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1000 results found for “Glyoxalase”
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Name :
HDHD1 HumanDescription:
Haloacid Dehalogenase-Like Hydrolase Domain Containing 1 Human Recombinant
Pseudouridine-5'-monophosphatase, 5'-PsiMPase, Haloacid dehalogenase-like hydrolase domain-containing protein 1, Haloacid dehalogenase-like hydrolase domain-containing protein 1A, Protein GS1, HDHD1, DXF68S1E, FAM16AX, GS1, HDHD1A.
Product # :
ENZ-028Price :
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Description
HDHD1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids (1-228 a.a.) and having a molecular mass of 27.4kDa. The HDHD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HDHD1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol,
0.1M NaCl and 1mM DTT.Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Haloacid dehalogenase-like hydrolase domain-containing protein 1A (HDHD1A) is a member of the adiponutrin family. HDHD1A is interesting because it is an X-linked gene that escapes X-inactivation. HDHD1A is particularly important in the perception of human X chromosome structural organization as well as the mechanism of X-inactivation.
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Synonyms
Pseudouridine-5'-monophosphatase, 5'-PsiMPase, Haloacid dehalogenase-like hydrolase domain-containing protein 1, Haloacid dehalogenase-like hydrolase domain-containing protein 1A, Protein GS1, HDHD1, DXF68S1E, FAM16AX, GS1, HDHD1A.
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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 MAAPPQPVTH LIFDMDGLLL DTERLYSVVF QEICNRYDKK YSWDVKSLVM GKKALEAAQI IIDVLQLPMS KEELVEESQT KLKEVFPTAA LMPGAEKLII HLRKHGIPFA LATSSGSASF DMKTSRHKEF FSLFSHIVLG DDPEVQHGKP DPDIFLACAK RFSPPPAMEK CLVFEDAPNG VEAALAAGMQ VVMVPDGNLS RDLTTKATLV LNSLQDFQPE LFGLPSYE.
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 :
FUT7 HumanDescription:
Fucosyltransferase 7 Human Recombinant
Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.
Product # :
ENZ-784Price :
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Description
FUT7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (37-342) and having a molecular mass of 37.9kDa.FUT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FUT7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Fucosyltransferase 7 (FUT7) is a golgi stack membrane protein which is involved in the creation of sialyl-Lewis X antigens. The FUT7 protein leads the synthesis of the E-selectin-binding sialyl-Lewis X moiety. FUT7 catalyzes alpha-1,3 glycosidic linkages involved in the expression of sialyl Lewis X antigens.
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Synonyms
Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.
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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 MGSPRGTPAP QPTITILVWH WPFTDQPPEL PSDTCTRYGI ARCHLSANRS LLASADAVVF HHRELQTRRS HLPLAQRPRG QPWVWASMES PSHTHGLSHL RGIFNWVLSY RRDSDIFVPY GRLEPHWGPS PPLPAKSRVA AWVVSNFQER QLRARLYRQL APHLRVDVFG RANGRPLCAS CLVPTVAQYR FYLSFENSQH RDYITEKFWR NALVAGTVPV VLGPPRATYE AFVPADAFVH VDDFGSAREL AAFLTGMNES RYQRFFAWRD RLRVRLFTDW RERFCAICDR YPHLPRSQVY EDLEGWFQA.
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 :
ALPL HumanDescription:
Alkaline Phosphatase Human Recombinant
Alkaline phosphatase liver/bone/kidney isozyme, phosphoamidase, Phosphocreatine phosphatase, aalkaline phosphatase, tissue-nonspecific isozyme isoform 1, ALPL, AP-TNAP, APTNAP, HOPS, HPPA, HPPC, HPPI, HPPO, TNALP, TNAP, TNS-ALP, TNSALP.
Product # :
ENZ-1190Price :
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Description
ALPL Human Recombinant produced in HEK293 is a single, glycosylated polypeptide chain containing 493 amino acids (18-501 a.a) and having a molecular mass of 54.3kDa. ALPL is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293.
Formulation
ALPL protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 40,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of 4-Methylumbelliferyl phosphate to phosphate and 4-Methylumbelliferone per minute at pH 8.8 at 37C.
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Synonyms
Alkaline phosphatase liver/bone/kidney isozyme, phosphoamidase, Phosphocreatine phosphatase, aalkaline phosphatase, tissue-nonspecific isozyme isoform 1, ALPL, AP-TNAP, APTNAP, HOPS, HPPA, HPPC, HPPI, HPPO, TNALP, TNAP, TNS-ALP, TNSALP.
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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
DGSLVPEKEK DPKYWRDQAQ ETLKYALELQ KLNTNVAKNV IMFLGDGMGV STVTAARILK GQLHHNPGEE TRLEMDKFPF VALSKTYNTN AQVPDSAGTA TAYLCGVKAN EGTVGVSAAT ERSRCNTTQG NEVTSILRWA KDAGKSVGIV TTTRVNHATP SAAYAHSADR DWYSDNEMPP EALSQGCKDI AYQLMHNIRD IDVIMGGGRK YMYPKNKTDV EYESDEKARG TRLDGLDLVD TWKSFKPRYK HSHFIWNRTE LLTLDPHNVD YLLGLFEPGD MQYELNRNNV TDPSLSEMVV VAIQILRKNP KGFFLLVEGG RIDHGHHEGK AKQALHEAVE MDRAIGQAGS LTSSEDTLTV VTADHSHVFT FGGYTPRGNS IFGLAPMLSD TDKKPFTAIL YGNGPGYKVV GGERENVSMV DYAHNNYQAQ SAVPLRHETH GGEDVAVFSK GPMAHLLHGV HEQNYVPHVM AYAACIGANL GHCAPAS HHHHHH.
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Background
The ALPL human recombinant, a variant of the alkaline phosphatase enzyme, has emerged as a significant focus of biomedical research due to its diverse biological functions and potential therapeutic applications. Alkaline phosphatase (ALPL) is an essential enzyme involved in various physiological processes, including bone mineralization, liver function, and immune regulation. The ALPL human recombinant, generated through recombinant DNA technology, offers a unique platform to explore the molecular complexity and therapeutic implications of this enzyme.
Understanding the molecular characteristics of ALPL is crucial to unravel its functional diversity. ALPL belongs to a family of enzymes that hydrolyze phosphate esters under alkaline conditions. The structural features, post-translational modifications, and molecular interactions of ALPL contribute to its complexity and enable its participation in multiple biological processes.
ALPL plays diverse roles in different tissues and physiological contexts. In bone, ALPL is involved in the regulation of mineralization, ensuring proper skeletal development and maintenance. In the liver, ALPL participates in bile acid metabolism and detoxification processes. Furthermore, ALPL has been implicated in immune regulation and inflammation modulation.
The therapeutic potential of the ALPL human recombinant is vast, offering opportunities for the diagnosis, treatment, and management of various diseases. ALPL-based therapies hold promise for addressing skeletal disorders, such as hypophosphatasia, where ALPL deficiency leads to impaired bone mineralization. ALPL's involvement in liver function also presents avenues for therapeutic interventions in liver diseases. Moreover, the immunomodulatory properties of ALPL highlight its potential role in immune-related disorders.
This research aims to provide a comprehensive analysis of the ALPL human recombinant, focusing on its molecular characteristics, biological functions, and therapeutic implications. By exploring the intricate nature of ALPL, we aim to shed light on its therapeutic potential and pave the way for future research in this exciting field.
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 :
AKR7A2 HumanDescription:
Aldo-Keto Reductase Family 7 Member A2 Human Recombinant
Aflatoxin B1 aldehyde reductase member 2, AFAR, AFAR1, AFB1-AR1, AKR7, Succinic semialdehyde reductase, SSA reductase, AFB1 aldehyde reductase 1, Aldoketoreductase 7, AKR7A2.
Product # :
ENZ-485Price :
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Description
AKR7A2 Human Recombinant fused to a 39 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 398 amino acids (1-359 a.a) and having a molecular mass of 44 kDa. The AKR7A2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR7A2 solution contains 20mM Tris-HCl pH-8, 1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: approximately 0.25-0.3 units/mg.
Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.More Info
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Introduction
AKR7A2 participates in the detoxification of aldehydes and ketones. AKR7A2 catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. AKR7A2 is involved in producing the neuromodulator gamma-hydroxybutyrate (GHB). AKR7A2 has extensive substrate specificity. AKR7A2 shows NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2 reduces 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). AKR7A2 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A2 takes part in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.
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Synonyms
Aflatoxin B1 aldehyde reductase member 2, AFAR, AFAR1, AFB1-AR1, AKR7, Succinic semialdehyde reductase, SSA reductase, AFB1 aldehyde reductase 1, Aldoketoreductase 7, AKR7A2.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEM LSAASRVVSR AAVHCALRSP PPEARALAMS RPPPPRVASV LGTMEMGRRM DAPASAAAVR AFLERGHTEL DTAFMYSDGQ SETILGGLGL GLGGGDCRVK IATKANPWDG KSLKPDSVRS QLETSLKRLQ CPQVDLFYLH APDHGTPVEE TLHACQRLHQ EGKFVELGLS NYASWEVAEI CTLCKSNGWI LPTVYQGMYN ATTRQVETEL FPCLRHFGLR FYAYNPLAGG LLTGKYKYED KDGKQPVGRF FGNSWAETYR NRFWKEHHFE AIALVEKALQ AAYGASAPSV TSAALRWMYH HSQLQGAHGD AVILGMSSLE QLEQNLAATE EGPLEPAVVD AFNQAWHLVA HECPNYFR.
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 :
DHRS4 HumanDescription:
Dehydrogenase/Reductase Member 4 Human Recombinant
Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.
Product # :
ENZ-207Price :
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Description
DHRS4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278) and having a molecular mass of 32.1kDa.DHRS4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHRS4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Dehydrogenase/reductase SDR family member 4 (DHRS4) is a member of the short-chain dehydrogenases/reductases (SDR) family. DHRS4 reduces all trans retinal and 9-cis retinal. In addition, the DHRS4 protein can catalyze the oxidation of all trans retinol with NADP as cofactor, but with a much lower efficiency. Furthermore, DHRS4 reduces alkyl phenyl ketones and alpha dicarbonyl compounds with aromatic rings, such as pyrimidine 4 aldehyde, 3 benzoylpyridine, 4 benzoylpyridine, menadione and 4 hexanoylpyridine.
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Synonyms
Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.
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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 MGSHMHKAGL LGLCARAWNS VRMASSGMTR RDPLANKVAL VTASTDGIGF AIARRLAQDG AHVVVSSRKQ QNVDQAVATL QGEGLSVTGT VCHVGKAEDR ERLVATAVKL HGGIDILVSN AAVNPFFGSI MDVTEEVWDK TLDINVKAPA LMTKAVVPEM EKRGGGSVVI VSSIAAFSPS PGFSPYNVSK TALLGLTKTL AIELAPRNIR VNCLAPGLIK TSFSRMLWMD KEKEESMKET LRIRRLGEPE DCAGIVSFLC SEDASYITGE TVVVGGGTPS RL.
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 :
GSTA1 HumanDescription:
Glutathione S-Transferase Alpha-1 Human Recombinant
GST2, GSTA1-1, GTH1, GSTA-1, GSTAI, GSTA-I, EC 2.5.1.18, Glutathione S-transferase A1, GST HA subunit 1, GST-epsilon, GST class-alpha member 1, GSTA1, MGC131939.
Product # :
ENZ-469Price :
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Description
GSTA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (1-222 a.a.) and having a molecular mass of 25.6 kDa. The GSTA1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is 35,000 pmol/min/ug, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.
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
GST2, GSTA1-1, GTH1, GSTA-1, GSTAI, GSTA-I, EC 2.5.1.18, Glutathione S-transferase A1, GST HA subunit 1, GST-epsilon, GST class-alpha member 1, GSTA1, MGC131939.
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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
MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF.
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 :
CTSZ Mouse, ActiveDescription:
Cathepsin-Z, Active Mouse Recombinant
Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.
Product # :
ENZ-1108Price :
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Description
CTSZ Mouse Recombinant produced in Baculovirus is a single, glycosylated, polypeptide chain containing 292 amino acids (23-306 aa) and having a molecular mass of 32.8kDa.CTSZ is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CTSZ solution (0.5 mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3,000 pmol/min/ug. One unit will convert 1 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25°C.
More Info
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Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.
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Synonyms
Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.
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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
ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT
RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV
WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE
KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV
RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH 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 :
DCTPP1 HumanDescription:
dCTP Pyrophosphatase 1 Human Recombinant
dCTP pyrophosphatase 1, RS21C6, XTP3TPA, Deoxycytidine-triphosphatase 1, dCTPase 1, XTP3-transactivated gene A protein, CDA03, MGC5627, XTP3-transactivated protein A, EC 3.6.1.12.
Product # :
ENZ-234Price :
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Description
DCTPP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 194 amino acids (1-170) and having a molecular mass of 21.2kDa.DCTPP1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DCTPP1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
DCTPP1, also known as dCTP pyrophosphatase 1, contains an epilepsy-associated repeat (EAR) domain that is predicted to participate in protein-protein interactions, most likely involved in ligand recognition. This protein functions to hydrolyze abnormal nucleotide triphosphates (NTPs) in cancer cells that, if unregulated, could be incorporated into nascent DNA or RNA.
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Synonyms
dCTP pyrophosphatase 1, RS21C6, XTP3TPA, Deoxycytidine-triphosphatase 1, dCTPase 1, XTP3-transactivated gene A protein, CDA03, MGC5627, XTP3-transactivated protein A, EC 3.6.1.12.
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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 MGSHMSVAGG EIRGDTGGED TAAPGRFSFS PEPTLEDIRR LHAEFAAERD WEQFHQPRNL LLALVGEVGE LAELFQWKTD GEPGPQGWSP RERAALQEEL SDVLIYLVAL AARCRVDLPL AVLSKMDINR RRYPAHLARS SSRKYTELPH GAISEDQAVG PADIPCDSTG QTST.
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 :
ACAD8 HumanDescription:
Acyl-Coenzyme A Dehydrogenase 8 Human Recombinant
Acyl-CoA dehydrogenase family member 8 mitochondrial, ACAD-8, Isobutyryl-CoA dehydrogenase, Activator-recruited cofactor 42 kDa component, ARC42, FLJ22590.
Product # :
ENZ-294Price :
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Description
ACAD8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 416 amino acids (23-415) and having a molecular mass of 45.1kDa.ACAD8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACAD8 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of ?-oxidationin Fatty acid metabolism.
Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer formation. -
Synonyms
Acyl-CoA dehydrogenase family member 8 mitochondrial, ACAD-8, Isobutyryl-CoA dehydrogenase, Activator-recruited cofactor 42 kDa component, ARC42, FLJ22590.
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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 MGSLVQTGHR SLTSCIDPSM GLNEEQKEFQ KVAFDFAARE MAPNMAEWDQ KELFPVDVMR KAAQLGFGGV YIQTDVGGSG LSRLDTSVIF EALATGCTST TAYISIHNMC AWMIDSFGNE EQRHKFCPPL CTMEKFASYC LTEPGSGSDA ASLLTSAKKQ GDHYILNGSK AFISGAGESD IYVVMCRTGG PGPKGISCIV VEKGTPGLSF GKKEKKVGWN SQPTRAVIFE DCAVPVANRI GSEGQGFLIA VRGLNGGRIN IASCSLGAAH ASVILTRDHL NVRKQFGEPL ASNQYLQFTL ADMATRLVAA RLMVRNAAVA LQEERKDAVA LCSMAKLFAT DECFAICNQA LQMHGGYGYL KDYAVQQYVR DSRVHQILEG SNEVMRILIS RSLLQE.
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 :
FOLH1 MouseDescription:
Folate Hydrolase 1 Mouse Recombinant
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
Product # :
ENZ-957Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FOLH1 Mouse Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 717 amino acids (45-752a.a) and having a molecular mass of 80.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). FOLH1 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The FOLH1 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Folate Hydrolase 1 (Folh1) is a single pass type 2 membrane protein which is expressed mainly in prostate epithelium. Folh1 which is a part of the peptidase M28 family and M28B subfamily has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase activity. Folh1 can be found in urinary bladder, kidney, testis, ovary, stomach, small intestine colon, and the capillary endothelium of various tumors. Therefore, Folh1 plays a role in directed imaging and therapy of recurrent of metastatic disease.
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Synonyms
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
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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
ADPKPSNEAT GNVSHSGMKK EFLHELKAEN IKKFLYNFTR TPHLAGTQNN FELAKQIHDQ WKEFGLDLVE LSHYDVLLSY PNKTHPNYIS IINEDGNEIF KTSLSEQPPP GYENISDVVP PYSAFSPQGT PEGDLVYVNY ARTEDFFKLE REMKISCSGK IVIARYGKVF RGNMVKNAQL AGAKGMILYS DPADYFVPAV KSYPDGWNLP GGGVQRGNVL NLNGAGDPLT PGYPANEHAY RHELTNAVGL PSIPVHPIGY DDAQKLLEHM GGPAPPDSSW KGGLKVPYNV GPGFAGNFST QKVKMHIHSY TKVTRIYNVI GTLKGALEPD RYVILGGHRD AWVFGGIDPQ SGAAVVHEIV RSFGTLKKKG RRPRRTILFA SWDAEEFGLL GSTEWAEEHS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVYNLTK ELQSPDEGFE GKSLYDSWKE KSPSPEFIGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWKTNKVSSY PLYHSVYETY ELVVKFYDPT FKYHLTVAQV RGAMVFELAN SIVLPFDCQS YAVALKKYAD TIYNISMKHP QEMKAYMISF DSLFSAVNNF TDVASKFNQR LQELDKSNPI LLRIMNDQLM YLERAFIDPL GLPGRPFYRH IIYAPSSHNK YAGESFPGIY DALFDISSKV NASKAWNEVK RQISIATFTV QAAAETLREV 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 :
TrxR YeastDescription:
Thioredoxin Reductase (NADPH) Yeast Recombinant
Thioredoxin Reductase (NADPH), NTR, TrxR.
Product # :
ENZ-278Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of protein contains 20mM phosphate buffer pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be 5.8 IU/mg.
More Info
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Introduction
Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.
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Synonyms
Thioredoxin Reductase (NADPH), NTR, TrxR.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized NTR in sterile 18MΩ-cm H2O.
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Unit Definition
One unit equals the change in absorbance at 412 nm per minute at 25°C using 0.2mM NADPH containing 5mM DTNB (pH 7.0).
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 :
DERA HumanDescription:
Deoxyribose-Phosphate Aldolase Human Recombinant
Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.
Product # :
ENZ-170Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DERA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (1-318) and having a molecular mass of 37.3 kDa.DERA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DERA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Deoxyribose-phosphate aldolase (DERA) is a member of the deoC/fbaB aldolase protein family involved in the carbohydrate degradation pathway. DERA catalyzes the conversion of 2-deoxy-D-ribose 5-phosphate to D-glyceraldehyde 3-phosphate and an acetyldehyde.
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Synonyms
Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.
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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 MSAHNRGTEL DLSWISKIQV NHPAVLRRAE QIQARRTVKK EWQAAWLLKA VTFIDLTTLS GDDTSSNIQR LCYKAKYPIR EDLLKALNMH DKGITTAAVC VYPARVCDAV KALKAAGCNI PVASVAAGFP AGQTHLKTRL EEIRLAVEDG ATEIDVVINR SLVLTGQWEA LYDEIRQFRK ACGEAHLKTI LATGELGTLT NVYKASMIAM MAGSDFIKTS TGKETVNATF PVAIVMLRAI RDFFWKTGNK IGFKPAGGIR SAKDSLAWLS LVKEELGDEW LKPELFRIGA STLLSDIERQ IYHHVTGRYA AYHDLPMS
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 :
CNDP2 HumanDescription:
CNDP Dipeptidase 2 Human Recombinant
Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.
Product # :
ENZ-681Price :
Quantity :
Shipping Method :
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Description
CNDP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 498 amino acids (1-475) and having a molecular mass of 55.3 kDa. CNDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CNDP2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CNDP Dipeptidase 2 (CNDP2), is a cytosolic, non-specific dipeptidase which is a part of the peptidase M20A protein family. CNDP2 is a secreted peptidase homologous to M20 peptidases. CNDP2 expresses through all adult and fetal tissue, though, an isoform missing exons 3 and 4 expresses in all fetal tissue in adult liver. Over expression of CPGL-B in hepatocellular carcinoma cells results in significant inhibition of HC cell viability, colony formation, cell invasiveness and tumor configuration.
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Synonyms
Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.
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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 MGSMAALTTL FKYIDENQDR YIKKLAKWVA IQSVSAWPEK RGEIRRMMEV AAADVKQLGG SVELVDIGKQ KLPDGSEIPL PPILLGRLGS DPQKKTVCIY GHLDVQPAAL EDGWDSEPFT LVERDGKLYG RGSTDDKGPV AGWINALEAY QKTGQEIPVN VRFCLEGMEE SGSEGLDELI FARKDTFFKD VDYVCISDNY WLGKKKPCIT YGLRGICYFF IEVECSNKDL HSGVYGGSVH EAMTDLILLM GSLVDKRGNI LIPGINEAVA AVTEEEHKLY DDIDFDIEEF AKDVGAQILL HSHKKDILMH RWRYPSLSLH GIEGAFSGSG AKTVIPRKVV GKFSIRLVPN MTPEVVGEQV TSYLTKKFAE LRSPNEFKVY MGHGGKPWVS DFSHPHYLAG RRAMKTVFGV EPDLTREGGS IPVTLTFQEA TGKNVMLLPV GSADDGAHSQ NEKLNRYNYI EGTKMLAAYL YEVSQLKD.
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 :
CAT HumanDescription:
Catalase Human Recombinant
Catalase, CAT.
Product # :
ENZ-629Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CAT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 547 amino acids (1-527) and having a molecular mass of 61.9kDa.CAT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CAT solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >30,000 unit/mg.More Info
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Introduction
Catalase (CAT) is a key antioxidant enzyme in the body’s defense against oxidative stress. Furthermore, Catalase is a heme enzyme which is present in the peroxisome of virtually all aerobic cells. Catalase converts the reactive oxygen species hydrogen peroxide to water and oxygen and thus diminishes the toxic effects of hydrogen peroxide. Catalase stimulates growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. Catalase gene polymorphisms are linked with decreases in catalase activity nevertheless, to date, acatalasemia is the only disease known to be caused by the CAT gene.
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Synonyms
Catalase, CAT.
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Physical Appearance
Sterile filtered yellowish 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 MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKKTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ GIKNLSVEDA ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFAYPD THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEQQPSALE HSIQYSGEVR RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK NFTEVHPDYG SHIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL.
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Unit Definition
One unit will decompose 1.0 umole of H2O2 per minute at pH 8.0 at 25°C.
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 :
Enterokinase HumanDescription:
Enteropeptidase/ Enterokinase, Light Chain Human Recombinant
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK,TMPRSS15, MGC133046, Transmembrane Protease Serine 15.
Product # :
ENZ-260Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Enterokinase Human produced in E.Coli cells is a single, non-glycosylated polypeptide chain containing 237 amino acids (785-1019aa ) and having a molecular mass of 26.4kDa. Enterokinase is purified by proprietary chromatographic techniques
Source
Escherichia Coli.
Formulation
Enterokinase 1mg/ml is supplied in 20mM Tris-HCl, pH 8.0, and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins. -
Synonyms
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK,TMPRSS15, MGC133046, Transmembrane Protease Serine 15.
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Physical Appearance
Liquid 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
MAIVGGSNAK EGAWPWVVGL YYGGRLLCGA SLVSSDWLVS AAHCVYGRNL EPSKWTAILG LHMKSNLTSP QTVPRLIDEI VINPHYNRRR KDNDIAMMHL EFKVNYTDYI QPICLPEENQ VFPPGRNCSI AGWGTVVYQG TTANILQEAD VPLLSNERCQ QQMPEYNITE NMICAGYEEG GIDSCQGDSG GPLMCQENNR WFLAGVTSFG YKCALPNRPG VYARVSRFTE WIQSFLH
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 :
ACP2 HumanDescription:
Acid Phosphatase-2 Human Recombinant
Acid Phosphatase 2, Lysosoma, EC 3.1.3.2 LAP, Lysosomal Acid Phosphatase, ACP2.
Product # :
ENZ-849Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 373 amino acids (31-380 a.a.) and having a molecular mass of 42.9kDa. ACP2 is fused to a 23 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
ACP2 protein solution (1mg/ml) contains 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Acid Phosphatase-2, also known as ACP2 is composed of two subunits, Alpha & beta, and is chemically as well as genetically distinct from red cell acid phosphatase. ACP2 belongs to a family of distinct isoenzymes which hydrolyze orthophosphoric monoesters to alcohol and phosphate. In addition, Acid phosphatase deficiency is caused by mutations in the ACP2-beta subunit as well as ACP3-alpha subunit genes.
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Synonyms
Acid Phosphatase 2, Lysosoma, EC 3.1.3.2 LAP, Lysosomal Acid Phosphatase, ACP2.
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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 MGSRSLRFVT LLYRHGDRSP VKTYPKDPYQ EEEWPQGFGQ LTKEGMLQHW ELGQALRQRY HGFLNTSYHR QEVYVRSTDF DRTLMSAEAN LAGLFPPNGM QRFNPNISWQ PIPVHTVPIT EDRLLKFPLG PCPRYEQLQN ETRQTPEYQN ESSRNAQFLD MVANETGLTD LTLETVWNVY DTLFCEQTHG LRLPPWASPQ TMQRLSRLKD FSFRFLFGIY QQAEKARLQG GVLLAQIRKN LTLMATTSQL PKLLVYSAHD TTLVALQMAL DVYNGEQAPY ASCHIFELYQ EDSGNFSVEM YFRNESDKAP WPLSLPGCPH RCPLQDFLRL TEPVVPKDWQ QECQLASGPA DTE
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 :
Urokinase HumanDescription:
Urokinase Human
Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.
Product # :
ENZ-264Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Urokinase is a two-chain glycoprotein containing 411 amino acids with 12 disulfide bonds. Its molecular weight is 54,000 Dalton.
Source
Human urine.
Formulation
The Urokinase was lyophilized from a concentrated (1mg/ml) solution containing phosphate buffer.
Purity
Greater than 90.0%.
More Info
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Introduction
Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
It can be obtained from human urine or kidney cell culture. -
Synonyms
Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Urokinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Urokinase should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Urokinase in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Contaminants
Free of: Hepatitis B surface antigen, Hepatitis C antibody and HIV I and II.
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Specific Activity
187,973IU/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.
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Name :
MMP9 MouseDescription:
Matrix Metalloproteinase-9 Mouse Recombinant
AW743869, Matrix metalloproteinase-9, 92 kDa type IV collagenase, Gelatinase B, GELB, Mmp9, MANDP2, B/MMP, B/MMP9, Clg4, Clg4b, Gel B, MMP-9, pro-MMP-9, 92 kDa gelatinase.
Product # :
ENZ-1191Price :
Quantity :
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Shipped with Ice Packs
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Description
MMP9 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-730 a.a) containing a total of 717 amino acids, having a molecular mass of 79.3kDa. MMP9 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
MMP9 protein solution (1mg/ml) containing 10% glycerol, 20mM Tris-HCl (pH 7.5), 1mM CaCl2 and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is greater than 1,500 pmol/min/ug and is defined by the amount of enzyme that cleaves 1pmole of Mca-PLGLDpa-AR-NH2 per minute at pH 7.5 at 37˚C.
More Info
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Synonyms
AW743869, Matrix metalloproteinase-9, 92 kDa type IV collagenase, Gelatinase B, GELB, Mmp9, MANDP2, B/MMP, B/MMP9, Clg4, Clg4b, Gel B, MMP-9, pro-MMP-9, 92 kDa gelatinase.
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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
APYQRQPTFV VFPKDLKTSN LTDTQLAEAY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS QTLKAIRTPR CGVPDVGRFQ TFKGLKWDHH NITYWIQNYS EDLPRDMIDD AFARAFAVWG EVAPLTFTRV YGPEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGAGVQ GDAHFDDDEL WSLGKGVVIP TYYGNSNGAP CHFPFTFEGR SYSACTTDGR NDGTPWCSTT ADYDKDGKFG FCPSERLYTE HGNGEGKPCV FPFIFEGRSY SACTTKGRSD GYRWCATTAN YDQDKLYGFC PTRVDATVVG GNSAGELCVF PFVFLGKQYS SCTSDGRRDG RLWCATTSNF DTDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPLYSYLEGF PLNKDDIDGI QYLYGRGSKP DPRPPATTTT EPQPTAPPTM CPTIPPTAYP TVGPTVGPTG APSPGPTSSP SPGPTGAPSP GPTAPPTAGS SEASTESLSP ADNPCNVDVF DAIAEIQGAL HFFKDGWYWK FLNHRGSPLQ GPFLTARTWP ALPATLDSAF EDPQTKRVFF FSGRQMWVYT GKTVLGPRSL DKLGLGPEVT HVSGLLPRRL GKALLFSKGR VWRFDLKSQK VDPQSVIRVD KEFSGVPWNS HDIFQYQDKA YFCHGKFFWR VSFQNEVNKV DHEVNQVDDV GYVTYDLLQC PHHHHHH.
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Background
The MMP9 mouse recombinant, a variant of the matrix metalloproteinase 9 enzyme, has emerged as a crucial focus of biomedical research due to its diverse biological functions and potential implications in various physiological and pathological processes. Matrix metalloproteinase 9 (MMP9) is a key enzyme involved in extracellular matrix remodeling, cell migration, and tissue homeostasis. The MMP9 mouse recombinant, generated through recombinant DNA technology, offers a valuable tool for investigating the molecular characteristics and biological roles of this enzyme.
Understanding the molecular characteristics of MMP9 is vital to unravel its functional significance. MMP9 belongs to the matrix metalloproteinase family, characterized by their ability to degrade various components of the extracellular matrix. MMP9 exhibits unique structural features, including a catalytic domain, a hemopexin-like domain, and a prodomain that regulates its activation. These characteristics contribute to the complexity of MMP9 and its involvement in multiple physiological and pathological processes.
MMP9 plays diverse roles in different biological contexts. It is involved in tissue remodeling processes, such as embryogenesis, wound healing, and tissue repair. Additionally, MMP9 participates in inflammatory responses, immune cell recruitment, and angiogenesis. The precise mechanisms underlying these functions are still being elucidated, highlighting the need for further investigation.
The MMP9 mouse recombinant offers exciting prospects for research and therapeutic applications. By utilizing this recombinant protein, scientists can investigate the role of MMP9 in disease progression, explore its interactions with other molecules, and potentially develop targeted therapies. MMP9 has been implicated in various diseases, including cancer metastasis, cardiovascular disorders, and neurodegenerative conditions, making it a promising candidate for therapeutic interventions.
This research aims to provide a comprehensive analysis of the MMP9 mouse recombinant, focusing on its molecular characteristics, biological roles, and potential therapeutic implications. By shedding light on the intricate nature of MMP9, we aim to contribute to a deeper understanding of its functional significance and pave the way for future research and therapeutic advancements.
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 :
NTMT1 HumanDescription:
N-Terminal Xaa-Pro-Lys N-Methyltransferase 1 Human Recombinant
NTMT1, N-Terminal Xaa-Pro-Lys N-Methyltransferase 1, X-Pro-Lys N-Terminal Protein Methyltransferase 1A, Alpha N-Terminal Protein Methyltransferase 1A , Methyltransferase-Like Protein 11A , N-Terminal RCC1 Methyltransferase, METTL11A, C9orf32, NTM1A, NRMT, Chromosome 9 Open Reading Frame 32, Methyltransferase Like 11A, EC 2.1.1.244, AD-003, HOMT1A, NRMT1.
Product # :
ENZ-929Price :
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Description
NTMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-223 a.a) and having a molecular mass of 28.1kDa. NTMT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NTMT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
N-terminal Xaa-Pro-Lys N-methyltrasferase1, also known as NTMT1 belongs to the methyltransferase superfamily. NTMT1 catalyzesthe transfer of the methyl group from the S-adenosyl-l-methionine to the protein ?-amine, resulting in the formation of S-adenosyl-l-homocysteine and ?-N-methylated proteins. NTMT1 is a remarkable potential anticancer targetsince it is overexpressed in gastrointestinal cancers in addition to his essential function in cell mitosis.
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Synonyms
NTMT1, N-Terminal Xaa-Pro-Lys N-Methyltransferase 1, X-Pro-Lys N-Terminal Protein Methyltransferase 1A, Alpha N-Terminal Protein Methyltransferase 1A , Methyltransferase-Like Protein 11A , N-Terminal RCC1 Methyltransferase, METTL11A, C9orf32, NTM1A, NRMT, Chromosome 9 Open Reading Frame 32, Methyltransferase Like 11A, EC 2.1.1.244, AD-003, HOMT1A, NRMT1.
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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 MGSEFMTSEV IEDEKQFYSK AKTYWKQIPP TVDGMLGGYG HISSIDINSS RKFLQRFLRE GPNKTGTSCA LDCGAGIGRI TKRLLLPLFR EVDMVDITED FLVQAKTYLG EEGKRVRNYF CCGLQDFTPE PDSYDVIWIQ WVIGHLTDQH LAEFLRRCKGSLRPNGIIVI KDNMAQEGVI LDDVDSSVCR DLDVVRRIIC SAGLSLLAEE RQENLPDEIY HVYSFALR.
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 :
METTL21A HumanDescription:
Methyltransferase Like 21A Human Recombinant
Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.
Product # :
ENZ-718Price :
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Description
METTL21A Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (93-218) and having a molecular mass of 17 kDa.METTL21A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The METTL21A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
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Introduction
METTL21A, which is a part of the methyltransferase superfamily, is a Protein-lysine methyltransferase that in vitro methylates HSPA1, HSPA5 and HSPA8.
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Synonyms
Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.
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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 MGSTDRKVAL EFLKSNVQAN LPPHIQTKTV VKELTWGQNL GSFSPGEFDL ILGADIIYLE ETFTDLLQTL EHLCSNHSVI LLACRIRYER DNNFLAMLER QFTVRKVHYD PEKDVHIYEA QKRNQKEDL.
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 :
PTPS HumanDescription:
6-Pyruvoyltetrahydropterin Synthase Human Recombinant
PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.
Product # :
ENZ-471Price :
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Description
6-PyruvoylTetrahydropterin Synthase Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145) and having a molecular mass of 18.5kDa. 6-PyruvoylTetrahydropterin Synthase is fused to a 20 amino acid His Tag at N-terminus and purified using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
6-PyruvoylTetrahydropterin Synthase is formulated in 20mM Tris-HCl buffer pH-8, 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
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Introduction
6-PyruvoylTetrahydropterin Synthase is part of the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. 6-PyruvoylTetrahydropterin Synthase catalyzes the elimination of inorganic triphosphate from dihydroneopterin triphosphate, which is the second and irreversible step in the biosynthesis of tetrahydrobiopterin from GTP. Tetrahydrobiopterin, is a necessary cofactor and regulator of a range of enzyme activities, including enzymes involved in serotonin biosynthesis and NO synthase activity. Mutations in 6-PyruvoylTetrahydropterin Synthase gene result in hyperphenylalaninemia.
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Synonyms
PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.
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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 MSTEGGGRRC QAQVSRRISF SASHRLYSKF LSDEENLKLF GKCNNPNGHG HNYKVVVTVH GEIDPATGMV MNLADLKKYM EEAIMQPLDH KNLDMDVPYF ADVVSTTENV AVYIWDNLQK VLPVGVLYKV KVYETDNNIV VYKGE.
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 :
WARS HumanDescription:
Tryptophanyl-tRNA Synthetase Human Recombinant
GAMMA-2, IFI53, IFP53, WRS, WARS, TrpRS, hWRS, EC=6.1.1.2, Tryptophanyl-tRNA synthetase, INF-induced protein 53, Tryptophan--tRNA ligase, GAMMA-2.
Product # :
ENZ-545Price :
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Description
WARS Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 491 amino acids (1-471 a.a.) and having a molecular mass of 55.3 kDa. The WARS is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl, 1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
WARS is part of the class I tRNA synthetase family. 2 types of tryptophanyl tRNA synthetase exist, a cytoplasmic form, called WARS, and a mitochondrial form, called WARS2. WARS catalyzes the aminoacylation of tRNA(trp) with tryptophan and is induced by INF. WARS controls ERK, Akt, and eNOS activation pathways that are related with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression.
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Synonyms
GAMMA-2, IFI53, IFP53, WRS, WARS, TrpRS, hWRS, EC=6.1.1.2, Tryptophanyl-tRNA synthetase, INF-induced protein 53, Tryptophan--tRNA ligase, GAMMA-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 MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY KAAAGEDYKA DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY DKLIVRFGSS KIDKELINRI ERATGQRPHH FLRRGIFFSH RDMNQVLDAY ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT KWLQDVFNVP LVIQMTDDEK YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY MGMSSGFYKN VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM SASDPNSSIF LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF MYLTFFLEDD DKLEQIRKDY TSGAMLTGEL KKALIEVLQP LIAEHQARRK EVTDEIVKEF MTPRKLSFDF 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 :
TARS Human, Sf9Description:
Threonyl-tRNA Synthetase Human Recombinant, Sf9
Threonyl-tRNA synthetase cytoplasmic, EC 6.1.1.3, Threonine-tRNA ligase, ThrRS, MGC9344, PL-7, TARS.
Product # :
ENZ-304Price :
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Description
PL-7 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 85kDa.PL-7 is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
PL-7 is supplied in 20mM HEPES buffer pH-8, 200mM NaCl, and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Threonyl-tRNA Synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge tRNA molecules with the respective amino acids. This 83 kDa protein is an autoantigen recognized by PL-7 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that PL-7 antibodies (similar to Jo-1 antibodies) indicate an increased risk for lung involvement, but this needs to be confirmed for a larger number of cases.
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Synonyms
Threonyl-tRNA synthetase cytoplasmic, EC 6.1.1.3, Threonine-tRNA ligase, ThrRS, MGC9344, PL-7, TARS.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels immuno-dot test).
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coating concentration
0.3-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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 :
MAT1A HumanDescription:
Methionine Adenosyltransferase I Alpha Human Recombinant
EC 2.5.1.6, MAT, MATA1, SAMS, SAMS1, Methionine adenosyltransferase 1, S-adenosylmethionine synthase isoform type-1, AdoMet synthase 1, MAT 1, Methionine adenosyltransferase I/III, MAT-I/III, MAT1A, AMS1.
Product # :
ENZ-493Price :
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Description
MAT1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 414 amino acids (1-395 a.a.) and having a molecular mass of 45.6 kDa. The MAT1A is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The MAT1A protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, 100mM NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MAT1A catalyzes a two-step reaction that involves the transfer of the adenosyl moiety of ATP to methionine to form S-adenosylmethionine and tripolyphosphate, which is subsequently cleaved to PPi and Pi. S-adenosylmethionine is the source of methyl groups for most biological methylations. MAT1A is found as a homotetramer (MAT I) or a homodimer (MAT III) whereas a third form, MAT II (gamma), is encoded by the MAT2A gene. Mutations in MAT1A gene are associated with methionine adenosyltransferase deficiency. MAT1A expression also correlates with a differentiated phenotype, whereas liver cells expressing MAT2A present a dedifferentiated phenotype and lowered AdoMet synthesis. Likewise, NFκB and TNFα cause a switch from MAT1A to MAT2A expression in human hepatocellular carcinoma (HCC), which facilitates cancer cell growth.
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Synonyms
EC 2.5.1.6, MAT, MATA1, SAMS, SAMS1, Methionine adenosyltransferase 1, S-adenosylmethionine synthase isoform type-1, AdoMet synthase 1, MAT 1, Methionine adenosyltransferase I/III, MAT-I/III, MAT1A, AMS1.
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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
MGSSHHHHHS SGLVPRGSHM NGPVDGLCDH SLSEGVFMFT SESVGEGHPD KICDQISDAV LDAHLKQDPN AKVACETVCK TGMVLLCGEI TSMAMVDYQR VVRDTIKHIG YDDSAKGFDF KTCNVLVALE QQSPDIAQCV HLDRNEEDVG AGDQGLMFGY ATDETEECMP LTIILAHKLN ARMADLRRSG LLPWLRPDSK TQVTVQYMQD NGAVIPVRIH TIVISVQHNE DITLEEMRRA LKEQVIRAVV PAKYLDEDTV YHLQPSGRFV IGGPQGDAGV TGRKIIVDTY GGWGAHGGGA FSGKDYTKVD RSAAYAARWV AKSLVKAGLC RRVLVQVSYA IGVAEPLSIS IFTYGTSQKT ERELLDVVHK NFDLRPGVIV RDLDLKKPIY QKTACYGHFG RSEFPWEVPR KLVF.
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.