Search: 1000 results found for "isomerase"

Description:

Streptokinase Recombinant

Streptokinase, SK.

Product # :

ENZ-315

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Description

Streptokinase Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 414 amino acids and having a molecular weight of 47.3kDa.The Streptokinase is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific biological activity measured by the ability of fibrin lysis in agarose plate was found to be 80000IU/mg.

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Introduction
Streptokinase is an extracellular metallo-enzymeproduced by beta-haemolytic streptococcusand is used as an effective and cheap clot-dissolving medicationin some cases of myocardial infarction(heart attack) and pulmonary embolism.
It belongs to a group of medications known as fibrinolytics, and works by activating plasminogenthrough cleavage to produce plasmin.
Synonyms
Streptokinase, SK.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Streptokinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Streptokinase 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 Streptokinase in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IAGPEWLLDR PSVNNSQLVV SVAGTVEGTN QDISLKFFEI DLTSRPAHGG KTEQGLSPKS KLFATDSGAM PHKLEKADLL KAIQEQLIAN VHSNDDYFEV IDFASDATIT DRNGKVYFAD KDGSVTLPIQ PVQEFLLKGH VRVRPYKEKP VQNQAKSVDV EYTVQFTPLN PDDDFRPALK DTKLLKTLAI GDTITSQELL AQAQSILNKN HPGYTIYERD SSIVTHDNDI FRTILPMDQE FTYHVKNREQ AYRINKKSGL NEEINNTDLI SEKYYVLKKG EKPYDPFDRS HLKLFTIKYV DVNTNELLKS EQLLTASERN LDFRDLYDPR DKAKLLYNNL DAFGIMDYTL TGKVEDNHDD TNRIITVYMG KRPEGENASY HLAYDKDRYT EEEREVYSYL RYTGTPIPDN PNDK.

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:

Monoglyceride Lipase Human Recombinant

Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.

Product # :

ENZ-019

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Description

MGLL Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 333 amino acids (1-313 a.a.) and having a molecular mass of 36.4kDa. The MGLL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MGLL solution (0.5mg/ml) contains 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
MGLL is a membrane-associated member of the serine hydrolase superfamily. MGLL is expressed in abundance in skeletal muscle and adipose tissue. MGLL functions jointly with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.
Synonyms
Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.
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 METGPEDPSS MPEESSPRRT PQSIPYQDLP HLVNADGQYL FCRYWKPTGT PKALIFVSHG AGEHSGRYEE LARMLMGLDL LVFAHDHVGH GQSEGERMVV SDFHVFVRDV LQHVDSMQKD YPGLPVFLLG HSMGGAIAIL TAAERPGHFA GMVLISPLVL ANPESATTFK VLAAKVLNLV LPNLSLGPID SSVLSRNKTE VDIYNSDPLI CRAGLKVCFG IQLLNAVSRV ERALPKLTVP FLLLQGSADR LCDSKGAYLL MELAKSQDKT LKIYEGAYHV LHKELPEVTN SVFHEINMWV SQRTATAGTA SPP.

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:

Aldo-Keto Reductase Family 1 Member D1 Human Recombinant

3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-Keto Reductase Family 1, Member D1, SRD5B1, Delta(4)-3-Ketosteroid 5-Beta-Reductase, Delta 4-3-Ketosteroid-5-Beta-Reductase, Delta(4)-3-Oxosteroid 5-Beta-Reductase, CBAS2, Steroid-5-Beta-Reductase, Beta Polypeptide 1 (3-Oxo-5 Beta-Steroid Delta 4-Dehydrogenase Beta 1), Aldo-Keto Reductase Family 1, Member D1 (Delta 4-3-Ketosteroid-5-Beta-Reductase), Aldo-Keto Reductase Family 1 Member D1, 3-Oxo-5-Beta-Steroid 4-Dehydrogenase, EC 1.3.1.3, 3o5bred.

Product # :

ENZ-931

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Description

AKR1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 326 amino acids (1-326 a.a.) and having a molecular mass of 37.3kDa. The AKR1D1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The AKR1D1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Aldo-keto reductase family 1 member D1 (AKR1D1) belongs to the AKR superfamily. The AKR family proteins are soluble NADPH oxidoreductases, which have vital roles in the metabolism of drugs, carcinogens and reactive aldehydes. AKR1D1 is also responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones that carry a delta (4)-3-1 structure. AKR1D1 is highly expressed in the liver, colon and testis. Deficiency of the AKR1D1 enzyme may contribute to hepatic dysfunction.
Synonyms
3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-Keto Reductase Family 1, Member D1, SRD5B1, Delta(4)-3-Ketosteroid 5-Beta-Reductase, Delta 4-3-Ketosteroid-5-Beta-Reductase, Delta(4)-3-Oxosteroid 5-Beta-Reductase, CBAS2, Steroid-5-Beta-Reductase, Beta Polypeptide 1 (3-Oxo-5 Beta-Steroid Delta 4-Dehydrogenase Beta 1), Aldo-Keto Reductase Family 1, Member D1 (Delta 4-3-Ketosteroid-5-Beta-Reductase), Aldo-Keto Reductase Family 1 Member D1, 3-Oxo-5-Beta-Steroid 4-Dehydrogenase, EC 1.3.1.3, 3o5bred.
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
MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE ALNKNVRFVE LLMWRDHPEY PFHDEY.

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 Human Recombinant

Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

Product # :

ENZ-192

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Description

GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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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
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
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 MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS

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 E2W Human Recombinant

Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.

Product # :

ENZ-117

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Description

UBE2W produced in E.Coli is a single, non-glycosylated polypeptide chain containing 171 amino acids (1-151 a.a.) and having a molecular mass of 19.5kDa.UBE2W is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

UBE2W solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
UBE2W receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2W catalyzes monoubiquitination and 'Lys-11'-linked polyubiquitination. UBE2W is broadly expressed, particularly at highest levels in the testis.
Synonyms
Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.
Physical Appearance
Sterile filtered colorless solution.
Stability
UBE2W Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT 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:

Shiga Like Toxin-1 Subunit B Recombinant

Product # :

STX-001

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Description

Recombinant Shiga Like Toxin-1 Subunit B is produced from E.Coli O157:H7 amino acids 2-90 of the Shiga Like Toxin-1 Subunit B.The Shiga Like Toxin 1 protein is fused to a 6xHis tag at its N-terminus and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Phosphate buffered saline and 25mM K₂CO₃.

Purity

Protein is >95% pure as determined by 12% PAGE (coomassie staining).

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Introduction
Shiga-like toxin (verotoxin) is a toxin produced by some strains of Escherichia coli. Shiga-like toxin is named for its similarity to the AB5-type Shiga toxin produced by the bacteria Shigella dysenteriae. There are two known types-SLT1 and SLT2. The Shiga-like toxin is linked with hemolytic-uremic syndrome. Shiga-like toxin requires highly specific receptors on the cells' surface in order to attach and enter the cell. Species such as cattle, swine, and deer which do not carry these receptors may harbor toxigenic bacteria without any ill effect, dropping them in their feces, from where they may be distributed to humans. Shiga Like Toxin-1 Subunit B has nontoxic action, it is the functional region which binds to the receptor. The Shiga Like Toxin-1 Subunit B can be useful in vaccine study, antibody test and other functional research.
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.
Purification Method
Purified by affinity 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:

Glutaminyl-Peptide Cyclotransferase Human Recombinant

Glutaminyl-Peptide Cyclotransferase, Glutaminyl Cyclase, QC, Glutaminyl-TRNA Cyclotransferase, Glutamyl Cyclase, EC 2.3.2.5, SQC, EC, GCT, Glutaminyl-peptide cyclotransferase.

Product # :

ENZ-912

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Description

QPCT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 339 amino acids (29-361a.a.) and having a molecular mass of 38.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). QPCT is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Glutaminyl-Peptide Cyclotransferase, also known as QPCT is a member of the glutaminyl-peptide cyclotransferase family. QPCT is responsible for the biosynthesis of pyroglutamyl peptides. Furthermore, QPCT is partial against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length following the second residue. QPCT catalyzes N-terminal pyroglutamate formation, also in vitro, it catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid.
Synonyms
Glutaminyl-Peptide Cyclotransferase, Glutaminyl Cyclase, QC, Glutaminyl-TRNA Cyclotransferase, Glutamyl Cyclase, EC 2.3.2.5, SQC, EC, GCT, Glutaminyl-peptide cyclotransferase.
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
VSPSASAWPE EKNYHQPAIL NSSALRQIAE GTSISEMWQN DLQPLLIERY PGSPGSYAAR QHIMQRIQRL QADWVLEIDT FLSQTPYGYR SFSNIISTLN PTAKRHLVLA CHYDSKYFSH WNNRVFVGAT DSAVPCAMML ELARALDKKL LSLKTVSDSK PDLSLQLIFF DGEEAFLHWS PQDSLYGSRH LAAKMASTPH PPGARGTSQL HGMDLLVLLD LIGAPNPTFP NFFPNSARWF ERLQAIEHEL HELGLLKDHS LEGRYFQNYS YGGVIQDDHI PFLRRGVPVL HLIPSPFPEV WHTMDDNEEN LDESTIDNLN KILQVFVLEY LHLHHHHHH.

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:

Hydroxyprostaglandin Dehydrogenase 15-(NAD) Mouse Recombinant

15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC:1.1.1.141), 15-PGDH, Hpgd, Pgdh1, Prostaglandin dehydrogenase 1.

Product # :

ENZ-1027

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Description

HPGD Mouse Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (1-269) and having a molecular mass of 31.6kDa. HPGD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
HPGD is the essential enzyme of prostaglandin degradation. 15-PGDH protein strongly decreases the biologic activity of these molecules by catalyzing the oxidation of the 15-hydroxyl group of prostaglandins to a keto group. GDH1 is involved in numerous physiologic and cellular processes, for instance inflammation.
Synonyms
15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC:1.1.1.141), 15-PGDH, Hpgd, Pgdh1, Prostaglandin dehydrogenase 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 MGSMHVNGKV ALVTGAAQGI GKAFAEALLL HGAKVALVDW NLEAGVKCKA ALDEQFEPQK TLFVQCDVAD QKQLRDTFRK VVDHFGRLDI LVNNAGVNNE KNWEQTLQIN LVSVISGTYL GLDYMSKQNG GEGGIIINMS SLAGLMPVAQ QPVYCASKHG IIGFTRSAAM AANLMKSGVR LNVICPGFVD TPILESIEKE ENMGQYIEYK DQIKAMMKFY GVLHPSTIAN GLINLIEDDA LNGAIMKITA SKGIHFQDYD ISPLLVKAPL TS.

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:

Poly (ADP-Ribose) Polymerase 2 Human Recombinant

ADPRT2, ADPRTL2, ADPRTL3, ARTD2, pADPRT-2, PARP-2, Poly [ADP-ribose] polymerase 2, hPARP-2, ADP-ribosyltransferase diphtheria toxin-like 2, NAD (+) ADP-ribosyltransferase 2, Poly [ADP-ribose] synthase 2.

Product # :

ENZ-694

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Description

PARP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (233-583a.a) and having a molecular mass of 42.5kDa. PARP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PARP2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Poly (ADP-Ribose) Polymerase 2 (PARP2) contains a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. PARP2 is capable of catalyzing a poly (ADP-ribosyl)ation reaction. The basic residues within the N-terminal area of this protein can bear potential DNA-binding properties, and can be engaged in the nuclear and/or nucleolar targeting of the protein. There has been found two alternatively spliced transcript variants encoding distinct isoforms.
Synonyms
ADPRT2, ADPRTL2, ADPRTL3, ARTD2, pADPRT-2, PARP-2, Poly [ADP-ribose] polymerase 2, hPARP-2, ADP-ribosyltransferase diphtheria toxin-like 2, NAD (+) ADP-ribosyltransferase 2, Poly [ADP-ribose] synthase 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 MGSHMQLDLR VQELIKLICN VQAMEEMMME MKYNTKKAPL GKLTVAQIKA GYQSLKKIED CIRAGQHGRA LMEACNEFYT RIPHDFGLRT PPLIRTQKEL SEKIQLLEAL GDIEIAIKLV KTELQSPEHP LDQHYRNLHC ALRPLDHESY EFKVISQYLQ STHAPTHSDY TMTLLDLFEV EKDGEKEAFR EDLHNRMLLW HGSRMSNWVG ILSHGLRIAP PEAPITGYMF GKGIYFADMS SKSANYCFAS RLKNTGLLLL SEVALGQCNE LLEANPKAEG LLQGKHSTKG LGKMAPSSAH FVTLNGSTVP LGPASDTGIL NPDGYTLNYN EYIVYNPNQV RMRYLLKVQF NFLQLW.

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

Description:

Arylsulfatase A Mouse Recombinant, Active

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

Product # :

ENZ-1088

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Description

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

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.
Synonyms
Arylsulfatase A, Arsa, As-2, AS-A, As2, ASA, AW212749, TISP73.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPSPPNILL IFADDLGYGD LGSYGHPSST TPNLDQLAEG GLRFTDFYVP VSLCTPSRAA LLTGRLPVRSGMYPGVLGPS SQGGLPLEEVTLAEVLAARG YLTGMAGKWH LGVGPEGAFL PPHQGFHRFL GIPYSHDQGP CQNLTCFPPD IPCKGGCDQG LVPIPLLANL TVEAQPPWLPGLEARYVSFS RDLMADAQRQ GRPFFLYYAS HHTHYPQFSG QSFTKRSGRG PFGDSLMELD GAVGALMTTV GDLGLLEETL VIFTADNGPELMRMSNGGCSGLLRCGKGTT FEGGVREPAL VYWPGHITPG VTHELASSLD LLPTLAALTG APLPNVTLDG VDISPLLLGT GKSPRKSVFFYPPYPDEIHG VFAVRNGKYK AHFFTQGSAH SDTTSDPACH AANRLTAHEP PLLYDLSQDP GENYNVLESI EGVSPEALQA LKHIQLLKAQYDAAMTFGPS QIAKGEDPAL QICCQPSCTP HPVCCHCPGS QSHHHHHH.

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

Description:

Polypeptide N-Acetylgalactosaminyltransferase 1 Mouse Recombinant

Polypeptide N-acetylgalactosaminyltransferase 1, Polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, Protein-UDP acetylgalactosaminyltransferase 1, polypeptide N-acetylgalactosaminyltransferase 1.

Product # :

ENZ-1066

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Description

GALNT1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 528 amino acids (41-559 a.a.) and having a molecular mass of 60.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).GALNT1 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

GALNT1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) , is part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.
Synonyms
Polypeptide N-acetylgalactosaminyltransferase 1, Polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, Protein-UDP acetylgalactosaminyltransferase 1, polypeptide N-acetylgalactosaminyltransferase 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
ADPGLPAGDV LELVQKPHEG PGEMGKPVVI PKEDQEKMKE MFKINQFNLM ASEMIALNRS LPDVRLEGCK TKVYPDNLPT TSVVIVFHNE AWSTLLRTVH SVINRSPRHM IEEIVLVDDA SERDFLKRPL ESYVKKLKVP VHVIRMEQRS GLIRARLKGA AVSRGQVITF LDAHCECTAG WLEPLLARIK HDRRTVVCPI IDVISDDTFE YMAGSDMTYG GFNWKLNFRW YPVPQREMDR RKGDRTLPVR TPTMAGGLFS IDRDYFQEIG TYDAGMDIWG GENLEISFRI WQCGGTLEIV TCSHVGHVFR KATPYTFPGG TGQIINKNNR RLAEVWMDEF KNFFYIISPG VTKVDYGDIS SRLGLRRKLQ CKPFSWYLEN IYPDSQIPRH YFSLGEIRNV ETNQCLDNMA RKENEKVGIF NCHGMGGNQV FSYTANKEIR TDDLCLDVSK LNGPVTMLKC HHLKGNQLWE YDPVKLTLQH VNSNQCLDKA TEEDSQVPSI RDCTGSRSQQ WLLRNVTLPE IFHHHHHH .

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:

Glucuronidase Beta Human Recombinant

GUSB, BG, MPS7, Glucuronidase Beta, EC 3.2.1.31, Beta-G1, Beta-D-Glucuronidase, Glucuronidase, Beta, Beta-Glucuronidasem.

Product # :

ENZ-1018

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Description

GUSB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 635 amino acids (23-651a.a) and having a molecular mass of 73.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GUSB is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GUSB 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.

Biological Activity

Specific activity is > 1600 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-Methylumbelliferone to 4- Methylum-belliferyl-β-D-glucosiduronic acid per minute at 37C and pH6.0.

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Introduction
Glucuronidase Beta (GUSB) is a lysosomal hydrolase which is taking part in the stepwise degradation of glucuronic acid-containing glycosaminoglycans and plays a significant role in the degradation of dermatan and keratin sulfates. GUSB is comprised of heparin sulfate, chondroitin sulfate and hyaluronan.
Synonyms
GUSB, BG, MPS7, Glucuronidase Beta, EC 3.2.1.31, Beta-G1, Beta-D-Glucuronidase, Glucuronidase, Beta, Beta-Glucuronidasem.
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
LQGGMLYPQE SPSRECKELD GLWSFRADFS DNRRRGFEEQ WYRRPLWESG PTVDMPVPSS FNDISQDWRL RHFVGWVWYE REVILPERWT QDLRTRVVLR IGSAHSYAIV WVNGVDTLEH EGGYLPFEAD ISNLVQVGPL PSRLRITIAI NNTLTPTTLP PGTIQYLTDT SKYPKGYFVQ NTYFDFFNYA GLQRSVLLYT TPTTYIDDIT VTTSVEQDSG LVNYQISVKG SNLFKLEVRL LDAENKVVAN GTGTQGQLKV PGVSLWWPYL MHERPAYLYS LEVQLTAQTS LGPVSDFYTL PVGIRTVAVT KSQFLINGKP FYFHGVNKHE DADIRGKGFD WPLLVKDFNL LRWLGANAFR TSHYPYAEEV MQMCDRYGIV VIDECPGVGL ALPQFFNNVS LHHHMQVMEE VVRRDKNHPA VVMWSVANEP ASHLESAGYY LKMVIAHTKS LDPSRPVTFV SNSNYAADKG APYVDVICLN SYYSWYHDYG HLELIQLQLA TQFENWYKKY QKPIIQSEYG AETIAGFHQD PPLMFTEEYQ KSLLEQYHLG LDQKRRKYVV GELIWNFADF MTEQSPTRVL GNKKGIFTRQ RQPKSAAFLL RERYWKIANE TRYPHSVAKS QCLENSLFTH HHHHH.

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

Description:

Hydroxyacid Oxidase 1 Human Recombinant

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

Product # :

ENZ-162

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Description

HAO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-370 a.a.) and having a molecular mass of 45kDa.HAO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Glycolate oxidase (HAO1) belongs to the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyzes the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate with reduction of oxygen to hydrogen peroxide. HAO1 is most abundantly expressed in the liver and pancreas and is most active on twocarbon substrates such as glycolate. Lately, HAO1 has been identified as a key contributor to hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.
Synonyms
Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.
Physical Appearance
Sterile filtered 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 KDRWGSMLPR LICINDYEQH AKSVLPKSIY DYYRSGANDE ETLADNIAAF SRWKLYPRML RNVAETDLST SVLGQRVSMP ICVGATAMQR MAHVDGELAT VRACQSLGTG MMLSSWATSS IEEVAEAGPE ALRWLQLYIY KDREVTKKLV RQAEKMGYKA IFVTVDTPYL GNRLDDVRNR FKLPPQLRMK NFETSTLSFS PEENFGDDSG LAAYVAKAID PSISWEDIKW LRRLTSLPIV AKGILRGDDA REAVKHGLNG ILVSNHGARQ LDGVPATIDV LPEIVEAVEG KVEVFLDGGV RKGTDVLKAL ALGAKAVFVG RPIVWGLAFQ GEKGVQDVLE ILKEEFRLAM ALSGCQNVKV IDKTLVRKNP LAVSKI.

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

Description:

Nei Endonuclease VIII-Like 2 Human Recombinant

Endonuclease 8-like 2, DNA glycosylase/AP lyase Neil2, DNA-(apurinic or apyrimidinic site) lyase Neil2, Endonuclease VIII-like 2, Nei homolog 2, NEH2, Nei-like protein 2, NEIL2, NEH2.

Product # :

ENZ-607

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Description

NEIL2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 356 amino acids (1-332) and having a molecular mass of 39.4kDa.NEIL2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NEIL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Endonuclease 8-like 2 (NEIL2) is a member of a class of DNA glycosylases homologous to the bacterial Fpg/Nei family. These glycosylases set off the first step in base excision repair by cleaving bases damaged by reactive oxygen species and introducing a DNA strand break through the associated lyase reaction. NEIL2 is involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. NEIL2 has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double stranded DNA (DNA bubbles). NEIL2 has insignificant or undetectable activity with 8-oxoguanine, thymine glycol, 2-hydroxyadenine, hypoxanthine, and xanthine. NEIL2 also has AP (apurinic/apyrimidinic) lyase activity and creates incisions in the DNA strand. NEIL2 cleaves the DNA backbone by beta-delta exclusion to produce a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. NEIL2 is found in the testis, skeletal muscle, heart, brain, placenta, lung, pancreas, kidney and liver.
Synonyms
Endonuclease 8-like 2, DNA glycosylase/AP lyase Neil2, DNA-(apurinic or apyrimidinic site) lyase Neil2, Endonuclease VIII-like 2, Nei homolog 2, NEH2, Nei-like protein 2, NEIL2, NEH2.
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 MGSHMPEGPL VRKFHHLVSP FVGQQVVKTG GSSKKLQPAS LQSLWLQDTQ VHGKKLFLRF DLDEEMGPPG SSPTPEPPQK EVQKEGAADP KQVGEPSGQK TLDGSSRSAE LVPQGEDDSE YLERDAPAGD AGRWLRVSFG LFGSVWVNDF SRAKKANKRG
DWRDPSPRLV LHFGGGGFLA FYNCQLSWSS SPVVTPTCDI LSEKFHRGQA LEALGQAQPV CYTLLDQRYF SGLGNIIKNE ALYRAGIHPL SLGSVLSASR REVLVDHVVE FSTAWLQGKF QGRPQHTQVY QKEQCPAGHQ VMKEAFGPED GLQRLTWWCP QCQPQLSEEP EQCQFS.

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:

Phosphogluconate Dehydrogenase, Active Human Recombinant

EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.

Product # :

ENZ-1128

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Description

PGD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-483) and having a molecular mass of 55.3 kDa.PGD Human is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 10unit/mg. One unit will oxidize 1.0 umole of 6-phospho-D-gluconate to D-ribulose 5- phosphate per minute at pH 8.0 at 25˚C, in the presence of beta-NADP.

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Introduction
6PGD is the 2nd dehydrogenase in the pentose phosphate shift. Pentose is crucial for the biosynthesis of nucleic acid. The pentose phosphate cycle is a prominent source of NADPH. 6PGD deficiency is mostly asymptomatic, and the inheritance of this deasis is autosomal dominant. PGD deficiency elevate the erythrocyte pyruvate kinase levels of activity & decreases glutathione synthetase, which causes hemolysis.
Synonyms
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
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 MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA

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:

Transketolase Human Recombinant

Transketolase, TK, TKT1, EC 2.2.1.1.

Product # :

ENZ-588

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Description

TKT Human Recombinant produced in E. coli is a single polypeptide chain containing 643 amino acids (1-623) and having a molecular mass of 70.0kDa.TKT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TKT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
TKT is a thiamine-dependent enzyme that takes part in the channeling of leftover sugar phosphates to glycolysis in the pentose phosphate pathway. Multiple alternatively spliced variants are known that encode the same protein.
Synonyms
Transketolase, TK, TKT1, EC 2.2.1.1.
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 MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE LLKMFGIDRD AIAQAVRGLI TKA.

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 2 Human Recombinant

ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.

Product # :

ENZ-680

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Description

GPT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 546 amino acids (1-523) and having a molecular mass of 60.3 kDa. GPT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GPT2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 7.5), 30% glycerol, 0.2M NaCl and 2mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.
Synonyms
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 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 MGSMQRAAAL VRRGCGPRTP SSWGRSQSSA AAEASAVLKV RPERSRRERI LTLESMNPQV KAVEYAVRGP IVLKAGEIEL ELQRGIKKPF TEVIRANIGD AQAMGQQPIT FLRQVMALCT YPNLLDSPSF PEDAKKRARR ILQACGGNSL GSYSASQGVN CIREDVAAYI TRRDGGVPAD PDNIYLTTGA SDGISTILKI LVSGGGKSRT GVMIPIPQYP LYSAVISELD AIQVNYYLDE ENCWALNVNE LRRAVQEAKD HCDPKVLCII NPGNPTGQVQ SRKCIEDVIH FAWEEKLFLL ADEVYQDNVY SPDCRFHSFK KVLYEMGPEY SSNVELASFH STSKGYMGEC GYRGGYMEVI NLHPEIKGQL VKLLSVRLCP PVSGQAAMDI VVNPPVAGEE SFEQFSREKE SVLGNLAKKA KLTEDLFNQV PGIHCNPLQG AMYAFPRIFI PAKAVEAAQA HQMAPDMFYC MKLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPVEKLKTV LQKVKDFHIN FLEKYA.

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

Description:

Beta-Glucocerebrosidase Human Recombinant

Glucosidase, Beta, Acid, D-Glucosyl-N-Acylsphingosine Glucohydrolase, Beta-Glucocerebrosidase, Acid Beta-Glucosidase, Glucosylceramidase, Alglucerase, EC 3.2.1.45, Beta-GC, GLUC, Glucosidase, Beta; Acid (Includes Glucosylceramidase), Glucosylceramidase-Like Protein, Lysosomal Glucocerebrosidase, GBA1, GCB, GC, Glucosylceramidase.

Product # :

ENZ-908

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Description

GBA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 503 amino acids (40-536a.a.) and having a molecular mass of 56.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). GBA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GBA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Beta-Glucocerebrosidase, also known as GBA is amember of the glycosyl hydrolase 30 family. GBA is a lysosomal enzyme which requires a signal peptide for transport across the membrane of the rough endoplasmic reticulum as well as glycosylation for transport into lysosomes. Furthermore, Gaucher disease is caused by a deficiency in the activity of the enzyme glucocerebrosidase.
Synonyms
Glucosidase, Beta, Acid, D-Glucosyl-N-Acylsphingosine Glucohydrolase, Beta-Glucocerebrosidase, Acid Beta-Glucosidase, Glucosylceramidase, Alglucerase, EC 3.2.1.45, Beta-GC, GLUC, Glucosidase, Beta; Acid (Includes Glucosylceramidase), Glucosylceramidase-Like Protein, Lysosomal Glucocerebrosidase, GBA1, GCB, GC, Glucosylceramidase.
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
ARPCIPKSFG YSSVVCVCNA TYCDSFDPPT FPALGTFSRY ESTRSGRRME LSMGPIQANH TGTGLLLTLQ PEQKFQKVKG FGGAMTDAAA LNILALSPPA QNLLLKSYFS EEGIGYNIIR VPMASCDFSI RTYTYADTPD DFQLHNFSLP EEDTKLKIPL IHRALQLAQR PVSLLASPWT SPTWLKTNGA VNGKGSLKGQ PGDIYHQTWA RYFVKFLDAY AEHKLQFWAV TAENEPSAGL LSGYPFQCLG FTPEHQRDFI ARDLGPTLAN STHHNVRLLM LDDQRLLLPH WAKVVLTDPE AAKYVHGIAV HWYLDFLAPA KATLGETHRL FPNTMLFASE ACVGSKFWEQ SVRLGSWDRG MQYSHSIITN LLYHVVGWTD WNLALNPEGG PNWVRNFVDS PIIVDITKDT FYKQPMFYHL GHFSKFIPEG SQRVGLVASQ KNDLDAVALM HPDGSAVVVV LNRSSKDVPL TIKDPAVGFL ETISPGYSIH TYLWRRQHHH 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:

Tryptophanase E.Coli Recombinant

Tryptophanase/L-cysteine desulfhydrase, PLP-dependent, Tryptophanase, TNAA, L-tryptophan indole-lyase, TNase, tnaA, ind.

Product # :

ENZ-852

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Description

TNAA Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 494 amino acids (1-471) and having a molecular mass of 55.2kDa.TNAA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TNAA solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Tryptophanase, also known as tnaA, catalyzes chemical reaction using 2 substrates which are L-tryptophan and H2O. tnaA protein's three products are indole, pyruvate, and NH3.
Synonyms
Tryptophanase/L-cysteine desulfhydrase, PLP-dependent, Tryptophanase, TNAA, L-tryptophan indole-lyase, TNase, tnaA, ind.
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 MGSMENFKHL PEPFRIRVIE PVKRTTRAYR EEAIIKSGMN PFLLDSEDVF IDLLTDSGTG AVTQSMQAAM MRGDEAYSGS RSYYALAESV KNIFGYQYTI PTHQGRGAEQ IYIPVLIKKR EQEKGLDRSK MVAFSNYFFD TTQGHSQING CTVRNVYIKE AFDTGVRYDF KGNFDLEGLE RGIEEVGPNN VPYIVATITS NSAGGQPVSL ANLKAMYSIA KKYDIPVVMD SARFAENAYF IKQREAEYKD WTIEQITRET YKYADMLAMS AKKDAMVPMG GLLCMKDDSF FDVYTECRTL CVVQEGFPTY GGLEGGAMER LAVGLYDGMN LDWLAYRIAQ VQYLVDGLEE IGVVCQQAGG HAAFVDAGKL LPHIPADQFP AQALACELYK VAGIRAVEIG SFLLGRDPKT GKQLPCPAEL LRLTIPRATY TQTHMDFIIE AFKHVKENAA NIKGLTFTYE PKVLRHFTAK LKEV.

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:

Thiol Peroxidase E.Coli Recombinant

Thiol peroxidase, Scavengase P20, tpx, yzzJ, b1324, JW1317.

Product # :

ENZ-135

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Description

TPX produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-168 a.a.) and having a molecular mass of 19.9kDa.TPX is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Recombinant TPX solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 10% glycerol, 2mM DTT and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Lipid hydroperoxide peroxidase (TPX) belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. TPX has an imperative role in thioredoxin peroxidase activity.
Synonyms
Thiol peroxidase, Scavengase P20, tpx, yzzJ, b1324, JW1317.
Physical Appearance
Sterile filtered liquid formulation 1 mg/ml.
Stability
TPX E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSQTVHFQGN PVTVANSIPQ AGSKAQTFTL VAKDLSDVTL GQFAGKRKVL NIFPSIDTGV CAASVRKFNQ LATEIDNTVV LCISADLPFA QSRFCGAEGL NNVITLSTFR NAEFLQAYGV AIADGPLKGL AARAVVVIDE NDNVIFSQLV DEITTEPDYE AALAVLKA.

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:

Cytidine Deaminase Human Recombinant

Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.

Product # :

ENZ-007

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Description

CDA Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids (1-146 a.a.) and having a molecular mass of 18.3kDa. The CDA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CDA solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 1mM DTT, 2mM EDTA, 100mM NaCl and 40% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 10,000pmol/min/ug, and is defined as the amount of required to deaminate 1.0pmole of cytidine per min at pH 7.5 at 25C.

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Introduction
Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. CDA is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as Ara-C and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function. CDA can form homotetramers and is generally expressed in granulocytes. Mutations in the CDA gene are linked to decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.
Synonyms
Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.
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 MAQKRPACTL KPECVQQLLV CSQEAKQSAY CPYSHFPVGA ALLTQEGRIF KGCNIENACY PLGICAERTA IQKAVSEGYK DFRAIAIASD MQDDFISPCG ACRQVMREFG TNWPVYMTKP DGTYIVMTVQ ELLPSSFGPE DLQKTQ.

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

Description:

Hexokinase-2 Human Recombinant

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

Product # :

PKA-227

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

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

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Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.
Synonyms
Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL GFTFSFPCHQTKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDISDIEGEKDGIR KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKENKGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG KGAAMVTAVAYRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS KETHASAPVK MLPTYVCATPDGTEKGDFLA LDLGGTNFRV LLVRVRNGKW GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG AALITAVACR IREAGQR.

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

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:

Aldolase B Fructose-Bisphosphate Human Recombinant

Fructose-bisphosphate aldolase B, Liver-type aldolase, ALDOB, ALDB, Aldolase B fructose-bisphosphate, ALDO2, aldolase 2, Aldolase B fructose-bisphosphatase.

Product # :

ENZ-245

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Description

ALDOB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 388 amino acids (1-364) and having a molecular mass of 42kDa.ALDOB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ALDOB 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
ALDOB is a tetrameric glycolytic enzyme which catalyzes the reversible cleavage of fructose 1-phosphate into dihydroxyacetone phosphate and glyceraldehyde. Fructose-bisphosphate aldolase B (ALDOB) is one of 3 known aldolase isoenzymes, and is located in the kidney and the small adult intestine where it is linked with aldolases A or C. ALDOB is regulated by Insulin and glucagon and is implicated in hereditary fructose intolerance disease.
Synonyms
Fructose-bisphosphate aldolase B, Liver-type aldolase, ALDOB, ALDB, Aldolase B fructose-bisphosphate, ALDO2, aldolase 2, Aldolase B fructose-bisphosphatase.
Physical Appearance
Sterile Filtered clear colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAHRFP ALTQEQKKEL SEIAQSIVAN GKGILAADES VGTMGNRLQR IKVENTEENR RQFREILFSV DSSINQSIGG VILFHETLYQ KDSQGKLFRN ILKEKGIVVG IKLDQGGAPL AGTNKETTIQ GLDGLSERCA QYKKDGVDFG KWRAVLRIAD
QCPSSLAIQE NANALARYAS ICQQNGLVPI VEPEVIPDGD HDLEHCQYVT EKVLAAVYKA LNDHHVYLEG TLLKPNMVTA GHACTKKYTP EQVAMATVTA LHRTVPAAVP GICFLSGGMS EEDATLNLNA INLCPLPKPW KLSFSYGRAL QASALAAWGG KAANKEATQE AFMKRAMANC
QAAKGQYVHT GSSGAASTQS LFTACYTY.

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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