Search: 1000 results found for "Isomerase"

Description:

Carboxylesterase 1 Human Recombinant

Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.

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ENZ-1099

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Description

CES1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 559 amino acids (19-568 a.a.) and having a molecular mass of 61.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CES1 protein solution (0.5mg/ml) contains 25mM Sodium Acetate (pH 4.0), 10% glycerol, 0.1M NaCl and 0.1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
CES1 is a part of the alpha/beta fold hydrolase familyand participates in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. CES1hydrolyzes aromatic and aliphatic esters, although it has no catalytic activity toward amides or a fatty acyl-CoA ester. CES1hydrolyzes the methyl ester group of cocaine to form benzoylecgonine and catalyzes the transesterification of cocaine to form cocaethylene. CES1also plays a role in detoxification in the lung and protection of the central nervous system from ester or amide compounds.CES1 is found in most tissues, mainly in the liver.
Synonyms
Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.
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
ADLGHPSSPP VVDTVHGKVL GKFVSLEGFA QPVAIFLGIP FAKPPLGPLR FTPPQPAEPW
SFVKNATSYP PMCTQDPKAG QLLSELFTNR KENIPLKLSE DCLYLNIYTP ADLTKKNRLP
VMVWIHGGGL MVGAASTYDG LALAAHENVV VVTIQYRLGI WGFFSTGDEH SRGNWGHLDQ
VAALRWVQDN IASFGGNPGS VTIFGESAGG ESVSVLVLSP LAKNLFHRAI SESGVALTSV
LVKKGDVKPL AEQIAITAGC KTTTSAVMVH CLRQKTEEEL LETTLKMKFL SLDLQGDPRE
SQPLLGTVID GMLLLKTPEE LQAERNFHTV PYMVGINKQE FGWLIPMQLM SYPLSEGQLD
QKTAMSLLWK SYPLVCIAKE LIPEATEKYL GGTDDTVKKK DLFLDLIADV MFGVPSVIVA
RNHRDAGAPT YMYEFQYRPS FSSDMKPKTV IGDHGDELFS VFGAPFLKEG ASEEEIRLSK
MVMKFWANFA RNGNPNGEGL PHWPEYNQKE GYLQIGANTQ AAQKLKDKEV AFWTNLFAKK AVEKPPQTEH IELHHHHHH.

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

Description:

Glutamic-Pyruvate Transaminase Mouse Recombinant

Alanine aminotransferase 1, ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1.

Product # :

ENZ-1030

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Description

GPT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 57.5kDa.GPT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GPT protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4), 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 40units/mg, and is defined as the amount of enzyme that convert 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.

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Introduction
GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.
Synonyms
Alanine aminotransferase 1, ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 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 MGSMASQRND RIQASRNGLK GKVLTLDTMN PCVRRVEYAV RGPIVQRALE LEQELRQGVK KPFTEVIRAN IGDAQAMGQR PITFFRQVLA LCVYPNLLSS PDFPEDAKRR AERILQACGG HSLGAYSISS GIQPIREDVA QYIERRDGGI PADPNNIFLS TGASDAIVTM LKLLVAGEGR ARTGVLIPIP QYPLYSAALA ELDAVQVDYY LDEERAWALD IAELRRALCQ ARDRCCPRVL CVINPGNPTG QVQTRECIEA VIRFAFEEGL FLMADEVYQD NVYAEGSQFH SFKKVLTEMG PPYATQQELA SFHSVSKGYM GECGFRGGYV EVVNMDAEVQ KQMAKLMSVR LCPPVPGQAL MGMVVSPPTP SEPSFKQFQA ERQEVLAELA AKAKLTEQVF NEAPGIRCNP VQGAMYSFPQ IQLPLKAVQR AQDLGLAPDM FFCLCLLEET GICVVPGSGF GQQEGTYHFR MTILPPMEKL RVLLEKLRHF HAKFTHEYS.

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:

Hydroxymethylbilane Synthase Human Recombinant

Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.

Product # :

ENZ-581

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Description

HMBS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-361) and having a molecular mass of 41.9kDa.HMBS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Porphobilinogen deaminase (HMBS) belongs to the hydroxymethylbilane synthase superfamily. HMBS is a cytoplasmic enzyme found in the heme synthesis pathway. HMBS is the 3rd enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of 4 porphobilinogen molecules into the linear hydroxymethylbilane. HMBS gene mutations cause errors in pyrrole metabolism which in turn lead to the autosomal dominant disease acute intermittent porphyria.
Synonyms
Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.
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 MGSHMSGNGN AAATAEENSP KMRVIRVGTR KSQLARIQTD SVVATLKASY PGLQFEIIAM STTGDKILDT ALSKIGEKSL FTKELEHALE KNEVDLVVHS LKDLPTVLPP GFTIGAICKR ENPHDAVVFH PKFVGKTLET LPEKSVVGTS SLRRAAQLQR
KFPHLEFRSI RGNLNTRLRK LDEQQEFSAI ILATAGLQRM GWHNRVGQIL HPEECMYAVG QGALGVEVRA KDQDILDLVG VLHDPETLLR CIAERAFLRH LEGGCSVPVA VHTAMKDGQL YLTGGVWSLD GSDSIQETMQ ATIHVPAQHE DGPEDDPQLV GITARNIPRG PQLAAQNLGI
SLANLLLSKG AKNILDVARQ LNDAH.

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

Description:

Matrix Metalloproteinase-13 Human Recombinant

CLG3, MANDP1, Matrix metalloproteinase-13, MMP-13, MMP13.

Product # :

ENZ-317

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Description

MMP-13 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (104-471 a.a.) and having a molecular mass of 44.7 kDa. MMP-13 is fused to a 23 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MMP-13 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Matrix Metalloproteinase-13 (MMP-13) is an enzyme that is a member of the MMP extracellular protease family. Extracellular protease enzymes, by virtue of their broad substrate specificities1, play a role in both normal and disease states of tissue proliferation. Among the targets of MMP-13 are collagen, gelatin, entactin, pro-TNF-a, and chemokine SDF-11-4.
MMP-13 is found in its latent form as a 52-56 kDa glycosylated proenzyme. Upon cleavage the 22-46 kDa5 MMP-1 becomes active in extracellular matrix remodeling.
Because of the prominent role that MMP-1 plays in cell migration and metastasis, it is an important target for inhibition screening.
Synonyms
CLG3, MANDP1, Matrix metalloproteinase-13, MMP-13, MMP13.
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 MGSYNVFPRT LKWSKMNLTY RIVNYTPDMT HSEVEKAFKK AFKVWSDVTP LNFTRLHDGI ADIMISFGIK EHGDFYPFDG PSGLLAHAFP PGPNYGGDAH FDDDETWTSS SKGYNLFLVA AHEFGHSLGL DHSKDPGALM FPIYTYTGKS HFMLPDDDVQ GIQSLYGPGD EDPNPKHPKT PDKCDPSLSL DAITSLRGET MIFKDRFFWR LHPQQVDAEL FLTKSFWPEL PNRIDAAYEH PSHDLIFIFR GRKFWALNGY DILEGYPKKI SELGLPKEVK KISAAVHFED TGKTLLFSGN QVWRYDDTNH IMDKDYPRLI EEDFPGIGDK VDAVYEKNGY IYFFNGPIQF EYSIWSNRIV RVMPANSILW C.

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

Description:

Thermostable dUTPase Pyrococcus Fruriosus Recombinant

Thermostable dUTPase, dUTPase.

Product # :

ENZ-281

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Source

Escherichia Coli.

Formulation

dUTPase is supplied in 20mM Tris-HCl (pH 8.2), 1mM DTT, 0.1mM EDTA, 100mM KCl, 0.1% Nonidet P40, 0.1% Tween 20 and 50% glycerol at a concentration of 1000U/µl of the enzyme.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Thermostable dUTPase, dUTPase.
Physical Appearance
Sterile filtered liquid formulation.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Unit Definition
One unit of enzyme catalyzes hadrylazation of 10 nanomoles of dUTP to dUMP in one hour at 85 Centigrade.
Specific Activity
10³U/ug.

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Description:

Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Human Recombinant

Phospholysine phosphohistidine inorganic pyrophosphate phosphatase, hLHPP, LHPP, HDHD2B.

Product # :

ENZ-575

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Description

LHPP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (1-270) and having a molecular mass of 33.5kDa.LHPP is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP) belongs to the HAD-like hydrolase superfamily. LHPP is an exceptional enzyme which hydrolyzes not only oxygen-phosphorus bonds in inorganic pyrophosphate but also nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate in vitro. LHPP is expressed in the liver, kidney and moderately in the brain.
Synonyms
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase, hLHPP, LHPP, HDHD2B.
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
MRGSHHHHHP WYASMTGGQQ MGRDLYDDDD KDRWGSHMAP WGKRLAGVRG VLLDISGVLY DSGAGGGTAI AGSVEAVARL KRSRLKVRFC TNESQKSRAE LVGQLQRLGF DISEQEVTAP APAACQILKE QGLRPYLLIH DGVRSEFDQI DTSNPNCVVI ADAGESFSYQ NMNNAFQVLM ELEKPVLISL GKGRYYKETS GLMLDVGPYM KALEYACGIK AEVVGKPSPE FFKSALQAIG VEAHQAVMIG DDIVGDVGGA QRCGMRALQV RTGKFRPSDE HHPEVKADGY VDNLAEAVDL LLQHADK.

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:

Glycyl-TRNA Synthetase Human Recombinant

Glycine--tRNA ligase, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, CMT2D, DSMAV, HMN5, SMAD1.

Product # :

ENZ-805

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Description

GARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids (43-289 a.a) and having a molecular mass of 30kDa.GARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GARS protein solution (0. 5mg/ml) containing 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
GARS is an (alpha)2 dimer which is a member of the class II family of tRNA synthetases. GARS is a glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases which charge tRNAs with their cognate amino acids. GARS catalyzes the attachment of glycine to tRNA(Gly). In addition, GARS is able to produce diadenosine tetraphosphate (Ap4A), which is a universal pleiotropic signaling molecule required for cell regulation pathways, by direct condensation of two ATPs. GARS has been demonstrated to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.
Synonyms
Glycine--tRNA ligase, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, CMT2D, DSMAV, HMN5, SMAD1.
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 MGSPISLPAA ASRSSMDGAG AEEVLAPLRL AVRQQGDLVR KLKEDKAPQV DVDKAVAELK ARKRVLEAKE LALQPKDDIV DRAKMEDTLK RRFFYDQAFA IYGGVSGLYD FGPVGCALKN NIIQTWRQHF IQEEQILEID CTMLTPEPVL KTSGHVDKFA DFMVKDVKNG ECFRADHLLK AHLQKLMSDK KCSVEKKSEM ESVLAQLDNY GQQELADLFV NYNVKSPITG NDLSPPVSFN LMFKTFIGPG.

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Description:

Deoxyribonuclease I Human Recombinant

EC 3.1.21.1, Deoxyribonuclease I, DNase I, DNL1, DRNI, FLJ38093, DNASE1.

Product # :

ENZ-319

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Description

Deoxyribonuclease I Human Recombinant produced in CHO is a glycosylated, polypeptide chain containing 260 amino acids and having a total molecular mass of 37,000 Dalton with a molecular formula of C1321H1999N339O396S9. DNase is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells.

Formulation

Each mg contains 150 µg calcium chloride dehydrate and 8.77 mg NaCl.

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Introduction
Deoxyribonuclease I Human Recombinant (rhDNase), an enzyme which selectively cleaves DNA. Recombinant Human Dnase is an endonuclease enzyme which splits phosphodiester linkages within polynucleotides, acting primarely on single stranded DNA (ssDNA), double stranded DNA (ddDNA) and chromatin. Dnase is activated by bivalent metals such as Mg+2 and Ca+2 .
Dnase enzymes are common reagents used in biochemical methods requiring diestion of DNA and recovery of RNA, or where DNA is to be removed without affecting structural proteins or enzymes. Dnase enzymes are also used in tissue culture to digest DNA from damaged cells, resulting in reduced viscosity, and for removal of membrane-bound DNA fragments.
Synonyms
EC 3.1.21.1, Deoxyribonuclease I, DNase I, DNL1, DRNI, FLJ38093, DNASE1.
Physical Appearance
Sterile liquid colorless solution at a concentration of 1mg/ml.
Stability
2 years when stored at 4°C, three weeks at 15°C, pH-6.3.
Unit Definition
Dnase is generally assayed according to the photometric method developed by Kunitz. One Dnase unit results in an increase in absorbance at 260nm of 0.001/minute at 25°C when acting upon highly polymerized solution of DNA at pH-5. Also 0.005 Kunitz unit digests 1µgof lambda phage DNA in 10 minutes at 37°C in50mM Tris, 1mMMg++, pH 7.8 in a 50ul reaction.
Specific Activity
1000IU/1mg.

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.

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:

Deoxyribose-Phosphate Aldolase E.Coli Recombinant

Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.

Product # :

ENZ-127

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Description

DERA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259 a.a.) and having a molecular mass of 29.9kDa.DERA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Deoxyribose-phosphate aldolase (DERA) is a member of the deoC/fbaB aldolase protein family involved in the carbohydrate degradation pathway. DERA catalyzes the conversion of 2-deoxy-D-ribose 5-phosphate to D-glyceraldehyde 3-phosphate and an acetyldehyde.
Synonyms
Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP RFIPIARKTL KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD LVKACKEACA AANVLLKVII ETGELKDEAL IRKASEISIK AGADFIKTST GKVAVNATPE SARIMMEVIR DMGVEKTVGF KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL LASLLKALGH GDGKSASSY.

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Description:

Glutamic-Oxaloacetic Transaminase 1 Human Recombinant, Active

EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

Product # :

ENZ-1001

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Description

GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GOT1 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8.0, 2mM DTT, 0.1M NaCl & 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 50 units/mg, and is defined as the amount of enzyme that converts 1umole of a-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C.

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Introduction
GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.
Synonyms
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
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 MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ.

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

Description:

Matrix Metalloproteinase-28 Human Recombinant

EPILYSIN, MM28, MMP-28, MMP25, Matrix metalloproteinase-28, MMP28.

Product # :

ENZ-768

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Description

MMP28 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (123-520a.a) and having a molecular mass of 47.3kDa. MMP28 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MMP28 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
MMP28, which belongs to the matrix metalloproteinase (MMP) family, takes part in the breakdown of extracellular matrix for both normal physiological processes, such as embryonic development, reproduction and tissue remodeling, and disease processes, like asthma and metastasis. MMP28 is a secreted enzyme which degrades casein. MMP28 participates in tissue homeostasis and in wound repair.
Synonyms
EPILYSIN, MM28, MMP-28, MMP25, Matrix metalloproteinase-28, MMP28.
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 MGSFAKQGNK WYKQHLSYRL VNWPEHLPEP AVRGAVRAAF QLWSNVSALE FWEAPATGPA DIRLTFFQGD HNDGLGNAFD GPGGALAHAF LPRRGEAHFD QDERWSLSRR RGRNLFVVLA HEIGHTLGLT HSPAPRALMA PYYKRLGRDA LLSWDDVLAV QSLYGKPLGG SVAVQLPGKL FTDFETWDSY SPQGRRPETQ GPKYCHSSFD AITVDRQQQL YIFKGSHFWE VAADGNVSEP RPLQERWVGL PPNIEAAAVS LNDGDFYFFK GGRCWRFRGP KPVWGLPQLC RAGGLPRHPD AALFFPPLRR LILFKGARYY VLARGGLQVE PYYPRSLQDW GGIPEEVSGA LPRPDGSIIF FRDDRYWRLD QAKLQATTSG RWATELPWMG CWHANSGSAL F.

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-Acetylneuraminic Acid Phosphatase Human Recombinant

N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.

Product # :

ENZ-009

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Description

NANP Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 284 amino acids (1-248 a.a.) and having a molecular mass of 31.9kDa. The NANP is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NANP solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol, 2mM DTT and 100mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
N-acylneuraminate-9-phosphatase (NANP) belongs to the haloacid dehalogenase (HAD) family and is responsible for dephosphorylating N-acylneuraminate 9-phosphate to form N-acylneuraminate (N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate). The catalytic activity of NANP is relies on the presence of magnesium and is inhibited by vanadate and calcium, which is typical of the HAD phosphatase family.
Synonyms
N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGLS RVRAVFFDLD NTLIDTAGAS RRGMLEVIKL LQSKYHYKEE AEIICDKVQV KLSKECFHPY NTCITDLRTS HWEEAIQETK GGAANRKLAE ECYFLWKSTR LQHMTLAEDV KAMLTELRKE VRLLLLTNGD RQTQREKIEA CACQSYFDAV VVGGEQREEK PAPSIFYYCC NLLGVQPGDC VMVGDTLETD IQGGLNAGLK ATVWINKNGI VPLKSSPVPH YMVSSVLELP ALLQSIDCKV SMST.

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Description:

Dimethylglycine Oxidase Recombinant

DMGO, Dimethylglycine Oxidase.

Product # :

ENZ-318

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Description

Dimethylglycine oxidase Recombinant originated from Arthrobacter globifomis fused to His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 850 amino acids and having a molecular mass of 92.1 kDa. The DMGO is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Recombinant Dimethylglycine Oxidase solution contains 20mM Tris-HCl pH7.5 and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Dimethylglycine oxidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative demethylation of dimethylglycine to yield sarcosine, formaldehyde, and hydrogen peroxide. The N-terminal region binds FAD covalently so it is yellowish.
Synonyms
DMGO, Dimethylglycine Oxidase.
Physical Appearance
Sterile filtered liquid formulation 1 mg/ml.
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 MASTPRIVII GAGIVGTNLA DELVTRGWNN ITVLDQGPLN MPGGSTSHAP GLVFQTNPSK TMASFAKYTVEKLLSLTEDG VSCFNQVGGL EVATTETRLA DLKRKLGYAA AWGIEGRLLS PAECQELYPL LDGENILGGL HVPSDGLASA ARAVQLLIKRTESAGVTYRG STTVTGIEQS GGRVTGVQTA DGVIPADIVV SCAGFWGAKI GAMIGMAVPL LPLAHQYVKT TPVPAQQGRN DQPNGARLPILRHQDQDLYY REHGDRYGIG SYAHRPMPVD VDTLGAYAPE TVSEHHMPSR LDFTLEDFLP AWEATKQLLP ALADSEIEDG FNGIFSFTPDGGPLLGESKE LDGFYVAEAV WVTHSAGVAK AMAELLTTGR SETDLGECDI TRFEDVQLTP EYVSETSQQN FVEIYDVLHP LQPRLSPRNLRVSPFHARHK ELGAFFLEAG GWERPYWFEA NAALLKEMPA EWLPPARDAW SGMFSSPIAA AEAWKTRTAV AMYDMTPLKR LEVSGPGALKLLQELTTADL AKKPGAVTYT LLLDHAGGVR SDITVARLSE DTFQLGANGN IDTAYFERAA RHQTQSGSAT DWVQVRDTTG GTCCIGLWGPLARDLVSKVS DDDFTNDGLK YFRAKNVVIG GIPVTAMRLS YVGELGWELY TSADNGQRLW DALWQAGQPF GVIAAGRAAF SSLRLEKGYRSWGTDMTTEH DPFEAGLGFA VKMAKESFIG KGALEGRTEE ASARRLRCLT IDDGRSIVLG KEPVFYKEQA VGYVTSAAYG YTVAKPIAYSYLPGTVSVGD SVDIEYFGRR ITATVTEDPL YDPKMTRLRG.

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Description:

Galactosidase-Beta 1 E.coli Recombinant

lacZ, beta-gal, β-gal.

Product # :

ENZ-041

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

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

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

Description:

Thymidylate Synthetase Human Recombinant

TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.

Product # :

ENZ-470

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Description

Thymidylate synthase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 333 amino acids (1-313 a.a.) and having a molecular mass of 37.8 kDa. The Thymidylate synthase fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Thymidylate synthase catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5,10-methylenetetrahydrofolate as a cofactor which maintains the dTMP (thymidine-5-prime monophosphate) pool vital for DNA replication and repair. Thymidylate synthase plays an important role as a cancer chemotherapeutic agent. Thymidylate synthase is the primary site of action for 5-fluoro-2-prime-deoxyuridine and several folate analogs.
Synonyms
TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.
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 MPVAGSELPR RPLPPAAQER DAEPRPPHGE LQYLGQIQHI LRCGVRKDDR TGTGTLSVFG MQARYSLRDE FPLLTTKRVF WKGVLEELLW FIKGSTNAKE LSSKGVKIWD ANGSRDFLDS LGFSTREEGD LGPVYGFQWR HFGAEYRDME SDYSGQGVDQ LQRVIDTIKT NPDDRRIIMC AWNPRDLPLM ALPPCHALCQ FYVVNSELSC QLYQRSGDMG LGVPFNIASY ALLTYMIAHI TGLKPGDFIH TLGDAHIYLN HIEPLKIQLQ REPRPFPKLR ILRKVEKIDD FKAEDFQIEG YNPHPTIKME MAV.

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

Description:

Glutamic-Pyruvate Transaminase Rat Recombinant

Alanine aminotransferase 1 (EC:2.6.1.2), ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, Gpt, Aat1, Gpt1.

Product # :

ENZ-918

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Description

GPT Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 57.5kDa. GPT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

GPT protein solution (1mg/ml) containing Phosphate Buffered Saline pH 7.4 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 60units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.

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Introduction
GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.
Synonyms
Alanine aminotransferase 1 (EC:2.6.1.2), ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, Gpt, Aat1, Gpt1.
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 MGSMASRVND QSQASRNGLK GKVLTLDTMN PCVRRVEYAV RGPIVQRALE LEQELRQGVK KPFTEVIRAN IGDAQAMGQR PITFFRQVLA LCVYPNLLSS PDFPEDAKRR AERILQACGG HSLGAYSISS GIQPIREDVA QYIERRDGGI PADPNNIFLS TGASDAIVTM LKLLVSGEGR ARTGVLIPIP QYPLYSAALA ELDAVQVDYY LDEERAWALD IAELRRALCQ ARDRCCPRVL CVINPGNPTG QVQTRECIEA VIRFAFKEGL FLMADEVYQD NVYAEGSQFH SFKKVLMEMG PPYSTQQELA SFHSVSKGYM GECGFRGGYV EVVNMDAEVQ KQMGKLMSVR LCPPVPGQAL MDMVVSPPTP SEPSFKQFQA ERQEVLAELA AKAKLTEQVF NEAPGIRCNP VQGAMYSFPQ VQLPLKAVQR AQELGLAPDM FFCLCLLEET GICVVPGSGF GQQEGTYHFR MTILPPMEKL RLLLEKLSHF HAKFTHEYS.

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:

Alkaline Phosphatase Liver/Bone/Kidney Mouse Recombinant

Alpl, Akp-2, Akp2, ALP, APTNAP, TNAP, TNSALP, HOPS, AP-TNAP, Alkaline phosphatase 2.

Product # :

ENZ-1008

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Description

ALPL produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 493 amino acids (19-503 a.a.) and having a molecular mass of 54.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). ALPL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 46,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of 4-Methylumbelliferyl phosphate to phosphate and 4-Methylumbelliferone per minute at pH 8.8 at 25C.

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Introduction
Alkaline Phosphatase Liver/Bone/Kidney (Alpl) is a part of the alkaline phosphatases family which comprises 4 related alkaline phosphatases. Alpl is a membrane-bound glycosylated enzyme which is not expressed in any particular tissue. Alpl takes part in skeletal mineralization.
Synonyms
Alpl, Akp-2, Akp2, ALP, APTNAP, TNAP, TNSALP, HOPS, AP-TNAP, Alkaline phosphatase 2.
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
VPEKERDPSY WRQQAQETLK NALKLQKLNT NVAKNVIMFL GDGMGVSTVT AARILKGQLH HNTGEETRLE MDKFPFVALS KTYNTNAQVP DSAGTATAYL CGVKANEGTV GVSAATERTR CNTTQGNEVT SILRWAKDAG KSVGIVTTTR VNHATPSAAY AHSADRDWYS DNEMPPEALS QGCKDIAYQL MHNIKDIDVI MGGGRKYMYP KNRTDVEYEL DEKARGTRLD GLDLISIWKS FKPRHKHSHY VWNRTELLAL DPSRVDYLLG LFEPGDMQYE LNRNNLTDPS LSEMVEVALR ILTKNLKGFF LLVEGGRIDH GHHEGKAKQA LHEAVEMDQA IGKAGAMTSQ KDTLTVVTAD HSHVFTFGGY TPRGNSIFGL APMVSDTDKK PFTAILYGNG PGYKVVDGER ENVSMVDYAH NNYQAQSAVP LRHETHGGED VAVFAKGPMA HLLHGVHEQN YIPHVMAYAS CIGANLDHCA WAGSGLEHHH HHH.

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-6 Adenine-Specific DNA Methyltransferase 1 Human Recombinant

N-6 Adenine-Specific DNA Methyltransferase 1 (Putative), N(6)-Adenine-Specific DNA Methyltransferase 1, HemK Methyltransferase Family Member 2, M.HsaHemK2P, C21orf127, HEMK2, Chromosome 21 Open Reading Frame 127, N6-DNA-Methyltransferase, EC 2.1.1.- , PRED28, N6AMT, MTQ2, HemK methyltransferase family member 2.

Product # :

ENZ-834

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Description

N6AMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 25.3kDa. N6AMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

N6AMT1 protein solution (0.25 mg/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
N-6 Adenine-Specific DNA Methyltransferase 1, also known as N6AMT1 is part of the methyltransferase family. N6AMT1 is implicated in the methylation of release factor I during translation termination. In addition, N6AMT1 is involved in converting the arsenic metabolite monomethylarsonous acid to the less toxic dimethylarsonic acid.
Synonyms
N-6 Adenine-Specific DNA Methyltransferase 1 (Putative), N(6)-Adenine-Specific DNA Methyltransferase 1, HemK Methyltransferase Family Member 2, M.HsaHemK2P, C21orf127, HEMK2, Chromosome 21 Open Reading Frame 127, N6-DNA-Methyltransferase, EC 2.1.1.- , PRED28, N6AMT, MTQ2, HemK methyltransferase family member 2.
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 MGSMAGENFA TPFHGHVGRG AFSDVYEPAE DTFLLLNALE AAAAELAGVE ICLEVGSGSG VVSAFLASMI GPQALYMCTD INPEAAACTL ETARCNKVHI QPVITDLVKG LLPRLTEKVD LLVFNPPYVV TPPQEVGSHG IEAAWAGGRN GREVMDRFFP LVPDLLSPRG LFYLVTIKEN NPEEILKIMK TKGLQGTTAL SRQAGQETLS VLKFTKS.

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:

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.

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

Description:

Carboxylesterase 1G Mouse Recombinant

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

Product # :

ENZ-947

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formulation
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Description

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

Source

Sf9, Baculovirus cells.

Formulation

CES1G protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

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

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Introduction
Carboxylesterase 1 (CES1G) belongs to a large family of carboxylesterases that are liable for the hydrolysis of ester and amide bonds. CES1G is also participates in the detoxification of xenobiotics prodrugs. CES1G shares the serine hydrolase fold observed in other esterases. CES1G found in rats and mice and is expressed mainly in liver, but also in kidney and lung.
Synonyms
Liver carboxylesterase 1, Acyl-coenzyme A:cholesterol acyltransferase, Carboxylesterase 1G, ES-x, CES1G.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPHPSLPPV VHTVHGKVLG KYVTLEGFSQ PVAVFLGVPF AKPPLGSLRF APPEPAEPWS FVKHTTSYPP LCYQNPEAAL RLAELFTNQR KIIPHKFSED CLYLNIYTPA DLTQNSRLPV MVWIHGGGLV IDGASTYDGV PLAVHENVVV VVIQYRLGIW GFFSTEDEHS RGNWGHLDQV AALHWVQDNI ANFGGNPGSV TIFGESAGGE SVSVLVLSPL AKNLFHRAIA QSSVIFNPCL FGRAARPLAK KIAALAGCKT TTSAAMVHCL RQKTEDELLE VSLKMKFGTV DFLGDPRESY PFLPTVIDGV LLPKAPEEIL AEKSFNTVPY MVGINKHEFG WIIPMFLDFP LSERKLDQKT AASILWQAYP ILNISEKLIP AAIEKYLGGT EDPATMTDLF LDLIGDIMFG VPSVIVSRSH RDAGAPTYMY EYQYRPSFVS DDRPQELLGD HADELFSVWG APFLKEGASE EEINLSKMVM KFWANFARNG NPNGEGLPHW PEYDQKEGYL QIGVPAQAAH RLKDKEVDFW TELRAKETAE RSSHREHVEL HHHHHH.

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

Description:

Protease Serine 28 Mouse Recombinant

Serine protease 28, Implantation serine proteinase 1, ISP-1, Strypsin, Tryptase-like proteinase.

Product # :

ENZ-987

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Description

PRSS28 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 256 amino acids (27-274a.a.) and having a molecular mass of 28.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). PRSS28 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

PRSS28 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Serine protease 28, also known as Prss28, is a member of the S1 serine proteinase family with a conserved Histidine-Aspartic Acid-Serine catalytic triad. Prss28 shows mixed substrate specificity which silences signaling through proteinase-activated receptors. Furthermore, Prss28 is involved with embryo hatching and its activity is vital for successful implantation.
Synonyms
Serine protease 28, Implantation serine proteinase 1, ISP-1, Strypsin, Tryptase-like proteinase.
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
KPVGIVGGQC TPPGKWPWQV SLRMYSYEVN SWVHICGGSI IHPQWILTAA HCIQSQDADP AVYRVQVGEV YLYKEQELLN ISRIIIHPDY NDVSKRFDLA LMQLTALLVT STNVSPVSLP KDSSTFDSTD QCWLVGWGNL LQRVPLQPPY QLHEVKIPIQ DNKSCKRAYR KKSSDEHKAV AIFDDMLCAG TSGRGPCFGD SGGPLVCWKS NKWIQVGVVS KGIDCSNNLP SIFSRVQSSL AWIHQHIQLE 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:

Glycogenin-1 Human Recombinant

Glycogenin-1, GYG1, GYG.

Product # :

ENZ-431

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Shipped with Ice Packs

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purity
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Description

GYG1 Human Recombinant fused with a 32 amino acid His-T7 tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 365 amino acids (1-333 a.a.) and having a molecular mass of 41.2kDa.The GYG1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GYG1 solution contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Glycogenin-1 (GYG1) is an enzyme involved in glycogen biosynthesis. GYG1 is the chief enzyme involved in glycogen polymerisation. Glycogenin-1 is vital for the function of self-glucosylates, using an inter-subunit mechanism, to form an oligosaccharide primer which acts as substrate for glycogen synthase. In addition, GYG1 has a role in regulating glycogen metabolism and the achievement of maximal glycogen levels in skeletal muscle. GYG1 mRNA and protein content and activity increase in the muscle during recovery from prolonged and exhaustive exercise. GYG1 is inactivated with glycogen catabolism which concurs with an increase in glycogenin gene expression as exercise and glycogenolysis advance. Glycogenin will remain covalently attached to the reducing end of the glycogen molecule.
Synonyms
Glycogenin-1, GYG1, GYG.
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
MHHHHHHMAS MTGGQQMGRD LYDDDDKDRW GSMTDQAFVT LTTNDAYAKG ALVLGSSLKQ HRTTRRLVVL ATPQVSDSMR KVLETVFDEV IMVDVLDSGD SAHLTLMKRP ELGVTLTKLH CWSLTQYSKC VFMDADTLVL ANIDDLFDRE ELSAAPDPGW PDCFNSGVFV YQPSVETYNQ LLHLASEQGS FDGGDQGILN TFFSSWATTD IRKHLPFIYN LSSISIYSYL PAFKVFGASA KVVHFLGRVK PWNYTYDPKT KSVKSEAHDP NMTHPEFLIL WWNIFTTNVL PLLQQFGLVK DTCSYVNVED VSGAISHLSL GEIPAMAQPF VSSEERKERW EQGQADYMGA DSFDNIKRKL DTYLQ.

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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