Search: 1000 results found for "Deaminase"

Description:

Ornithine Decarboxylase 1 Human Recombinant

ODC, Ornithine decarboxylase 1, EC 4.1.1.17.

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ENZ-181

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Description

ODC1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 484 amino acids (1-461) and having a molecular mass of 53.5 kDa.ODC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ODC1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Ornithine decarboxylase is the preliminary and rate-limiting enzyme in the biosynthetic pathway of polyamines and it takes part in the alteration of ornithine to putrescine. ODC1 is a key member of various biological processes, such as cell growth, transformation, differentiation and apoptosis. Overexpression of the ODC1 gene has a vital part in cell proliferation and the progress of cancer.
Synonyms
ODC, Ornithine decarboxylase 1, EC 4.1.1.17.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNNFGNE EFDCHFLDEG FTAKDILDQK INEVSSSDDK DAFYVADLGD ILKKHLRWLK ALPRVTPFYA VKCNDSKAIV KTLAATGTGF DCASKTEIQL VQSLGVPPER IIYANPCKQV SQIKYAANNG VQMMTFDSEV ELMKVARAHP KAKLVLRIAT DDSKAVCRLS VKFGATLRTS RLLLERAKEL NIDVVGVSFH VGSGCTDPET FVQAISDARC VFDMGAEVGF SMYLLDIGGG FPGSEDVKLK FEEITGVINP ALDKYFPSDS GVRIIAEPGR YYVASAFTLA VNIIAKKIVL KEQTGSDDED ESSEQTFMYY VNDGVYGSFN CILYDHAHVK PLLQKRPKPD EKYYSSSIWG PTCDGLDRIV ERCDLPEMHV GDWMLFENMG AYTVAAASTF NGFQRPTIYY VMSGPAWQLM QQFQNPDFPP EVEEQDASTL PVSCAWESGM KRHRAACASA SINV

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.

Description:

Cathepsin-D Human Recombinant

Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

Product # :

ENZ-378

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Description

CTSD produced in HEK293 cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-412 a.a.) and having a molecular mass of 43.4kDa. CTSD is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells

Formulation

CTSD at 1mg/ml in 50mM MES, pH5.5, 100mM NaCl and 20% Glycerol.

Purity

Greater than 95% as determined by SDS-PAGE

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Introduction
Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.
Synonyms
Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
Amino Acid Sequence
LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RLHHHHHH
Enzymatic Activity
> 20 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-3.5 at 25C.

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.

Description:

Insulin-Degrading Enzyme Human Recombinant

Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.

Product # :

ENZ-1192

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Description

IDE Human, Active Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (42-1019 a.a) containing a total of 984 amino acids, having a molecular mass of 114 kDa. IDE is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IDE solution (0.5mg/ml) contains 10% Glycerol, 100mM NaCl, 0.05% Brij35 and 20mM Tris-HCl buffer (pH 7.5).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is greater than 3,000 pmol/min/ug in which 1 unit will convert 1.0 pmole of Mca-RPPGFSAFK(Dnp)-OH to MCA-Pro-Leu-OH per minute at pH 7.5 at 25°C.

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Synonyms
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.
Physical Appearance
Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MNNPAIKRIG NHITKSPEDK REYRGLELAN GIKVLLISDP TTDKSSAALD VHIGSLSDPP NIAGLSHFCE HMLFLGTKKY PKENEYSQFL SEHAGSSNAF TSGEHTNYYF DVSHEHLEGA LDRFAQFFLC PLFDESCKDR EVNAVDSEHE KNVMNDAWRL FQLEKATGNP KHPFSKFGTG NKYTLETRPN QEGIDVRQEL LKFHSAYYSS NLMAVCVLGR ESLDDLTNLV VKLFSEVENK NVPLPEFPEH PFQEEHLKQL YKIVPIKDIR NLYVTFPIPD LQKYYKSNPG HYLGHLIGHE GPGSLLSELK SKGWVNTLVG GQKEGARGFM FFIINVDLTE EGLLHVEDII LHMFQYIQKL RAEGPQEWVF QECKDLNAVA FRFKDKERPR GYTSKIAGIL HYYPLEEVLT AEYLLEEFRP DLIEMVLDKL RPENVRVAIV SKSFEGKTDR TEEWYGTQYK QEAIPDEVIK KWQNADLNGK FKLPTKNEFI PTNFEILPLE KEATPYPALI KDTAMSKLWF KQDDKFFLPK ACLNFEFFSP FAYVDPLHCN MAYLYLELLK DSLNEYAYAA ELAGLSYDLQ NTIYGMYLSV KGYNDKQPIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIPQLLS RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS
QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGY IVFSGPRRAN GIQGLRFIIQ SEKPPHYLES RVEAFLITME KSIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI ISQQYNFDRD NTEVAYLKTL TKEDIIKFYK EMLAVDAPRR HKVSVHVLAR EMDSCPVVGE FPCQNDINLS QAPALPQPEV IQNMTEFKRG LPLFPLVKPH INFMAAKLHH HHHH.
Background
Insulin-degrading enzyme (IDE) is a crucial protease that plays a significant role in maintaining glucose homeostasis by degrading insulin and other bioactive peptides. Dysregulation of IDE has been implicated in various metabolic disorders, particularly type 2 diabetes mellitus. IDE is also associated with the clearance of amyloid-beta peptides in the brain, making it relevant to Alzheimer's disease pathology. Studying the recombinant form of IDE is fundamental to understanding its functional mechanisms and exploring potential avenues for therapeutic interventions.
The primary goal of this research is to express and purify recombinant IDE using diverse expression systems. Recombinant DNA techniques will be employed to construct expression vectors containing the IDE gene, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant IDE will be purified using affinity chromatography or other appropriate methods, facilitating subsequent biochemical and biophysical characterization.
The second objective is to investigate the substrate specificity and catalytic activity of the purified IDE. In vitro enzymatic assays will be conducted to analyse the ability of the recombinant IDE to degrade insulin and other potential substrates. The effects of various factors, such as pH, temperature, and potential modulators, on IDE activity will be evaluated. Additionally, the interactions between IDE and its substrates will be explored using binding assays.
The third objective is to elucidate the three-dimensional structure of the IDE recombinant using techniques like X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Structural insights into the active site and binding pockets of IDE will provide valuable information for understanding its substrate recognition and catalytic mechanisms. This knowledge could be instrumental in designing targeted therapeutic compounds.
By characterizing the IDE recombinant, this research aims to contribute to our understanding of its role in insulin metabolism, glucose regulation, and potential therapeutic applications. The findings from this study may have implications for the development of novel treatments for diabetes and other related disorders.

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.

Description:

Insulin-Degrading Enzyme Human Recombinant

Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulin Protease, EC 3.4.24.56, Insulinase, INSULYSIN, Insulysin, EC 3.4.24, IDE.

Product # :

ENZ-813

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Description

IDE Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Leu1019) containing 1026 amino acids including a 7 aa His tag at C-terminus. The total calculated molecular mass is 119kDa.

Source

Escherichia Coli.

Formulation

IDE filtered (0.4µm) in 20mM Tris buffer, 50mM NaCl, pH 8.0 and 10% (w/v) glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Insulin-Degrading Enzyme (IDE) is a zinc metallopeptidase which degrades intracellular insulin, and thus terminates insulins activity, as well as playing a part in intercellular peptide signaling by degrading various peptides such as amylin, bradykinin, and kallidin. The preferential affinity of the IDE enzyme for insulin results in insulin-mediated inhibition of the degradation of additional peptides such as beta-amyloid. Deficiencies in IDE protein's function are linked with Alzheimer's disease and type 2 diabetes mellitus nevertheless mutations in the IDE gene have not been demonstrated to be causative for these diseases. Insulin-Degrading Enzyme localizes mainly to the cytoplasm however in some cell types it localizes to the extracellular space, cell membrane, peroxisome, and mitochondrion. In addition, IDE degrades amyloid formed by APP and IAPP. Furthermore, IDE plays a part in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.
Synonyms
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulin Protease, EC 3.4.24.56, Insulinase, INSULYSIN, Insulysin, EC 3.4.24, IDE.
Physical Appearance
Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIAGLSHFC EHMLFLGTKK YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDESCKD REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVRQE LLKFHSAYYS SNLMAVCVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ LYKIVPIKDI RNLYVTFPIP DLQKYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV AFRFKDKERP RGYTSKIAGI LHYYPLEEVL TAEYLLEEFR PDLIEMVLDK LRPENVRVAI VSKSFEGKTD RTEEWYGTQY KQEAIPDEVI KKWQNADLNG KFKLPTKNEF IPTNFEILPL EKEATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKIIEKMA TFEIDEKRFE IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL SRLHIEALLH GNITKQAALG IMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ QRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKSIEDMTEE AFQKHIQALA IRRLDKPKKL SAECAKYWGE IISQQYNFDR DNTEVAYLKT LTKEDIIKFY KEMLAVDAPR RHKVSVHVLA REMDSCPVVG EFPCQNDINL SQAPALPQPE VIQNMTEFKR GLPLFPLVKP HINFMAAKL E HHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Isocitrate Dehydrogenase 3 (NAD+) Gamma Human Recombinant

Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial, Isocitric dehydrogenase subunit gamma, NAD(+)-specific ICDH subunit gamma, IDH3G, H-IDHG.

Product # :

ENZ-205

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Description

IDH3G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (40-393) and having a molecular mass of 41.1kDa.IDH3G is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The IDH3G solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl, 5mM DTT and 2mM EDTA.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Isocitrate dehydrogenase [NAD] subunit gamma (IDH3G) mitochondrial is a member of the isocitrate and isopropylmalate dehydrogenases family. Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. The IDH3G is a gamma subunit of one isozyme of isocitrate dehydrogenase which belongs to a distinct subclass, which utilizes NAD(+) as the electron acceptor, and is restricted to the mitochondrial matrix.
Synonyms
Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial, Isocitric dehydrogenase subunit gamma, NAD(+)-specific ICDH subunit gamma, IDH3G, H-IDHG.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MFSEQTIPPS AKYGGRHTVT MIPGDGIGPE LMLHVKSVFR HACVPVDFEE VHVSSNADEE DIRNAIMAIR RNRVALKGNI ETNHNLPPSH KSRNNILRTS LDLYANVIHC KSLPGVVTRH KDIDILIVRE NTEGEYSSLE HESVAGVVES LKIITKAKSL RIAEYAFKLA QESGRKKVTA VHKANIMKLG DGLFLQCCRE VAARYPQITF ENMIVDNTTM QLVSRPQQFD VMVMPNLYGN IVNNVCAGLV GGPGLVAGAN YGHVYAVFET ATRNTGKSIA NKNIANPTAT LLASCMMLDH LKLHSYATSI RKAVLASMDN ENMHTPDIGG QGTTSEAIQD VIRHIRVING RAVEA.

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.

Description:

Deoxyribose-Phosphate Aldolase E.Coli Recombinant

Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.

Product # :

ENZ-127

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Description

DERA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259 a.a.) and having a molecular mass of 29.9kDa.DERA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DERA solution (1mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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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.
Synonyms
Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP RFIPIARKTL KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD LVKACKEACA AANVLLKVII ETGELKDEAL IRKASEISIK AGADFIKTST GKVAVNATPE SARIMMEVIR DMGVEKTVGF KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL LASLLKALGH GDGKSASSY.

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.

Description:

Malate Dehydrogenase 1 Human Recombinant

MDH-s, MDHA, MOR2.

Product # :

ENZ-256

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Description

MDH1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-334 a.a.) and having a molecular mass of 37.4 kDa. The MDH1 is fused to an 8 amino acid His tag at C-terminus and purified by conventional chromatography.

Source

Escherichia Coli.

Formulation

The MDH1 1mg/ml protein solution contains 20mM Tris-HCl pH-8, 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 cleaves 1umole of oxalacetate and beta-NADH to L-malate and beta-NAD per minute at pH8.0 at 25°C.

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Introduction
MDH1 catalyzes the reversible oxidation of malate to oxaloacetate, using the NAD/NADH cofactor system in the citric acid cycle. MDH1 is abundantly found in the cytoplasm and is involved in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH1 regulates p53-dependent cell-cycle arrest and apoptosis in response to glucose deprivation.
Synonyms
MDH-s, MDHA, MOR2.
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). Please prevent freeze-thaw cycles.
Amino Acid Sequence
MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC ALPLLKDVIA TDKEDVAFKD LDVAILVGSM PRREGMERKD LLKANVKIFK SQGAALDKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKAQIALK LGVTANDVKN VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFVTTVQQR GAAVIKARKL SSAMSAAKAI CDHVRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV EGLPINDFSR EKMDLTAKEL TEEKESAFEF LSSALEHHHH 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.

Description:

Isovaleryl Coenzyme A Dehydrogenase Human Recombinant

FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.

Product # :

ENZ-490

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Description

IVD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (33-426 a.a.) and having a molecular mass of 45.3 kDa. The IVD is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.

Source

Escherichia Coli.

Formulation

The IVD protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.
Synonyms
FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHSLLPVDDA INGLSEEQRQ LRQTMAKFLQ EHLAPKAQEI DRSNEFKNLR EFWKQLGNLG VLGITAPVQY GGSGLGYLEH VLVMEEISRA SGAVGLSYGA HSNLCINQLV RNGNEAQKEK YLPKLISGEY IGALAMSEPN AGSDVVSMKL KAEKKGNHYI LNGNKFWITN GPDADVLIVY AKTDLAAVPA SRGITAFIVE KGMPGFSTSK KLDKLGMRGS NTCELIFEDC KIPAANILGH ENKGVYVLMS GLDLERLVLA GGPLGLMQAV LDHTIPYLHV REAFGQKIGH FQLMQGKMAD MYTRLMACRQ YVYNVAKACD EGHCTAKDCA GVILYSAECA TQVALDGIQC FGGNGYINDF PMGRFLRDAK LYEIGAGTSE VRRLVIGRAF NADFH.

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.

Description:

Alcohol Dehydrogenase 1C Human Recombinant

Alcohol dehydrogenase 1C (class I) gamma polypeptide, Alcohol dehydrogenase subunit gamma, alcohol dehydrogenase 3 (class I) gamma polypeptide, ADH gamma subunit, aldehyde reductase, ADH3, EC 1.1.1.1, EC 1.1.1.

Product # :

ENZ-622

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Description

ADH1C Human Recombinant produced in E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4 kDa.ADH1C is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ADH1C solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.
Synonyms
Alcohol dehydrogenase 1C (class I) gamma polypeptide, Alcohol dehydrogenase subunit gamma, alcohol dehydrogenase 3 (class I) gamma polypeptide, ADH gamma subunit, aldehyde reductase, ADH3, EC 1.1.1.1, EC 1.1.1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSTAGK VIKCKAAVLW ELKKPFSIEE VEVAPPKAHE VRIKMVAAGI CRSDEHVVSG NLVTPLPVIL GHEAAGIVES VGEGVTTVKP GDKVIPLFTP QCGKCRICKN PESNYCLKND LGNPRGTLQD GTRRFTCSGK PIHHFVGVST FSQYTVVDEN AVAKIDAASP LEKVCLIGCG FSTGYGSAVK VAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIAVDIN KDKFAKAKEL GATECINPQD YKKPIQEVLK EMTDGGVDFS FEVIGRLDTM MASLLCCHEA CGTSVIVGVP PDSQNLSINP MLLLTGRTWK GAIFGGFKSK ESVPKLVADF MAKKFSLDAL ITNILPFEKI NEGFDLLRSG KSIRTVLTF.

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.

Description:

Isopentenyl-Diphosphate Delta Isomerase 1 Human Recombinant

Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.

Product # :

ENZ-189

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Description

IDI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-228) and having a molecular mass of 28.6kDa.IDI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The IDI1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Isopentenyl-diphosphate isomerase 1 (IDI1) belongs to the IPP isomerase type I family and is involved in cholesterol biosynthesis. IDI1 is a peroxisomally-localized enzyme which catalyzes the interconversion of isopentenyl diphosphate (IPP) to its highly electrophilic isomer, dimethylallyl diphosphate (DMAPP), which is the substrate for the sequential reaction that results in the synthesis of farnesyl diphosphate and, eventually, cholesterol. Peroxisomal deficiency diseases such as Zellweger syndrome and neonatal adrenoleukodystrophy show a reduction in IPP isomerase activity.
Synonyms
Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MMPEINTNHL DKQQVQLLAE MCILIDENDN KIGAETKKNC HLNENIEKGL LHRAFSVFLF NTENKLLLQQ RSDAKITFPG CFTNTCCSHP LSNPAELEES DALGVRRAAQ RRLKAELGIP LEEVPPEEIN YLTRIHYKAQ SDGIWGEHEI DYILLVRKNV
TLNPDPNEIK SYCYVSKEEL KELLKKAASG EIKITPWFKI IAATFLFKWW DNLNHLNQFV DHEKIYRM.

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.

Description:

UDP-Galactose-4-Epimerase Human Recombinant

UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.

Product # :

ENZ-537

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Description

GALE Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40.4 kDa. The GALE is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GALE Human solution containing 20mM Tris pH-8, 5mM DTT, 0.1M NaCl, 1mM EDTA & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.
Synonyms
UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR RVQELTGRSV EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK PLDYYRVNLT GTIQLLEIMK AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT GGCTNPYGKS KFFIEEMIRD LCQADKTWNA VLLRYFNPTG AHASGCIGED PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD YIHVVDLAKG HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA.

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.

Description:

Biotinidase Human Recombinant

Biotinidase, EC 3.5.1.12, Biotinase, EC 3.5.1.

Product # :

ENZ-1004

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Description

BTD Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 510 amino acids (44-545a.a) and having a molecular mass of 57.8kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). BTD is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

BTD protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Biotinidase also known BTD, belongs to the nitrilase superfamily, which contains 12 families of nitrilases, amidases, carbamylases, and N-acyltrasferases. BTD catalyzes the hydrolysis of biocytin, the product of biotin-dependent carboxylase degradation, to biotin and lysine. BTD has a vital regulatory part in chromatin/DNA function. Mutations in BTD protein lead to Biotinidase deficiency.
Synonyms
Biotinidase, EC 3.5.1.12, Biotinase, EC 3.5.1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
AHTGEESVAD HHEAEYYVAA VYEHPSILSL NPLALISRQE ALELMNQNLD IYEQQVMTAA QKDVQIIVFP EDGIHGFNFT RTSIYPFLDF MPSPQVVRWN PCLEPHRFND TEVLQRLSCM AIRGDMFLVA NLGTKEPCHS SDPRCPKDGR YQFNTNVVFS NNGTLVDRYR KHNLYFEAAF DVPLKVDLIT FDTPFAGRFG IFTCFDILFF DPAIRVLRDY KVKHVVYPTA WMNQLPLLAA IEIQKAFAVA FGINVLAANV HHPVLGMTGS GIHTPLESFW YHDMENPKSH LIIAQVAKNP VGLIGAENAT GETDPSHSKF LKILSGDPYC EKDAQEVHCD EATKWNVNAP PTFHSEMMYD NFTLVPVWGK EGYLHVCSNG LCCYLLYERP TLSKELYALG VFDGLHTVHG TYYIQVCALV RCGGLGFDTC GQEITEATGI FEFHLWGNFS TSYIFPLFLT SGMTLEVPDQ LGWENDHYFL RKSRLSSGLV TAALYGRLYE RDLEHHHHHH.

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Description:

Glutamic-Oxaloacetic Transaminase 2 Mouse Recombinant

Transaminase A, KAT4, KATIV, KAT-4, KAT-IV,Kynurenine Aminotransferase 4.

Product # :

ENZ-1095

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Description

GOT2 Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (30-430 a.a.) and having a molecular mass of 46.8kDa. Mouse GOT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GOT2 solution (0.5mg/ml) contains PBS, pH 7.4 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Activity is greater than 20 units/mg, and is defined as the amount of enzyme that converts 1umole of alpha-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25℃.

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Introduction
GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 takes part in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.
Synonyms
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV,Kynurenine Aminotransferase 4.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSWWTHVEM GPPDPILGVT EAFKRDTNSK KMNLGVGAYR DDNGKPYVLP SVRKAEAQIA AKNLDKEYLP IGGLAEFCKA SAELALGENN EVLKSGRFVT VQTISGTGAL RVGASFLQRF FKFSRDVFLP KPSWGNHTPI FRDAGMQLQG YRYYDPKTCG FDFSGALEDI SKIPEQSVLL LHACAHNPTG VDPRPEQWKE IASVVKKKNL FAFFDMAYQG FASGDGDKDA WAVRHFIEQG INVCLCQSYA KNMGLYGERV GAFTVVCKDA EEAKRVESQL KILIRPLYSN PPLNGARIAA TILTSPDLRK QWLQEVKGMA DRIISMRTQL VSNLKKEGSS HNWQHITDQI GMFCFTGLKP EQVERLTKEF SVYMTKDGRI SVAGVTSGNV GYLAHAIHQV.

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Description:

Lactate Dehydrogenase B Mouse Recombinant

L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.

Product # :

ENZ-1052

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Description

LDHB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-334 a.a) and having a molecular mass of 39kDa.LDHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LDHB protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 150 units/mg, in which one unit will 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5.

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Introduction
Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
Synonyms
L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage, it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMATLKEK LIASVADDEA AVPNNKITVV GVGQVGMACA ISILGKSLAD ELALVDVLED KLKGEMMDLQ HGSLFLQTPK IVADKDYSVT ANSKIVVVTA GVRQQEGESR LNLVQRNVNV FKFIIPQIVK YSPDCTIIVV SNPVDILTYV TWKLSGLPKH RVIGSGCNLD SARFRYLMAE KLGIHPSSCH GWILGEHGDS SVAVWSGVNV AGVSLQELNP EMGTDNDSEN WKEVHKMVVD SAYEVIKLKG YTNWAIGLSV ADLIESMLKN LSRIHPVSTM VKGMYGIENE VFLSLPCILN ARGLTSVINQ KLKDDEVAQL RKSADTLWDI QKDLKDL.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glutamate Dehydrogenase 1 Human Recombinant

Glutamate Dehydrogenase 1, GLUD, GDH 1, EC 1.4.1.3, GDH, GDH1, Glutamate Dehydrogenase (NAD(P)+), Glutamate Dehydrogenase 1 Mitochondrial, EC 1.4.1, GLUD1.

Product # :

ENZ-792

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Description

GLUD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 528 amino acids (54-558) and having a molecular mass of 58.4kDa.GLUD1 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The GLUD1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Glutamate dehydrogenase 1, mitochondrial precursor (GLUD1) is a member of the Glu/Leu/Phe/Val dehydrogenases family. GLUD1 is a mitochondrial glutamate dehydrogenase, which converts L-glutamate into alpha-ketoglutarate. GLUD1 has a pivotal role in nitrogen metabolism in plants and animals. GLUD1 is observed in all organisms and catalyzes the oxidative deamination of 1-glutamate to 2-oxoglutarate. The GLUD1 enzyme has a vital role in regulating amino acid induced insulin secretion. GLUD1 gene mutations cause hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 enzyme is allosterically activated by ADP and inhibited by GTP and ATP.
Synonyms
Glutamate Dehydrogenase 1, GLUD, GDH 1, EC 1.4.1.3, GDH, GDH1, Glutamate Dehydrogenase (NAD(P)+), Glutamate Dehydrogenase 1 Mitochondrial, EC 1.4.1, GLUD1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY NEAGVTFT.

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Description:

Ribonuclease 2 Human Recombinant

EDN, RNS2, ribonuclease A family member 2, RAF3, non-secretory ribonuclease, Eosinophil-derived neurotoxin, RNase UpI-2, Ribonuclease 2, RNase 2, Ribonuclease US.

Product # :

ENZ-1175

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Description

RNASE2 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 143 amino acids (28-161 a.a.) and having a molecular mass of 16.5kDa.RNASE2 is fused to a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

RNASE2 Human protein (1mg/ml) is formulated in 20% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
RNASE2, also known as EDN, is best-known as one of the 4 major proteins found in the large specific granules of human eosinophilic leukocytes. This protein is also expressed constitutively in human liver tissue and its expression can be induced in macrophages by proinflammatory stimuli. RNASE2 is a non-secretory ribonuclease which belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. Diseases associated with EDN include Dermatitis, Atopic, 8 and Pulmonary Eosinophilia.
Synonyms
EDN, RNS2, ribonuclease A family member 2, RAF3, non-secretory ribonuclease, Eosinophil-derived neurotoxin, RNase UpI-2, Ribonuclease 2, RNase 2, Ribonuclease US.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPKPPQFTW AQWFETQHIN MTSQQCTNAM QVINNYQRRC KNQNTFLLTT FANVVNVCGN PNMTCPSNKT RKNCHHSGSQ VPLIHCNLTT PSPQNISNCR YAQTPANMFY IVACDNRDQR RDPPQYPVVP VHLDRIIHHH HHH

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.

Description:

Hydroxysteroid (17-beta) Dehydrogenase 8 Human Recombinant

E2 17-beta-dehydrogenase 8, 17-beta-hydroxysteroid dehydrogenase 8, 17-beta-HSD 8, 3-oxoacyl-[acyl-carrier-protein] reductase, Protein Ke6, Ke-6, Really interesting new gene 2 protein, Testosterone 17-beta-dehydrogenase 8, HSD17B8, FABGL, HKE6, RING2, KE6, FABG, H2-KE6, SDR30C1, D6S2245E, dJ1033B10.9.

Product # :

ENZ-108

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Description

HSD17B8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261 a.a.) and having a molecular mass of 29.1kDa.HSD17B8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HSD17B8 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 150mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
E2 17-beta-dehydrogenase 8 (HSD17B8) is a member of the short-chain dehydrogenases/reductases (SDR) family. In mice, the HSD17B8 protein is a 17-beta-hydroxysteroid dehydrogenase which can regulate the concentration of biologically active estrogens and androgens. HSD17B8 is preferentially an oxidative enzyme and inactivates E2, testosterone, and DHT. However, the HSD17B8 enzyme has some reductive activity and can synthesize E2 from E1. HSD17B8 may have a role in biosynthesis of fatty acids in mitochondria.
Synonyms
E2 17-beta-dehydrogenase 8, 17-beta-hydroxysteroid dehydrogenase 8, 17-beta-HSD 8, 3-oxoacyl-[acyl-carrier-protein] reductase, Protein Ke6, Ke-6, Really interesting new gene 2 protein, Testosterone 17-beta-dehydrogenase 8, HSD17B8, FABGL, HKE6, RING2, KE6, FABG, H2-KE6, SDR30C1, D6S2245E, dJ1033B10.9.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASQLQNRLR SALALVTGAG SGIGRAVSVR LAGEGATVAA CDLDRAAAQE TVRLLGGPGS KEGPPRGNHA AFQADVSEAR AARCLLEQVQ ACFSRPPSVV VSCAGITQDE FLLHMSEDDW DKVIAVNLKG TFLVTQAAAQ ALVSNGCRGS IINISSIVGK VGNVGQTNYA ASKAGVIGLT QTAARELGRH GIRCNSVLPG FIATPMTQKV PQKVVDKITE MIPMGHLGDP EDVADVVAFL ASEDSGYITG TSVEVTGGLF M.

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Description:

Glutamic-Oxaloacetic Transaminase 1 Mouse Recombinant

Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.

Product # :

ENZ-872

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Description

GOT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (1-413a.a) and having a molecular mass of 48.6kDa.GOT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GOT1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.
Synonyms
Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPPSVF AQVPQAPPVL VFKLTADFRD DPDPRKVNLG VGAYRTDESQ PWVLPVVRKV EQKIANDNSL NHEYLPILGL AEFRSCASRL VLGDNSPAIR ENRVGGVQSL GGTGALRIGA DFLGRWYNGT DNKNTPIYVS SPTWENHNAV FSAAGFKDIR PYCYWDAEKR GLDLQGFLND LENAPEFSIF VLHACAHNPT GTDPTPEQWK QIAAVMQRRF LFPFFDSAYQ GFASGDLEKD AWAIRYFVSE GFELFCAQSF SKNFGLYNER VGNLTVVGKE SDSVLRVLSQ MEKIVRITWS NPPAQGARIV AATLSDPELF KEWKGNVKTM ADRILTMRSE LRARLEALKT PGTWSHITEQ IGMFSFTGLN PKQVEYLVNE KHIYLLPSGR INMCGLTTKN LDYVATSIHE AVTKIQ.

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.

Description:

Hydroxysteroid (17-beta) Dehydrogenase 10 Human Recombinant

17b-HSD10, ABAD, CAMR, DUPXp11.22, ERAB, HADH2, HCD2, MHBD, MRPP2, MRX17, MRX31, SCHAD, MRXS10, SDR5C1.

Product # :

PRO-823

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Description

HSD17B10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 271 amino acids (12-261 a.a.) and having a molecular mass of 28.1 kDa. HSD17B10 protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

HSD17B10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT & 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
HSD17B10 functions in mitochondrial tRNA maturation. HSD17B10 is part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5''-ends. HSD17B10 interacts with intracellular amyloid-beta, and contributes to the neuronal dysfunction associated with Alzheimer disease.
Synonyms
17b-HSD10, ABAD, CAMR, DUPXp11.22, ERAB, HADH2, HCD2, MHBD, MRPP2, MRX17, MRX31, SCHAD, MRXS10, SDR5C1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ AKKLGNNCVF APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT YNLKKGQTHT LEDFQRVLDV NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPIG IRVMTIAPGL FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI IENPFLNGEV IRLDGAIRMQ P.

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.

Description:

N-Acetyltransferase 1 Human Recombinant

N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.

Product # :

ENZ-144

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Description

NAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-290) and having a molecular mass of 36.1 kDa.The NAT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NAT1 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 2mM DTT and 10% Glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
NAT1 is a member of the arylamine N-acetyltransferase family. NAT1 catalyzes N- or O-acetylation of heterocyclic and arylamine substrates in the detoxification of a large number of drugs. Several alleles triggering high levels of N-acetyltransferase activity were linked to colon and urinary bladder cancers, since NAT1 also bioactivate numerous known carcinogens. NAT1 aids metabolize drugs and other xenobiotics, and takes part in the detoxification of a plethora of hydrazine and arylamine drugs.
Synonyms
N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.
Physical Appearance
NAT1 is supplied as a sterile filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDIEAYLERI GYKKSRNKLD LETLTDILQH QIRAVPFENL NIHCGDAMDL GLEAIFDQVV RRNRGGWCLQ VNHLLYWALT TIGFETTMLG GYVYSTPAKK YSTGMIHLLL QVTIDGRNYI VDAGFGRSYQ MWQPLELISG KDQPQVPCIF RLTEENGFWY LDQIRREQYI PNEEFLHSDL LEDSKYRKIY SFTLKPRTIE DFESMNTYLQ TSPASVFTSK SFCSLQTPDG VHCLVGFTLT HRRFNYKDNT DLIEFKTLSE EEIEKVLKNI FNISLQRKLV PKHGDRFFTI

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.

Description:

Isocitrate Dehydrogenase-1 Human Recombinant

Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

Product # :

ENZ-193

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Description

IDH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 434 amino acids (1-414) and having a molecular mass of 48.8 kDa.IDH1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The IDH1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl,
1mM DTT, 0.1mM PMSF and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

The Specific activity is > 0.7 units/ml. One unit will convert 1.0 umole of isocitrate to alpha-ketoglutarate per minute at pH7.5 at 25C.

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Introduction
Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.
Synonyms
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKHNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPSD GTQKVTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK ELAFFANALE EVSIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKIKLA QAKL

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.

Description:

Alcohol Dehydrogenase 6 Human Recombinant

Alcohol dehydrogenase 6, ADH6, ADH-5.

Product # :

ENZ-619

Price :

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Shipping Method :

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Description

ADH6 Human Recombinant produced E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4kDa.ADH6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ADH6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Alcohol dehydrogenase 6 (ADH6) belongs to the alcohol dehydrogenase family. Alcohol dehydrogenase family members metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH6 is expressed in the stomach as well as in the liver, and it contains a glucocorticoid response element upstream of its 5’ UTR, which is a steroid hormone receptor binding site.
Synonyms
Alcohol dehydrogenase 6, ADH6, ADH-5.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSTTGQ VIRCKAAILW KPGAPFSIEE VEVAPPKAKE VRIKVVATGL CGTEMKVLGS KHLDLLYPTI LGHEGAGIVE SIGEGVSTVK PGDKVITLFL PQCGECTSCL NSEGNFCIQF KQSKTQLMSD GTSRFTCKGK SIYHFGNTST FCEYTVIKEI SVAKIDAVAP LEKVCLISCG FSTGFGAAIN TAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIGVDVN KEKFKKAQEL GATECLNPQD LKKPIQEVLF DMTDAGIDFC FEAIGNLDVL AAALASCNES YGVCVVVGVL PASVQLKISG QLFFSGRSLK GSVFGGWKSR QHIPKLVADY MAEKLNLDPL ITHTLNLDKI NEAVELMKTG KCIRCILLL.

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.

Description:

8-Oxoguanine DNA Glycosylase Human Recombinant

HMMH, HOGG1, MUTM, OGH1, AP lyase.

Product # :

ENZ-253

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

OGG1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a.) and having a molecular mass of 41.2 kDa. The OGG1 is fused to 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

0.5mg/ml solution containing PBS (pH-7.4) and 40% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3'' to the lesion.
Synonyms
HMMH, HOGG1, MUTM, OGH1, AP lyase.
Physical Appearance
Sterile filtered colourless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH TGSMPARALL PRRMGHRTLA STPALWASIP CPRSELRLDL VLPSGQSFRW REQSPAHWSG VLADQVWTLT QTEEQLHCTV YRGDKSQASR PTPDELEAVR KYFQLDVTLA QLYHHWGSVD SHFQEVAQKF QGVRLLRQDP IECLFSFICS SNNNIARITG MVERLCQAFG PRLIQLDDVT YHGFPSLQAL AGPEVEAHLR KLGLGYRARY VSASARAILE EQGGLAWLQQ LRESSYEEAH KALCILPGVG TKVADCICLM ALDKPQAVPV DVHMWHIAQRDYSWHPTTSQ AKGPSPQTNK ELGNFFRSLW GPYAGWAQAV LFSADLRQCR HAQEPPAKRRKGSKGPEG.

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.

Description:

Renalase Human Recombinant

Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.

Product # :

ENZ-653

Price :

Quantity :

Shipping Method :

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Description

RNLS Human Recombinant produced in E. coli is a single polypeptide chain containing 349 amino acids (18-342) and having a molecular mass of 38.8 kDa.RNLS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The RNLS solution contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Renalase (RNLS) is a flavin adenine dinucleotide-dependent amine oxidase which is secreted into the blood from the kidney. RNLS acts as a hormone which metabolizes circulating catecholamines that have an active role in the sympathetic and parasympathetic nervous systems. High catecholamine concentration activates plasma RNLS and promotes its secretion and synthesis.
Synonyms
Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMALLRRQ TSGPLYLAVW DKAEDSGGRM TTACSPHNPQ CTADLGAQYI TCTPHYAKKH QRFYDELLAY GVLRPLSSPI EGMVMKEGDC NFVAPQGISS IIKHYLKESG AEVYFRHRVT QINLRDDKWE VSKQTGSPEQ FDLIVLTMPV PEILQLQGDI TTLISECQRQ QLEAVSYSSR YALGLFYEAG TKIDVPWAGQ YITSNPCIRF VSIDNKKRNI ESSEIGPSLV IHTTVPFGVT YLEHSIEDVQ ELVFQQLENI LPGLPQPIAT KCQKWRHSQV TNAAANCPGQ MTLHHKPFLA CGGDGFTQSN FDGCITSALC VLEALKNYI

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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