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Search results

1000 results found for “dna polymerase”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    ENOPH1 Human

    Description:

    Enolase-Phosphatase-1 Human Recombinant

    Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.

    Product # :

    ENZ-077

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    Description

    ENOPH1 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 281 amino acids (1-261 a.a.) and having a molecular mass of 31kDa. The ENOPH1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ENOPH1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Enolase-phosphatase E1 (ENOPH1) belongs to the MasA family of the HAD (halo-acid dehalogenase)-like hydrolase superfamily. ENOPH1 is a bifunctional enzyme which demonstrates both phosphatase and atypical enolase activities. ENOPH1 has a significant role in the ubiquitous methionine salvage pathway which is a biochemical pathway found in all organisms that regulate methionine levels in the cell.

    • Synonyms

      Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.

    • 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 MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIEENVK EYLQTHWEEE ECQQDVSLLR KQAEEDAHLD GAVPIPAASG NGVDDLQQMI QAVVDNVCWQ MSLDRKTTAL KQLQGHMWRA AFTAGRMKAE FFADVVPAVR KWREAGMKVY IYSSGSVEAQ KLLFGHSTEG DILELVDGHF DTKIGHKVES ESYRKIADSI GCSTNNILFL TDVTREASAA EEADVHVAVV VRPGNAGLTD DEKTYYSLIT SFSELYLPSS T.

    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.

    Enoph1 Human
  • View Data Sheet

    Name :

    GCAT Human

    Description:

    Glycine C-Acetyltransferase Human Recombinant

    2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

    Product # :

    ENZ-705

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    Description

    GCAT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (22-419 a.a) and having a molecular mass of 45kDa.GCAT is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.

    • Synonyms

      2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

    • 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 MSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP.

    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.

    Gcat Human
  • View Data Sheet

    Name :

    LDHB Human, His

    Description:

    Lactate Dehydrogenase B Human Recombinant, His Tag

    LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.

    Product # :

    ENZ-539

    Price :

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    • purity
    • biological activity
    • More Info

    Description

    LDHB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-334 a.a.) and having a molecular mass of 38.8 kDa. The LDHB is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LDHB Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 6 units/mg. in which one unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C.

    More Info

    • Introduction

      LDHB is part of the lactate dehydrogenase family. LDHB is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LDHB catalyzes the oxidation of hydroxybutyrate, and frequently called Hydroxybutyrate Dehydrogenase (HBD). The LDH family consists of three members, LDH-A, LDH-B and LDH-C. LDHs function as powerful markers for germ cell tumors.

    • Synonyms

      LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.

    • 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 MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL.

    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.

    Ldhb Human
  • View Data Sheet

    Name :

    CES1G Mouse

    Description:

    Carboxylesterase 1G Mouse Recombinant

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

    Product # :

    ENZ-947

    Price :

    Quantity :

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    • description
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    • More Info

    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.

    More Info

    • 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.

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    Ces1 Mouse
  • View Data Sheet

    Name :

    GPT Human

    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.

    More Info

    • 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

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    Gpt Human
  • View Data Sheet

    Name :

    GOT2 Human, Active

    Description:

    Glutamic-Oxaloacetic Transaminase 2 Human Recombinant, Active

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

    Product # :

    ENZ-998

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    Description

    GOT2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (30-430 a.a.) and having a molecular mass of 47kDa. The GOT2 fused to a 23 amino acid his tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GOT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 60 units/mg, and is defined as the amount of enzyme that convert 1umole of α-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C.

    More Info

    • Introduction

      GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 is invloved in amino acid metabolism and the urea and tricarboxylic acid cycles. The 2 enzymes are homodimeric and demonstrate 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 MGSSSWWTHV EMGPPDPILG VTEAFKRDTN SKKMNLGVGA YRDDNGKPYV LPSVRKAEAQ IAAKNLDKEY LPIGGLAEFC KASAELALGE NSEVLKSGRF VTVQTISGTG ALRIGASFLQ RFFKFSRDVF LPKPTWGNHT PIFRDAGMQL QGYRYYDPKT CGFDFTGAVE DISKIPEQSV LLLHACAHNP TGVDPRPEQW KEIATVVKKR NLFAFFDMAY QGFASGDGDK DAWAVRHFIE QGINVCLCQS YAKNMGLYGE RVGAFTMVCK DADEAKRVES QLKILIRPMY SNPPLNGARI AAAILNTPDL RKQWLQEVKV MADRIIGMRT QLVSNLKKEG STHNWQHITD QIGMFCFTGL KPEQVERLIK EFSIYMTKDG RISVAGVTSS NVGYLAHAIH QVTK.

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    Got2 Human Active
  • View Data Sheet

    Name :

    MDH2 Mouse

    Description:

    Malate Dehydrogenase 2 Mouse Recombinant

    M-MDH, MDH, MOR1.

    Product # :

    ENZ-1068

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    Description

    MDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (25-338a.a.) and having a molecular mass of 35.4kDa. MDH2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MDH2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 800 units/mg, and is defined as the amount of enzyme that cleaves 1umole of oxaloacetate and beta-NADH to Lmalate and beta-NAD per minute at pH8.0 at 37°C.

    More Info

    • Introduction

      MDH2 catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. MDH2 is localized to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highy expressed in the adrenal system, small intestine, heart and pancreas.

    • Synonyms

      M-MDH, MDH, MOR1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAKVAVLGAS GGIGQPLSLL LKNSPLVSRL TLYDIAHTPG VAADLSHIET RANVKGYLGP EQLPDCLKGC DVVVIPAGVP RKPGMTRDDL FNTNATIVAT LTAACAQHCP EAMVCIIANP VNSTIPITAE VFKKHGVYNP NKIFGVTTLD IVRANTFVAE LKGLDPARVN VPVIGGHAGK TIIPLISQCT PKVDFPQDQL ATLTGRIQEA GTEVVKAKAG AGSATLSMAY AGARFVFSLV DAMNGKEGVV ECSFVQSKET ECTYFSTPLL LGKKGLEKNL GIGKITPFEE KMIAEAIPEL KASIKKGEDF VKNMK.

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    Mdh2 Mouse
  • View Data Sheet

    Name :

    ADK Mouse

    Description:

    Adenosine Kinase Mouse Recombinant

    AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase.

    Product # :

    PKA-105

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    Description

    ADK produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-361a.a.) and having a molecular mass of 42.5kDa.ADK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ADK protein solution (1mg/ml) contains 20% glycerol, 20mM Tris-HCl buffer (pH8.0), 1mM EDTA & 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100 pmol/min/ug and is defined as the amount of enzyme that convert 1.0 pmole of adenosine to AMP per minute at pH 7.5 at 37C in a couple system with PK and LDH. 

    More Info

    • Introduction

      Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.

    • Synonyms

      AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase.

    • 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 MGSMAAADEP KPKKLKVEAP QALSENVLFG MGNPLLDISA VVDKDFLDKY SLKPNDQILA EDKHKELFDE LVKKFKVEYH AGGSTQNSMK VAQWLIQEPH KAATFFGCIG IDKFGEILKR KAADAHVDAH YYEQNEQPTG TCAACITGGN RSLVANLAAA NCYKKEKHLD LERNWVLVEK ARVYYIAGFF LTVSPESVLK VARYAAENNR VFTLNLSAPF ISQFFKEALM DVMPYVDILF GNETEAATFA REQGFETKDI KEIAKKAQAL PKVNSKRQRT VIFTQGRDDT IVAAENDVTA FPVLDQNQEE IIDTNGAGDA FVGGFLSQLV SDKPLTECIR AGHYAASVII RRTGCTFPEK PDFH.

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    Adenosine Kinase Mouse
  • View Data Sheet

    Name :

    AMD1 Human

    Description:

    Adenosylmethionine Decarboxylase 1 Human Recombinant

    Adenosylmethionine decarboxylase 1, S-adenosylmethionine decarboxylase proenzyme, AdoMetDC, S-adenosylmethionine decarboxylase 1, SAMDC, AMD, EC 4.1.1.50.

    Product # :

    ENZ-624

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    Description

    AMD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (68-334) and having a molecular mass of 33.4 kDa.AMD1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The AMD1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adenosylmethionine decarboxylase proenzyme (AMD1) is synthesized originally as an inactive proenzyme. Putrescine stimulates both the proenzyme processing and the catalytic activity. The catalytic activity is inhibited by iodoacetic acid. The active enzyme formation entails a self-maturation process in which the active site pyruvoyl group is produced from an internal serine residue using an autocatalytic post-translational modification.

    • Synonyms

      Adenosylmethionine decarboxylase 1, S-adenosylmethionine decarboxylase proenzyme, AdoMetDC, S-adenosylmethionine decarboxylase 1, SAMDC, AMD, EC 4.1.1.50.

    • 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

      GSSHHHHHH SSGLVPRGSH MGSHMSSMFV SKRRFILKTC GTTLLLKALV PLLKLARDYS GFDSIQSFFY SRKNFMKPSH QGYPHRNFQE EIEFLNAIFP NGAAYCMGRM NSDCWYLYTL DFPESRVISQ PDQTLEILMS ELDPAVMDQF YMKDGVTAKD VTRESGIRDL IPGSVIDATM FNPCGYSMNG MKSDGTYWTI HITPEPEFSY VSFETNLSQT SYDDLIRKVV EVFKPGKFVT TLFVNQSSKC RTVLASPQKI EGFKRLDCQS AMFNDYNFVF TSFAKKQQQQ QS

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    Amd1 Human
  • View Data Sheet

    Name :

    ASNS Mouse

    Description:

    Asparagine Synthetase Mouse Recombinant

    Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase. 

    Product # :

    ENZ-1100

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    Description

    ASNS produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 567 amino acids (1-561a.a.) and having a molecular mass of 65.1 kDa.ASNS is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ASNS protein solution ( 0.25mg/ml ) contains PBS (pH 7.4) and 40% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.

    • Synonyms

      Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.

    • 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

      MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPDMRIPK NGIEKHLLRE TFEDCNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDEMMSA SQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK WINATDPSAR TLTHYKS AAK AHHHHHH.

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    Asns Mouse
  • View Data Sheet

    Name :

    BTD Human

    Description:

    Biotinidase Human Recombinant

    Biotinidase, EC 3.5.1.12, Biotinase, EC 3.5.1.

    Product # :

    ENZ-1004

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    Description

    BTD Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 510 amino acids (44-545a.a) and having a molecular mass of 57.8kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). BTD is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Biotinidase also known BTD, belongs to the nitrilase superfamily, which contains 12 families of nitrilases, amidases, carbamylases, and N-acyltrasferases. BTD catalyzes the hydrolysis of biocytin, the product of biotin-dependent carboxylase degradation, to biotin and lysine. BTD has a vital regulatory part in chromatin/DNA function. Mutations in BTD protein lead to Biotinidase deficiency.

    • Synonyms

      Biotinidase, EC 3.5.1.12, Biotinase, EC 3.5.1.

    • 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

      AHTGEESVAD HHEAEYYVAA VYEHPSILSL NPLALISRQE ALELMNQNLD IYEQQVMTAA QKDVQIIVFP EDGIHGFNFT RTSIYPFLDF MPSPQVVRWN PCLEPHRFND TEVLQRLSCM AIRGDMFLVA NLGTKEPCHS SDPRCPKDGR YQFNTNVVFS NNGTLVDRYR KHNLYFEAAF DVPLKVDLIT FDTPFAGRFG IFTCFDILFF DPAIRVLRDY KVKHVVYPTA WMNQLPLLAA IEIQKAFAVA FGINVLAANV HHPVLGMTGS GIHTPLESFW YHDMENPKSH LIIAQVAKNP VGLIGAENAT GETDPSHSKF LKILSGDPYC EKDAQEVHCD EATKWNVNAP PTFHSEMMYD NFTLVPVWGK EGYLHVCSNG LCCYLLYERP TLSKELYALG VFDGLHTVHG TYYIQVCALV RCGGLGFDTC GQEITEATGI FEFHLWGNFS TSYIFPLFLT SGMTLEVPDQ LGWENDHYFL RKSRLSSGLV TAALYGRLYE RDLEHHHHHH.

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    Btd Human
  • View Data Sheet

    Name :

    ACP6 Human

    Description:

    Acid Phosphatase-6 Human Recombinant

    Acid Phosphatase 6, Lysophosphatidic, Acid Phosphatase-Like Protein 1, PACPL1, ACPL1, LPAP, Lysophosphatidic Acid Phosphatase Type 6, Lysophosphatidic Acid Phosphatase 6, Acid Phosphatase Like 1, EC 3.1.3.2, Lysophosphatidic acid phosphatase type 6.

    Product # :

    ENZ-865

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    Description

    ACP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (33-428a.a) and having a molecular mass of 47.7kDa. ACP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACP6 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1000 units/mg, and is defined as the amount of enzyme which hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at PH 5.0 at 37C.

    More Info

    • Introduction

      Acid Phosphatase-6, also known as ACP6 is Hydrolyzes lysophosphatidic acid (LPA) which contains a medium length fatty acid chain to the corresponding monoacylglycerol. ACP6 shows highest activity with lysophosphatidic acid which contains myristate (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower activity with C18:0 as well as C6:0 lysophosphatidic acid.

    • Synonyms

      Acid Phosphatase 6, Lysophosphatidic, Acid Phosphatase-Like Protein 1, PACPL1, ACPL1, LPAP, Lysophosphatidic Acid Phosphatase Type 6, Lysophosphatidic Acid Phosphatase 6, Acid Phosphatase Like 1, EC 3.1.3.2, Lysophosphatidic acid phosphatase type 6.

    • 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 MGSELQEADG QCPVDRSLLK LKMVQVVFRH GARSPLKPLP LEEQVEWNPQ LLEVPPQTQF DYTVTNLAGG PKPYSPYDSQ YHETTLKGGM FAGQLTKVGM QQMFALGERL RKNYVEDIPF LSPTFNPQEV FIRSTNIFRN LESTRCLLAG LFQCQKEGPI IIHTDEADSE VLYPNYQSCW SLRQRTRGRR QTASLQPGIS EDLKKVKDRM GIDSSDKVDF FILLDNVAAE QAHNLPSCPM LKRFARMIEQ RAVDTSLYIL PKEDRESLQM AVGPFLHILE SNLLKAMDSA TAPDKIRKLY LYAAHDVTFI PLLMTLGIFD HKWPPFAVDL TMELYQHLES KEWFVQLYYH GKEQVPRGCP DGLCPLDMFL NAMSVYTLSP EKYHALCSQT QVMEVGNEE.

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    Acp6 Human
  • View Data Sheet

    Name :

    MDH2 Human

    Description:

    Malate Dehydrogenase 2 Human Recombinant

    M-MDH, MDH, MOR1.

    Product # :

    ENZ-247

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    Description

    MDH2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (25-338 a.a.) and having a molecular mass of 35.2 kDa. The MDH2 is fused to a 21 amino acid His tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The MDH2 1mg/ml protein solution contains 20mM Tris-HCl pH-7.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 30 units/mg, and is defined as the amount of enzyme that cleaves 1umole of oxalacetate and beta-NADH to L-malate and beta-NAD per minute at pH7.5 at 25°C.

    More Info

    • Introduction

      MDH2 catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. MDH2 is localized to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highy expressed in the adrenal system, small intestine, heart and pancreas.

    • Synonyms

      M-MDH, MDH, MOR1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAKVAVLGAS GGIGQPLSLL LKNSPLVSRL TLYDIAHTPG VAADLSHIET KAAVKGYLGP EQLPDCLKGC DVVVIPAGVP RKPGMTRDDL FNTNATIVAT LTAACAQHCP EAMICVIANP VNSTIPITAE VFKKHGVYNP NKIFGVTTLD IVRANTFVAE LKGLDPARVN VPVIGGHAGK TIIPLISQCT PKVDFPQDQL TALTGRIQEA GTEVVKAKAG AGSATLSMAY AGARFVFSLV DAMNGKEGVV ECSFVKSQET ECTYFSTPLL LGKKGIEKNL GIGKVSSFEE KMISDAIPEL KASIKKGEDF VKTLK.

    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.

    Mdh2 Human
  • View Data Sheet

    Name :

    C1GALT1 Human

    Description:

    Core 1 Beta3-Gal-T1 Human Recombinant

    Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 1.

    Product # :

    ENZ-721

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    Description

    C1GALT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (30-363 a.a) and having a molecular mass of 41.4kDa.C1GALT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    C1GALT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Core 1 Beta3-Gal-T1 also known as,C1GALT1 creates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for lots of extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice have shown that this gene takes a main role in angiogenesis, thrombopoiesis and kidney homeostasis.

    • Synonyms

      Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 1.

    • 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 MGSLLGEKVD TQPNVLHNDP HARHSDDNGQ NHLEGQMNFN ADSSQHKDEN TDIAENLYQK VRILCWVMTG PQNLEKKAKH VKATWAQRCN KVLFMSSEEN KDFPAVGLKT KEGRDQLYWK TIKAFQYVHE HYLEDADWFL KADDDTYVIL DNLRWLLSKY DPEEPIYFGR RFKPYVKQGY MSGGAGYVLS KEALKRFVDA FKTDKCTHSS SIEDLALGRC MEIMNVEAGD SRDTIGKETF HPFVPEHHLI KGYLPRTFWY WNYNYYPPVE GPGCCSDLAV SFHYVDSTTM YELEYLVYHL RPYGYLYRYQ PTLPERILKE ISQANKNEDT KVKLGNP.

    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.

    C1Galt1 Human
  • View Data Sheet

    Name :

    Staphylokinase

    Description:

    Staphylokinase Recombinant

    Staphylokinase, SakSTAR, Neutral proteinase, Protease III, SAK.

    Product # :

    ENZ-288

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    • sds-page

    Description

    Staphylokinase Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 136 amino acids and having a molecular weight of 16kDa.The Staphylokinase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The biological activity measured by the ability of fibrin lysis in agarose plate was found to be 50,000IU/mg.

    sds-page

    Staphylokinase sds-page - Product image 1

    More Info

    • Introduction

      Staphylokinase (SAK) is a 136-amino acidenzymefrom Staphylococcus aureus. It is positively regulated by the "agr" gene regulator. It activates plasminogen, which in turn can degrade various host proteins during infection.

    • Synonyms

      Staphylokinase, SakSTAR, Neutral proteinase, Protease III, SAK.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SAK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SAK 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 SAKin sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Staphylokinase
  • View Data Sheet

    Name :

    NT5C2 Human

    Description:

    5'-Nucleotidase Cytosolic II Human Recombinant

    Cytosolic purine 5'-nucleotidase, Cytosolic 5'-nucleotidase II, NT5C2, NT5B, NT5CP, PNT5, GMP, cN-II.

    Product # :

    ENZ-173

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    Description

    NT5C2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 581 amino acids (1-561 a.a.) and having a molecular mass of 67.1kDa.NT5C2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NT5C2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NT5C2 (NT5B/PNT5) has a vital role in the maintenance of purine/pyrimidine nucleotides. NT5C2 contains a phosphotransferase active site which catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. Furthermore, NT5C2 regulates the level of inosine monophosphate (IMP) and guanosine monophosphate (GMP) pools inside cells by way of hydrolysis.

    • Synonyms

      Cytosolic purine 5'-nucleotidase, Cytosolic 5'-nucleotidase II, NT5C2, NT5B, NT5CP, PNT5, GMP, cN-II.

    • 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 MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA PQEITHCHDE DDDEEEEEEE E.

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    Nt5C2 Human
  • View Data Sheet

    Name :

    COMT Human

    Description:

    Catechol-O-Methyltransferase Human Recombinant

    COMT, EC 2.1.1.6, Catechol O-methyltransferase.

    Product # :

    ENZ-400

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    Description

    COMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (51-271 a.a.) & having a molecular mass of 24.4 kDa. The COMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COMT protein in 20mM Tris-HCl buffer, pH-8, 1mM MgCl2 and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to catechol substrates such as the neurotransmitters. This O-methylation results in one of the main degradative pathways of the catecholamine transmitters. COMT COMT is located in the postsynaptic neuron and is involved in the metabolism of catechol estrogen drugs used in the treatment of hypertension, asthma, Parkinson disease and the inactivation of catecholamine neurotransmitters though enzymatic degradation. COMT appears in tissues in 2 forms, a soluble form and a membrane-bound form which differ in their N-termini. COMT inhibitors increase its availability and are used in the treatment of patients with Parkinson's disease.

    • Synonyms

      COMT, EC 2.1.1.6, Catechol O-methyltransferase.

    • 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

      MGDTKEQRIL NHVLQHAEPG NAQSVLEAID TYCEQKEWAM NVGDKKGKIV DAVIQEHQPS VLLELGAYCG YSAVRMARLL SPGARLITIE INPDCAAITQ RMVDFAGVKD KVTLVVGASQ DIIPQLKKKY DVDTLDMVFL DHWKDRYLPD TLLLEECGLL RKGTVLLADN VICPGAPDFL AHVRGSSCFE CTHYQSFLEY REVVDGLEKA IYKGPGSEAG P.

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    Comt Human
  • View Data Sheet

    Name :

    FUT3 Human

    Description:

    Fucosyltransferase 3 Human Recombinant

    Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.

    Product # :

    ENZ-745

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    Description

    FUT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (35-361 a.a) and having a molecular mass of 40.6kDa.FUT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FUT3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fucosyltransferase 3 (FUT3) catalyzes alpha-1, 3 and alpha-1, 4 glycosidic linkages which take part in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. FUT3 takes part in blood group Lewis determination; Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme. FUT3 also operates on the corresponding 1, 4-galactosyl derivative, creating1, 3-L-fucosyl links.

    • Synonyms

      Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.

    • 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 MGSRVSRDDA TGSPRAPSGS SRQDTTPTRP TLLILLWTWP FHIPVALSRC SEMVPGTADC HITADRKVYP QADTVIVHHW DIMSNPKSRL PPSPRPQGQR WIWFNLEPPP NCQHLEALDR YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH PPLNLSAKTE LVAWAVSNWK PDSARVRYYQ SLQAHLKVDV YGRSHKPLPK GTMMETLSRY KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD LARYLQELDK DHARYLSYFR WRETLRPRSF SWALDFCKAC WKLQQESRYQ TVRSIAAWFT.

    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.

    Fut3 Human
  • View Data Sheet

    Name :

    Ornithine Aminotransferase Human

    Description:

    Ornithine Aminotransferase Human Recombinant

    DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.

    Product # :

    ENZ-472

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    Description

    Ornithine Aminotransferase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (33-439 a.a.) and having a molecular wieght of 45.2kDa.The Ornithine Aminotransferase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Ornithine Aminotransferase protein solution contains 20mM Tris, pH-8, and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ornithine Aminotransferase is a mitochondrial enzyme which is an important factor that converts arginine and ornithine into the major excitatory and inhibitory neurotransmitters glutamate and GABA. Ornithine Aminotransferase mutations result in a deficiency that cause the autosomal recessive eye disease Gyrate Atrophy.

    • Synonyms

      DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.

    • 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

      MTVQGPPTSD DIFEREYKYG AHNYHPLPVA LERGKGIYLW DVEGRKYFDF LSSYSAVNQG HCHPKIVNAL KSQVDKLTLT SRAFYNNVLG EYEEYITKLF NYHKVLPMNT GVEAGETACK LARKWGYTVK GIQKYKAKIV AAGNFWGRT LSAISSSTDP TSYDGFGPFM PGFDIIPYND LPALERALQD PNVAAFMVEP IQGEAGVVVP DPGYLMGVRE LCTRHQVLFI ADEIQTGLAR TGRWLAVDYE NVRPDIVLLG KALSGGLYPV SAVLCDDDIM LTIKPGEHGS TYGGNPLGCR VAIAALEVLE EENLAENADK LGIILRNELM KLPSDVVTAV RGKGLLNAIV IKETKDWDAW KVCLRLRDNG LLAKPTHGDI IRFAPPLVIK EDELRESIEI INKTILSF.

    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.

    Ornithine Aminotransferase Human
  • View Data Sheet

    Name :

    ACP5 Human, His

    Description:

    Acid Phosphatase-5 Human Recombinant, His Tag

    Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, EC 3.1.3.2, TrATPase, SPENCDI, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TR-AP, TRAP, ACP5.

    Product # :

    ENZ-913

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    Description

    ACP5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (22-325 a.a) and having a molecular mass of 35.1kDa.ACP5 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACP5 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37C.

    More Info

    • Introduction

      Acid Phosphatase-5, also known as ACP5 is a member of the Purple acid phosphatase family. ACP5 is implicated in osteopontin as well as bone sialoprotein dephosphorylation. ACP5 expression appears to increase in certain pathological states for instance Gaucher & Hodgkin diseases, the hairy cell, the B-cell, as well as the T-cell leukemias.

    • Synonyms

      Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, EC 3.1.3.2, TrATPase, SPENCDI, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TR-AP, TRAP, ACP5.

    • 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

      ATPALRFVAV GDWGGVPNAP FHTAREMANA KEIARTVQIL GADFILSLGD NFYFTGVQDI NDKRFQETFE DVFSDRSLRK VPWYVLAGNH DHLGNVSAQI AYSKISKRWN FPSPFYRLHF KIPQTNVSVA IFMLDTVTLC GNSDDFLSQQ PERPRDVKLA RTQLSWLKKQ LAAAREDYVL VAGHYPVWSI AEHGPTHCLV KQLRPLLATY GVTAYLCGHD HNLQYLQDEN GVGYVLSGAG NFMDPSKRHQ RKVPNGYLRF HYGTEDSLGG FAYVEISSKE MTVTYIEASG KSLFKTRLPR RARPHHHHHH.

    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.

    Acp5 Human
  • View Data Sheet

    Name :

    PRTFDC1 Human

    Description:

    Phosphoribosyl Transferase Domain Containing 1 Human Recombinant

    Phosphoribosyltransferase domain-containing protein 1, PRTFDC1, HHGP.

    Product # :

    ENZ-142

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    Description

    PRTFDC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-225 a.a.) and having a molecular mass of 28.1kDa.PRTFDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRTFDC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoribosyltransferase domain-containing protein 1 (PRTFDC1) is a member of the purine/pyrimidine phosphoribosyltransferase family. PRTFDC1 has a low, barely measurable phosphoribosyltransferase activity (in vitro). PRTFDC1 can bind GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). PRTFDC1 is not expected to impact purine metabolism or GMP salvage.

    • Synonyms

      Phosphoribosyltransferase domain-containing protein 1, PRTFDC1, HHGP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      PRTFDC1 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 MGSMAGSSEE APDYGRGVVI MDDWPGYDLN LFTYPQHYYG DLEYVLIPHG IIVDRIERLA KDIMKDIGYS DIMVLCVLKG GYKFCADLVE HLKNISRNSD RFVSMKVDFI RLKSYRNDQS MGEMQIIGGD DLSTLAGKNV LIVEDVVGTG RTMKALLSNI EKYKPNMIKV ASLLVKRTSR SDGFRPDYAG FEIPNLFVVG YALDYNEYFR DLNHICVINE HGKEKYRV.

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    Prtfdc1 Human
  • View Data Sheet

    Name :

    PIN4 Human

    Description:

    Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 4 Human Recombinant

    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.

    Product # :

    ENZ-106

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    • More Info

    Description

    PIN4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (1-156 a.a.) and having a molecular mass of 18.8kDa.PIN4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PIN4 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-HCl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (PIN4) is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and is vital for cell cycle regulation. PIN4 has 2 different isoforms: PAR14 and PAR17. Furthermore, Pin4 protein binds to double-stranded DNA under physiological salt conditions.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.

    • 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 MPMAGLLKGL VRQLERFSVQ QQASKMPPKG KSGSGKAGKG GAASGSDSAD KKAQGPKGGG NAVKVRHILC EKHGKIMEAM EKLKSGMRFN EVAAQYSEDK ARQGGDLGWM TRGSMVGPFQ EAAFALPVSG MDKPVFTDPP VKTKFGYHII MVEGRK.

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    Pin4 Human
  • View Data Sheet

    Name :

    NQO1 Human, Active

    Description:

    NAD(P)H Dehydrogenase Quinone 1, Active 1 Human Recombinant

    NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    Product # :

    ENZ-1107

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    • description
    • source
    • formulation
    • purity
    • biological activity
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    Description

    NQO1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids ( 1-274aa ) and having a molecular mass of 33.0 kDa. NQO1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NQO1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 pmol/min/ug. One unit will convert 1 pmoles resazurin to resorufin per minute at pH 7.5 at 25°C.

    More Info

    • Introduction

      NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.

    • Synonyms

      NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    • 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 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES
      DLYAMNFNPI ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF
      QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG
      IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP
      LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK

    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.

    Nqo1 Enzyme
  • View Data Sheet

    Name :

    RNPA E.Coli

    Description:

    Ribonuclease P protein component E.Coli Recombinant

    ECK3696, Rnase P protein, RnaseP protein, b3704, JW3681, Ribonuclease P protein component, EC 3.1.26.5, Protein C5.

    Product # :

    ENZ-1169

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    • description
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    Description

    RNPA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (1-119a.a) and having a molecular mass of 13.7kDa.RNPA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNPA protein solution (0.25mg/ml) in Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Rnase P protein, AKA rnpA, is an important enzyme consisting of the C5 protein (which encoded by rnpA) and the catalytic M1 RNA (encoded by rnpB) subunits. rnpA is ribonucleoprotein that catalyzes the removal of the 50- leader elements of precursor tRNAs and generates the mature 50-end of tRNAs. This step is critical for theformation of functional tRNA molecules in bacteria, archaea and eukarya. More importantly, it has lately been established that RNase P is essential for the endonucleolytic separation of certain polycistronic tRNA transcripts such as valV valW, leuQ leuP leuV and secG leuU. Therefore, it was hypothesized that the essential function of RNase P might be related to the complete absence of a particular tRNAthat was dependent on the enzyme for initial separation from polycistronic transcripts.

    • Synonyms

      ECK3696, Rnase P protein, RnaseP protein, b3704, JW3681, Ribonuclease P protein component, EC 3.1.26.5, Protein C5.

    • 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

      MVKLAFPREL RLLTPSQFTF VFQQPQRAGT PQITILGRLN SLGHPRIGLT VAKKNVRRAH ERNRIKRLTR ESFRLRQHEL PAMDFVVVAK KGVADLDNRA LSEALEKLWR RHCRLARGS

    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.

    Rnpa Ribonuclease P 2
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