Search results
1000 results found for “hydratase”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
LGMN HumanDescription:
Legumain Human Recombinant
Legumain, PRSC1, Protease, Cysteine, 1 (Legumain), Asparaginyl Endopeptidase, Protease, Cysteine 1, EC 3.4.22.34, Cysteine Protease 1, LGMN1, AEP.
Product # :
ENZ-923Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (18-433 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 422 amino acids and having a molecular mass of 48.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).LGMN is purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LGMN protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Legumain, also known as LGMN, is a cysteine endopeptidase which demonstrates strict specificity for hydrolysis of asparaginyl bonds. Furthermore, LGMN can also cleave aspartyl bonds slowly, in particular under acidic conditions. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.
-
Synonyms
Legumain, PRSC1, Protease, Cysteine, 1 (Legumain), Asparaginyl Endopeptidase, Protease, Cysteine 1, EC 3.4.22.34, Cysteine Protease 1, LGMN1, AEP.
-
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
VPIDDPEDGG KHWVVIVAGS NGWYNYRHQA DACHAYQIIH RNGIPDEQIV VMMYDDIAYS EDNPTPGIVI NRPNGTDVYQ GVPKDYTGED VTPQNFLAVL RGDAEAVKGI GSGKVLKSGP QDHVFIYFTD HGSTGILVFP NEDLHVKDLN ETIHYMYKHK MYRKMVFYIE ACESGSMMNH LPDNINVYAT TAANPRESSY ACYYDEKRST YLGDWYSVNW MEDSDVEDLT KETLHKQYHL VKSHTNTSHV MQYGNKTIST MKVMQFQGMK RKASSPVPLP PVTHLDLTPS PDVPLTIMKR KLMNTNDLEE SRQLTEEIQR HLDARHLIEK SVRKIVSLLA ASEAEVEQLL SERAPLTGHS CYPEALLHFR THCFNWHSPT YEYALRHLYV LVNLCEKPYP LHRIKLSMDH VCLGHYHHHH 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.
- View Data Sheet
Name :
ProMatrilysinDescription:
ProMatrix Metalloproteinase-7 Recombinant
Product # :
ENZ-272Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
Source
Escherichia Coli.
Formulation
The protein contains the following additives 25mM Tris-HCl (pH 7.5),150mM NaCl, 5mM CaCl2, 0.01% Brij-35 and 0.02% NaN3.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity was found to be 1400 IU/mg.More Info
-
Physical Appearance
Sterile clear liquid 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.
-
Unit Definition
One unit is defined as the digestion of 1 µg Azocoll/min at 37°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.
- View Data Sheet
Name :
ACOT7 HumanDescription:
Acyl-CoA Thioesterase 7 Human Recombinant
Cytosolic acyl coenzyme A thioester hydrolase, Acyl-CoA thioesterase 7, Brain acyl-CoA hydrolase, BACH, CTE-IIa, CTE-II, Long chain acyl-CoA thioester hydrolase, ACOT7, ACT, ACH1, LACH, LACH1, hBACH, RP1-120G22.10.
Product # :
ENZ-214Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ACOT7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-370) and having a molecular mass of 42.6kDa.ACOT7 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACOT7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Acyl-CoA Thioesterase 7 (ACOT7) belongs to the acyl coenzyme family. ACOT7 hydrolyzes the CoA thioester of palmitoyl-CoA and other long-chain fatty acids. Decreased expression of the ACOT7 protein may be linked to mesial temporal lobe epilepsy.
-
Synonyms
Cytosolic acyl coenzyme A thioester hydrolase, Acyl-CoA thioesterase 7, Brain acyl-CoA hydrolase, BACH, CTE-IIa, CTE-II, Long chain acyl-CoA thioester hydrolase, ACOT7, ACT, ACH1, LACH, LACH1, hBACH, RP1-120G22.10.
-
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 MARPGLIHSA PGLPDTCALL QPPAASAAAA PSMSGPDVET PSAIQICRIM RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC VAALARVERT DFLSPMCIGE VAHVSAEITY TSKHSVEVQV NVMSENILTG AKKLTNKATL WYVPLSLKNV DKVLEVPPVV YSRQEQEEEG RKRYEAQKLE RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT LHGFVHGGVT MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE GKGRYLQMKA KRQGHAEPQP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ADH1A HumanDescription:
Alcohol Dehydrogenase 1A Human Recombinant
Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1A, ADH1.
Product # :
ENZ-580Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ADH1A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (1-375) and having a molecular mass of 42kDa.ADH1A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ADH1A 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.
More Info
-
Introduction
Alcohol dehydrogenase 1A (ADH1A) is a member of the alcohol dehydrogenase family. ADH1A has a key role in ethanol metabolism. ADH1A along with coenzyme NAD catalyzes the reversible conversion of organic alcohols to ketones or aldehydes. The physiologic function of ADH1A in the liver is the elimination of ethanol formed by microorganisms in the intestinal tract. ADH1A is monomorphic and predominant in fetal and infant livers, growing to be less active in gestation and only weakly active during adulthood.
-
Synonyms
Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1A, ADH1.
-
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 MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK
IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK
FSLDALITHV LPFEKINEGF DLLHSGKSIR TILMF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
AKR1C3 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member C3 Human Recombinant, His Tag
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
Product # :
ENZ-406Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
AKR1C3 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 39 kDa. The AKR1C3 is fused to a 20 amino acid His tag purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1C3 solution contains 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: approximately < 0.1 units/mg.
Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.More Info
-
Introduction
AKR1C3 is part of the aldo/keto reductase superfamily, which has at least 40 identified proteins. AKR1C3 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. AKR1C3 displays overlapping but distinct substrate specificity. AKR1C3 catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. AKR1C3 is involved in the pathogenesis of allergic diseases such as asthma. AKR1C3 controls cell growth and/or differentiation. AKR1C3 takes part in adrenal testosterone production. AKR1C3 expression is affected by metabolic disease, and its levels are considerably reduced in response to diet-induced weight loss and correlate with leptin levels.
-
Synonyms
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
-
Physical Appearance
Sterile Filtered clear colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKPGLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD RNLHYFNSDS FASHPNYPYS DEY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ALDH1A1 HumanDescription:
Aldehyde Dehydrogenase 1A1 Human Recombinant
ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.
Product # :
ENZ-453Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
The ALDH1A1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 54.8kDa and containing 501 amino acids (1-501 a.a.).
Source
Escherichia Coli.
Formulation
The ALDH1A1 protein solution is formulated in 50mM Tris-HCl pH-7.5 and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
ALDH1A1 is part of the aldehyde dehydrogenases family.
Aldehyde dehydrogenase is the 2nd protein of the main oxidative pathway of alcohol metabolism. Cytosolic and mitochondrial are 2 main liver isoforms of ALDH that are differentiateed by their electrophoretic mobility, kinetic property, & subcellular localization. The majority of Caucasians have two main isozymes, whereas just about 50% of Orientals have only the cytosolic form, excluding the mitochondrial form. ALDH1A1 is also a member of the group of corneal crystallins that assist the transparency of the cornea.
(Retinal + NAD+ + H2O = retinoate + NADH). -
Synonyms
ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLYKLADLIERDR LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKIGPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN S.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TRXR E.ColiDescription:
Thioredoxin Reductase E.Coli Recombinant
TRXB, TRXR, Thioredoxin Reductase.
Product # :
ENZ-507Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TRXR E.coli Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 321 amino acids (1-321 a.a.) and having a molecular mass of 34.6 kDa. TRXR protein is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
TRXR E.Coli solution containing 20mM Tris HCl pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is 4-5 units/ml, and was measured in a coupled assay with DTNB and NADPH. The amount of TNB generated by NADPH was measured in absorbance at 412 nm.More Info
-
Introduction
TRXR is a ubiquitous enzyme which participates in various cellular processes such as cell growth, p53 activity, and protection against oxidation stress. The mammalian Thioredoxin reductase cleaves thioredoxins as well as non-disulfide substrates such as selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxidec.
-
Synonyms
TRXB, TRXR, Thioredoxin Reductase.
-
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
MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MAP E.coliDescription:
Methionine Aminopeptidase E.Coli Recombinant
Methionine aminopeptidase, MAP, Peptidase M, map, b0168, JW0163.
Product # :
ENZ-123Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MAP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-264 a.a.) and having a molecular mass of 31.5kDa.MAP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAP protein solution (1mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Methionine aminopeptidases and designated peptidase M proteins belong to the M24 family of proteins. MAP protein removes the amino-terminal methionine residue from nascent polypeptides. The active site of MAP contains 2 adjacent divalent metal ions connected by a water molecule or hydroxide ion.
-
Synonyms
Methionine aminopeptidase, MAP, Peptidase M, map, b0168, JW0163.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL RKDDTIPAII SHDE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MDH1 HumanDescription:
Malate Dehydrogenase 1 Human Recombinant
MDH-s, MDHA, MOR2.
Product # :
ENZ-256Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
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.
More Info
-
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.
- View Data Sheet
Name :
RNLS HumanDescription:
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-653Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
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.
- View Data Sheet
Name :
MTHFS HumanDescription:
5,10-Methenyltetrahydrofolate Synthetase Human Recombinant
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
Product # :
ENZ-096Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MTHFS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-203a.a.) and having a molecular mass of 25.4 kDa. MTHFS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MTHFS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 5mM DTT and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
MTHFS is a cytosolic protein which takes part in the formate metabolic process. MTHFS along with a magnesium cofactor catalyzes the ATP-dependent reaction which reduces 5-formyltetrahydrofolate (5-MTHF) to 5,10-methenyltetrahydrofolate(MTHF). MTHF is the substrate used by MTHFR (methylenetetrahydrofolate reductase) to generate 5-MTHF. In addition, MTHF is a coenzyme used in thymidine biosynthesis by thymidylate synthase (FAD).
-
Synonyms
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAAAVSSAK RSLRGELKQR LRAMSAEERL RQSRVLSQKV IAHSEYQKSK RISIFLSMQD EIETEEIIKD IFQRGKICFI PRYRFQSNHM DMVRIESPEE ISLLPKTSWN IPQPGEGDVR EEALSTGGLD LIFMPGLGFD KHGNRLGRGK GYYDAYLKRC LQHQEVKPYT LALAFKEQIC LQVPVNENDM KVDEVLYEDS STA
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GLB1 HumanDescription:
Galactosidase-Beta 1 Human Recombinant
lacZ, beta-gal, b-gal, Acid beta-galactosidase, Lactase, Elastin receptor 1
Product # :
ENZ-1136Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GLB1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 662 amino acids (24-677 a.a.) and having a molecular mass of 74.6 kDa.GLB1 is fused to an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GLB1 Human protein (0.25mg/ml) is formulated in 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Beta-galactosidase or GLB1 is a B-galactosidase found in the lysosome. This enzyme hydrolyzes the finale B-galactose from the precursors ganglioside & keratin sulfate. GLB1 has a crucial part in the creation of elastogenesis (extracellular elastic fibers) and connective tissue development. This enzyme is similar to elastin-binding protein which is a key part in non-integrin cell surface receptor. In cells that extort elastin GLB1 is linked to tropoelastin intracellularly and act as recycling molecular chaperone.
-
Synonyms
lacZ, beta-gal, b-gal, Acid beta-galactosidase, Lactase, Elastin receptor 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
LRNATQRMFE IDYSRDSFLK DGQPFRYISG SIHYSRVPRF YWKDRLLKMK MAGLNAIQTY VPWNFHEPWP GQYQFSEDHD VEYFLRLAHE LGLLVILRPG PYICAEWEMG GLPAWLLEKE SILLRSSDPD YLAAVDKWLG VLLPKMKPLL YQNGGPVITV QVENEYGSYF ACDFDYLRFL QKRFRHHLGD DVVLFTTDGA HKTFLKCGAL QGLYTTVDFG TGSNITDAFL SQRKCEPKGP LINSEFYTGW LDHWGQPHST IKTEAVASSL YDILARGASV NLYMFIGGTN FAYWNGANSP YAAQPTSYDY DAPLSEAGDL TEKYFALRNI IQKFEKVPEG PIPPSTPKFA YGKVTLEKLK TVGAALDILC PSGPIKSLYP LTFIQVKQHY GFVLYRTTLP QDCSNPAPLS SPLNGVHDRA YVAVDGIPQG VLERNNVITL NITGKAGATL DLLVENMGRV NYGAYINDFK GLVSNLTLSS NILTDWTIFP LDTEDAVRSH LGGWGHRDSG HHDEAWAHNS SNYTLPAFYM GNFSIPSGIP DLPQDTFIQF PGWTKGQVWI NGFNLGRYWP ARGPQLTLFV PQHILMTSAP NTITVLELEW APCSSDDPEL CAVTFVDRPV IGSSVTYDHP SKPVEKRLMP PPPQKNKDSW LDHVLEHHHH 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.
- View Data Sheet
Name :
MMP 3 HumanDescription:
Matrix Metalloproteinase-3 Human Recombinant
CHDS6, MMP-3, SL-1, STMY, STMY1, STR1, Stromelysin-1, Matrix metalloproteinase-3, Transin-1, MMP3.
Product # :
ENZ-774Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MMP 3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (100-477a.a) and having a molecular mass of 45.2kDa. MMP 3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP 3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.
-
Synonyms
CHDS6, MMP-3, SL-1, STMY, STMY1, STR1, Stromelysin-1, Matrix metalloproteinase-3, Transin-1, MMP3.
-
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 MGSFRTFPGI PKWRKTHLTY RIVNYTPDLP KDAVDSAVEK ALKVWEEVTP LTFSRLYEGE ADIMISFAVR EHGDFYPFDG PGNVLAHAYA PGPGINGDAH FDDDEQWTKD TTGTNLFLVA AHEIGHSLGL FHSANTEALM YPLYHSLTDL TRFRLSQDDI NGIQSLYGPP PDSPETPLVP TEPVPPEPGT PANCDPALSF DAVSTLRGEI LIFKDRHFWR KSLRKLEPEL HLISSFWPSL PSGVDAAYEV TSKDLVFIFK GNQFWAIRGN EVRAGYPRGI HTLGFPPTVR KIDAAISDKE KNKTYFFVED KYWRFDEKRN SMEPGFPKQI AEDFPGIDSK IDAVFEEFGF FYFFTGSSQL EFDPNAKKVT HTLKSNSWLN 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.
- View Data Sheet
Name :
METAP1 HumanDescription:
Methionyl Aminopeptidase 1 Human Recombinant
Methionine aminopeptidase 1, MAP 1, MetAP 1, Peptidase M 1, METAP1, KIAA0094, MAP1A, MetAP1A.
Product # :
ENZ-604Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
METAP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386) and having a molecular mass of 45.7kDa.METAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The METAP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 3mM DTT, 40% glycerol, 200mM NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Methionine aminopeptidase 1 (METAP1) is a member of the peptidase M24A family. METAP1 removes the amino-terminal methionine from nascent proteins. METAP1 releases N-terminal amino acids, preferentially methionine, from peptides and arylamides. METAP1 is essential for normal progression through the cell cycle. The active site of METAP1 contains 2 adjacent divalent metal ions linked by a water molecule or hydroxide ion.
-
Synonyms
Methionine aminopeptidase 1, MAP 1, MetAP 1, Peptidase M 1, METAP1, KIAA0094, MAP1A, MetAP1A.
-
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 MGSMAAVETR VCETDGCSSE AKLQCPTCIK LGIQGSYFCS QECFKGSWAT HKLLHKKAKD EKAKREVSSW TVEGDINTDP WAGYRYTGKL RPHYPLMPTR PVPSYIQRPD YADHPLGMSE SEQALKGTSQ IKLLSSEDIE GMRLVCRLAR EVLDVAAGMI
KPGVTTEEID HAVHLACIAR NCYPSPLNYY NFPKSCCTSV NEVICHGIPD RRPLQEGDIV NVDITLYRNG YHGDLNETFF VGEVDDGARK LVQTTYECLM QAIDAVKPGV RYRELGNIIQ KHAQANGFSV VRSYCGHGIH KLFHTAPNVP HYAKNKAVGV MKSGHVFTIE PMICEGGWQD
ETWPDGWTAV TRDGKRSAQF EHTLLVTDTG CEILTRRLDS ARPHFMSQF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
DERADescription:
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-127Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
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.
More Info
-
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.
- View Data Sheet
Name :
NDUFS4 HumanDescription:
Histidine NADH Dehydrogenase Fe-S Protein 4 Human Recombinant
AQDQ, NDUFS4, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 mitochondrial, NADH-ubiquinone oxidoreductase 18 kDa subunit, Complex I-18 kDa, CI-18 kDa, Complex I-AQDQ, CI-AQDQ.
Product # :
ENZ-421Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NDUFS4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (43-175 a.a.) and having a molecular mass of 15.5 kDa.The NDUFS4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFS4 solution contains 20mM Tris pH-8 & 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
NDUFS4 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), the primary multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I is involved in cellular ATP production, the main source of energy for numerous vital processes in living cells. NDUFS4 removes electrons from NADH and passes them by a series of diverse protein-coupled redox centers to the electron acceptor ubiquinone. NDUFS4 presents a hotspot of mutations in the genetic apparatus of oxidative phosphorylation and the correct assembly of the subunit it encodes is essential for completion of the assembly of complex I.
-
Synonyms
AQDQ, NDUFS4, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 mitochondrial, NADH-ubiquinone oxidoreductase 18 kDa subunit, Complex I-18 kDa, CI-18 kDa, Complex I-AQDQ, CI-AQDQ.
-
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
MAQDQTQDTQ LITVDEKLDI TTLTGVPEEH IKTRKVRIFV PARNNMQSGV NNTKKWKMEF DTRERWENPL MGWASTADPL SNMVLTFSTK EDAVSFAEKN GWSYDIEERK VPKPKSKSYG ANFSWNKRTR VSTK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GAMT HumanDescription:
Guanidinoacetate N-Methyltransferase Human Recombinant
PIG2, TP53I2, GAMT, Guanidinoacetate N-methyltransferase.
Product # :
ENZ-460Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human GAMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (1-236 a.a) and having a molecular mass of 28.4 kDa. GAMT is fused to a 20 amino acids His-Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The GAMT protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GAMT is a methyltransferase that transfers guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects GAMT gene result in neurologic syndromes and muscular hypotonia, probably due to creatine deficiency and accumulation of guanidinoacetate in the brain of affected individuals. GAMT take parts in the two-step synthesis of creatine from the protein building blocks glycine, arginine, and methionine. GAMT takes part in supplying the energy for muscle contraction, and is in addition a significant player in nervous system functioning. GAMT is active in the liver, pancreas, and kidne.
-
Synonyms
PIG2, TP53I2, GAMT, Guanidinoacetate N-methyltransferase.
-
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 MSAPSATPIF APGENCSPAW GAAPAAYDAA DTHLRILGKP VMERWETPYM HALAAAASSK GGRVLEVGFG MAIAASKVQE APIDEHWIIE CNDGVFQRLR DWAPRQTHKV IPLKGLWEDV APTLPDGHFD GILYDTYPLS EETWHTHQFN FIKNHAFRLL KPGGVLTYCN LTSWGELMKS KYSDITIMFE ETQVPALLEA GFRRENIRTE VMALVPPADC RYYAFPQMIT PLVTKG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CTSD HumanDescription:
Cathepsin-D Human Recombinant
Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.
Product # :
ENZ-378Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
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
More Info
-
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.
- View Data Sheet
Name :
XYLT2 HumanDescription:
Xylosyltransferase 2 Human Recombinant
Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.
Product # :
ENZ-1086Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
XYLT2 Human Recombinant is a single, glycosylated polypeptide chain containing 839 amino acids (Gly37-Arg865, luminal domain, isoform 1, natural variant with Thr305) and having a molecular mass of 94.0kDa. XYLT2 is fused to an N-terminal linker (2 extra a.a), C-terminal linker (2 extra a.a) and C-terminal His-tag (6 extra a.a).
Source
HEK293 Cells.
Formulation
XYLT2 filtered (0.4 µm) and lyophilized in 0.05 M PBS and 0.075 M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
XYLT2 or Xylosyltransferase 2 is an enzyme which is expressed in ubiquitous and is part of the glycosyltransfe-rases family. XYLT2 promotes proteoglycans formation by attaching GAG chains to the substrate protein via transfer of xylose molecule from the donor (nucleoside diphosphate) to the protein’s serine residues. XYLT2 is present in the ER and the cis part of the Golgi, furthermore the protein is released to the extracellular matrix.
-
Synonyms
Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. XYLT2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
ASGLEEDEAG EKGRQRKPRP LDPGEGSKDT DSSAGRRGST GRRHGRWRGR AESPGVPVAK VVRAVTSRQR ASRRVPPAPP PEAPGRQNLS GAAAGEALVG AAGFPPHGDT GSVEGAPQPT DNGFTPKCEI VGKDALSALA RASTKQCQQE IANVVCLHQA GSLMPKAVPR HCQLTGKMSP GIQWDESQAQ QPMDGPPVRI AYMLVVHGRA IRQLKRLLKA VYHEQHFFYI HVDKRSDYLH REVVELAQGY DNVRVTPWRM VTIWGGASLL TMYLRSMRDL LEVPGWAWDF FINLSATDYP TRTNEELVAF LSKNRDKNFL KSHGRDNSRF IKKQGLDRLF HECDSHMWRL GERQIPAGIV VDGGSDWFVL TRSFVEYVVY TDDPLVAQLR QFYTYTLLPA ESFFHTVLEN SLACETLVDN NLRVTNWNRK LGCKCQYKHI VDWCGCSPND FKPQDFLRLQ QVSRPTFFAR KFESTVNQEV LEILDFHLYG SYPPGTPALK AYWENTYDAA DGPSGLSDVM LTAYTAFARL SLHHAATAAP PMGTPLCRFE PRGLPSSVHL YFYDDHFQGY LVTQAVQPSA QGPAETLEMW LMPQGSLKLL GRSDQASRLQ SLEVGTDWDP KERLFRNFGG LLGPLDEPVA VQRWARGPNL TATVVWIDPT YVVATSYDIT VDTETEVTQY KPPLSRPLRP GPWTVRLLQF WEPLGETRFL VLPLTFNRKL PLRKDDASWL HAGPPHNEYM EQSFQGLSSI LNLPQPELAE EAAQRHTQLT GPALEAWTDR ELSSFWSVAG LCAIGPSPCP SLEPCRLTSW SSLSPDPKSE LGPVKADGRL RKLHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NT5M HumanDescription:
5',3'-Nucleotidase, Mitochondrial Human Recombinant
5'(3')-deoxyribonucleotidase mitochondrial, 5',3'-nucleotidase, mitochondrial, Deoxy-5'-nucleotidase 2, dNT-2, NT5M, DNT2.
Product # :
ENZ-160Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NT5M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (32-228 a.a.) and having a molecular mass of 25.1kDa.NT5M is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NT5M protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
NT5M is a member of the 5'(3')-deoxyribonucleotidase family. NT5M localizes to the mitochondrial matrix. The NT5M enzyme dephosphorylates the 5'- and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides. The NT5M gene is located on chromosome 17 p11.2 in the critical region deleted in the Smith-Magenis syndrome (SMS), a genetic disease of unidentified etiology.
-
Synonyms
5'(3')-deoxyribonucleotidase mitochondrial, 5',3'-nucleotidase, mitochondrial, Deoxy-5'-nucleotidase 2, dNT-2, NT5M, DNT2.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGGRALRVLV DMDGVLADFE GGFLRKFRAR FPDQPFIALE DRRGFWVSEQ YGRLRPGLSE KAISIWESKN FFFELEPLPG AVEAVKEMAS LQNTDVFICT SPIKMFKYCP YEKYAWVEKY FGPDFLEQIV LTRDKTVVSA DLLIDDRPDI TGAEPTPSWE HVLFTACHNQ HLQLQPPRRR LHSWADDWKA ILDSKRPC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GLRX1 YeastDescription:
Glutaredoxin 1 Yeast Recombinant
Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin 1.
Product # :
ENZ-361Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Glutaredoxin Saccharamyces cerevisiae Recombinant containing 6x His tag at C-Terminus produced in E.Coli is a single, non-glycosylated, Polypeptide chain having a molecular mass of 16 kDa.
Source
Escherichia Coli.
Formulation
Glutaredoxin solution contains PBS, pH-7.5 & 0.01% Na Azide.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.
-
Synonyms
Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin 1.
-
Physical Appearance
Sterile Filtered clear colorless solution.
-
Stability
1 week at 2-10°C. For long term store at -20 to -80°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.
- View Data Sheet
Name :
MMP2 MouseDescription:
Matrix Metalloproteinase-2 Mouse Recombinant
72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
Product # :
ENZ-1117Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MMP2 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 644 amino acids (30-662 aa) and having a molecular mass of 72.4kDa.MMP2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The MMP2 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
MMP-2 or gelatinase A, is secreted by fibroblasts, cardiomyocytes, and myofibroblasts. MMP-2 has a broad feild of substrates, that contain elastin, collagen, fibroblast growth factor, endothelin, MMP-9, plasminogen, MMP-13 and TGF-beta, pointing towards bread roles of MMP-2. MMP-2 activity boosts at day four post-MI and attains a maximum by day seven.
-
Synonyms
72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
-
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
ADPEFAPSPI IKFPGDVAPK TDKELAVQYL NTFYGCPKES CNLFVLKDTL KKMQKFFGLP QTGDLDQNTI ETMRKPRCGN PDVANYNFFP RKPKWDKNQI TYRIIGYTPD LDPETVDDAF ARALKVWSDV TPLRFSRIHD GEADIMINFG RWEHGDGYPF DGKDGLLAHA FAPGTGVGGD SHFDDDELWT LGEGQVVRVK YGNADGEYCK FPFLFNGREY SSCTDTGRSD GFLWCSTTYN FEKDGKYGFC PHEALFTMGG NADGQPCKFP FRFQGTSYNS CTTEGRTDGY RWCGTTEDYD RDKKYGFCPE TAMSTVGGNS EGAPCVFPFT FLGNKYESCT SAGRNDGKVW CATTTNYDDD RKWGFCPDQG YSLFLVAAHE FGHAMGLEHS QDPGALMAPI YTYTKNFRLS HDDIKGIQEL YGPSPDADTD TGTGPTPTLG PVTPEICKQD IVFDGIAQIR GEIFFFKDRF IWRTVTPRDK PTGPLLVATF WPELPEKIDA VYEAPQEEKA VFFAGNEYWV YSASTLERGY PKPLTSLGLP PDVQQVDAAF NWSKNKKTYI FAGDKFWRYN EVKKKMDPGF PKLIADSWNA IPDNLDAVVD LQGGGHSYFF KGAYYLKLEN QSLKSVKFGS IKSDWLGCHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LOX HumanDescription:
Lysyl Oxidase Human Recombinant
Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.
Product # :
ENZ-829Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
LOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (169-417a.a) and having a molecular mass of 31.4kDa.LOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LOX protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Lysyl Oxidase also known as LOX is an extracellular copper enzyme which initiates the crosslinking of collagens and elastin. LOX catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. Adding up to crosslinking extracellular matrix proteins, LOX plays a part in tumor suppression. Moreover, defects in LOX are the cause of autosomal recessive cutis laxa type I, CL type I. Two transcript variants encoding dissimilar isoforms have been found for LOX.
-
Synonyms
Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.
-
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 MGSDDPYNPY KYSDDNPYYN YYDTYERPRP GGRYRPGYGT GYFQYGLPDL VADPYYIQAS TYVQKMSMYN LRCAAEENCL ASTAYRADVR DYDHRVLLRF PQRVKNQGTS DFLPSRPRYS WEWHSCHQHY HSMDEFSHYD LLDANTQRRV AEGHKASFCL EDTSCDYGYH RRFACTAHTQ GLSPGCYDTY GADIDCQWID ITDVKPGNYI LKVSVNPSYL VPESDYTNNV VRCDIRYTGH HAYASGCTIS PY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
METAP1D HumanDescription:
Methionyl Aminopeptidase 1D Human Recombinant
MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.
Product # :
ENZ-759Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
METAP1D Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (20-335a.a) and having a molecular mass of 37.4kDa. METAP1D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The METAP1D solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Methionyl Aminopeptidase 1D (METAP1D) is a part of the peptidase M24A family. METAP1D which is overexpressed in colon cancer cell lines participates in tumorigenesis. METAP1D eliminates methionine from the N-terminus of nascent proteins.
-
Synonyms
MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSSPLNHI YLHKQSSSQQ RRNFFFRRQR DISHSIVLPA AVSSAHPVPK HIKKPDYVTT GIVPDWGDSI EVKNEDQIQG LHQACQLARH VLLLAGKSLK VDMTTEEIDA LVHREIISHN AYPSPLGYGG FPKSVCTSVN NVLCHGIPDS RPLQDGDIIN IDVTVYYNGY HGDTSETFLV GNVDECGKKL VEVARRCRDE AIAACRAGAP FSVIGNTISH ITHQNGFQVC PHFVGHGIGS YFHGHPEIWH HANDSDLPME EGMAFTIEPI ITEGSPEFKV LEDAWTVVSL DNQRSAQFEH TVLITSRGAQ ILTKLPHEA.
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.