect cells.
Formulation
PI3Ka solution in 25mM HEPES, pH 8.0, 25mM NaCl, 2.5mM MgCl2 and 50% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
PI3Ka plays a specific role in apoptosis in human colon cancer cells. Injection of neutralizing antibodies specific to PI3Ka into adenocarcinoma cells induced apoptosis, a response that was reverted by treating cells with caspase inhibitor. It was also shown that PI3Ka mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
PI3Ka is a key regulator of the initiation of keratinocyte differentiation. A decrease in PI3Ka activity results in a loss of keratinocyte adhesion to the extracellular membrane and the initiation of early phase differentiation. -
Synonyms
Phosphoinositide 3-kinase alpha p110a/p85a, PI3Ka, 2.7.1.137, Phosphatidylinositol 3-kinase, 1-phosphatidylinositol 3-kinase, PI3-kinase, PtdIns-3-kinase, Type I phosphatidylinositol kinase, Type III phosphoinositide 3-kinase.
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Physical Appearance
Sterile filtered liquid formualtion.
-
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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Unit Definition
1 unit is defined as 1 picomole phosphate transferred to PIP2 per minute.
-
Specific Activity
1,000 U/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 :
GNPNAT1 HumanDescription:
Glucosamine-Phosphate N-Acetyltransferase 1 Human Recombinant
Gpnat1, GNPNAT, GNA1, EC 2.3.1.4, FLJ10607, Glucosamine-Phosphate N-Acetyltransferase 1, Phosphoglucosamine acetylase, Phosphoglucosamine transacetylase, Glucosamine 6-Phosphate N-Acetyltransferase.
Product # :
ENZ-037Price :
Quantity :
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Description
GNPNAT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-184a.a.) and having a molecular mass of 23.1KDa.GNPNAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GNPNAT1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
GNPNAT1 is a member of the GNA1 subfamily of the larger acetyltransferase family of proteins. GNPNAT1 is limited to the Golgi apparatus and the endosome. GNPNAT1 is vital for UDPGlcNAc biosynthesis pathway. GNPNAT1 catalyzes the synthesis of GlcNAc6P from AcCoA and GlcN6P, a step in the UDP-GlcNAc6P formation pathway.
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Synonyms
Gpnat1, GNPNAT, GNA1, EC 2.3.1.4, FLJ10607, Glucosamine-Phosphate N-Acetyltransferase 1, Phosphoglucosamine acetylase, Phosphoglucosamine transacetylase, Glucosamine 6-Phosphate N-Acetyltransferase.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKPDETP MFDPSLLKEV DWSQNTATFS PAISPTHPGE GLVLRPLCTA DLNRGFFKVL GQLTETGVVS PEQFMKSFEH MKKSGDYYVT VVEDVTLGQI VATATLIIEH KFIHSCAKRG RVEDVVVSDE CRGKQLGKLL LSTLTLLSKK LNCYKITLEC
LPQNVGFYKK FGYTVSEENY MCRRFLK
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 :
MMP 8 Human, HisDescription:
Matrix Metalloproteinase-8 Human Recombinant, His Tag
CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.
Product # :
ENZ-766Price :
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Description
MMP 8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (101-467a.a) and having a molecular mass of 44.3kDa. MMP 8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP 8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form.
Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I.
Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes. -
Synonyms
CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.
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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 MGSLTPGNPK WERTNLTYRI RNYTPQLSEA EVERAIKDAF ELWSVASPLI FTRISQGEAD INIAFYQRDH GDNSPFDGPN GILAHAFQPG QGIGGDAHFD AEETWTNTSA NYNLFLVAAH EFGHSLGLAH SSDPGALMYP NYAFRETSNY SLPQDDIDGI QAIYGLSSNP IQPTGPSTPK PCDPSLTFDA ITTLRGEILF FKDRYFWRRH PQLQRVEMNF ISLFWPSLPT GIQAAYEDFD RDLIFLFKGN QYWALSGYDI LQGYPKDISN YGFPSSVQAI DAAVFYRSKT YFFVNDQFWR YDNQRQFMEP GYPKSISGAF PGIESKVDAV FQQEHFFHVF SGPRYYAFDL IAQRVTRVAR GNKWLNCRYG.
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 :
TAF9 HumanDescription:
TAF9 Recombinant Human
TAF9 RNA polymerase II TATA box binding protein (TBP)-associated factor 32kDa, TAFII32, AK6, CINAP, TAFII31, TAF2G, CGI-137, MGC1603, MGC3647, MGC5067, TAFIID32, Coilin-interacting nuclear ATPase protein, Transcription initiation factor TFIID 31/32 kDa subunit, STAF31/32, ATP-AMP transphosphorylase 6, h RNA polymerase II TBP-associated factor subunit G, CINAP, AD-004, CIP, adenylate kinase isoenzyme 6, adrenal gland protein AD-004, coilin interacting protein, MGC:1603, MGC:3647, MGC:5067, EC 2.7.4.3.
Product # :
ENZ-065Price :
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Description
TAF9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (1-172.a.a) and having a molecular mass of 22.2kDa. TAF9 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TAF9 Human solution (0.5mg/1ml) containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
TAF9 is a universal transcription factor which enables the preinitiation complex assembly by direct interactions with the TATA promoter element. TAF9 is a multisubunit complex consisting of a small TATA-binding polypeptide and other TBP-associated factors (TAFs) and performs as a channel for regulatory signals.
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Synonyms
TAF9 RNA polymerase II TATA box binding protein (TBP)-associated factor 32kDa, TAFII32, AK6, CINAP, TAFII31, TAF2G, CGI-137, MGC1603, MGC3647, MGC5067, TAFIID32, Coilin-interacting nuclear ATPase protein, Transcription initiation factor TFIID 31/32 kDa subunit, STAF31/32, ATP-AMP transphosphorylase 6, h RNA polymerase II TBP-associated factor subunit G, CINAP, AD-004, CIP, adenylate kinase isoenzyme 6, adrenal gland protein AD-004, coilin interacting protein, MGC:1603, MGC:3647, MGC:5067, EC 2.7.4.3.
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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
MGSSHHHHHH SSGLVPRGSH MLLPNILLTG TPGVGKTTLG KELASKSGLK YINVGDLARE EQLYDGYDEE YDCPILDEDR VVDELDNQMR EGGVIVDYHG CDFFPERWFH IVFVLRTDTN VLYERLETRG YNEKKLTDNI QCEIFQVLYE EATASYKEEI VHQLPSNKPE ELENNVDQIL KWIEQWIKDH NS
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 :
LDHA MouseDescription:
Lactate Dehydrogenase A Mouse Recombinant
L-lactate dehydrogenase A chain, LDH-A, LDH muscle subunit, LDH-M.
Product # :
ENZ-952Price :
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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.
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Name :
MMLV RTDescription:
Moloney Murine Leukemia Virus Reverse Trancscriptase Recombinant
Product # :
ENZ-310Price :
Quantity :
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Description
MMLV (Moloney Murine Leukemia Virus) Reverse Transcriptase is a DNA polymerase that synthesizes a complementary DNA strands from single-stranded RNA, DNA, or an RNA-DNA hybrid as a template. This recombinant enzyme was purified from E.coli, which carried a modified MMLV-RT gene. Compared to AMV Reverse Transcriptase, this enzyme has a much weaker 5' - 3' ribonuclease H activity, which allows the syntesis of longer cDNAs (>7kb).
Source
Recombinant E. coli strain.
Formulation
50mM Tris-HCl, 0.1M NaCl, 0.1% Triton X-100, 2mM DTT, 0.1mM EDTA and 50% glycerol.
More Info
-
Physical Appearance
Sterile Filtered clear solution (200 U/µl).
-
Stability
Stable for 5 days at 10°C, for longer period of time store at -20°C. Please prevent freeze-thaw cycles.
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Unit Definition
One unit is defined as the amount of enzyme required to catalyze the incorporation of 1nmol of deoxyribonucleotide into acid-insoluble forms in 10 minutes at 37oC, using poly(A)-oligo(dT)12-18 as the template-primer. Standard cDNA Synthesis Conditions50mM Tris-HCl (pH8.3), 75mM KCl, 3mM MgCl2, 10mM DTT, 1.0mM each dATP, dGTP, dCTP, and dTTP, 0.2 mg radom hexamer,1-5mg RNA, 200units M-MLV RT. The reaction volume was 20ml and the incubation was 45 min at 42oC.
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 :
NDK E.ColiDescription:
Nucleoside Diphosphate Kinase E.Coli Recombinant
Nucleoside diphosphate kinase, NDK, NDP kinase, Nucleoside-2-P kinase, b2518, JW2502.
Product # :
PKA-034Price :
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Description
NDK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-143 a.a.) and having a molecular mass of 18kDa.NDK is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NDK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Nucleoside diphosphate kinase (Ndk) is an enzyme which catalyzes the exchange of phosphate groups between different nucleoside diphosphates. Ndk’s activity sustains equilibrium between the concentrations of various nucleoside triphosphates for example, when GTP is produced in the citric acid (Krebs) cycle is converted to ATP. Ndk has a key role in the synthesis of nucleoside triphosphates other than ATP.
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Synonyms
Nucleoside diphosphate kinase, NDK, NDP kinase, Nucleoside-2-P kinase, b2518, JW2502.
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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 MGSHMAIERT FSIIKPNAVA KNVIGNIFAR FEAAGFKIVG TKMLHLTVEQ ARGFYAEHDG KPFFDGLVEF MTSGPIVVSV LEGENAVQRH RDLLGATNPA NALAGTLRAD YADSLTENGT HGSDSVESAA REIAYFFGEG EVCPRTR.
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 :
MSRA HumanDescription:
Methionine Sulfoxide Reductase A Human Recombinant
Mitochondrial peptide methionine sulfoxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, Protein-methionine-S-oxide reductase, PMSR, MSRA.
Product # :
ENZ-621Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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- purity
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Description
MSRA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (24-235) and having a molecular mass of 26.2kDa.The MSRA is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MSRA protein solution (0.5mg/ml) is supplied in 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Methionine sulfoxide reductase A (MSRA) is a member of the MsrA Met sulfoxide reductase family. The MSRA enzyme has a vital function as a repair enzyme for proteins which have been inactivated by oxidation. MSRA catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. The three substrates of the MSRA enzyme are peptide-L-methionine, thioredoxin disulfide, and H2O, while its 2 products are peptide-L-methionine (R)-S-oxide and thioredoxin. The MSRA protein is ubiquitous and extremely conserved. Human and animal studies have shown the ultimate levels of expression in kidney and nervous tissue.
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Synonyms
Mitochondrial peptide methionine sulfoxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, Protein-methionine-S-oxide reductase, PMSR, MSRA.
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Physical Appearance
Sterile Filtered clear 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 MGSHMGNSAS NIVSPQEALP GRKEQTPVAA KHHVNGNRTV EPFPEGTQMA VFGMGCFWGA ERKFWVLKGV YSTQVGFAGG YTSNPTYKEV CSEKTGHAEV VRVVYQPEHM SFEELLKVFW ENHDPTQGMR QGNDHGTQYR SAIYPTSAKQ MEAALSSKEN YQKVLSEHGF GPITTDIREG QTFYYAEDYH QQYLSKNPNG YCGLGGTGVS CPVGIKK.
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 :
FUT5 HumanDescription:
Fucosyltransferase 5 Human Recombinant
FUT-5
Product # :
ENZ-1199Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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Description
The FUT5 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FUT5 His-Tagged Fusion Protein produced in E. coli, is a 30kDa protein containing 172 amino acid residues of the FUT5 Human, 203-374 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
FUT-5
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized FUT5 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Fucosyltransferase 5 also known as FUT5 is a glycosyltransferase which takes part in the biosynthesis of glycolipids and glycoproteins. FUT5 mainly catalyzes the transfer of fucose (a monosaccharide) to the type 2 chain of oligosaccharides (Galβ1-4GlcNAc). FUT5 takes an important part in various biological processes which include regulation of inflammation, cell-cell interactions and immune response modulation. FUT5 is expressed mainly in tissues such as the pancreas, liver and various immune cells.
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 :
MPO HumanDescription:
Myeloperoxidase Human
Myeloperoxidase, EC 1.11.1.7, MPO.
Product # :
ENZ-074Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MPO is a natural protein having a molecular mass of 150kDa containing 2 subunits each of a heavy chain with 64kDa and a light chain with 13kDa. MPO is isolated from human peripheral blood polymorphonuclear leukocytes.
Source
Human peripheral blood polymorphonuclear leukocytes.
Formulation
MPO solution is supplied in 20mM HEPES buffer pH-7.5, 200mM NaCl and 20% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
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Introduction
Myeloperoxidase is an important enzyme used by granulocytes during phagocytic lysis of foreign particles engulfed. In normal tissues and in a variety of myeloproliferative disorders myeloid cells of both neutrophilic and eosinophilic types, at all stages of maturation, exhibit strong cytoplasmic reactivity for MPO. Erythroid precursors, megakaryocytes, lymphoid cells, mast cells, and plasma cells are nonreactive. MPO is not observed in the neoplastic cells of a wide variety of epithelial tumors and sarcomas. MPO is useful in differentiating between myeloid and lymphoid leukemias.
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Synonyms
Myeloperoxidase, EC 1.11.1.7, MPO.
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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.
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.