Search: 1000 results found for "deaminase"

Description:

L-Lactate Dehydrogenase E.Coli Recombinant

L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.

Product # :

ENZ-618

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Description

lldD E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 45.3kDa.lldD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The lldD solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
L-lactate dehydrogenase (lldD) is present in a various organisms, including plants and animals. lldD is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concurrent interconversion of NADH and NAD+. Seeing that lldD can catalyze the oxidation of hydroxybutyrate, it is occasionally called Hydroxybutyrate Dehydrogenase (HBD).
Synonyms
L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.
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 MGSHMIISAA SDYRAAAQRI LPPFLFHYMD GGAYSEYTLR RNVEDLSEVA LRQRILKNMS DLSLETTLFN EKLSMPVALA PVGLCGMYAR RGEVQAAKAA DAHGIPFTLS TVSVCPIEEV APAIKRPMWF QLYVLRDRGF MRNALERAKA AGCSTLVFTV DMPTPGARYR DAHSGMSGPN AAMRRYLQAV THPQWAWDVG LNGRPHDLGN ISAYLGKPTG LEDYIGWLGN NFDPSISWKD LEWIRDFWDG PMVIKGILDP EDARDAVRFG ADGIVVSNHG GRQLDGVLSS ARALPAIADA VKGDIAILAD SGIRNGLDVV RMIALGADTV LLGRAFLYAL ATAGQAGVAN LLNLIEKEMK VAMTLTGAKS ISEITQDSLV QGLGKELPAA LAPMAKGNAA.

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:

Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant

Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

Product # :

ENZ-844

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Description

ENTPD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (44-485 a.a) and having a molecular mass of 52kDa. ENTPD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ENTPD3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.
Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.
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 MGSQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPP.

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:

Tissue Plasminogen Activator (311-562 a.a.) Human Recombinant

Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.

Product # :

ENZ-1023

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Description

TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 261 amino acids (311-562 a.a.) and having a molecular mass of 29.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).TPA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TPA protein solution (0.5mg/ml) contains 50mM MES (pH 5.0), 5mM CaCl2, 1mM DTT, 0.5M NaCl and 30% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
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
ADPIKGGLFA DIASHPWQAA IFAKHRRSPG ERFLCGGILI SSCWILSAAH CFQERFPPHH LTVILGRTYR VVPGEEEQKF EVEKYIVHKE FDDDTYDNDI ALLQLKSDSS RCAQESSVVR TVCLPPADLQ LPDWTECELS GYGKHEALSP FYSERLKEAH VRLYPSSRCT SQHLLNRTVT DNMLCAGDTR SGGPQANLHD ACQGDSGGPL VCLNDGRMTL VGIISWGLGC GQKDVPGVYT KVTNYLDWIR DNMRPHHHHH H.

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

Description:

Glutathione Peroxidase 3 Human Recombinant

Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.

Product # :

ENZ-579

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Description

GPX3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (21-226) and having a molecular mass of 25.7kDa.GPX3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GPX3 solution contains 20mM Tris-HCl buffer (pH7.5), 40% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Glutathione peroxidase 3 (GPX3) is a member of the glutathione peroxidase family, which acts in the detoxification of hydrogen peroxide. GPX3 shields cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. The GPX3 protein is one of only a few proteins known in higher vertebrates to contain selenocysteine, which occurs at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA.
Synonyms
Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.
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 MQSRGQEKSK MDCHGGISGT IYEYGALTID GEEYIPFKQY AGKYVLFVNV ASYCGLTGQY IELNALQEEL APFGLVILGF PCNQFGKQEP GENSEILPTL KYVRPGGGFV PNFQLFEKGD VNGEKEQKFY TFLKNSCPPT SELLGTSDRL FWEPMKVHDI RWNFEKFLVG PDGIPIMRWH HRTTVSNVKM DILSYMRRQA ALGVKRK.

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:

Glucosidase Beta Acid 3 Human Recombinant

Cytosolic beta-glucosidase, Cytosolic beta-glucosidase-like protein 1, GBA3, CBG, CBGL1, Glucosidase Beta Acid 3, GH1, Glycoside Hydrolase Family 1, GLUC, KLRP.

Product # :

ENZ-831

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Description

GBA3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 492 amino acids (1-469 a.a.) and having a molecular mass of 56.1kDa.GBA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

GBA3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Glucosidase Beta Acid 3, also known as GBA3, hydrolyzes various types of glycosides. GBA3 takes part in a nonlysosomal catabolic pathway of glycosylceramide. GBA3 is a protein coding gene which acts as beta-glycosylceramidase.
Synonyms
Cytosolic beta-glucosidase, Cytosolic beta-glucosidase-like protein 1, GBA3, CBG, CBGL1, Glucosidase Beta Acid 3, GH1, Glycoside Hydrolase Family 1, GLUC, KLRP.
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 MGSMAFPAGF GWAAATAAYQ VEGGWDADGK GPCVWDTFTH QGGERVFKNQ TGDVACGSYT LWEEDLKCIK QLGLTHYRFS LSWSRLLPDG TTGFINQKGI DYYNKIIDDL LKNGVTPIVT LYHFDLPQTL EDQGGWLSEA IIESFDKYAQ FCFSTFGDRV KQWITINEAN VLSVMSYDLG MFPPGIPHFG TGGYQAAHNL IKAHARSWHS YDSLFRKKQK GMVSLSLFAV WLEPADPNSV SDQEAAKRAI TFHLDLFAKP IFIDGDYPEV VKSQIASMSQ KQGYPSSRLP EFTEEEKKMI KGTADFFAVQ YYTTRLIKYQ ENKKGELGIL QDAEIEFFPD PSWKNVDWIY VVPWGVCKLL KYIKDTYNNP VIYITENGFP QSDPAPLDDT QRWEYFRQTF QELFKAIQLD KVNLQVYCAW SLLDNFEWNQ GYSSRFGLFH VDFEDPARPR VPYTSAKEYA KIIRNNGLEA HL.

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

Description:

Glutamate-Cysteine Ligase, Modifier Subunit Human Recombinant

Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.

Product # :

ENZ-636

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Description

GCLM Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (1-274) and having a molecular mass of 33.3kDa.GCLM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GCLM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Glutamate-cysteine ligase (GCLM) is the first rate limiting enzyme of glutathione synthesis. The GCLM enzyme is comprised of 2 subunits, a heavy catalytic subunit and a light regulatory subunit. GCLM deficiency is associated with some forms of hemolytic anemia.
Synonyms
Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.
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 MGSHMGTDSR AAKALLARAR TLHLQTGNLL NWGRLRKKCP STHSEELHDC IQKTLNEWSS QINPDLVREF PDVLECTVSH AVEKINPDER EEMKVSAKLF IVESNSSSST RSAVDMACSV LGVAQLDSVI IASPPIEDGV NLSLEHLQPY WEELENLVQS KKIVAIGTSD LDKTQLEQLY QWAQVKPNSN QVNLASCCVM PPDLTAFAKQ FDIQLLTHND PKELLSEASF QEALQESIPD IQAHEWVPLW LLRYSVIVKS RGIIKSKGYI LQAKRRGS.

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:

Methyltransferase Like 1 Human Recombinant

Methyltransferase-Like 1, TRM8, tRNA(m7G46)-methyltransferase, tRNA (guanine-N(7)-)-methyltransferase , C12orf1, YDL201w, D1075-like gene product, FLJ95748, EC 2.1.1.33.

Product # :

ENZ-054

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Description

Recombinant Human METTL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-276a.a.) and having a molecular mass of 33.6kDa.METTL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The METTL1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT, 50mM NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
METTL1 is recognized as tRNA (guanine-N(7)-)-methyltransferase that is a part of the methyltransferase superfamily. METTL1 displays high sequence similarity to yeast ORF YDL201w and can be inactivated by phosphorylation. METTL1 protein has a conserved S-adenosylmethionine-binding motif and ccatalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Synonyms
Methyltransferase-Like 1, TRM8, tRNA(m7G46)-methyltransferase, tRNA (guanine-N(7)-)-methyltransferase , C12orf1, YDL201w, D1075-like gene product, FLJ95748, EC 2.1.1.33.
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 MAAETRNVAG AEAPPPQKRY YRQRAHSNPM ADHTLRYPVK PEEMDWSELY PEFFAPLTQN QSHDDPKDKK EKRAQAQVEF ADIGCGYGGL LVELSPLFPD TLILGLEIRV KVSDYVQDRI RALRAAPAGG FQNIACLRSN AMKHLPNFFY KGQLTKMFFL FPDPHFKRTK HKWRIISPTL LAEYAYVLRV GGLVYTITDV LELHDWMCTH FEEHPLFERV PLEDLSEDPV VGHLGTSTEE GKKVLRNGGK NFPAIFRRIQ DPVLQAVTSQ TSLPGH

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:

Phosphodiesterase 6H cGMP-Specific Cone Gamma Human Recombinant

Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.

Product # :

ENZ-819

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Description

PDE6H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (1-83 a.a) and having a molecular mass of 11.5 kDa. PDE6H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PDE6H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 2mM DTT and 0.1mM PMSF.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
PDE6H belongs to the rod/cone cGMP-PDE gamma subunit family, which selectively catalyze the hydrolysis of 3 cyclic phosphate bonds in adenosine and/or guanine 3,5 cyclic monophosphate (cAMP and/or cGMP). This family regulates the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDE6H is the inhibitory (or gamma) subunit of the cone-specific cGMP phosphodiesterase, which is atetramer composed of two catalytic chains (alpha and beta), and two inhibitory chains (gamma). PDE6H is particularly expressed in the retina, and is implicated in the transmission and amplification of the visual signal. Mutations in PDE6H have been associated with retinal cone dystrophy type 3A.
Synonyms
Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.
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 MGSMSDNTTL PAPASNQGPT TPRKGPPKFK QRQTRQFKSK PPKKGVKGFG DDIPGMEGLG TDITVICPWE AFSHLELHEL AQFGII.

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:

Tyrosylprotein Sulfotransferase 2 Human Recombinant

Protein-tyrosine sulfotransferase 2, EC 2.8.2.20, Tyrosylprotein sulfotransferase 2, TPST-2, TPST2, TANGO13B.

Product # :

ENZ-707

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Description

TPST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (26-377) and having a molecular mass of 41kDa.TPST2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TPST2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Tyrosylprotein Sulfotransferase 2 (TPST2) is a member of the protein sulfotransferase family. TPST2 is a widely expressed protein, which catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The TPST2 protein is a type II integral membrane protein located in the Golgi body.
Synonyms
Protein-tyrosine sulfotransferase 2, EC 2.8.2.20, Tyrosylprotein sulfotransferase 2, TPST-2, TPST2, TANGO13B.
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 MGSQQVLECR AVLAGLRSPR GAMRPEQEEL VMVGTNHVEY RYGKAMPLIF VGGVPRSGTT LMRAMLDAHP EVRCGEETRI IPRVLAMRQA WSKSGREKLR LDEAGVTDEV LDAAMQAFIL EVIAKHGEPA RVLCNKDPFT LKSSVYLSRL FPNSKFLLMV RDGRASVHSM ITRKVTIAGF DLSSYRDCLT KWNKAIEVMY AQCMEVGKEK CLPVYYEQLV LHPRRSLKLI LDFLGIAWSD AVLHHEDLIG KPGGVSLSKI ERSTDQVIKP VNLEALSKWT GHIPGDVVRD MAQIAPMLAQ LGYDPYANPP NYGNPDPFVI NNTQRVLKGD YKTPANLKGY FQVNQNSTSS HLGSS.

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:

Tyrosyl-DNA Phosphodiesterase 2 Human Recombinant

AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein II.

Product # :

ENZ-698

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Description

TDP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362) and having a molecular mass of 43.3kDa. TDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TDP2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Tyrosyl-DNA Phosphodiesterase 2 (TDP2), belongs to the CCR4/nocturin family of divalent cation-dependent phosphodiesterases.TDP2 associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. TDP2 is characterized by similar sequence and structure as APE1 endonuclease, which participates in DNA repair and the activation of transcription factors.
Synonyms
AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein 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
MGSSHHHHHH SSGLVPRGSH MGSMELGSCL EGGREAAEEE GEPEVKKRRL LCVEFASVAS CDAAVAQCFL AENDWEMERA LNSYFEPPVE ESALERRPET ISEPKTYVDL TNEETTDSTT SKISPSEDTQ QENGSMFSLI TWNIDGLDLN NLSERARGVC SYLALYSPDV IFLQEVIPPY YSYLKKRSSN YEIITGHEEG YFTAIMLKKS RVKLKSQEII PFPSTKMMRN LLCVHVNVSG NELCLMTSHL ESTRGHAAER MNQLKMVLKK MQEAPESATV IFAGDTNLRD REVTRCGGLP NNIVDVWEFL GKPKHCQYTW DTQMNSNLGI TAACKLRFDR IFFRAAAEEG HIIPRSLDLL GLEKLDCGRF PSDHWGLLCN LDIIL.

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:

Acid Phosphatase-2 Human Recombinant

Acid Phosphatase 2, Lysosoma, EC 3.1.3.2 LAP, Lysosomal Acid Phosphatase, ACP2.

Product # :

ENZ-849

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Description

ACP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 373 amino acids (31-380 a.a.) and having a molecular mass of 42.9kDa. ACP2 is fused to a 23 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

ACP2 protein solution (1mg/ml) contains 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Acid Phosphatase-2, also known as ACP2 is composed of two subunits, Alpha & beta, and is chemically as well as genetically distinct from red cell acid phosphatase. ACP2 belongs to a family of distinct isoenzymes which hydrolyze orthophosphoric monoesters to alcohol and phosphate. In addition, Acid phosphatase deficiency is caused by mutations in the ACP2-beta subunit as well as ACP3-alpha subunit genes.
Synonyms
Acid Phosphatase 2, Lysosoma, EC 3.1.3.2 LAP, Lysosomal Acid Phosphatase, ACP2.
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 MGSRSLRFVT LLYRHGDRSP VKTYPKDPYQ EEEWPQGFGQ LTKEGMLQHW ELGQALRQRY HGFLNTSYHR QEVYVRSTDF DRTLMSAEAN LAGLFPPNGM QRFNPNISWQ PIPVHTVPIT EDRLLKFPLG PCPRYEQLQN ETRQTPEYQN ESSRNAQFLD MVANETGLTD LTLETVWNVY DTLFCEQTHG LRLPPWASPQ TMQRLSRLKD FSFRFLFGIY QQAEKARLQG GVLLAQIRKN LTLMATTSQL PKLLVYSAHD TTLVALQMAL DVYNGEQAPY ASCHIFELYQ EDSGNFSVEM YFRNESDKAP WPLSLPGCPH RCPLQDFLRL TEPVVPKDWQ QECQLASGPA DTE

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:

ADP-Ribosylarginine Hydrolase Human Recombinant

[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.

Product # :

ENZ-631

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Description

ADPRH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 42.1kDa.ADPRH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ADPRH solution (0.5mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
ADP-ribosylarginine hydrolase (ADPRH) is a member of the ADP-ribosylglycohydrolase family. ADPRH catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. The human ADPRH enzyme is DTT-independent as opposed to the rat and mouse enzymes, which require DTT for maximal activity.
Synonyms
[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.
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 MGSHMEKYVA AMVLSAAGDA LGYYNGKWEF LQDGEKIHRQ LAQLGGLDAL DVGRWRVSDD TVMHLATAEA LVEAGKAPKL TQLYYLLAKH YQDCMEDMDG RAPGGASVHN AMQLKPGKPN GWRIPFNSHE GGCGAAMRAM CIGLRFPHHS QLDTLIQVSI ESGRMTHHHP TGYLGALASA LFTAYAVNSR PPLQWGKGLM ELLPEAKKYI VQSGYFVEEN LQHWSYFQTK WENYLKLRGI LDGESAPTFP ESFGVKERDQ FYTSLSYSGW GGSSGHDAPM IAYDAVLAAG DSWKELAHRA FFHGGDSDST AAIAGCWWGV MYGFKGVSPS NYEKLEYRNR
LEETARALYS LGSKEDTVIS L.

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:

Horseradish Peroxidase

Horseradish Peroxidase, HRP, EC 1.11.1.7.

Product # :

ENZ-321

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Description

HRP consists of the basic isoenzyme having a molecular weight of 44 kDa.The Horseradish Peroxidase is purified by affinity chromatography, which results in an enzyme of high specific activity and purity.

Source

Root extracts of horseradish.

Purity

(A403/A275) = RZ: 3.0.

Biological Activity

276 U/mg (25°C, guaiacol as the hydrogen donor, pH-7 and H₂O₂ as substrates).

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Introduction
The enzyme horseradish peroxidase, found in horseradish, is used extensively in molecular biologyand in antibody amplification and detection, among other things. For example, "In recent years the technique of marking neurons with the enzyme horseradish peroxidase (HRP) has become a major tool. In its brief history, this method has probably been used by more neurobiologists than have used the Golgi stainsince its discovery in 1870." Horseradish peroxidase is also highly used in techniques such as Western blottingand ELISAs.
HRP is widely used as an enzymatic label in immunoassays. Usually, the enzyme is coupled to antibodies, lectins or haptens. Coupling to antibodies etc. may be performed through the carbohydrate side chains of the HRP.
Synonyms
Horseradish Peroxidase, HRP, EC 1.11.1.7.
Physical Appearance
Sterile Filtered red-brown lyophilized powder.
Stability
Lyophilized HRP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HRP should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized HRP in sterile 18MΩ-cm H2O not less than 100 µg/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:

Arylsulfatase A Human Recombinant

Arylsulfatase A, ASA, EC 3.1.6.8, Cerebroside-sulfatase, ARSA, MLD.

Product # :

ENZ-706

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Description

ARSA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 512 amino acids (21-509) and having a molecular mass of 54.3kDa.ARSA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90% 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, ASA, EC 3.1.6.8, Cerebroside-sulfatase, ARSA, MLD.
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 MGSRPPNIVL IFADDLGYGD LGCYGHPSST TPNLDQLAAG GLRFTDFYVP VSLCTPSRAA LLTGRLPVRM GMYPGVLVPS SRGGLPLEEV TVAEVLAARG YLTGMAGKWH LGVGPEGAFL PPHQGFHRFL GIPYSHDQGP CQNLTCFPPA TPCDGGCDQG LVPIPLLANL SVEAQPPWLP GLEARYMAFA HDLMADAQRQ DRPFFLYYAS HHTHYPQFSG QSFAERSGRG PFGDSLMELD AAVGTLMTAI GDLGLLEETL VIFTADNGPE TMRMSRGGCS GLLRCGKGTT YEGGVREPAL AFWPGHIAPG VTHELASSLD LLPTLAALAG APLPNVTLDG FDLSPLLLGT GKSPRQSLFF YPSYPDEVRG VFAVRTGKYK AHFFTQGSAH SDTTADPACH ASSSLTAHEP PLLYDLSKDP GENYNLLGGV AGATPEVLQA LKQLQLLKAQ LDAAVTFGPS QVARGEDPAL QICCHPGCTP RPACCHCPDP HA.

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:

Acetylserotonin O-Methyltransferase Human Recombinant

HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

Product # :

ENZ-664

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Description

ASMT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298 a.a) and having a molecular mass of 35.3kDa.ASMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ASMT is a member of the methyltransferase superfamily. ASMT participates in melatonin biosynthesis. ASMT Expressed in brain, retina and pineal gland, ASMT utilities to catalyze the final reaction in the synthesis of melatonin, particularly the conversion of S-adenosyl-L-methionine and N-acetylserotonin to S-adenosyl-Lhomocysteine and melatonin.
Synonyms
HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.
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 MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGDF FKDPLPEADL YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD EDRRGPLLTQ LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK

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-2 Human Recombinant

Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

Product # :

ENZ-324

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sds-page

Description

ENO2 Human Recombinant expressed in E. coli contains 434 amino acids and its Mw is 47 kDa. The Enolase-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ENO2 is supplied in 20mM Tris pH-7.5, 0.1M KCl, 5mM MgSO4.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

> 25,000 pmol/min/ug, determined by the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37C.

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Introduction
Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.
Synonyms
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles.
Amino Acid Sequence
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE ARFAGHNFRN PSVL.

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 E2I Human Recombinant, His Tag

SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.

Product # :

ENZ-274

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Description

Ubiquitin-Conjugating Enzyme E2I Human Recombinant produced in E.coli is a 19.5 kDa protein containing 171 amino acids.The UBE2I protein contains 6xHis tag and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated (1mg/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
Human Ubquitin Conjugating Enzyme 9 (Ubc9) is a member of the E2 family and is specific for the conjugation of SUMO to a variety of target proteins. SUMO conjugation to target proteins is mediated by a different, but analogous, pathway to ubiquitinylation. This E2 is unusual in that it interacts directly with protein substrates that are modified by sumolyation, and may play a role in substrate recognition. Ubc9 can mediate the conjugation of SUMO-1 to a variety of proteins including RanGAP1, I?B?, and PML without the requirement of an E3 ligase.
Synonyms
SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized UBE2I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2I 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 UBE2I in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHHHHHHAMGTLNMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGT
MNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFH
PNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTI
YCQNRVEYEKRVRAQAKKFAPS.

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:

Peroxisomal Trans-2-enoyl-CoA Reductase Human Recombinant

Peroxisomal trans-2-enoyl-CoA reductase, TERP, HSA250303, SDR29C1, 2,4-dienoyl-CoA reductase-related protein, DCR-RP, pVI-ARL, EC 1.3.1.38, HPDHASE, putative short chain alcohol dehydrogenase, short chain dehydrogenase/reductase family 29C member 1.

Product # :

ENZ-177

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Description

PECR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-303) and having a molecular mass of 35.1 kDa.PECR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PECR is the main enzyme for a projected peroxisomal chain elongation pathway and is primarily expressed in kidney and liver.
Synonyms
Peroxisomal trans-2-enoyl-CoA reductase, TERP, HSA250303, SDR29C1, 2,4-dienoyl-CoA reductase-related protein, DCR-RP, pVI-ARL, EC 1.3.1.38, HPDHASE, putative short chain alcohol dehydrogenase, short chain dehydrogenase/reductase family 29C member 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 MGSHMASWAK GRSYLAPGLL QGQVAIVTGG ATGIGKAIVK ELLELGSNVV IASRKLERLK SAADELQANL PPTKQARVIP IQCNIRNEEE VNNLVKSTLD TFGKINFLVN NGGGQFLSPA EHISSKGWHA VLETNLTGTF YMCKAVYSSW MKEHGGSIVN IIVPTKAGFP LAVHSGAARA GVYNLTKSLA LEWACSGIRI NCVAPGVIYS QTAVENYGSW GQSFFEGSFQ KIPAKRIGVP EEVSSVVCFL LSPAASFITG QSVDVDGGRS LYTHSYEVPD HDNWPKGAGD LSVVKKMKET FKEKAKL

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:

Methyltransferase Like 21A Human Recombinant

Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.

Product # :

ENZ-718

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Description

METTL21A Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (93-218) and having a molecular mass of 17 kDa.METTL21A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The METTL21A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
METTL21A, which is a part of the methyltransferase superfamily, is a Protein-lysine methyltransferase that in vitro methylates HSPA1, HSPA5 and HSPA8.
Synonyms
Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.
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 MGSTDRKVAL EFLKSNVQAN LPPHIQTKTV VKELTWGQNL GSFSPGEFDL ILGADIIYLE ETFTDLLQTL EHLCSNHSVI LLACRIRYER DNNFLAMLER QFTVRKVHYD PEKDVHIYEA QKRNQKEDL.

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:

Aminopeptidase Puromycin Sensitive Human Recombinant

PSA, MP100, AAP-S, Puromycin-sensitive aminopeptidase, Cytosol alanyl aminopeptidase, aminopeptidase puromycin sensitive.

Product # :

ENZ-1196

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Description

NPEPPS Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 925 amino acids (1-919 a.a.) and having a molecular mass of 104kDa. NPEPPS is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

NPEPPS protein solution (0.25mg/ml) containing 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 800 pmol/min/ug and is defined as the amount of enzyme that cleaves 1 pmole of H-Leu[1]AMC per minute at pH7.0 at 37°C.

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Synonyms
PSA, MP100, AAP-S, Puromycin-sensitive aminopeptidase, Cytosol alanyl aminopeptidase, aminopeptidase puromycin sensitive.
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
MWLAAAAPSL ARRLLFLGPP PPPLLLLVFS RSSRRRLHSL GLAAMPEKRP FERLPADVSP INYSLCLKPD LLDFTFEGKL EAAAQVRQAT NQIVMNCADI DIITASYAPE GDEEIHATGF NYQNEDEKVT LSFPSTLQTG TGTLKIDFVG ELNDKMKGFY RSKYTTPSGE VRYAAVTQFE ATDARRAFPC WDEPAIKATF DISLVVPKDR VALSNMNVID RKPYPDDENL VEVKFARTPV MSTYLVAFVV GEYDFVETRS KDGVCVRVYT PVGKAEQGKF ALEVAAKTLP FYKDYFNVPY PLPKIDLIAI ADFAAGAMEN GLVTYRETA LLIDPKNSCS SSRQWVALVV GHELAHQWFG NLVTMEWWTH LWLNEGFASW IEYLCVDHCF PEYDIWTQFV SADYTRAQEL DALDNSHPIE VSVGHPSEVD EIFDAISYSK GASVIRMLHD YIGDKDFKKG MNMYLTKFQQ KNAATEDLWE SLENASGKPI AAVMNTWTKQ MGFPLIYVEA EQVEDDRLLR LSQKKFCAGG SYVGEDCPQW MVPITISTSE DPNQAKLKIL MDKPEMNVVL KNVKPDQWVK LNLGTVGFYR TQYSSAMLES LLPGIRDLSL PPVDRLGLQN DLFSLARAGI ISTVEVLKVM EAFVNEPNYT VWSDLSCNLG ILSTLLSHTD FYEEIQEFVK DVFSPIGERL GWDPKPGEGH LDALLRGLVL GKLGKAGHKA TLEEARRRFK DHVEGKQILS ADLRSPVYLT VLKHGDGTTL DIMLKLHKQA DMQEEKNRIE RVLGATLLPD LIQKVLTFAL SEEVRPQDTV SVIGGVAGGS KHGRKAAWKF IKDNWEELYN RYQGGFLISR LIKLSVEGFA VDKMAGEVKA FFESHPAPSA ERTIQQCCEN ILLNAAWLKR DAESIHQYLL QRKASPPTVH HHHHH.
Background
NPEPPS is involved in the proteolytic degradation of misfolded or damaged proteins, contributing to the maintenance of protein homeostasis within the cell. It specifically removes N-terminal amino acids from peptides, thereby regulating their activity and facilitating their further degradation by other proteases.
This enzyme is particularly important in the nervous system, where it degrades neuropeptides and helps regulate synaptic signaling and neuronal communication.

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:

Prolyl Endopeptidase Human Recombinant

Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.

Product # :

ENZ-828

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Description

PREP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 733 amino acids (1-710 a.a) and having a molecular mass of 83.1kDa. PREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PREP protein solution (0.25mg/ml) containing PBS buffer (pH 7.4), 30% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Prolyl Endopeptidase , also known as PREP is a cytosolic prolyl endopeptidase which cleaves peptide bonds on the C-terminal side of prolyl residues within peptides which are up to about 30 a.a long. In addition, Prolyl endopeptidases have been shown to be implicated in the maturation and degradation of peptide hormones and neuropeptides.
Synonyms
Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.
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 MGSMLSLQYP DVYRDETAVQ DYHGHKICDP YAWLEDPDSE QTKAFVEAQN KITVPFLEQC PIRGLYKERM TELYDYPKYS CHFKKGKRYF YFYNTGLQNQ RVLYVQDSLE GEARVFLDPN ILSDDGTVAL RGYAFSEDGE YFAYGLSASG SDWVTIKFMK VDGAKELPDV LERVKFSCMA WTHDGKGMFY NSYPQQDGKS DGTETSTNLH QKLYYHVLGT DQSEDILCAE FPDEPKWMGG AELSDDGRYV LLSIREGCDP VNRLWYCDLQ QESSGIAGIL KWVKLIDNFE GEYDYVTNEG TVFTFKTNRQ SPNYRVINID FRDPEESKWK VLVPEHEKDV LEWIACVRSN FLVLCYLHDV KNILQLHDLT TGALLKTFPL DVGSIVGYSG QKKDTEIFYQ FTSFLSPGII YHCDLTKEEL EPRVFREVTV KGIDASDYQT VQIFYPSKDG TKIPMFIVHK KGIKLDGSHP AFLYGYGGFN ISITPNYSVS RLIFVRHMGG ILAVANIRGG GEYGETWHKG GILANKQNCF DDFQCAAEYL IKEGYTSPKR LTINGGSNGG LLVAACANQR PDLFGCVIAQ VGVMDMLKFH KYTIGHAWTT DYGCSDSKQH FEWLVKYSPL HNVKLPEADD IQYPSMLLLT ADHDDRVVPL HSLKFIATLQ YIVGRSRKQS NPLLIHVDTK AGHGAGKPTA KVIEEVSDMF AFIARCLNVD WIP.

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:

Mannoside Acetylglucosaminyltransferase 2 Human Recombinant, Sf9

Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II.

Product # :

ENZ-1077

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Description

MGAT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 427 amino acids (30-447a.a.) and having a molecular mass of 49.3kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MGAT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

MGAT2 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 7.5), 10% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.
Synonyms
Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase 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
ADPRQRKNEA LAPPLLDAEP ARGAGGRGGD HPSVAVGIRR VSNVSAASLV PAVPQPEADN LTLRYRSLVY QLNFDQTLRN VDKAGTWAPR ELVLVVQVHN RPEYLRLLLD SLRKAQGIDN VLVIFSHDFW STEINQLIAG VNFCPVLQVF FPFSIQLYPN EFPGSDPRDC PRDLPKNAAL
KLGCINAEYP DSFGHYREAK FSQTKHHWWW KLHFVWERVK ILRDYAGLIL FLEEDHYLAP DFYHVFKKMW KLKQQECPEC DVLSLGTYSA SRSFYGMADK VDVKTWKSTE HNMGLALTRN AYQKLIECTD TFCTYDDYNW DWTLQYLTVS CLPKFWKVLV PQIPRIFHAG DCGMHHKKTC
RPSTQSAQIE SLLNNNKQYM FPETLTISEK FTVVAISPPR KNGGWGDIRD HELCKSYRRL QHHHHHH.

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

Description:

N-Acetylgalactosaminidase Alpha Human Recombinant

Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.

Product # :

ENZ-963

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Description

NAGA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 400 amino acids (18-411) and having a molecular mass of 45.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NAGA is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NAGA protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
N-Acetylgalactosaminidase Alpha (NAGA) is a lysosomal exoglycosidase which removes terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids. NAGA is necessary for the breakdown of glycolipids.
Synonyms
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
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
LDNGLLQTPP MGWLAWERFR CNINCDEDPK NCISEQLFME MADRMAQDGW RDMGYTYLNI DDCWIGGRDA SGRLMPDPKR FPHGIPFLAD YVHSLGLKLG IYADMGNFTC MGYPGTTLDK VVQDAQTFAE WKVDMLKLDG CFSTPEERAQ GYPKMAAALN ATGRPIAFSC SWPAYEGGLP PRVNYSLLAD ICNLWRNYDD IQDSWWSVLS ILNWFVEHQD ILQPVAGPGH WNDPDMLLIG NFGLSLEQSR AQMALWTVLA APLLMSTDLR TISAQNMDIL QNPLMIKINQ DPLGIQGRRI HKEKSLIEVY MRPLSNKASA LVFFSCRTDM PYRYHSSLGQ LNFTGSVIYE AQDVYSGDII SGLRDETNFT VIINPSGVVM WYLYPIKNLE MSQQHHHHHH.

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.

Product # :

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.

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