Search: 1000 results found for "Chitinase"

Description:

Histidine NADH Dehydrogenase Fe-S Protein 2 Human Recombinant

CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.

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ENZ-737

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Description

NDUFS2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (77-463a.a) and having a molecular mass of 46.5kDa. NDUFS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NDUFS2 solution (0.25mg/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
NDUFS2 is a core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysis. Complex I takes part in the transfer of electrons from NADH to the respiratory chain. Histidine NADH Dehydrogenase Fe-S Protein 2 (NDUFS2) is required for catalytic activity. Imperfections in NDUFS2 are the source of complex I mitochondrial respiratory chain deficiency, which is characterized by many symptoms including liver failure, cardiomyopathy and neurodegeneration.
Synonyms
CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.
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 MGSVKNITLN FGPQHPAAHG VLRLVMELSG EMVRKCDPHI GLLHRGTEKL IEYKTYLQAL PYFDRLDYVS MMCNEQAYSL AVEKLLNIRP PPRAQWIRVL FGEITRLLNH IMAVTTHALD LGAMTPFFWL FEEREKMFEF YERVSGARMH AAYIRPGGVH QDLPLGLMDD IYQFSKNFSL RLDELEELLT NNRIWRNRTI DIGVVTAEEA LNYGFSGVML RGSGIQWDLR KTQPYDVYDQ VEFDVPVGSR GDCYDRYLCR VEEMRQSLRI IAQCLNKMPP GEIKVDDAKV SPPKRAEMKT SMESLIHHFK LYTEGYQVPP GATYTAIEAP KGEFGVYLVS DGSSRPYRCK IKAPGFAHLA GLDKMSKGHM LADVVAIIGT QDIVFGEVDR.

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:

Asparagine tRNA Synthetase Brugia Malayi Recombinant

Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.

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ENZ-941

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Description

AsnRS Brugia Malayi Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 568 amino acids (including a 6xHis Tag at N-terminus) and having a molecular mass of 64.5kDa.The AsnRS is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AsnRS 0.2µm filtered solution containing 20mM HEPES, pH7.4, 100mM NaCl, 5mM MgCl2, 5mM b-Mercaptoethanol and 10 % Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The AsnRS enzyme is a member of the ligases family, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. An asparagine-tRNA ligase is an enzyme which catalyzes the chemical reaction: ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn. The three substrates of the AsnRS enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its three products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).
Synonyms
Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.
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 MTVYICPETG DDGNDGSELK PLRTLYQAMI ITKSSKGDFL IRTKKDGKQV WEAASKTALK KSWKRYEQEM LKNEKVAAKM LEKDATEVGV KAALEEAKKV QIELDTSLSY ITGVKIRDLV KHRNERVCIK GWIHRMRRQG KSLMFFILRD GTGFLQVLLM DKLCQTYDAL TVNTECTVEI YGAIKEVPEG KEAPNGHELI ADFWKIIGNA PSGGIDNVLN EEASVDKMLD NRHLVIRGEN AAALLRLRAA ATRAMREHFY NAGYVEVAPP TLVQTQVEGG STLFNLDYFG EQSFLTQSSQ LYLETCIPTL GDVFLHCSVL QGGKISHSST LAEYAHVEAE CPFITLDDLM EKIEELVCDT VDRLLADEEA KKLLEHINPK FQPPERPFLR MEYKDAIKWL QEHNVENEFG NTFTYGEDIA EAAERFMTDT INKPILLNRF PSEIKAFYMQ RDAKDNTLTE SVDLLMPGVG EIVGGSMRIW KFDELSKAFK NVEIDPKPYY WYLDQRLYGT CPHGGYGLGL ERFICWLTNT NHIRDVCLYP RFVGRCVP.

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:

Biliverdin Reductase B Mouse Recombinant

Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.

Product # :

ENZ-1074

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Description

BLVRB Mouse Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-206 a.a) and having a molecular mass of 24.6kDa.BLVRB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BLVRB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.
Synonyms
Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.
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 MGSMTVKKIA IFGATGRTGL TTLAQAVQAG YEVTVLVRDS SRLPSEGPQP AHVVVGDVRQ AADVDKTVAG QEAVIVLLGT GNDLSPTTVM SEGTRNIVTA MKAHGVDKVV ACTSAFLLWD PTKVPPRLQD VTDDHIRMHK ILQESGLKYV AVMPPHIGDQ PLTGAYTVTL DGRGPSRVIS KHDLGHFMLR CLTTNEYDGH TTYPSHQYD.

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:

Deoxyribodipyrimidine photo-lyase E.Coli Recombinant

800x600 ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

Product # :

ENZ-362

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Description

800x600 800x600 phrB E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 495 amino acids (1-472) and having a molecular mass of 56.1kDa.phrB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The phrB solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Deoxyribodipyrimidine photo-lyase (phrB) is a member of the DNA photolyase class-1 family. phrB takes part in repair of UV radiation-inducedDNA damage. phrB catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidinedimers (in cis-syn configuration), which are formed between closest bases on the same DNA strand uponexposure to ultraviolet radiation.
Synonyms
ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708.
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 MGSMTTHLVW FRQDLRLHDN LALAAACRNS SARVLALYIA TPRQWATHNM SPRQAELINA QLNGLQIALA EKGIPLLFRE VDDFVASVEI VKQVCAENSV THLFYNYQYE VNERARDVEV ERALRNVVCE GFDDSVILPP GAVMTGNHEM YKVFTPFKNA WLKRLREGMP ECVAAPKVRS SGSIEPSPSI TLNYPRQSFD TAHFPVEEKA AIAQLRQFCQ NGAGEYEQQR DFPAVEGTSR LSASLATGGL SPRQCLHRLL AEQPQALDGG AGSVWLNELI WREFYRHLIT YHPSLCKHRP FIAWTDRVQW QSNPAHLQAW QEGKTGYPIV DAAMRQLNST GWMHNRLRMI TASFLVKDLL IDWREGERYF MSQLIDGDLA ANNGGWQWAA STGTDAAPYF RIFNPTTQGE KFDHEGEFIR QWLPELRDVP GKVVHEPWKW AQKAGVTLDY PQPIVEHKEA RVQTLAAYEA ARKGK.

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Description:

Galactose-1-Phosphate Uridylyltransferase Human Recombinant

Galactose-1-phosphate uridylyltransferase, Gal-1-P uridylyltransferase, UDP-glucose--hexose-1-phosphate uridylyltransferase, GALT.

Product # :

ENZ-358

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Description

GALT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-379) and having a molecular mass of 45.9kDa.GALT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GALT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Galactose-1-Phosphate Uridylyltransferase (GALT) catalyzes the 2nd step of the “Leloir pathway” of galactose metabolism, specifically the conversion of UDP-glucose + galactose-1-phosphate to glucose-1-phosphate + UDP-galactose. The deficiency of the GALT enzyme results in typical galactosemia in humans and may be fatal in the newborn stage if lactose is not eliminated from the diet. Galactosemia pathophysiology has not been clearly defined.
Synonyms
Galactose-1-phosphate uridylyltransferase, Gal-1-P uridylyltransferase, UDP-glucose--hexose-1-phosphate uridylyltransferase, GALT.
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 MGSHMSRSGT DPQQRQQASE ADAAAATFRA NDHQHIRYNP LQDEWVLVSA HRMKRPWQGQ VEPQLLKTVP RHDPLNPLCP GAIRANGEVN PQYDSTFLFD NDFPALQPDA PSPGPSDHPL FQAKSARGVC KVMCFHPWSD VTLPLMSVPE IRAVVDAWAS VTEELGAQYP WVQIFENKGA MMGCSNPHPH CQVWASSFLP DIAQREERSQ QAYKSQHGEP LLMEYSRQEL LRKERLVLTS EHWLVLVPFW ATWPYQTLLL PRRHVRRLPE LTPAERDDLA SIMKKLLTKY DNLFETSFPY SMGWHGAPTG SEAGANWNHW QLHAHYYPPL LRSATVRKFM VGYEMLAQAQ RDLTPEQAAE RLRALPEVHY HLGQKDRETA TIA.

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Description:

Hydroxyacid Oxidase 1 Human Recombinant, Active

Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.

Product # :

ENZ-1094

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Description

HAO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-370 a.a) and having a molecular mass of 45.0kDa. HAO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HAO1 protein solution (1mg/ml) contains 20% glycerol, 20mM Tris-Hcl (pH8.0) and 0.5M NaCl.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 3000 pmol/min/ug, and defined as the amount of enzyme that oxidize glyoxylate at pH 8.0 at 25C.

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Introduction
Glycolate oxidase (HAO1) is a part of the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyses the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate by reducing oxygen to hydrogen peroxide. HAO1 is expressed mainly in the liver and pancreas and is most active on twocarbon substrates such as glycolate. HAO1 isthe main cause of hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.
Synonyms
Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.
Physical Appearance
Sterile filtered yellowish 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 KDRWGSMLPR LICINDYEQH AKSVLPKSIY DYYRSGANDE ETLADNIAAF SRWKLYPRMLRNVAETDLST SVLGQRVSMP ICVGATAMQR MAHVDGELAT VRACQSLGTG MMLSSWATSS IEEVAEAGPE ALRWLQLYIY KDREVTKKLVRQAEKMGYKA IFVTVDTPYL GNRLDDVRNR FKLPPQLRMK NFETSTLSFS PEENFGDDSG LAAYVAKAID PSISWEDIKW LRRLTSLPIVAKGILRGDDA REAVKHGLNG ILVSNHGARQ LDGVPATIDV LPEIVEAVEG KVEVFLDGGV RKGTDVLKAL ALGAKAVFVG RPIVWGLAFQGEKGVQDVLE ILKEEFRLAM ALSGCQNVKV IDKTLVRKNP LAVSKI.

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:

Guanine Deaminase Human Recombinant

Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.

Product # :

ENZ-970

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Description

GDA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 454amino acids (1-454 a.a) and having a molecular mass of 51kDa. GDA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDA protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.
Synonyms
Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.
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
MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ QEKLAKEWCF KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSSIDLPLL EWLTKYTFPA EHRFQNIDFA EEVYTRVVRR TLKNGTTTAC YFATIHTDSS LLLADITDKF GQRAFVGKVC MDLNDTFPEY KETTEESIKE TERFVSEMLQ KNYSRVKPIV TPRFSLSCSE TLMGELGNIA KTRDLHIQSH ISENRDEVEA VKNLYPSYKN YTSVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS NILLINKVNE KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI NPKASDSPID LFYGDFFGDI SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV.

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:

Peptidase D Human Recombinant

Xaa-Pro dipeptidase, X-Pro dipeptidase, Imidodipeptidase, Peptidase D, Proline dipeptidase, Prolidase, PRD, PEPD, Xaa-Pro dipeptidase isoform 1, PROLIDASE.

Product # :

ENZ-856

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Description

PEPD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-493a.a.) and having a molecular mass of 56.9kDa.PEPD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Peptidase D, also known as PEPD, Is a part of the peptidase family. PEPD is involved in collagen metabolism due to the high level of iminoacids in collagen. PEPD recycles proline, and sets the pace for the production of collagen. PEPD is also parts dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position.
Synonyms
Xaa-Pro dipeptidase, X-Pro dipeptidase, Imidodipeptidase, Peptidase D, Proline dipeptidase, Prolidase, PRD, PEPD, Xaa-Pro dipeptidase isoform 1, PROLIDASE.
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 MGSMAAATGP SFWLGNETLK VPLALFALNR QRLCERLRKN PAVQAGSIVV LQGGEETQRY CTDTGVLFRQ ESFFHWAFGV TEPGCYGVID VDTGKSTLFV PRLPASHATW MGKIHSKEHF KEKYAVDDVQ YVDEIASVLT SQKPSVLLTL RGVNTDSGSVCREASFDGIS KFEVNNTILH PEIVECRVFK TDMELEVLRY TNKISSEAHR EVMKAVKVGM KEYELESLFE HYCYSRGGMR HSSYTCICGS GENSAVLHYG HAGAPNDRTI QNGDMCLFDM GGEYYCFASD ITCSFPANGK FTADQKAVYE AVLRSSRAVM GAMKPGVWWP DMHRLADRIH LEELAHMGIL SGSVDAMVQA HLGAVFMPHG LGHFLGIDVH DVGGYPEGVE RIDEPGLRSL RTARHLQPGM VLTVEPGIYF IDHLLDEALA DPARASFLNR EVLQRFRGFG GVRIEEDVVV TDSGIELLTC VPRTVEEIEA CMAGCDKAFT PFSGPK.

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:

Thiamine Triphosphatase Human Recombinant

MGC2652, THTP, THTPASE.

Product # :

ENZ-249

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Description

Recombinant Human THTPA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230 a.a.) and having a molecular mass of 27.7 kDa. THTPA is fused to a 20 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

The THTPA 1mg/ml protein solution contains 20mM Tris-HCL buffer, pH-8, 1mM DTT and 10% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
THTPA enzyme is part of the THTPase family. THTPA is localized to the cytoplasm and expressed at small quantities in a variety of tissues, including testis, uterus, prostate, bladder, lung and kidney. THTPA is a hydrolase that catalyzes the H2O-dependent hydrolysis of thiamine triphosphate (THTP) to thiamine diphosphate (THDP), the main form of thiamine within the cell. THTPA occurs as a monomer and is activated at an optimal pH of 8.5.
Synonyms
MGC2652, THTP, THTPASE.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store THTPA 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 MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA DHWLRRREDS GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG LGAGDVAAVL GPLGLQEVAS FVTKRSAWKL VLLGADEEEP QLRVDLDTAD FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG.

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:

Cyclophilin-F Rat Recombinant Bioactive

Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.

Product # :

ENZ-1019

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Description

Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206 a.a) and having a molecular mass of 21.2Da. Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Cyclophilin F protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 1,300 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmol of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.

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Introduction
PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
Synonyms
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.
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 MGSCSDGGAR GANSSSQNPL VYLDVGADGQ PLGRVVLELK ADVVPKTAEN FRALCTGEKG FGYKGSTFHR VIPAFMCQAG DFTNHNGTGG KSIYGSRFPD ENFTLKHVGP GVLSMANAGP NTNGSQFFIC TIKTDWLDGK HVVFGHVKEG MDVVKKIESF GSKSGKTSKK IVITDCGQLS.

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:

IMP Dehydrogenase 1 Human Recombinant

EC 1.1.1.205, IMP (inosine monophosphate) dehydrogenase 1, LCA11, RP10, IMPDH 1, IMPD 1, IMPDH-I, SwSS2608, DKFZp781N0678.

Product # :

ENZ-525

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Description

IMPDH1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 534 amino acids (1-514 a.a.) and having a molecular mass of 57.5 kDa. The IMPDH1 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IMPDH1 Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
IMPDH1 is a rate limiting enzyme in the de novo synthesis of guanine nucleotides and consequently participates in the regulation of cell growth. IMPDH1 takes part in the development of malignancy and the growth progression of some tumors. IMPDH1 performs as a homotetramer to regulate cell growth. IMPDH1 catalyzes the synthesis of xanthine monophosphate (XMP) from inosine-5''-monophosphate (IMP). Defects in this gene are a cause of retinitis pigmentosa type 10 (RP10).
Synonyms
EC 1.1.1.205, IMP (inosine monophosphate) dehydrogenase 1, LCA11, RP10, IMPDH 1, IMPD 1, IMPDH-I, SwSS2608, DKFZp781N0678.
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 MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKMRHGFS GIPITETGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRIELVVAPA GVTLKEANEI LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS QKQLLCGAAV GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGARSLSVLR SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY.

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:

Aldehyde Dehydrogenase 1A1 Human Recombinant, Active

ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

Product # :

ENZ-1179

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Description

The ALDH1A1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 54.8kDa and containing 501 amino acids (1-501 a.a.).

Source

Escherichia Coli.

Formulation

The ALDH1A1 protein solution is formulated at 1mg/ml in 50mM Tris-HCl pH-7.5 and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

> 700 pmol/min/ug, as determined by the increase of NADH in absorbance at 340nm resulting from the reduction of NAD at pH 8.8 at 37C.

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Introduction
ALDH1A1 is part of the aldehyde dehydrogenases family.
Aldehyde dehydrogenase is the 2nd protein of the main oxidative pathway of alcohol metabolism. Cytosolic and mitochondrial are 2 main liver isoforms of ALDH that are differentiateed by their electrophoretic mobility, kinetic property, & subcellular localization. The majority of Caucasians have two main isozymes, whereas just about 50% of Orientals have only the cytosolic form, excluding the mitochondrial form. ALDH1A1 is also a member of the group of corneal crystallins that assist the transparency of the cornea.
(Retinal + NAD+ + H2O = retinoate + NADH).
Synonyms
ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
Amino Acid Sequence
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLYKLADLIERDR LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKIGPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN S.

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

Description:

Galactosidase-Beta 1 Human Recombinant

lacZ, beta-gal, b-gal, Acid beta-galactosidase, Lactase, Elastin receptor 1

Product # :

ENZ-1136

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Description

GLB1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 662 amino acids (24-677 a.a.) and having a molecular mass of 74.6 kDa.GLB1 is fused to an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GLB1 Human protein (0.25mg/ml) is formulated in 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Beta-galactosidase or GLB1 is a B-galactosidase found in the lysosome. This enzyme hydrolyzes the finale B-galactose from the precursors ganglioside & keratin sulfate. GLB1 has a crucial part in the creation of elastogenesis (extracellular elastic fibers) and connective tissue development. This enzyme is similar to elastin-binding protein which is a key part in non-integrin cell surface receptor. In cells that extort elastin GLB1 is linked to tropoelastin intracellularly and act as recycling molecular chaperone.
Synonyms
lacZ, beta-gal, b-gal, Acid beta-galactosidase, Lactase, Elastin receptor 1
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
LRNATQRMFE IDYSRDSFLK DGQPFRYISG SIHYSRVPRF YWKDRLLKMK MAGLNAIQTY VPWNFHEPWP GQYQFSEDHD VEYFLRLAHE LGLLVILRPG PYICAEWEMG GLPAWLLEKE SILLRSSDPD YLAAVDKWLG VLLPKMKPLL YQNGGPVITV QVENEYGSYF ACDFDYLRFL QKRFRHHLGD DVVLFTTDGA HKTFLKCGAL QGLYTTVDFG TGSNITDAFL SQRKCEPKGP LINSEFYTGW LDHWGQPHST IKTEAVASSL YDILARGASV NLYMFIGGTN FAYWNGANSP YAAQPTSYDY DAPLSEAGDL TEKYFALRNI IQKFEKVPEG PIPPSTPKFA YGKVTLEKLK TVGAALDILC PSGPIKSLYP LTFIQVKQHY GFVLYRTTLP QDCSNPAPLS SPLNGVHDRA YVAVDGIPQG VLERNNVITL NITGKAGATL DLLVENMGRV NYGAYINDFK GLVSNLTLSS NILTDWTIFP LDTEDAVRSH LGGWGHRDSG HHDEAWAHNS SNYTLPAFYM GNFSIPSGIP DLPQDTFIQF PGWTKGQVWI NGFNLGRYWP ARGPQLTLFV PQHILMTSAP NTITVLELEW APCSSDDPEL CAVTFVDRPV IGSSVTYDHP SKPVEKRLMP PPPQKNKDSW LDHVLEHHHH HH

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

Description:

Prolylcarboxypeptidase Human Recombinant

Angiotensinase-C, PRCP, Proline Carboxypeptidase.

Product # :

ENZ-1178

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Description

PRCP Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-496 a.a) containing a total of 481 amino acids, having a molecular mass of 54.3 kDa. PRCP is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The PRCP solution (0.25mg/ml) contains 30% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 3,000 pmol/min/μg, and is defined as the amount of enzyme that converts 1pmole of Z-ProAla-OH/min. at pH-4 at 25˚C.

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Introduction
PRCP is a plasma protein which takes part in the cleavage of C-terminal amino acids linked to proline in proteinfor example angiotensin-2 & 3 at acidic pHenvironment rather than at neutral pHwhich exhibit less activity. This cleavage is important since Angiotensin-2 takes part in regulation of blood pressure & electrolyte balance which is essential to hypertension.
Synonyms
Angiotensinase-C, PRCP, Proline Carboxypeptidase.
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
LRPALRALGS LHLPTNPTSL PAVAKNYSVL YFQQKVDHFG FNTVKTFNQR YLVADKYWKK NGGSILFYTG NEGDIIWFCN NTGFMWDVAE ELKAMLVFAE HRYYGESLPF GDNSFKDSRH LNFLTSEQAL ADFAELIKHL KRTIPGAENQ PVIAIGGSYG GMLAAWFRMK YPHMVVGALA ASAPIWQFED LVPCGVFMKI VTTDFRKSGP HCSESIHRSW DAINRLSNTG SGLQWLTGALHLCSPLTSQD IQHLKDWISE TWVNLAMVDY PYASNFLQPL PAWPIKVVCQ YLKNPNVSDS LLLQNIFQAL NVYYNYSGQV KCLNISETAT SSLGTLGWSY QACTEVVMPF CTNGVDDMFE PHSWNLKELS DDCFQQWGVR PRPSWITTMY GGKNISSHTN IVFSNGELDP WSGGGVTKDI TDTLVAVTIS EGAHHLDLRT KNALDPMSVL LARSLEVRHM KNWIRDFYDS AGKQ 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:

Sorbitol Dehydrogenase Human Recombinant

EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH

Product # :

ENZ-1151

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Description

SORD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-357a.a.) and having a molecular mass of 38.3kDa.SORD is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SORD solution (0.5mg/ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.5) and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity > 15unit/mg. Defined by the amount of enzyme that catalyze the reduction 1.0 umole of D-fructose to D-sorbitol per minute at pH 7.5 at 37˚C.

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Introduction
SORD, also referred to as sorbitol dehydrogenase, belongs to the zinc-containing alcohol dehydrogenase family. It is widely produced. The lens of the eyeand the kidney are the protein highest production areas. Zinc-dependent interconversion of polyols, like sorbitol and xylitol, are enzymatically catalysed to their respective ketoses by SORD.
Synonyms
EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,
SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH
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
MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP

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:

2S albumin Recombinant

Product # :

ALR-022

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Description

Recombinant 2S albumin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 14kDa.Cor a 14.0101 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

Cor a 14.0101 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Seed storage proteins have been identified as major allergens in several other tree nuts and peanut. 2S albumin Cor a 14.0101 is a seed storage protein in hazelnut. Sensitization to Cor a 14.0101 may cause a severe allergic reaction, mainly in children.
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.Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgE-type human antibodies.2. Immunodot test with positive/negative samples
Applications
Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.

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-B Mouse Recombinant

Cathepsin B, Cathepsin B1, CTSB.

Product # :

PRO-2304

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Description

CTSB Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 330 amino acids (18-339a.a.) and having a molecular mass of 36.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTSB is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Cathepsin B preproprotein (CTSB) is a papain-family cysteine protease which is normally located in lysosomes. CTSB is able to degrade several extracellular matrix components at both neutral and acidic pH and has been implicated in the progression of some human and rodent tumors progression and arthritis.
Synonyms
Cathepsin B, Cathepsin B1, CTSB.
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
HDKPSFHPLS DDLINYINKQ NTTWQAGRNF YNVDISYLKK LCGTVLGGPK LPGRVAFGED IDLPETFDAR EQWSNCPTIG QIRDQGSCGS CWAFGAVEAI SDRTCIHTNG RVNVEVSAED LLTCCGIQCG DGCNGGYPSG AWSFWTKKGL VSGGVYNSHV GCLPYTIPPC EHHVNGSRPP CTGEGDTPRC NKSCEAGYSP SYKEDKHFGY TSYSVSNSVK EIMAEIYKNG PVEGAFTVFS DFLTYKSGVY KHEAGDMMGG HAIRILGWGV ENGVPYWLAA NSWNLDWGDN GFFKILRGEN HCGIESEIVA GIPRTDQYWG RFLEHHHHHH.

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:

Aldehyde Dehydrogenase 1A1 Human Recombinant

ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

Product # :

ENZ-453

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Description

The ALDH1A1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 54.8kDa and containing 501 amino acids (1-501 a.a.).

Source

Escherichia Coli.

Formulation

The ALDH1A1 protein solution is formulated in 50mM Tris-HCl pH-7.5 and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
ALDH1A1 is part of the aldehyde dehydrogenases family.
Aldehyde dehydrogenase is the 2nd protein of the main oxidative pathway of alcohol metabolism. Cytosolic and mitochondrial are 2 main liver isoforms of ALDH that are differentiateed by their electrophoretic mobility, kinetic property, & subcellular localization. The majority of Caucasians have two main isozymes, whereas just about 50% of Orientals have only the cytosolic form, excluding the mitochondrial form. ALDH1A1 is also a member of the group of corneal crystallins that assist the transparency of the cornea.
(Retinal + NAD+ + H2O = retinoate + NADH).
Synonyms
ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
Amino Acid Sequence
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLYKLADLIERDR LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKIGPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN S.

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

Description:

RNA Exonuclease 2 Human Recombinant

REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.

Product # :

ENZ-715

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Description

REXO2 Human Recombinant produced in E. coli is a single polypeptide chain containing 235 amino acids (26-237) and having a molecular mass of 26.8kDa. REXO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The REXO2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
EXO2 is a 3'-to-5' exonuclease specific for small (primarily 5 nucleotides or less in length) single-stranded RNA and DNA oligomers. RNA Exonuclease 2 (REXO2) takes part in DNA repair, replication, and recombination, and in RNA processing and degradation. EXO2 is involved in resistance of human cells to UV-C-induced cell death via its part in the DNA repair process.
Synonyms
REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.
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 MGSVREGGAA MAAGESMAQR MVWVDLEMTG LDIEKDQIIE MACLITDSDL NILAEGPNLI IKQPDELLDS MSDWCKEHHG KSGLTKAVKE STITLQQAEY EFLSFVRQQT PPGLCPLAGN SVHEDKKFLD KYMPQFMKHL HYRIIDVSTV KELCRRWYPE EYEFAPKKAA SHRALDDISE SIKELQFYRN NIFKKKIDEK KRKIIENGEN EKTVS.

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:

Creatine Kinase Muscle Human Recombinant

Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM

Product # :

CKI-287

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Description

Recombinant Human CKMM produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.The CKMM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Human CKMM solution contains 500 mM NaCl, 20mM Tris-HCl, 4mM CaCl2, 4mM MgCl2and 60 mM B-mercaptoethanol, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
Synonyms
Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM
Physical Appearance
Sterile Filtered colorless liquid formulation.
Stability
CKMM although stable at 10°C for 7 days, should be stored below -18°C.Please prevent 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:

Folate Hydrolase 1 Mouse Recombinant

Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.

Product # :

ENZ-957

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Description

FOLH1 Mouse Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 717 amino acids (45-752a.a) and having a molecular mass of 80.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). FOLH1 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The FOLH1 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Folate Hydrolase 1 (Folh1) is a single pass type 2 membrane protein which is expressed mainly in prostate epithelium. Folh1 which is a part of the peptidase M28 family and M28B subfamily has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase activity. Folh1 can be found in urinary bladder, kidney, testis, ovary, stomach, small intestine colon, and the capillary endothelium of various tumors. Therefore, Folh1 plays a role in directed imaging and therapy of recurrent of metastatic disease.
Synonyms
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
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
ADPKPSNEAT GNVSHSGMKK EFLHELKAEN IKKFLYNFTR TPHLAGTQNN FELAKQIHDQ WKEFGLDLVE LSHYDVLLSY PNKTHPNYIS IINEDGNEIF KTSLSEQPPP GYENISDVVP PYSAFSPQGT PEGDLVYVNY ARTEDFFKLE REMKISCSGK IVIARYGKVF RGNMVKNAQL AGAKGMILYS DPADYFVPAV KSYPDGWNLP GGGVQRGNVL NLNGAGDPLT PGYPANEHAY RHELTNAVGL PSIPVHPIGY DDAQKLLEHM GGPAPPDSSW KGGLKVPYNV GPGFAGNFST QKVKMHIHSY TKVTRIYNVI GTLKGALEPD RYVILGGHRD AWVFGGIDPQ SGAAVVHEIV RSFGTLKKKG RRPRRTILFA SWDAEEFGLL GSTEWAEEHS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVYNLTK ELQSPDEGFE GKSLYDSWKE KSPSPEFIGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWKTNKVSSY PLYHSVYETY ELVVKFYDPT FKYHLTVAQV RGAMVFELAN SIVLPFDCQS YAVALKKYAD TIYNISMKHP QEMKAYMISF DSLFSAVNNF TDVASKFNQR LQELDKSNPI LLRIMNDQLM YLERAFIDPL GLPGRPFYRH IIYAPSSHNK YAGESFPGIY DALFDISSKV NASKAWNEVK RQISIATFTV QAAAETLREV AHHHHHH.

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

Description:

Ubiquitin Conjugating Enzyme E2B Human Recombinant

Ubiquitin-conjugating enzyme E2 B, EC 6.3.2.19, Ubiquitin-protein ligase B, Ubiquitin carrier protein B, HR6B, hHR6B, E2-17 kDa UBC2, HHR6B, RAD6B, E2-17kDa, UBE2B.

Product # :

ENZ-340

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

Ubiquitin Conjugating Enzyme E2B Human Recombinant produced in E.coli is a 19 kDa protein containing 166 amino acids.The UE2B protein contains 6xHis tag and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated (1 mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.

Purity

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

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Introduction
This E2 enzyme encodes for the human homolog of the yeast DNA repair gene RAD6, which is induced by DNA damaging agents. UBE2B can conjugate ubiquitin to histone H2A in an E3- independent manner in vitro, and is essential for the multi-ubiquitination and degradation of N-end rule substrates. Additionally, UBE2B may have a role in sepsis-induced muscle protein proteolysis and cancer-induced cachexia.
Synonyms
Ubiquitin-conjugating enzyme E2 B, EC 6.3.2.19, Ubiquitin-protein ligase B, Ubiquitin carrier protein B, HR6B, hHR6B, E2-17 kDa UBC2, HHR6B, RAD6B, E2-17kDa, UBE2B.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized UBE2B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2B should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized UBE2B in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHHHHHHAMGQLRSMSTPARRRLMRDFKRLQEDPPVGVSGAPSENN
IMQWNAVIFGPEGTPFEDGTFKLVIEFSEEYPNKPPTVRFLSKMFHPNVY
ADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNSPANSQAAQLYQE
NKREYEKRVSAIVEQSWNDS.

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:

Acyl-Coenzyme A Dehydrogenase C-2 to C-3 Human Recombinant

ACAD3, SCAD, EC 1.3.99.2, Short-chain specific acyl-CoA dehydrogenase, mitochondrial, Butyryl-CoA dehydrogenase, ACADS.

Product # :

ENZ-467

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Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
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Description

ACADS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (25-412 a.a.) and having a molecular mass of 44 kDa. The ACADS protein is fused to a 20 amino acid His Tag at N-terminus and purified by standard chromatogrpahy techniques.

Source

Escherichia Coli.

Formulation

The protein contains 20mM Tris buffer pH-8, 1mM DTT, 20% glycerol and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
ACADS is a tetrameric mitochondrial flavoprotein, which is part of the acyl-CoA dehydrogenase family. ACADS catalyzes the first step of the mitochondrial fatty acid beta-oxidation pathway. Mutations in ACADS have been associated with Short Chain Acyl-CoA Dehydrogenase Deficiency.
Synonyms
ACAD3, SCAD, EC 1.3.99.2, Short-chain specific acyl-CoA dehydrogenase, mitochondrial, Butyryl-CoA dehydrogenase, ACADS.
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 MLHTIYQSVE LPETHQMLLQ TCRDFAEKEL FPIAAQVDKE HLFPAAQVKK MGGLGLLAMD VPEELGGAGL DYLAYAIAME EISRGCASTG VIMSVNNSLY LGPILKFGSK EQKQAWVTPF TSGDKIGCFA LSEPGNGSDA GAASTTARAE GDSWVLNGTK AWITNAWEAS AAVVFASTDR ALQNKSISAF LVPMPTPGLT LGKKEDKLGI RGSSTANLIF EDCRIPKDSI LGEPGMGFKI AMQTLDMGRI GIASQALGIA QTALDCAVNY AENRMAFGAP LTKLQVIQFK LADMALALES ARLLTWRAAM LKDNKKPFIK EAAMAKLAAS EAATAISHQA IQILGGMGYV TEMPAERHYR DARITEIYEG TSEIQRLVIA GHLLRSYRS.

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:

Hexokinase-2 Human Recombinant

Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.

Product # :

PKA-227

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
biological activity
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Description

HK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-917) fused to a 20 His tag at the N-terminal encoding the sequence of 937 amino acids in total and having a molecular mass of 104.1 kDa.HXK2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) contains 20mM Tris-HCl pH8.0 and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is 3-4 units/ml obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. In the coupled mode, one unit will produce 1.0 umole of NADPH per minute as glucose is phosphorylated by ATP at pH 7.4 at 30C.

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Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.
Synonyms
Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.
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 avoid freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL GFTFSFPCHQTKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDISDIEGEKDGIR KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKENKGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG KGAAMVTAVAYRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS KETHASAPVK MLPTYVCATPDGTEKGDFLA LDLGGTNFRV LLVRVRNGKW GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG AALITAVACR IREAGQR.

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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