Search: 1000 results found for "atpase"

Description:

Modulator Of Apoptosis 1 Human Recombinant

Modulator Of Apoptosis 1, MAP1, PNMA4, Paraneoplastic Ma Antigen Family Member 4, Paraneoplastic Antigen Ma4, MAP-1, Paraneoplastic Antigen Like 4.

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PRO-1750

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Description

MOAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 374 amino acids (1-351a.a) and having a molecular mass of 41.9kDa.MOAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MOAP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Modulator of apoptosis 1 (MOAP1), is a member of the PNMA family and contains one BH3-like domain and one RASSF1-binding domain. MOAP1 was recognized by its interaction with apoptosis regulator BAX protein. MOAP1 includes a Bcl-2 homology 3 (BH3)-like motif, which is essential for the association with BAX. In addition, once over expressed MOAP1 mediates caspase-dependent apoptosis.
Synonyms
Modulator Of Apoptosis 1, MAP1, PNMA4, Paraneoplastic Ma Antigen Family Member 4, Paraneoplastic Antigen Ma4, MAP-1, Paraneoplastic Antigen Like 4.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTLRLLE DWCRGMDMNP RKALLIAGIS QSCSVAEIEE ALQAGLAPLG EYRLLGRMFR RDENRKVALV GLTAETSHAL VPKEIPGKGG IWRVIFKPPD PDNTFLSRLN EFLAGEGMTV GELSRALGHE NGSLDPEQGM IPEMWAPMLA QALEALQPALQCLKYKKLRV FSGRESPEPG EEEFGRWMFH TTQMIKAWQV PDVEKRRRLL ESLRGPALDV IRVLKINNPL ITVDECLQAL EEVFGVTDNP RELQVKYLTT YQKDEEKLSA YVLRLEPLLQ KLVQRGAIER DAVNQARLDQ VIAGAVHKTI RRELNLPEDG PAPGFLQLLV LIKDYEAAEEEEALLQAILE GNFT

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:

Adenosylhomocysteinase Human Recombinant

EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, Adenosylhomocysteinase.

Product # :

ENZ-532

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Description

AHCY Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 452 amino acids (1-432 a.a.) and having a molecular mass of 49.8 kDa. The AHCY is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AHCY Human solution containing 20mM Tris pH-8, & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.
Synonyms
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, Adenosylhomocysteinase.
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 MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMRERYS ASKPLKGARI AGCLHMTVET AVLIETLVTL GAEVQWSSCN IFSTQDHAAA AIAKAGIPVY AWKGETDEEY LWCIEQTLYF KDGPLNMILD DGGDLTNLIH TKYPQLLPGI RGISEETTTG VHNLYKMMAN GILKVPAINV NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI ITEIDPINAL QAAMEGYEVT TMDEACQEGN IFVTTTGCID IILGRHFEQM KDDAIVCNIG HFDVEIDVKW LNENAVEKVN IKPQVDRYRL KNGRRIILLA EGRLVNLGCA MGHPSFVMSN SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMS CDGPFKPDHY RY.

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:

Mannose Phosphate Isomerase Human Recombinant

Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.

Product # :

ENZ-169

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Description

MPI Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 382 amino acids (1-362) and having a molecular mass of 41.9 kDa.The MPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The MPI solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
MPI is a member of the mannose-6-phosphate isomerase type 1 family. Although MPI is expressed in all tissues, it can be found more abundantly in heart, brain and skeletal muscle. Localized to the cytoplasm, MPI exploits zinc as a cofactor and catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate. Mutations in the MPI gene are the cause of carbohydrate-deficient glycoprotein syndrome, type Ib.
Synonyms
Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.
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 MAAPRVFPLS CAVQQYAWGK MGSNSEVARL LASSDPLAQI AEDKPYAELW MGTHPRGDAK ILDNRISQKT LSQWIAENQD SLGSKVKDTF NGNLPFLFKV LSVETPLSIQ AHPNKELAEK LHLQAPQHYP DANHKPEMAI ALTPFQGLCG FRPVEEIVTF LKTAAGNNME DIFGELLLQL HQQYPGDIGC FAIYFLNLLT LKPGEAMFLE ANVPHAYLKG DCVECMACSD NTVRAGLTPK FIDVPTLCEM LSYTPSSSKD RLFLPTRSQE DPYLSIYDPP VPDFTIMKTE VPGSVTEYKV LALDSASILL MVQGTVIAST PTTQTPIPLQ RGGVLFIGAN ESVSLKLTEP KDLLIFRACC LL

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:

Phosphoadenosine phosphosulfate reductase E.Coli Recombinant

Phosphoadenosine phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, PAPS reductase, thioredoxin dependent, PAPS sulfotransferase, PAdoPS reductase, cysH, b2762, JW2732.

Product # :

ENZ-131

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Description

CYSH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-244 a.a.) and having a molecular mass of 30.1kDa.CYSH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CYSH protein solution (0.5mg/ml) conteins 20% Glycerol, Phosphate-Buffered Saline (pH 7.4) and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
CysH (Phosphoadenosine phosphosulfate reductase) is a member of the PAPS reductase family, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The 3 substrates of the CysH enzyme are adenosine 3',5'-bisphosphate, sulfite, and thioredoxin disulfide, whereas its two products are 3'-phosphoadenylyl sulfate and thioredoxin.
Synonyms
Phosphoadenosine phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, PAPS reductase, thioredoxin dependent, PAPS sulfotransferase, PAdoPS reductase, cysH, b2762, JW2732.
Physical Appearance
Sterile filtered colorless solution.
Stability
CYSH E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG LHEG.

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:

Sialidase 1 Human Recombinant

Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

Product # :

ENZ-645

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Description

NEU1 Human Recombinant produced in E. coli is a single polypeptide chain containing 393 amino acids (48-415) and having a molecular mass of 42.9 kDa.NEU1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The NEU1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Sialidase 1 (NEU1) is a lysosomal enzyme which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, the NEU1 enzyme is part of a heterotrimeric complex in cooperation with beta-galactosidase and cathepsin A. NEU1 gene mutations may lead to sialidosis, a lysosomal storage disease that can be the type 1 (cherry red -myoclonus syndrome or normosomatic type), which is late-onset, or the type 2 (the dysmorphic type), which takes place at an earlier age with increased acuteness.
Synonyms
Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.
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 MGSHMENDFG LVQPLVTMEQ LLWVSGRQIG SVDTFRIPLI TATPRGTLLA FAEARKMSSS DEGAKFIALR RSMDQGSTWS PTAFIVNDGD VPDGLNLGAV VSDVETGVVF LFYSLCAHKA GCQVASTMLV WSKDDGVSWS TPRNLSLDIG TEVFAPGPGS GIQKQREPRK GRLIVCGHGT LERDGVFCLL SDDHGASWRY GSGVSGIPYG QPKQENDFNP DECQPYELPD GSVVINARNQ NNYHCHCRIV LRSYDACDTL RPRDVTFDPE LVDPVVAAGA VVTSSGIVFF SNPAHPEFRV NLTLRWSFSN GTSWRKETVQ LWPGPSGYSS LATLEGSMDG EEQAPQLYVL YEKGRNHYTE SISVAKISVY GTL

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:

Nudix Type Motif 9 Human Recombinant

ADP-ribose pyrophosphatase mitochondrial, ADP-ribose diphosphatase, ADP-ribose phosphohydrolase, Adenosine diphosphoribose pyrophosphatase, ADPR-PPase, Nucleoside diphosphate-linked moiety X motif 9, Nudix motif 9, NUDT9, NUDT10, PSEC0099, UNQ3012/PRO9771.

Product # :

ENZ-137

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Description

NUDT9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (47-350 a.a.) and having a molecular mass of 36.5kDa (molecular weight on SDS-PAGE will appear higher).NUDT9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NUDT9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
NUDT9 is a member of a superfamily of Nudix hydrolases. NUDT9 functions as a highly specific adenosine diphosphate ribose pyrophosphatase which hydrolyzes ADP ribose to AMP and ribose 5'-phosphate. In addition, NUDT9 may be involved in the regulation of the menstrual cycle and may be related to the proliferation of glandular cells in the human endometrium.
Synonyms
ADP-ribose pyrophosphatase mitochondrial, ADP-ribose diphosphatase, ADP-ribose phosphohydrolase, Adenosine diphosphoribose pyrophosphatase, ADPR-PPase, Nucleoside diphosphate-linked moiety X motif 9, Nudix motif 9, NUDT9, NUDT10, PSEC0099, UNQ3012/PRO9771.
Physical Appearance
Sterile Filtered colorless solution.
Stability
NUDT9 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNTNVMSGSN GSKENSHNKA RTSPYPGSKV ERSQVPNEKV GWLVEWQDYK PVEYTAVSVL AGPRWADPQI SESNFSPKFN EKDGHVERKS KNGLYEIENG RPRNPAGRTG LVGRGLLGRW GPNHAADPII TRWKRDSSGN KIMHPVSGKH ILQFVAIKRK DCGEWAIPGG MVDPGEKISA TLKREFGEEA LNSLQKTSAE KREIEEKLHK LFSQDHLVIY KGYVDDPRNT DNAWMETEAV NYHDETGEIM DNLMLEAGDD AGKVKWVDIN DKLKLYASHS QFIKLVAEKR DAHWSEDSEA DCHAL.

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:

ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5 Human Recombinant

ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.

Product # :

ENZ-755

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Description

ST3GAL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (83-418a.a) and having a molecular mass of 41kDa. ST3GAL5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ST3GAL5 protein solution (1mg/ml) containing In 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, also know as ST3GAL5 belongs to the glycosyltransferase family 29 and localized to the Golgi apparatus. ST3GAL5 is known to play a part in the induction of cell differentiation, modulation of cell proliferation, maintenance of fibroblast morphology, signal transduction, and integrin-mediated cell adhesion. ST3GAL5 is a type II membrane protein which catalyzes the formation of GM3 with lactosylceramide as the substrate. Mutation in this ST3GAL5 has been connected with Amish infantile epilepsy syndrome. Transcript variants encoding various isoforms have been found for this gene.
Synonyms
ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLKLNYTT EECDMKKMHY VDPDHVKRAQ KYAQQVLQKE CRPKFAKTSM ALLFEHRYSV DLLPFVQKAP KDSEAESKYD PPFGFRKFSS KVQTLLELLP EHDLPEHLKA KTCRRCVVIG SGGILHGLEL GHTLNQFDVV IRLNSAPVEG YSEHVGNKTT IRMTYPEGAP LSDLEYYSND LFVAVLFKSV DFNWLQAMVK KETLPFWVRL FFWKQVAEKI PLQPKHFRIL NPVIIKETAF DILQYSEPQS RFWGRDKNVP TIGVIAVVLA THLCDEVSLA GFGYDLNQPR TPLHYFDSQC MAAMNFQTMH NVTTETKFLL KLVKEGVVKD LSGGIDREF

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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:

Glutathione S-Transferase Alpha 1 Mouse Recombinant

Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.

Product # :

ENZ-873

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Description

GSTA1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.a) and having a molecular mass of 28kDa.GSTA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GSTA1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The specific activity is defined as the amount of enzyme that conjugate 1.0 pmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C and is > 4,000 pmol/min/ug.

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Introduction
Membrane-bound & Cytosolic forms of GST are encoded by 2 separate supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. There are 8 different classes of soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTA1 is found in a cluster mapped to chromosome 6, and is highly expressed in the liver. GSTA1 protects the cells from reactive oxygen species.
Synonyms
Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAGKPVL HYFNARGRME CIRWLLAAAG VEFEEKFIQS PEDLEKLKKD GNLMFDQVPM VEIDGMKLAQ TRAILNYIAT KYDLYGKDMK ERALIDMYSE GILDLTEMIG QLVLCPPDQR EAKTALAKDR TKNRYLPAFE KVLKSHGQDY LVGNRLTRVD IHLLEVLLYV EEFDASLLTP FPLLKAFKSR ISSLPNVKKF LQPGSQRKPP MDAKQIQEAR KAFKIQ.

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

Description:

Methylmalonyl CoA Epimerase Human Recombinant

GLOD2, Methylmalonyl CoA Epimerase, Glyoxalase Domain Containing 2, DL-methylmalonyl-CoA Racemase.

Product # :

ENZ-013

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Description

MCEE produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (37-176a.a.) and having a molecular mass of 17.3kDa.MCEE is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MCEE protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT, 0.1mM PMSF and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
MCEE catalyzes the interconversion of D- and L-methylmalonyl-CoA throughout the degradation of branched chain amino acids, odd chain-length fatty acids, and other metabolites. MCEE protein deficiency is an autosomal recessive inborn error of amino acid metabolism, involving valine, threonine, isoleucine and methionine. This organic aciduria can appear in the neonatal period with life-threatening metabolic acidosis, hyperammonemia, feeding difficulties, pancytopenia and coma.
Synonyms
GLOD2, Methylmalonyl CoA Epimerase, Glyoxalase Domain Containing 2, DL-methylmalonyl-CoA Racemase.
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 MQVTGSVWNL GRLNHVAIAV PDLEKAAAFY KNILGAQVSE AVPLPEHGVS VVFVNLGNTK MELLHPLGRD SPIAGFLQKN KAGGMHHICI EVDNINAAVM DLKKKKIRSL SEEVKIGAHG KPVIFLHPKD CGGVLVELEQ A

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:

Matrix Metalloproteinase-9 Mouse Recombinant

Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

Product # :

ENZ-1177

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Description

MMP9 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 717 amino acids (20-730 a.a.) and having a molecular mass of 79.3 kDa. MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

MMP9 Mouse protein solution (0.25mg/ml) contains 20mM Tris-HCl pH-7.5, 10mM CaCl2, 100mM NaCl, 0.05% Brij35 and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

Biological Activity

Defined as the amount of enzyme that cleaves 1pmol of Mca-PLGLDpa-AR-NH2 per minute at pH 7.5 at 25C. Specific activity is > 500 pmol/min/ug.

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Introduction
MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.
Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
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
APYQRQPTFV VFPKDLKTSN LTDTQLAEAY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS QTLKAIRTPR CGVPDVGRFQ TFKGLKWDHH NITYWIQNYS EDLPRDMIDD AFARAFAVWG EVAPLTFTRV YGPEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGAGVQ GDAHFDDDEL WSLGKGVVIP TYYGNSNGAP CHFPFTFEGR SYSACTTDGR NDGTPWCSTT ADYDKDGKFG FCPSERLYTE HGNGEGKPCV FPFIFEGRSY SACTTKGRSD GYRWCATTAN YDQDKLYGFC PTRVDATVVG GNSAGELCVF PFVFLGKQYS SCTSDGRRDG RLWCATTSNF DTDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPLYSYLEGF PLNKDDIDGI QYLYGRGSKP DPRPPATTTT EPQPTAPPTM CPTIPPTAYP TVGPTVGPTG APSPGPTSSP SPGPTGAPSP GPTAPPTAGS SEASTESLSP ADNPCNVDVF DAIAEIQGAL HFFKDGWYWK FLNHRGSPLQ GPFLTARTWP ALPATLDSAF EDPQTKRVFF FSGRQMWVYT GKTVLGPRSL DKLGLGPEVT HVSGLLPRRL GKALLFSKGR VWRFDLKSQK VDPQSVIRVD KEFSGVPWNS HDIFQYQDKA YFCHGKFFWR VSFQNEVNKV DHEVNQVDDV GYVTYDLLQC P-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:

Histidine NADH Dehydrogenase Fe-S Protein 3 Human Recombinant

CI-30, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondria, Complex I-30kD, CI-30kD, NADH-ubiquinone oxidoreductase 30 kDa subunit.

Product # :

ENZ-662

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Description

Recombinant Human NDUFS3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 249amino acids (37-264 a.a.) and having a molecular mass of 28.7 kDa. NDUFS3 is fused to a 21 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

The NDUFS3 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 (NDUFS3) is a member of the complex I 30 kDa subunit family. NDUFS3 is one of the iron-sulfur protein (IP) components of mitochondrial NADH:ubiquinone oxidoreductase (complex I). This complex is the first enzyme complex in the electron transport chain of mitochondria. The iron-sulfur protein (IP) fraction of complex I consists of seven subunits. NDUFS3 gene mutations are linked with Leigh syndrome resulting from mitochondrial complex indefficiency.
Synonyms
CI-30, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondria, Complex I-30kD, CI-30kD, NADH-ubiquinone oxidoreductase 30 kDa subunit.
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 MESAGADTRP TVRPRNDVAH KQLSAFGEYV AEILPKYVQQ VQVSCFNELE VCIHPDGVIP VLTFLRDHTN AQFKSLVDLT AVDVPTRQNR FEIVYNLLSL RFNSRIRVKT YTDELTPIES AVSVFKAANW YEREIWDMFG VFFANHPDLR RILTDYGFEG HPFRKDFPLS GYVELRYDDE VKRVVAEPVE LAQEFRKFDL NSPWEAFPVY RQPPESLKLE AGDKKPDAK

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:

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.

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:

Glutathione S-Transferase Schistosoma Japonicum Recombinant

Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase.

Product # :

ENZ-1147

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Description

GST S. Japonicum Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-218) and having a molecular mass of 25.4 kDa.

Source

Escherichia Coli.

Formulation

GST S. Japonicum protein solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 30unit/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

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Introduction
Glutathione S-transferase, also known as GST, is an antioxidant enzyme. It is the primary defense mechanism from reactive oxygen in the cell. The enzyme GST reduces hydroperoxides of lipids via a Se-independent glutathione peroxidase actions. GST detoxifies peroxidation of lipids bi-products, for example 4-hydroxynonenal.
Synonyms
Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK

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-S Mouse Recombinant

Cathepsin S, Ctss, Cats.

Product # :

ENZ-954

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Description

CTSS Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 325 amino acids (24-340 a.a.) and having a molecular mass of 36.9kDa.CTSS is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CTSS protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.
Synonyms
Cathepsin S, Ctss, Cats.
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
EQLQRDP TLDYHWDLWK KTHEKEYKDK NEEEVRRLIW EKNLKFIMIH NLEYSMGMHT YQVGMNDMGD MTNEEISCRM GALRISRQSP KTVTFRSYSN RTLPDTVDWR EKGCVTEVKY QGSCGACWAF SAVGALEGQL KLKTGKLISL SAQNLVDCSN EEKYGNKGCG GGYMTEAFQY IIDNGGIEAD ASYPYKAMDE KCHYNSKNRA ATCSRYIQLP FGDEDALKEA VATKGPVSVG IDASHSSFFF YKSGVYDDPS CTGNVNHGVL VVGYGTLDGK DYWLVKNSWG LNFGDQGYIR MARNNKNHCG IASYCSYPEI LEHHHHHHDY WLVKNSWGLN FGDQGYIRMA RNNKNHCGIA
SYCSYPEILE 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:

DIM1 Dimethyladenosine Transferase 1 Human Recombinant

Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.

Product # :

ENZ-628

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Description

DIMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-313) and having a molecular mass of 37.5kDa.DIMT1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DIMT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 30% glycerol, 2mM DTT, 200mM NaCl and 2mM EDTA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.
Synonyms
Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.
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 MMPKVKSGAI GRRRGRQEQR RELKSAGGLM FNTGIGQHIL KNPLIINSII DKAALRPTDV VLEVGPGTGN MTVKLLEKAK KVVACELDPR LVAELHKRVQ GTPVASKLQV LVGDVLKTDL PFFDTCVANL PYQISSPFVF KLLLHRPFFR CAILMFQREF ALRLVAKPGD KLYCRLSINT QLLARVDHLM KVGKNNFRPP PKVESSVVRI EPKNPPPPIN FQEWDGLVRI TFVRKNKTLS AAFKSSAVQQ LLEKNYRIHC SVHNIIIPED FSIADKIQQI LTSTGFSDKR ARSMDIDDFI RLLHGFNAEG IHFS.

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:

Elastase-2 Mouse Recombinant

Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.

Product # :

ENZ-1105

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Description

ELANE Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (27-265a.a.) fused to a 6 aa His Tag at C-terminus containing 245 amino acids and having a molecular mass of 26.8kDa.ELANE shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

ELANE protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 30% Glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Elastase-2 (ELANE) is a serine protease that belongs to the chymotrypsin family. ELANE breaks down elastin, an elastic fiber together with collagen and controls the mechanical properties of connective tissue. The neutrophil form breaks down the Outer membrane protein A (OmpA) of E. coli and other Gram-negative bacteria. ELANEis inhibited by the acute-phase protein alpha 1-antitrypsin (A1AT), which binds almost irreversibly to the active site of elastase and trypsin.A1AT is usually secreted by the liver cells into the serum. A1AD leads to uninhibited destruction of elastic fiber by elastase.
Synonyms
Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.
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
SEIVGGRPAR PHAWPFMASL QRRGGHFCGA TLIARNFVMS AAHCVNGLNF RSVQVVLGAH
DLRRQERTRQ TFSVQRIFEN GFDPSQLLND IVIIQLNGSA TINANVQVAQ LPAQGQGVGD
RTPCLAMGWG RLGTNRPSPS VLQELNVTVV TNMCRRRVNV CTLVPRRQAG ICFGDSGGPL
VCNNLVQGID SFIRGGCGSG LYPDAFAPVA EFADWINSII RSHNDHLLTH PKDREGRTNH HHHHH

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:

Recombinant Human Heparanase-1 Active

Product # :

ENZ-1032

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Description

Heparanase Active Enzyme is produced in CHO cells.The protein is purified by several orthogonal chromatography steps.

Formulation

Heparanase Active Enzyme is supplied in20mM Acetate buffer and 750mM NaCl pH 5.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific activity of Heparanase Active Enzyme in-house standard is about 0.7 Units (1 unit = 1 μmole of reducing ends of heparan sulfate substrate formed per minute per mg Heparanase Active Enzyme at 37°C). The enzymatic activity of each Heparanase Active Enzyme batch is comparable to the standard as determined by activity assay in which immobilized heparan, released due to heparanase activity, is quantified colorimetrically. Recommended reaction buffer: 20 mM Citrate Phosphate buffer, pH 5.4; 50mM NaCl; 1mM CaCl2.

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Introduction
Heparanase is an endo β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).
Data Sheet
To view the FULL VERSION data sheet click Heparanase-1 Active Enzyme
Specificity
Heparanase Active Enzyme is identified by Western blot analysis with polyclonalrabbit anti-HPA1 antibodies as 2 subunits of 8-kDa and 50-kDa.
Shipping Conditions
Heparanase Active Enzyme is shipped frozen on dry ice unless stated otherwise by the customer. Shipping fees to N. America and W. Europe is $400 Shipping fees to Asia, Australia and E. Europe is $500
Storage Procedures
Store at –80ºC, avoid repeated freeze-thaw cycles.

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

Description:

Dual Specificity Phosphatase 3 Human Recombinant

Dual specificity phosphatase 3, VHR, Vaccinia virus phosphatase VH1-related, Dual specificity protein phosphatase VHR, Vaccinia H1-related phosphatase, serine/threonine specific protein phosphatase.

Product # :

ENZ-176

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Description

DUSP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (1-185) and having a molecular mass of 22.6 kDa.DUSP3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The DUSP3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Specific activity: >1,750 units/mg. Enzymatic activity was confirmed by measuring the amount of enzyme hydrolyzing 1 nmole of p-nitrophenyl phosphate (pNPP) per minute at 37C, pH7.5 using 10mM of substrate.

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Introduction
DUSP3 belongs to the dual specificity protein phosphatase subfamily which inactivates their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. DUSP3 negatively regulate members of the mitogen-activated protein kinase superfamily that are related to cellular proliferation and differentiation. DUSP3 is expressed in both breast and ovarian tissues and displays activity both for tyrosine-protein phosphate and serine-protein phosphate, but exhibits a strong preference toward phosphotyrosines, specifically dephosphorylates and inactivates ERK1 and ERK2.
Synonyms
Dual specificity phosphatase 3, VHR, Vaccinia virus phosphatase VH1-related, Dual specificity protein phosphatase VHR, Vaccinia H1-related phosphatase, serine/threonine specific protein phosphatase.
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 MSGSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVTPRIYVG NASVAQDIPK LQKLGITHVL NAAEGRSFMH VNTNANFYKD SGITYLGIKA NDTQEFNLSA YFERAADFID QALAQKNGRV LVHCREGYSR SPTLVIAYLM MRQKMDVKSA LSIVRQNREI GPNDGFLAQL CQLNDRLAKE GKLKP.

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:

Thiosulfate sulfurtransferase E.Coli Recombinant

ECK3411, JW3388, b3425, Thiosulfate sulfurtransferase GlpE.

Product # :

ENZ-714

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Description

glpE Recombinant produced in E. coli is a single polypeptide chain containing 131 amino acids (1-108) and having a molecular mass of 14.5kDa. glpE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The glpE solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Thiosulfate sulfurtransferase (glpE) is a mitochondrial matrix enzyme which is encoded by the nucleus. Escherichia coli glpE is a prototype for the single-domain rhodanese superfamily. glpE catalyzes the sulfur-transfer reaction in which a sulfur atom is transferred from thiosulfate to cyanide by a double-displacement mechanism.
Synonyms
ECK3411, JW3388, b3425, Thiosulfate sulfurtransferase GlpE.
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 MGSMDQFECI NVADAHQKLQ EKEAVLVDIR DPQSFAMGHA VQAFHLTNDT LGAFMRDNDF DTPVMVMCYH GNSSKGAAQY LLQQGYDVVY SIDGGFEAWQ RQFPAEVAYG A.

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:

Alpha-Galactosidase E.coli Recombinant

Mel-7, Alpha-galactosidase, b4119, JW4080.

Product # :

ENZ-609

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Description

melA E. coli Recombinant produced in E. coli is a single polypeptide chain containing 474 amino acids (1-451) and having a molecular mass of 53.0kDa.melA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
melA is a member of the glycosyl hydrolase 4 family. melA catalyze the hydrolysis of saccharides containing o-1,6,-galactoside bonds. melA catalyze the same reaction in E.coli, human and yeast but is found in different cellular sections: The E.coli melA is a cytoplasmic protein and the human and yeast melA are secretory proteins. Thus, even though the active enzyme from all three species has almost an equal molecular weight, structural resemblances, as well as dissimilarities, are probable.
Synonyms
Mel-7, Alpha-galactosidase, b4119, JW4080.
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 MGSMMSAPKI TFIGAGSTIF VKNILGDVFH REALKTAHIA LMDIDPTRLE ESHIVVRKLM DSAGASGKIT CHTQQKEALE DADFVVVAFQ IGGYEPCTVT DFEVCKRHGL EQTIADTLGP GGIMRALRTI PHLWQICEDM TEVCPDATML NYVNPMAMNT WAMYARYPHI KQVGLCHSVQ GTAEELARDL NIDPATLRYR CAGINHMAFY LELERKTADG SYVNLYPELL AAYEAGQAPK PNIHGNTRCQ NIVRYEMFKK LGYFVTESSE HFAEYTPWFI KPGREDLIER YKVPLDEYPK RCVEQLANWH KELEEYKKAS RIDIKPSREY ASTIMNAIWT GEPSVIYGNV RNDGLIDNLP QGCCVEVACL VDANGIQPTK VGTLPSHLAA LMQTNINVQT LLTEAILTEN RDRVYHAAMM DPHTAAVLGI DEIYALVDDL IAAHGDWLPG WLHR.

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:

Matrix Metalloproteinase-9 Rat Recombinant

Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

Product # :

ENZ-1185

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Description

MMP9 Rat produced in HEK293 cells is a single, glycosylated polypeptide chain containing 695 amino acids (20-708 a.a.) and having a molecular mass of 77.2kDa. MMP9 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

MMP9 Rat protein solution (0.5mg/ml) contains 20mM Tris-HCl pH-7.5, 100mM NaCl , 1mM CaCl2 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

> 2000 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-7.5 at 25C.

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Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
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
APHQRQPTYV VFPRDLKTSN LTDTQLAEDY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS ETLKAIRSPR CGVPDVGKFQ TFEGDLKWHH HNITYWIQSY TEDLPRDVID DSFARAFAVW SAVTPLTFTR VYGLEADIVI QFGVAEHGDG YPFDGKDGLL AHAFPPGPGI QGDAHFDDDE LWSLGKGAVV PTYFGNANGA PCHFPFTFEG RSYLSCTTDG RNDGKPWCGT TADYDTDRKY GFCPSENLYT EHGNGDGKPC VFPFIFEGHS YSACTTKGRS DGYRWCATTA NYDQDKLYGF CPTRADVTVT GGNSAGEMCV FPFVFLGKQY STCTGEGRSD GRLWCATTSN FDADKKWGFC PDQGYSLFLV AAHEFGHALG LDHSSVPEAL MYPMYHYHED SPLHEDDIKG IQHLYGRGSK PDPRPPATTA AEPQPTAPPT MCPTAPPMAY PTGGPTVAPT GAPSPGPTGP PTAGPSEAPT ESSTPVDNPC NVDVFDAIAD IQGALHFFKD GRYWKFSNHG GSQLQGPFLI ARTWPALPAK LNSAFEDPQS KKIFFFSGRK MWVYTGQTVL GPRSLDKLGL GSEVTLVTGL LPRRGGKALL ISRERIWKFD LKSQKVDPQS VTRLDNEFSG VPWNSHNVFH YQDKAYFCHD KYFWRVSFHN RVNQVDHVAY VTYDLLQCPH HHHHH.
Background
Matrix metalloproteinase-9 (MMP-9) is a key member of the matrix metalloproteinase family involved in the remodeling of the extracellular matrix (ECM). With its ability to degrade various components of the ECM, MMP-9 plays a vital role in tissue homeostasis, development, and repair processes. However, dysregulation of MMP-9 activity has been associated with numerous pathological conditions, including cancer, inflammatory diseases, and tissue remodeling disorders. This research paper aims to provide a comprehensive analysis of the functions, regulatory mechanisms, and implications of the MMP-9 protein. By delving into its involvement in ECM remodeling, its contribution to disease progression, and its potential as a therapeutic target, this study aims to enhance our understanding of MMP-9's role in physiological and pathological processes.
Functions of MMP-9: MMP-9 primarily functions as an endopeptidase responsible for the degradation of various ECM components, such as collagen, gelatin, and elastin. Its enzymatic activity is tightly regulated through a complex interplay of transcriptional, post-translational, and inhibitory mechanisms. Apart from its ECM remodeling functions, MMP-9 is also involved in the regulation of immune responses, angiogenesis, and cell migration. Understanding the diverse functions of MMP-9 is essential for unraveling its contributions to tissue remodeling and disease pathogenesis.
Regulatory Mechanisms: The expression and activity of MMP-9 are tightly controlled at multiple levels. Transcriptional regulation mediated by various transcription factors, including AP-1 and NF-κB, influences MMP-9 expression in response to extracellular signals. Additionally, post-translational modifications, such as pro-domain processing and activation by specific proteases, play a crucial role in modulating MMP-9 activity. Furthermore, the action of endogenous inhibitors, such as tissue inhibitors of metalloproteinases (TIMPs), serves as a regulatory mechanism to prevent excessive ECM degradation. Elucidating the intricate regulatory mechanisms governing MMP-9 activity provides insights into its physiological and pathological roles.
Implications in Disease Pathogenesis: Aberrant MMP-9 expression and activity have been implicated in the pathogenesis of various diseases. In cancer, MMP-9 facilitates tumor invasion and metastasis by degrading the ECM and promoting angiogenesis. Inflammatory diseases, such as rheumatoid arthritis and chronic obstructive pulmonary disease, exhibit increased MMP-9 activity, contributing to tissue damage and inflammation. Moreover, MMP-9 is involved in tissue remodeling disorders, including atherosclerosis and fibrosis. Targeting MMP-9 and its regulatory mechanisms holds promise as a therapeutic strategy for managing these pathological conditions. Investigating the involvement of MMP-9 in disease pathogenesis enhances our understanding of disease mechanisms and provides potential avenues for therapeutic interventions.
Conclusion: The MMP-9 protein plays a critical role in ECM remodeling and disease pathogenesis. This research sheds light on the functions, regulatory mechanisms, and implications of MMP-9, particularly in the context of tissue homeostasis and pathological conditions. Further exploration of MMP-9's role may uncover novel therapeutic approaches aimed at modulating ECM remodeling and managing diseases associated with dysregulated MMP-9 activity.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on MMP-9 for a comprehensive list of references and sources.

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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