Search: 1000 results found for "Ligase"

Description:

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.

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ENZ-1117

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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.

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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.

Description:

ASRGL1 Human Recombinant

ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.

Product # :

ENZ-837

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Description

ASRGL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 34.4kDa.ASRGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ASRGL1 protein solution (0.5mg/ml) containing Phosphate buffer saline, (pH 7.4) ,10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ASRGL1 is a 308 amino acid protein which is a member of the Ntn-hydrolase family. ASRGL1 is an autoantigenic protein which is present in the mid-piece of sperm after obstruction of the male reproductive tract. ASRGL1 is expressed highly in the testis, but is also expressed in the brain, kidney and gastrointestinal tissues. High levels of ASRGL1 are also detected in ovarian, uterine and mammary tumors in comparison with normal tissues of the same origin.
Synonyms
ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.
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 MGSMNPIVVV HGGGAGPISK DRKERVHQGM VRAATVGYGI LREGGSAVDA VEGAVVALED DPEFNAGCGS VLNTNGEVEM DASIMDGKDL SAGAVSAVQC IANPIKLARL VMEKTPHCFL TDQGAAQFAA AMGVPEIPGE KLVTERNKKR LEKEKHEKGA QKTDCQKNLG TVGAVALDCK GNVAYATSTG GIVNKMVGRV GDSPCLGAGG YADNDIGAVS TTGHGESILK VNLARLTLFH IEQGKTVEEA ADLSLGYMKS RVKGLGGLIV VSKTGDWVAK WTSTSMPWAA AKDGKLHFGI DPDDTTITDL P.

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

Description:

Carboxylesterase 1G Mouse Recombinant

Liver carboxylesterase 1, Acyl-coenzyme A:cholesterol acyltransferase, Carboxylesterase 1G, ES-x, CES1G.

Product # :

ENZ-947

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Description

CES1G produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 556 amino acids (19-565 a.a.) and having a molecular mass of 61.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). CES1G is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CES1G 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.

Biological Activity

Specific activity is > 2,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of p-nitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37C.

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Introduction
Carboxylesterase 1 (CES1G) belongs to a large family of carboxylesterases that are liable for the hydrolysis of ester and amide bonds. CES1G is also participates in the detoxification of xenobiotics prodrugs. CES1G shares the serine hydrolase fold observed in other esterases. CES1G found in rats and mice and is expressed mainly in liver, but also in kidney and lung.
Synonyms
Liver carboxylesterase 1, Acyl-coenzyme A:cholesterol acyltransferase, Carboxylesterase 1G, ES-x, CES1G.
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
ADPHPSLPPV VHTVHGKVLG KYVTLEGFSQ PVAVFLGVPF AKPPLGSLRF APPEPAEPWS FVKHTTSYPP LCYQNPEAAL RLAELFTNQR KIIPHKFSED CLYLNIYTPA DLTQNSRLPV MVWIHGGGLV IDGASTYDGV PLAVHENVVV VVIQYRLGIW GFFSTEDEHS RGNWGHLDQV AALHWVQDNI ANFGGNPGSV TIFGESAGGE SVSVLVLSPL AKNLFHRAIA QSSVIFNPCL FGRAARPLAK KIAALAGCKT TTSAAMVHCL RQKTEDELLE VSLKMKFGTV DFLGDPRESY PFLPTVIDGV LLPKAPEEIL AEKSFNTVPY MVGINKHEFG WIIPMFLDFP LSERKLDQKT AASILWQAYP ILNISEKLIP AAIEKYLGGT EDPATMTDLF LDLIGDIMFG VPSVIVSRSH RDAGAPTYMY EYQYRPSFVS DDRPQELLGD HADELFSVWG APFLKEGASE EEINLSKMVM KFWANFARNG NPNGEGLPHW PEYDQKEGYL QIGVPAQAAH RLKDKEVDFW TELRAKETAE RSSHREHVEL 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:

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:

Lysophospholipase II Human Recombinant

Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.

Product # :

ENZ-076

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Description

LYPLA2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 251 amino acids (1-231 a.a.) and having a molecular mass of 26.9kDa. The LYPLA2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LYPLA2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Acyl-protein thioesterase 2 (LYPLA2) is lysophospholipase which acts on biological membranes to regulate the multifunctional lysophospholipids. LYPLA2 may hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS.
Synonyms
Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.
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 MCGNTMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRAFPQAAN GSAKDLAILQ CHGELDPMVP VRFGALTAEK LRSVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V.

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:

Serine Dehydratase-Like Human Recombinant

Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.

Product # :

ENZ-180

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Description

SDSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 37.3 kDa.SDSL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The SDSL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.1M NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
SDSL belongs to the serine/threonine dehydratase family and function as a serinespecific dehydratase. SDSL utilizes pyridoxal phosphate and is one of three key enzymes which take part in the metabolism of Glycine and serine.
Synonyms
Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.
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 MGSHMDGPVA EHAKQEPFHV VTPLLESWAL SQVAGMPVFL KCENVQPSGS FKIRGIGHFC QEMAKKGCRH LVCSSGGNAG IAAAYAARKL GIPATIVLPE STSLQVVQRL QGEGAEVQLT GKVWDEANLR AQELAKRDGW ENVPPFDHPL IWKGHASLVQ ELKAVLRTPP GALVLAVGGG GLLAGVVAGL LEVGWQHVPI IAMETHGAHC FNAAITAGKL VTLPDITSVA KSLGAKTVAA RALECMQVCK IHSEVVEDTE AVSAVQQLLD DERMLVEPAC GAALAAIYSG LLRRLQAEGC LPPSLTSVVV IVCGGNNINS RELQALKTHL GQV.

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:

Aspartylglucosaminidase Human Recombinant

Aspartylglucosaminidase, AGU, ASRG, GA.

Product # :

ENZ-854

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Description

AGA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 346 amino acids (24-346 a.a.) and having a molecular mass of 37kDa.AGA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

AGA protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.
Synonyms
Aspartylglucosaminidase, AGU, ASRG, GA.
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 MGSSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCI.

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:

CNDP Dipeptidase 1 Human Recombinant, Active

Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.

Product # :

ENZ-1022

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Description

CNDP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 489 amino acids (27-507 a.a.) and having a molecular mass of 54.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).CNDP1 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is >3,000 pmol/min/ug, and as measured by the hydrolysis of carnosine per minute at pH6.8 at 25°C.

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Introduction
CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.
Synonyms
Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.
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
SPSPPPALLE KVFQYIDLHQ DEFVQTLKEW VAIESDSVQP VPRFRQELFR MMAVAADTLQ RLGARVASVD MGPQQLPDGQ SLPIPPVILA ELGSDPTKGT VCFYGHLDVQ PADRGDGWLT DPYVLTEVDG KLYGRGATDN KGPVLAWINA VSAFRALEQD LPVNIKFIIE GMEEAGSVAL EELVEKEKDR FFSGVDYIVI SDNLWISQRK PAITYGTRGN SYFMVEVKCR DQDFHSGTFG GILHEPMADL VALLGSLVDS SGHILVPGIY DEVVPLTEEE INTYKAIHLD LEEYRNSSRV EKFLFDTKEE ILMHLWRYPS LSIHGIEGAF DEPGTKTVIP GRVIGKFSIR LVPHMNVSAV EKQVTRHLED VFSKRNSSNK MVVSMTLGLH PWIANIDDTQ YLAAKRAIRT VFGTEPDMIR DGSTIPIAKM FQEIVHKSVV LIPLGAVDDG EHSQNEKINR WNYIEGTKLF AAFFLEMAQL HLEHHHHHH.

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:

Enolase-3 Human Recombinant

Enolase 3 (beta, muscle), Muscle-specific enolase, Skeletal muscle enolase, MSE, 2-phospho-D-glycerate hydrolyase, beta-enolase, GSD13, EC 4.2.1.11, EC 4.2.1.

Product # :

ENZ-183

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Description

ENO3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 454 amino acids (1-434) and having a molecular mass of 49.0 kDa.ENO3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ENO3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
ENO3 is one of three enolase isoenzymes in mammals. The homodimer ENO3 is located in skeletal muscle cells of adults and has a part in converting phosphoglyceric acid to phosphenolpyruvic acid in the glycolytic pathway. Mutations in ENO3 gene is linked to metabolic myopathies which is caused by low stability of the enzyme.
Synonyms
Enolase 3 (beta, muscle), Muscle-specific enolase, Skeletal muscle enolase, MSE, 2-phospho-D-glycerate hydrolyase, beta-enolase, GSD13, EC 4.2.1.11, EC 4.2.1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK GVLKAVENIN STLGPALLQK KLSVADQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK AIFAGRKFRN PKAK.
Unit Definition
One unit will convert 1.0 umole of 2-phosphoglycerate to phospho(enol)pyruvate per minute at pH7.5 at 25°C.
Specific Activity
> 1.5 units/ml.

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:

Beta-Secretase 2 Mouse Recombinant, HEK

BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

Product # :

ENZ-1188

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Description

BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa. BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

BACE2 (0.25mg/ml) is filtered in 10% (w/v) glycerol and Phosphate-Buffered Saline pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 20 pmol/min/ug in which one unit will convert 1.0pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to Mca- Pro-Leu-OH per minute at pH 3.5 at 25C.

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Synonyms
BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.
Physical Appearance
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
AVPALAPAPF TLPLQVARAT NHRASAVPGL GTPELPRADG LALALEPVRA TANFLAMVDN LQGDSGRGYY LEMLIGTPPQ KVQILVDTGS SNFAVAGAPH SYIDTYFDSE SSSTYHSKGF DVTVKYTQGS WTGFVGEDLV TIPKGFNSSF LVNIATIFES ENFFLPGIKW NGILGLAYAA LAKPSSSLET FFDSLVAQAK IPDIFSMQMC GAGLPVAGSG TNGGSLVLGG IEPSLYKGDI
WYTPIKEEWY YQIEILKLEI GGQNLNLDCR EYNADKAIVD SGTTLLRLPQ KVFDAVVEAV ARTSLIPEFS DGFWTGAQLA CWTNSETPWA YFPKISIYLR DENASRSFRI TILPQLYIQP MMGAGFNYEC YRFGISSSTN ALVIGATVME GFYVVFDRAQ RRVGFAVSPC AEIEGTTVSE ISGPFSTEDI ASNCVPAQAL NEP HHHHHH.
Background
BACE2 protein, a member of the beta-secretase family, has gained attention as a key player in the pathogenesis of neurological disorders, particularly Alzheimer's disease. This research aims to explore the function and potential therapeutic implications of BACE2 protein in neurodegenerative conditions. Understanding the role of BACE2 protein can provide valuable insights into its significance as a therapeutic target for the development of novel treatment strategies.
Function of BACE2 Protein:
BACE2 is a transmembrane aspartic protease predominantly expressed in the central nervous system. It exhibits distinct cleavage activity on various protein substrates, including neuregulins, APP-like proteins, and TGF-β. Unlike its close homolog BACE1, BACE2 has been proposed to have non-amyloidogenic processing capabilities and has shown potential neuroprotective effects.
Implications of BACE2 Protein in Alzheimer's Disease:
Alzheimer's disease is characterized by the accumulation of amyloid-beta (Aβ) peptides in the brain, which are generated through the sequential cleavage of amyloid precursor protein (APP). BACE1 is primarily responsible for the cleavage of APP, leading to the production of toxic Aβ peptides. In contrast, BACE2 has been suggested to compete with BACE1, thereby reducing the levels of Aβ generation. This has led to speculation about the neuroprotective role of BACE2 and its potential as a therapeutic target for Alzheimer's disease.
BACE2 Protein and Neuronal Survival:
Emerging evidence suggests that BACE2 may play a role in promoting neuronal survival and function. Studies have shown that BACE2 deficiency leads to impaired synaptic plasticity, reduced dendritic branching, and altered neurotransmitter release. BACE2 has also been implicated in the regulation of axonal growth and guidance during development. These findings highlight the potential importance of BACE2 in maintaining neuronal integrity.
Association of BACE2 Protein with Other Neurological Disorders:
Apart from Alzheimer's disease, BACE2 has been implicated in other neurological conditions as well. Genetic studies have identified BACE2 gene variants associated with an increased risk of Parkinson's disease, suggesting its involvement in the pathogenesis of this disorder. Furthermore, BACE2 has been linked to the regulation of insulin signaling and glucose homeostasis, making it a potential target for diabetes-associated cognitive decline.
Therapeutic Implications of BACE2 Protein:
Given its potential neuroprotective effects and modulatory role in amyloid processing, BACE2 protein has emerged as a promising therapeutic target for neurodegenerative disorders. Strategies aimed at enhancing BACE2 activity or selectively activating BACE2-mediated non-amyloidogenic processing pathways hold promise for reducing amyloid pathology and preserving neuronal function. However, further research is needed to better understand the complex mechanisms underlying BACE2 function and to develop safe and effective therapeutic interventions.
Conclusion:
The investigation of BACE2 protein has provided valuable insights into its role in neurodegenerative diseases, particularly Alzheimer's disease. The potential neuroprotective effects and modulation of amyloid processing pathways by BACE2 make it an intriguing therapeutic target. Future studies should focus on unraveling the precise mechanisms by which BACE2 influences disease pathogenesis and developing strategies to harness its therapeutic potential. The exploration of BACE2 protein opens new avenues for the development of innovative treatment approaches for neurodegenerative 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:

Aconitase-1 Human Recombinant

Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.

Product # :

ENZ-056

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Description

ACO1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 912 amino acids (1-889a.a.) and having a molecular mass of 100.8kDa.ACO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ACO1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
2mM DTT, 100mM NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
ACO1 has a part in an iron sensor. ACO1 catalyzes the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process.
Synonyms
Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.
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 MGSMSNPFAH LAEPLDPVQP GKKFFNLNKL EDSRYGRLPF SIRVLLEAAI RNCDEFLVKK QDIENILHWN VTQHKNIEVP FKPARVILQD FTGVPAVVDF AAMRDAVKKL GGDPEKINPV CPADLVIDHS IQVDFNRRAD SLQKNQDLEF ERNRERFEFL KWGSQAFHNM RIIPPGSGII HQVNLEYLAR VVFDQDGYYY PDSLVGTDSH TTMIDGLGIL GWGVGGIEAE AVMLGQPISM VLPQVIGYRL MGKPHPLVTS TDIVLTITKH LRQVGVVGKF VEFFGPGVAQ LSIADRATIA NMCPEYGATA AFFPVDEVSI TYLVQTGRDE EKLKYIKKYL QAVGMFRDFN DPSQDPDFTQ VVELDLKTVV PCCSGPKRPQ DKVAVSDMKK DFESCLGAKQ GFKGFQVAPE HHNDHKTFIY DNTEFTLAHG SVVIAAITSC TNTSNPSVML GAGLLAKKAV DAGLNVMPYI KTSLSPGSGV VTYYLQESGV MPYLSQLGFD VVGYGCMTCI GNSGPLPEPV VEAITQGDLV AVGVLSGNRN FEGRVHPNTR ANYLASPPLV IAYAIAGTIR IDFEKEPLGV NAKGQQVFLK DIWPTRDEIQ AVERQYVIPG MFKEVYQKIE TVNESWNALA TPSDKLFFWN SKSTYIKSPP FFENLTLDLQ PPKSIVDAYV LLNLGDSVTT DHISPAGNIA RNSPAARYLT NRGLTPREFN SYGSRRGNDA VMARGTFANI RLLNRFLNKQ APQTIHLPSG EILDVFDAAE RYQQAGLPLI VLAGKEYGAG SSRDWAAKGP FLLGIKAVLA ESYERIHRSN LVGMGVIPLE YLPGENADAL GLTGQERYTI IIPENLKPQM KVQVKLDTGK TFQAVMRFDT DVELTYFLNG GILNYMIRKM AK

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Description:

Aldolase C Fructose-Bisphosphate Mouse Recombinant

Aldolase 3, Brain-type aldolase, Scrapie-responsive protein 2, Zebrin II, Aldo3, Scrg2, Fructose-bisphosphate aldolase C, ALDOC.

Product # :

ENZ-868

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Description

ALDOC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-363 a.a) and having a molecular mass of 41.9kDa.ALDOC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ALDOC solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.
Synonyms
Aldolase 3, Brain-type aldolase, Scrapie-responsive protein 2, Zebrin II, Aldo3, Scrg2, Fructose-bisphosphate aldolase C, ALDOC.
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 MGSHMPHSYP ALSAEQKKEL SDIALRIVTP GKGILAADES VGSMAKRLSQ IGVENTEENR RLYRQVLFSA DDRVKKCIGG VIFFHETLYQ KDDNGVPFVR TIQDKGILVG IKVDKGVVPL AGTDGETTTQ GLDGLLERCA QYKKDGADFA KWRCVLKISD RTPSALAILE NANVLARYAS ICQQNGIVPI VEPEILPDGD HDLKRCQYVT EKVLAAVYKA LSDHHVYLEG TLLKPNMVTP GHACPIKYSP EEIAMATVTA LRRTVPPAVP GVTFLSGGQS EEEASLNLNA INRCPLPRPW ALTFSYGRAL QASALNAWRG QRDNAGAATE EFIKRAEMNG LAAQGRYEGS GDGGAAAQSL YIANHAY

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Description:

Dihydrolipoamide Dehydrogenase Human Recombinant

EC 1.8.1.4, DLD, DLDH, GCSL, PHE3, Dihydrolipoyl dehydrogenase mitochondrial, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein, LAD, E3.

Product # :

ENZ-502

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Description

DLD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 511 amino acids (36-509 a.a.) and having a molecular mass of 54.4 kDa. The DLD is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DLD solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
DLD is an L protein of the mitochondrial glycine cleavage system which is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. DLD mutations were found in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.
Synonyms
EC 1.8.1.4, DLD, DLDH, GCSL, PHE3, Dihydrolipoyl dehydrogenase mitochondrial, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein, LAD, E3.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMADQ PIDADVTVIG SGPGGYVAAI KAAQLGFKTV CIEKNETLGG TCLNVGCIPS KALLNNSHYY HMAHGKDFAS RGIEMSEVRL NLDKMMEQKS TAVKALTGGI AHLFKQNKVV HVNGYGKITG KNQVTATKAD GGTQVIDTKN ILIATGSEVT PFPGITIDED TIVSSTGALS LKKVPEKMVV IGAGVIGVEL GSVWQRLGAD VTAVEFLGHV GGVGIDMEIS KNFQRILQKQ GFKFKLNTKV TGATKKSDGK IDVSIEAASG GKAEVITCDV LLVCIGRRPF TKNLGLEELG IELDPRGRIP VNTRFQTKIP NIYAIGDVVA GPMLAHKAED EGIICVEGMA GGAVHIDYNC VPSVIYTHPE VAWVGKSEEQ LKEEGIEYKV GKFPFAANSR AKTNADTDGM VKILGQKSTD RVLGAHILGP GAGEMVNEAA LALEYGASCE DIARVCHAHP TLSEAFREAN LAASFGKSIN F.

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Description:

Enteropeptidase/ Enterokinase Bovine Recombinant His Tag

Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.

Product # :

ENZ-655

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Description

Enterokinase Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 241 amino acids with a 6 × His at C-terminus and having a molecular mass of 28.0kDa.The Enterokinase Bovine is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Bovine EK is supplied in 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.

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Introduction
Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.
Synonyms
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
Physical Appearance
Sterile liquid solution.
Stability
One year when stored at -20°C. Please avoid freeze-thaw cycles.
Unit Definition
One unit is defined as the amount of enzyme needed to cleave 50ug of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, and 2mM CaCl2.

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:

G/U Mismatch-Specific DNA Glycosylase E.Coli Recombinant

xanthine DNA glycosylase, dug, ECK3058, JW3040, ygjF, G/U mismatch-specific DNA glycosylase, Double-strand-specific uracil glycosylase, Mismatch-specific uracil DNA-glycosylase, mug.

Product # :

ENZ-703

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Description

MUG Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (1-168) and having a molecular mass of 21.1kDa. MUG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
G/U mismatch-specific DNA glycosylase (mug) is a part of the TDG/mug DNA glycosylase family. Mug is necessary for DNA damage lesion repair in stationary-phase cells. Mug protein removes three N4-ethenocytosine and takes away s the uracil base from mismatches in the order of U:G>U:A. The enzyme Uracil-N-Glycosylase removes uracil from the DNA leaving an AP position. Mug is also able to hydrolyzing the carbon-nitrogen bond among the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine plays a role in substrate recognition.
Synonyms
xanthine DNA glycosylase, dug, ECK3058, JW3040, ygjF, G/U mismatch-specific DNA glycosylase, Double-strand-specific uracil glycosylase, Mismatch-specific uracil DNA-glycosylase, mug.
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 MGSMVEDILA PGLRVVFCGI NPGLSSAGTG FPFAHPANRF WKVIYQAGFT DRQLKPQEAQ HLLDYRCGVT KLVDRPTVQA NEVSKQELHA GGRKLIEKIE DYQPQALAIL GKQAYEQGFS QRGAQWGKQT LTIGSTQIWV LPNPSGLSRV SLEKLVEAYR ELDQALVVRG R.

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:

Leukotriene A4 Hydrolase Human Recombinant

Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.

Product # :

ENZ-869

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Description

LTA4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 634 amino acids (1-611 a.a) and having a molecular mass of 71.7kDa.LTA4H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LTA4H protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Leukotriene A-4 hydrolase (LTA4H) is a bifunctional enzyme that converts leukotriene A4 to leukotriene B4 and functions as an aminopeptidase. The LTA4H enzyme is a member of the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). LTA4H participates in arachidonic acid metabolism.
Synonyms
Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.
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 MGSMPEIVDT CSLASPASVC RTKHLHLRCS VDFTRRTLTG TAALTVQSQE DNLRSLVLDT KDLTIEKVVI NGQEVKYALG ERQSYKGSPM EISLPIALSK NQEIVIEISF ETSPKSSALQ WLTPEQTSGK EHPYLFSQCQ AIHCRAILPC QDTPSVKLTY TAEVSVPKEL VALMSAIRDG ETPDPEDPSR KIYKFIQKVP IPCYLIALVV GALESRQIGP RTLVWSEKEQ VEKSAYEFSE TESMLKIAED LGGPYVWGQY DLLVLPPSFP YGGMENPCLT FVTPTLLAGD KSLSNVIAHE ISHSWTGNLV TNKTWDHFWL NEGHTVYLER HICGRLFGEK FRHFNALGGW GELQNSVKTF GETHPFTKLV VDLTDIDPDV AYSSVPYEKG FALLFYLEQL LGGPEIFLGF LKAYVEKFSY KSITTDDWKD FLYSYFKDKV DVLNQVDWNA WLYSPGLPPI KPNYDMTLTN ACIALSQRWI TAKEDDLNSF NATDLKDLSS HQLNEFLAQT LQRAPLPLGH IKRMQEVYNF NAINNSEIRF RWLRLCIQSK WEDAIPLALK MATEQGRMKF TRPLFKDLAA FDKSHDQAVR TYQEHKASMH PVTAMLVGKD LKVD.

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

Description:

Galactosidase-Beta 1 E.coli Recombinant

lacZ, beta-gal, β-gal.

Product # :

ENZ-041

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Description

The E.Coli derived recombinant protein Beta-galactosidase (114 kDa) is enzymatically inactive and Non-reactive with human serum.

Source

Escherichia Coli.

Formulation

Beta-Galactosidase (1mg/1ml) is formulated in 8M urea, 20mM Tris-HCl pH 8.0, and 10mM beta-mercaptoethanol

Purity

Protein is >95% pure as determined by SDS-PAGE, by measuring optical density at 280 nm and by method of Bradford et al.

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Introduction
Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.
Synonyms
lacZ, beta-gal, β-gal.
Physical Appearance
Sterile filtered colorless solution.
Stability
Protein should be stored for Short Term at 4°C and for long term at -20°C.
Purification Method
Purified by proprietary chromatographic technique.

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:

Aminoacylase-1 Human Recombinant

N-acyl-L-amino-acid amidohydrolase, ACY-1, ACY1D, ACYLASE, ACY1,EC 3.5.1.143.

Product # :

ENZ-296

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Description

ACY1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-408 a.a.) and having a molecular mass of 48kDa. The ACY1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ACY1 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes.
Synonyms
N-acyl-L-amino-acid amidohydrolase, ACY-1, ACY1D, ACYLASE, ACY1,EC 3.5.1.143.
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 MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYARG AQDMKCVSIQ YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ
RPEFHALRAG FALDEGIANP TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMNLTLEP EIMPAATDNR YIRAVGVPAL GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS VPALPSDS.

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:

Phosphoglycerate Mutase 1 Human Recombinant, Active

Phosphoglycerate mutase isozyme B, PGAM-B, PGAMA.

Product # :

ENZ-979

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biological activity
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Description

PGAM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids (1-254 a.a.) and having a molecular mass of 30.9 kDa. The PGAM1 is fused to a 20 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PGAM1 1mg/ml protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

Specific activity is >300 units/mg, in which One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37C.

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Introduction
PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.
Synonyms
Phosphoglycerate mutase isozyme B, PGAM-B, PGAMA.
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 MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR KAMEAVAAQG KAKK.

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:

CNDP Dipeptidase 1 Mouse Recombinant

Beta-Ala-His dipeptidase, CNDP dipeptidase 1, Carnosine dipeptidase 1.

Product # :

ENZ-977

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Description

CNDP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 500 amino acids (1-492 a.a.) and having a molecular mass of 56.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). CNDP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.
Synonyms
Beta-Ala-His dipeptidase, CNDP dipeptidase 1, Carnosine dipeptidase 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
MFSSAHSGLL EKLFHYIDLH QDEFVQTLKE WVAIESDSVQ PVPRLRQKLF QMMALAADKL RNLGAGVESI DLGSQQMPDG QSLPIPPILL AELGSDPEKP TVCFYGHLDV QPAQKDDGWL TDPYTLTEVD GKLYGRGATD NKGPVLAWIN AVSTFRALQQ DLPVNIKLIL EGMEEAGSIA LEELVMREKD HFFSSVDYIV ISDNLWLSQR KPALTYGTRG NCYFTVEVKC RDQDFHSGTF GGILNEPMAD LVALLGSLVD SSGHILIPGI YDQMAPITEG EKTMYKNIDM DLEEYQNINQ VEKFLFDTKE ELLMHLWRYP SLSIHGIEGA FDEPGTKTVI PGRVLGKFSI RLVPTMSPSV VEKQVTQHLE AVFSKRNSFN KMAVSMVLGL HPWTANVNDT QYLAAQRTIK TVFGVNPDMI RDGSTIPIAK IFQAITQKSV MMLPLGAVDD GEHSQNEKIN RWNYIQGSKL FAAFFLELSK QHSGHQMPSS VYLEHHHHHH.

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:

Arylsulfatase A Mouse Recombinant, Active

Arylsulfatase A, Arsa, As-2, AS-A, As2, ASA, AW212749, TISP73.

Product # :

ENZ-1088

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Description

ARSA Mouse Recombinant produced in Sf9 is a single, glycosylated polypeptide chain containing 498 amino acids (18-506) and having a molecular mass of 53.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ARSA Mouse is fused to an 9 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.
Synonyms
Arylsulfatase A, Arsa, As-2, AS-A, As2, ASA, AW212749, TISP73.
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
ADPSPPNILL IFADDLGYGD LGSYGHPSST TPNLDQLAEG GLRFTDFYVP VSLCTPSRAA LLTGRLPVRSGMYPGVLGPS SQGGLPLEEVTLAEVLAARG YLTGMAGKWH LGVGPEGAFL PPHQGFHRFL GIPYSHDQGP CQNLTCFPPD IPCKGGCDQG LVPIPLLANL TVEAQPPWLPGLEARYVSFS RDLMADAQRQ GRPFFLYYAS HHTHYPQFSG QSFTKRSGRG PFGDSLMELD GAVGALMTTV GDLGLLEETL VIFTADNGPELMRMSNGGCSGLLRCGKGTT FEGGVREPAL VYWPGHITPG VTHELASSLD LLPTLAALTG APLPNVTLDG VDISPLLLGT GKSPRKSVFFYPPYPDEIHG VFAVRNGKYK AHFFTQGSAH SDTTSDPACH AANRLTAHEP PLLYDLSQDP GENYNVLESI EGVSPEALQA LKHIQLLKAQYDAAMTFGPS QIAKGEDPAL QICCQPSCTP HPVCCHCPGS QSHHHHHH.

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:

FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant

FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.

Product # :

ENZ-338

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biological activity
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Description

SlyD Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids and having a molecular mass of 21 kDa.

Source

Escherichia Coli.

Formulation

SlyD protein solution contains 20mM Tris pH-7.5.

Purity

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

Biological Activity

Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

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Introduction
SlyD accessiton#: NP_755987 is a putative folding helper protein from the Escherichia coli cytosol, which has N-terminal prolyl isomerase domain of the FKBP type and a most likely unstructured C-terminal tail. SlyD is an important factor in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, and exhibits several activities including that of a peptidyl-prolyl isomerase.
Synonyms
FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.
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
MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH.

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:

Biphenyl Hydrolase-Like Human Recombinant

Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.

Product # :

ENZ-055

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Description

BPHL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 275 amino acids (38-291a.a.) and having a molecular mass of 31.1kDa.BPHL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The BPHL protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT, 50mM NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
BPHL is a Serine hydrolase that is a part of the AB hydrolase superfamily which catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL takes part in detoxification processes and is a specific alpha-amino acid ester hydrolase which favors small, hydrophobic, and aromatic side chains and does not have a strict necessity for the leaving group except for favoring a primary alcohol.
Synonyms
Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.
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
MGSSHHHHHH SSGLVPRGSH MSVTSAKVAV NGVQLHYQQT GEGDHAVLLL PGMLGSGETD FGPQLKNLNK KLFTVVAWDP RGYGHSRPPD RDFPADFFER DAKDAVDLMK ALKFKKVSLL GWSDGGITAL IAAAKYPSYI HKMVIWGANA YVTDEDSMIY EGIRDVSKWS ERTRKPLEAL YGYDYFARTC EKWVDGIRQF KHLPDGNICR HLLPRVQCPA LIVHGEKDPL VPRFHADFIH KHVKGSRLHL MPEGKHNLHL RFADEFNKLA EDFLQ

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:

Phospholipase A1 Member A Human Recombinant

Phospholipase A1 Member A, PSPLA1, PS-PLA1, Phosphatidylserine-Specific Phospholipase A1alpha, EC 3.1.1.-, NMD, Phosphatidylserine-Specific Phospholipase A1, PLA1A.

Product # :

ENZ-794

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Description

PLA1A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 454 amino acids (26-456) and having a molecular mass of 49.5kDa.PLA1A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PLA1A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Phospholipase A1 Member A (PLA1A) is a phospholipase which hydrolyzes fatty acids at the sn-1 position of phosphatidylserine and 1-acyl-2-lysophosphatidylserine. The secreted PLA1A protein hydrolyzes phosphatidylserine in liposomes. PLA1A hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1-acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI). PLA1A isoform 2 hydrolyzes lyso-PS but not PS. The hydrolysis of lyso-PS in peritoneal mast cells activated by receptors for IgE leads to stimulation of histamine production.
Synonyms
Phospholipase A1 Member A, PSPLA1, PS-PLA1, Phosphatidylserine-Specific Phospholipase A1alpha, EC 3.1.1.-, NMD, Phosphatidylserine-Specific Phospholipase A1, PLA1A.
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 MGSDAPPTPQ PKCADFQSAN LFEGTDLKVQ FLLFVPSNPS CGQLVEGSSD LQNSGFNATL GTKLIIHGFR VLGTKPSWID TFIRTLLRAT NANVIAVDWI YGSTGVYFSA VKNVIKLSLE ISLFLNKLLV LGVSESSIHI IGVSLGAHVG GMVGQLFGGQ LGQITGLDPA GPEYTRASVE ERLDAGDALF VEAIHTDTDN LGIRIPVGHV DYFVNGGQDQ PGCPTFFYAG YSYLICDHMR AVHLYISALE NSCPLMAFPC ASYKAFLAGR CLDCFNPFLL SCPRIGLVEQ GGVKIEPLPK EVKVYLLTTS SAPYCMHHSL VEFHLKELRN KDTNIEVTFL SSNITSSSKI TIPKQQRYGK GIIAHATPQC QINQVKFKFQ SSNRVWKKDR TTIIGKFCTA LLPVNDREKM VCLPEPVNLQ ASVTVSCDLK IACV.

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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