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Search results

1000 results found for “glycosylase”

Name

Description

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  • View Data Sheet

    Name :

    Carboxypeptidase B Rat

    Description:

    Carboxypeptidase-B Rat Recombinant

    Carboxypeptidase B, Cpb1, Cpb.

    Product # :

    ENZ-475

    Price :

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    Description

    Recombinant Rat Carboxypeptidase-B is expressed in E.Coli having a Mw of 31kDa is purified by standard chromatography techniques. Recombinant Rat Carboxypeptidase-B is free from foreign enzymes such as carboxypeptidase A & chymotrypsin. Recombinant Carboxypeptidase-B is free from protease inhibitors such as PMSF and EDTA.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 100mM NaCl, mannitol and 20mM Tris pH-7.5.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    170 units/mg protein.

    More Info

    • Introduction

      Carboxypeptidase B (EC 3.4.17.2) catalyzes hydrolysis of the basic amino acids lysine, arginine and ornithine from the C-terminal end of polypeptides. The Mw was found to be 34.5 kDa, optimun pH-7.9, and pI-6. Carboxypeptidase B is inhibited by arginine, lysine and ornithine. The enzyme is not inhibited by di-isopropylfluorophosphate (DFP), but it is inhibited by metal chelating agents, e.g., EDTA, 1,10-phenanthroline.

    • Synonyms

      Carboxypeptidase B, Cpb1, Cpb.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Store the lyophilized Carboxypeptidase-B at 4°C. Upon reconstitute the protein should be stored at 4°C for 2 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Rat Carboxypeptidase-B in sterile 18MΩ-cm H2O or 25mM Tris-HCl pH 7.65 not less than 100µg/ml , which can then be further diluted to other aqueous solutions.

    • Unit Definition

      One Unit hydrolyzes one micromole of hippuryl-L-arginine per minute at 25°C, pH-7.65.

    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.

    Carboxypeptidase B Rat
  • View Data Sheet

    Name :

    Dopa Decarboxylase Human

    Description:

    Dopa Decarboxylase Human Recombinant

    DDC, AADC, Aromatic-L-amino-acid decarboxylase, DOPA decarboxylase.

    Product # :

    ENZ-413

    Price :

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    Description

    Dopa decarboxylase human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 503 amino acids (1-480 a.a.) and having a molecular mass of 56.4 kDa. The Dopa decarboxylase is fused to a 23 amino acid His Tag at N-terminus and purified by conventional chromatpgraphy.

    Source

    Escherichia Coli.

    Formulation

    The Dopa decarboxylase protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dopa decarboxylase is a homodimeric, pyridoxal phosphate dependent enzyme.
      Dopa decarboxylase is involved in 2 metabolic pathways, synthesizing 2 significant neurotransmitters the take part in numerous clinical disorders, including Parkinson’s disease. Dopa decarboxylase is located in different areas of the brain and is mostly found in basal ganglia. Dopa decarboxylase catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopa, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. Defects in Dopa decarboxylase leads to aromatic L-amino-acid decarboxylase deficiency (AADCD). AADCD deficiency is an inborn error in neurotransmitter metabolism that causes combined serotonin and catecholamine deficiency.

    • Synonyms

      DDC, AADC, Aromatic-L-amino-acid decarboxylase, DOPA decarboxylase.

    • 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 TRSMNASEFR RRGKEMVDYV ANYMEGIEGR QVYPDVEPGY LRPLIPAAAP QEPDTFEDII NDVEKIIMPG VTHWHSPYFF AYFPTASSYP AMLADMLCGA IGCIGFSWAA SPACTELETV MMDWLGKMLE LPKAFLNEKA GEGGGVIQGS ASEATLVALL AARTKVIHRL QAASPELTQA AIMEKLVAYS SDQAHSSVER AGLIGGVKLK AIPSDGNFAM RASALQEALE RDKAAGLIPF FMVATLGTTT CCSFDNLLEV GPICNKEDIW LHVDAAYAGS AFICPEFRHL LNGVEFADSF NFNPHKWLLV NFDCSAMWVK KRTDLTGAFR LDPTYLKHSH QDSGLITDYR HWQIPLGRRF RSLKMWFVFR MYGVKGLQAY IRKHVQLSHE FESLVRQDPR FEICVEVILG LVCFRLKGSN KVNEALLQRI NSAKKIHLVP CHLRDKFVLR FAICSRTVES AHVQRAWEHI KELAADVLRA ERE.

    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.

    Dopa Decarboxylase Human
  • View Data Sheet

    Name :

    ART4 Human

    Description:

    ADP-Ribosyltransferase 4 Human Recombinant

    ARTC4, DOK1, CD297 Antigen, Dombrock Blood Group, ADP-Ribosyltransferase 4, Ecto-ADP-Ribosyltransferase 4.

    Product # :

    ENZ-1072

    Price :

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    Description

    ART4 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 248 amino acids (47-285 a.a.) and having a molecular mass of 28.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). ART4 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ART4 protein solution (0.25mg/ml) contains Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ecto-ADP-Ribosyltransferase 4 or ART4 is typed as a glycosylphosphatidylinositol (GPI)-linked membrane protein which carries Dombrock blood group antigens. The development of this protein takes place at the highest levels in the fetal liver. the process of the ART4 development is regulated while the erythroid differentiation process occurs. ART4 is a is part of the Ribosyltransferase family.

    • Synonyms

      ARTC4, DOK1, CD297 Antigen, Dombrock Blood Group, ADP-Ribosyltransferase 4, Ecto-ADP-Ribosyltransferase 4.

    • 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

      ADPSEVAIKI DFDFAPGSFD DQYQGCSKQV MEKLTQGDYF TKDIEAQKNY FRMWQKAHLA WLNQGKVLPQ NMTTTHAVAI LFYTLNSNVH SDFTRAMASV ARTPQQYERS FHFKYLHYYL TSAIQLLRKD SIMENGTLCY EVHYRTKDVH FNAYTGATIR FGQFLSTSLL KEEAQEFGNQ TLFTIFTCLG APVQYFSLKK EVLIPPYELF KVINMSYHPR GDWLQLRSTG NLSTYNCQLL KAHHHHHH.

    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.

    Art4 Human
  • View Data Sheet

    Name :

    ALKBH3 Human

    Description:

    ALKB Alkylation Repair Homolog 3 Human Recombinant

    Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3, Alkylated DNA repair protein alkB homolog 3, DEPC-1, Prostate cancer antigen 1, ALKBH3, ABH3, DEPC1, PCA1, FLJ43614, MGC118790, MGC118792, MGC118793.

    Product # :

    ENZ-101

    Price :

    Quantity :

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    Description

    ALKBH3 Human Recombinant fused to 39 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 325 amino acids (1-286 a.a.) and having a molecular mass of 37.9kDa. The ALKBH3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ALKBH3 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.

    More Info

    • Introduction

      ALKBH3 belongs to the ALKB family of proteins and acts as a dioxygenase with a preference for RNA and single stranded DNA substrates. ALKBH3 protein repairs 1-methyladenine and 3-methylcytosine lesions in alkylated DNA and RNA and its activity is stimulated by ascorbate. ALKBH3 is expressed in a broad array of tissues and localizes to the cytoplasm and the nucleus.

    • Synonyms

      Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3, Alkylated DNA repair protein alkB homolog 3, DEPC-1, Prostate cancer antigen 1, ALKBH3, ABH3, DEPC1, PCA1, FLJ43614, MGC118790, MGC118792, MGC118793.

    • 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 KDRWGSELDM EEKRRRARVQ GAWAAPVKSQ AIAQPATTAK SHLHQKPGQT WKNKEHHLSD REFVFKEPQQ VVRRAPEPRV IDREGVYEIS LSPTGVSRVC LYPGFVDVKE ADWILEQLCQ DVPWKQRTGI REDITYQQPR LTAWYGELPY TYSRITMEPN PHWHPVLRTL KNRIEENTGH TFNSLLCNLY RNEKDSVDWH SDDEPSLGRC PIIASLSFGA TRTFEMRKKP PPEENGDYTY VERVKIPLDH GTLLIMEGAT QADWQHRVPK EYHSREPRVN LTFRTVYPDP RGAPW.

    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.

    Alkbh3 Human
  • View Data Sheet

    Name :

    GSTM1 Mouse, His

    Description:

    Glutathione S-Transferase M1 Mouse Recombinant, His Tag

    GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.

    Product # :

    ENZ-456

    Price :

    Quantity :

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    Description

    GSTM1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 28.1kDa. The GTM1 is fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM1 solution contains 20 mM Tris-HCl buffer ( pH8.0), 1mM DTT and 10% glycerol

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is < 11 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

    More Info

    • Introduction

      Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

    • Synonyms

      GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 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 MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK.

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    Gstm1 Mouse His
  • View Data Sheet

    Name :

    GSTM2 Human

    Description:

    Glutathione S-Transferase MU 2 Human Recombinant

    Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    Product # :

    ENZ-003

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    Description

    GSTM2 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 238 amino acids (1-218 a.a.) and having a molecular mass of 27.9kDa. The GSTM2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol,
    0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is < 25 units/mg, and is defined as the amount of enzyme that conjugate 1.0 µmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.

    More Info

    • Introduction

      Glutathione S-transferase Mu 2 (GSTM2) belongs to the glutathione s-transferase (GST) family of proteins. GSTM2 is a glutathione S-transferase that belongs to the mu class. There are 8 families of GST proteins, specifically: alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have various functions throughout the cell. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are structured in a gene cluster on chromosome 1p13.3 and are proven to be highly polymorphic. These genetic variants can change an individual''s susceptibility to carcinogens and toxins as well as have an effect on the toxicity and efficacy of several drugs.

    • Synonyms

      Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    • 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 MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK.

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    Gstm2 Human
  • View Data Sheet

    Name :

    T4 DNA

    Description:

    T4 DNA Ligase Recombinant

    DNA ligase 4, EC 6.5.1.1, DNA ligase IV, Polydeoxyribonucleotide synthase [ATP] 4.

    Product # :

    ENZ-286

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    Description

    T4 DNA Ligase 55.3kDa protein catalyzes the formation of a phosphodiester bond between juxtaposed 5' -phosphate and 3' -hydroxyl termini in duplex DNA or RNA. This enzyme will join blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA, RNA or DNA/RNA hybrids.

    Source

    E.Coli, cloned gene-30, bacteriophage T4.

    Formulation

    50% glycerol, 20mM Tris-HCl (pH-7.5), 50mM KCl, 1mM DTT and 0.1mM EDTA.

    More Info

    • Synonyms

      DNA ligase 4, EC 6.5.1.1, DNA ligase IV, Polydeoxyribonucleotide synthase [ATP] 4.

    • Physical Appearance

      400U/ul solution.

    • Stability

      Store T4 DNA Ligase 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.

    • Applications

      Cloning of restriction enzyme generated DNA fragments.

      Cloning of PCR products.

      Joining of double-stranded oligonucleotide linkers or adaptors to DNA.

      Site-directed mutagenesis.

      Amplified fragment length polymorphism (AFLP).

      Ligase-mediated RNA detection.

      Nick repair in duplex DNA, RNA or DNA/RNA hybrids.

      Self-circularization of linear DNA

    • Reaction Conditions

      50mM Tris-HCl, pH7.5 at 25°C, 10mM MgCl2, 10mM DTT and 1mM ATP. Incubate at 16 °C

    • Inactivation

      T4 DNA Ligase can be inhibited by NaCl/KCl at a concentrations >than 200mM or by heating at 65 °C for 10 min or at 70 °C for 5 min.

    • Unit Definition

      1U is the amount of T4 DNA Ligase required to ligate > than 50% DNA fragments in a 20μl ligation reaction system, 6μg of λDNA-Hind III decomposition product reacts at 16°C for 30 minutes.

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    T4 Dna Ligase
  • View Data Sheet

    Name :

    NMNAT1 Human, Active

    Description:

    Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant , Active

    NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.

    Product # :

    ENZ-1002

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    Description

    NMNAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-279 a.a.) and having a molecular mass of 36 kDa. The NMNAT1 is fused to a 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NMNAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 7,000 pmol/min/ug, and was obtained by measuring the beta-NAD from nicotinamide mononucleotide and ATP per minute at pH 8.0 at 37C.

    More Info

    • Introduction

      NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

    • Synonyms

      NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.

    • 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 KDRWGSMENS EKTEVVLLAC GSFNPITNMH LRLFELAKDY MNGTGRYTVV KGIISPVGDA YKKKGLIPAY HRVIMAELAT KNSKWVEVDT WESLQKEWKE TLKVLRHHQE KLEASDCDHQ QNSPTLERPG RKRKWTETQD SSQKKSLEPK TKAVPKVKLL CGADLLESFA VPNLWKSEDI TQIVANYGLI CVTRAGNDAQ KFIYESDVLW KHRSNIHVVN EWIANDISST KIRRALRRGQSIRYLVPDLV QEYIEKHNLY SSESEDRNAG VILAPLQRNT AEAKT.

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    Nmnat1 Human Active
  • View Data Sheet

    Name :

    NANS Human

    Description:

    N-acetylneuraminic acid synthase Human Recombinant

    Sialic acid synthase, N-acetylneuraminate synthase, N-acetylneuraminate-9-phosphate synthase, N-acetylneuraminic acid phosphate synthase, N-acetylneuraminic acid synthase, NANS, SAS.

    Product # :

    ENZ-024

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    Description

    NANS 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 379 amino acids (1-359 a.a.) and having a molecular mass of 42.4kDa. The NANS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NANS solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NANS is a 359 amino acid protein that contains one AFP (antifreeze proteins)-like domain and functions in the biosynthesis of sialic acids. The ubiquitously expressed NANS enzymatically catalyzes the H2O-dependent formation of N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), both of which are sialic acids. NANS uses N-acetylmannosamine 6-phosphate as a substrate for Neu5Ac synthesis and mannose 6-phosphate as a substrate for KDN synthesis.

    • Synonyms

      Sialic acid synthase, N-acetylneuraminate synthase, N-acetylneuraminate-9-phosphate synthase, N-acetylneuraminic acid phosphate synthase, N-acetylneuraminic acid synthase, NANS, SAS.

    • 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 MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC AKFQKSELEF KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR YAEEVGIFFT ASGMDEMAVE FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC FLQCTSAYPL QPEDVNLRVI SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT LDKTWKGSDH SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV DNHGKKIKS.

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    Nans Human
  • View Data Sheet

    Name :

    SRM Human

    Description:

    Spermidine Synthase Human Recombinant

    Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.

    Product # :

    ENZ-027

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    Description

    SRM 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 322 amino acids (1-302 a.a.) and having a molecular mass of 36kDa. The SRM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SRM solution (1 mg/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.

    More Info

    • Introduction

      SRM is an enzyme which catalyzes the transfer of the propylamine group from S-adenosylmethioninamine to putrescine in the biosynthesis of spermidine. The polyamines putrescine, spermine and spermidine are ubiquitous polycationic mediators of cell growth and differentiation. The SRM protein is one of four enzymes in the polyamine-biosynthetic pathway and completes the final step of spermidine biosynthesis.

    • Synonyms

      Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.

    • 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 MEPGPDGPAA SGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV VQCEIDEDVI QVSKKFLPGM AIGYSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP AESLFKESYY QLMKTALKED GVLCCQGECQ WLHLDLIKEM RQFCQSLFPV VAYAYCTIPT YPSGQIGFML CSKNPSTNFQ EPVQPLTQQQ VAQMQLKYYN SDVHRAAFVL PEFARKALND VS.

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    Srm Human
  • View Data Sheet

    Name :

    TALDO1 Human

    Description:

    Transaldolase Human Recombinant

    TAL, TAL-H, TALDOR, TALH, TALDO1.

    Product # :

    ENZ-255

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    Description

    TALDO1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids (1-337) and having a molecular mass of 39.7 kDa. TALDO1 is fused to 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TALDO1 1mg/ml protein solution contains 20 mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TALDO1 is a important enzyme of the non-oxidative pentose phosphate pathway supplying ribose-5-phosphate for nucleic acid synthesis and NADPH for lipid biosynthesis. TALDO1 delivers a dihydroxyacetone group from donor compounds (fructose 6-phosphate or sedoheptulose 7-phosphate) to aldehyde acceptor compounds. TALDO1 is expressed at selectively great levels in oligodendrocytes of the brain. TALDO1 Deficiency results in accumulation of erythritol, D-arabitol, and ribitol.

    • Synonyms

      TAL, TAL-H, TALDOR, TALH, TALDO1.

    • 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 MSSSPVKRQR MESALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL AAAQMPAYQE LVEEAIAYGR KLGGSQEDQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA RARRLIELYK EAGISKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE AGVTLISPFV GRILDWHVAN TDKKSYEPLE DPGVKSVTKI YNYYKKFSYK TIVMGASFRN TGEIKALAGC DFLTISPKLL GELLQDNAKL VPVLSAKAAQ ASDLEKIHLD EKSFRWLHNE DQMAVEKLSD GIRKFAADAV KLERMLTERM FNAENGK.

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    Taldo1 Human
  • View Data Sheet

    Name :

    MMLV RT

    Description:

    Moloney Murine Leukemia Virus Reverse Trancscriptase Recombinant

    Product # :

    ENZ-310

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    Description

    MMLV (Moloney Murine Leukemia Virus) Reverse Transcriptase is a DNA polymerase that synthesizes a complementary DNA strands from single-stranded RNA, DNA, or an RNA-DNA hybrid as a template. This recombinant enzyme was purified from E.coli, which carried a modified MMLV-RT gene. Compared to AMV Reverse Transcriptase, this enzyme has a much weaker 5' - 3' ribonuclease H activity, which allows the syntesis of longer cDNAs (>7kb).

    Source

    Recombinant E. coli strain.

    Formulation

    50mM Tris-HCl, 0.1M NaCl, 0.1% Triton X-100, 2mM DTT, 0.1mM EDTA and 50% glycerol.

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    • Physical Appearance

      Sterile Filtered clear solution (200 U/µl).

    • Stability

      Stable for 5 days at 10°C, for longer period of time store at -20°C. Please prevent freeze-thaw cycles.

    • Unit Definition

      One unit is defined as the amount of enzyme required to catalyze the incorporation of 1nmol of deoxyribonucleotide into acid-insoluble forms in 10 minutes at 37oC, using poly(A)-oligo(dT)12-18 as the template-primer. Standard cDNA Synthesis Conditions50mM Tris-HCl (pH8.3), 75mM KCl, 3mM MgCl2, 10mM DTT, 1.0mM each dATP, dGTP, dCTP, and dTTP, 0.2 mg radom hexamer,1-5mg RNA, 200units M-MLV RT. The reaction volume was 20ml and the incubation was 45 min at 42oC.

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    M Mlv Reverse Transcriptase
  • View Data Sheet

    Name :

    IDI2 Human

    Description:

    Isopentenyl-Diphosphate Delta Isomerase 2 Human Recombinant

    Isopentenyl-diphosphate Delta-isomerase 2, Isopentenyl pyrophosphate isomerase 2, IPP isomerase 2, IPPI2, IDI2.

    Product # :

    ENZ-107

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    Description

    IDI2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (1-227 a.a.) and having a molecular mass of 28.9kDa.IDI2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IDI2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Isopentenyl-diphosphate Delta-isomerase 2 (IDI2) is a member of the IPP isomerase type 1 family. IDI2 catalyzes the 1,3-allylic reorganization of the homoallylic substrate isopentenyl (IPP) to its extremely electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).

    • Synonyms

      Isopentenyl-diphosphate Delta-isomerase 2, Isopentenyl pyrophosphate isomerase 2, IPP isomerase 2, IPPI2, IDI2.

    • 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 MSDINLDWVD RRQLQRLEEM LIVVDENDKV IGADTKRNCH LNENIEKGLL HRAFSVVLFN TKNRILIQQR SDTKVTFPGY FTDSCSSHPL YNPAELEEKD AIGVRRAAQR RLQAELGIPG EQISPEDIVF MTIYHHKAKS DRIWGEHEIC YLLLVRKNVT LNPDPSETKS ILYLSQEELW ELLEREARGE VKVTPWLRTI AERFLYRWWP HLDDVTPFVE LHKIHRV.

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    Idi2 Human
  • View Data Sheet

    Name :

    MMP 1 Human

    Description:

    Matrix Metalloproteinase-1 Human Recombinant

    CLG, CLGN, Matrix metalloproteinase-1, MMP-1.

    Product # :

    ENZ-765

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    Description

    MMP 1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (100-469a.a) and having a molecular mass of 45kDa. MMP 1 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMP-1 can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

    • Synonyms

      CLG, CLGN, Matrix metalloproteinase-1, MMP-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 MGSFVLTEGN PRWEQTHLTY RIENYTPDLP RADVDHAIEK AFQLWSNVTP LTFTKVSEGQ ADIMISFVRG DHRDNSPFDG PGGNLAHAFQ PGPGIGGDAH FDEDERWTNN FREYNLHRVA AHELGHSLGL SHSTDIGALM YPSYTFSGDV QLAQDDIDGI QAIYGRSQNP VQPIGPQTPK ACDSKLTFDA ITTIRGEVMF FKDRFYMRTN PFYPEVELNF ISVFWPQLPN GLEAAYEFAD RDEVRFFKGN KYWAVQGQNV LHGYPKDIYS SFGFPRTVKH IDAALSEENT GKTYFFVANK YWRYDEYKRS MDPGYPKMIA HDFPGIGHKV DAVFMKDGFF YFFHGTRQYK FDPKTKRILT LQKANSWFNC RKN.

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    Mmp 1 Enzyme
  • View Data Sheet

    Name :

    NMNAT1 Mouse

    Description:

    Nicotinamide Nucleotide Adenylyltransferase 1 Mouse Recombinant

    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.

    Product # :

    ENZ-1049

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    Description

    NMNAT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285 a.a) and having a molecular mass of 34.7kDa. NMNAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMNAT1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

    • Synonyms

      Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.

    • Physical Appearance

      Sterile filtered colourless 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 MGSMDSSKKT EVVLLACGSF NPITNMHLRL FELAKDYMHA TGKYSVIKGI ISPVGDAYKK KGLIPAHHRI IMAELATKNS HWVEVDTWES LQKEWVETVK VLRYHQEKLA TGSCSYPQSS PALEKPGRKR KWADQKQDSS PQKPQEPKPT GVPKVKLLCG ITNDISSTKI RRALRRGQSI RYLVPDLVQE YIEKHELYNT ESEGRNAGVT LAPLQRNAAE AKHNHSTL.

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    Nmnat1 Mouse
  • View Data Sheet

    Name :

    NAGK Human

    Description:

    N-Acetylglucosamine Kinase Human Recombinant

    N-acetylglucosamine kinase, GNK, GlcNAc kinase, N-acetyl-D-glucosamine kinase, HSA242910, EC 2.7.1.59.

    Product # :

    PKA-027

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    Description

    NAGK Human Recombinant produced in E. coli is a single polypeptide chain containing 367 amino acids (1-344) and having a molecular mass of 39.8kDa.NAGK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NAGK solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAGK is a member of the eukaryotic-type N-acetylglucosamine kinase family. NAGK converts endogenous N-acetylglucosamine (GlcNAc), a key component of complex carbohydrates, from lysosomal degradation or alimentary sources into GlcNAc 6-phosphate. NAGK is a prominent salvage enzyme of amino sugar metabolism in mammals. NAGK cooperates with STK16 and LNX1 and has ManNAc kinase activity.

    • Synonyms

      N-acetylglucosamine kinase, GNK, GlcNAc kinase, N-acetyl-D-glucosamine kinase, HSA242910, EC 2.7.1.59.

    • 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 MGSMAAIYGG VEGGGTRSEV LLVSEDGKIL AEADGLSTNH WLIGTDKCVE RINEMVNRAK RKAGVDPLVP LRSLGLSLSG GDQEDAGRIL IEELRDRFPY LSESYLITTD AAGSIATATP DGGVVLISGT GSNCRLINPD GSESGCGGWG HMMGDEGSAY WIAHQAVKIV FDSIDNLEAA PHDIGYVKQA MFHYFQVPDR LGILTHLYRD FDKCRFAGFC RKIAEGAQQG DPLSRYIFRK AGEMLGRHIV AVLPEIDPVL FQGKIGLPIL CVGSVWKSWE LLKEGFLLAL TQGREIQAQN FFSSFTLMKL RHSSALGGAS LGARHIGHLL PMDYSANAIA FYSYTFS

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    Nagk Human
  • View Data Sheet

    Name :

    GST, His

    Description:

    Glutathione S-Transferase Recombinant, His Tag

    Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    Product # :

    ENZ-451

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    Description

    Recombinant Schistosoma japonicum GST full length protein contains a total of 244 amino acids (1-218 a.a.) expressed in E.coli, having a molecular mass of 28.3kDa. The GST protein is fused to a 20 amino acids His-Tag at N-terminus. The GST protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GST is supplied in PBS pH 7.4 & 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    >10 units/mg, & is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH-6.5 at 25C.

    More Info

    • Introduction

      Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
      The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions.

    • Synonyms

      Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    • 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 MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMAIIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALDVVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.

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    Glutathione S Transferase His
  • View Data Sheet

    Name :

    GSTM5 Human

    Description:

    Glutathione S-Transferase MU 5 Human Recombinant

    Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.

    Product # :

    ENZ-623

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    Description

    GSTM5 Human Recombinant produced in E. coli is a single polypeptide chain containing 242 amino acids (1-218) and having a molecular mass of 28.2 kDa.GSTM5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GSTM5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      Glutathione S-transferase mu 5 (GSTM5) belongs to the glutathione s-transferase (GST) family of proteins. There are 8 families of GST proteins, specifically alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is comprised of proteins which have various functions throughout the cell. GSTM5 belongs to the mu class of enzymes which function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. GSTM5 has an imperative role in detoxification. GSTM5 conjugates reduced glutathione to a large number of exogenous and endogenous hydrophobic electrophiles.

    • Synonyms

      Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.

    • 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 MGSHMPMTLG YWDIRGLAHA IRLLLEYTDS SYVEKKYTLG DAPDYDRSQW LNEKFKLGLD FPNLPYLIDG AHKITQSNAI LRYIARKHNL CGETEEEKIR VDILENQVMD NHMELVRLCY DPDFEKLKPK YLEELPEKLK LYSEFLGKRP WFAGDKITFV DFLAYDVLDM KRIFEPKCLD AFLNLKDFIS RFEGLKKISA YMKSSQFLRG LLFGKSATWN SK

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    Gstm5 Human
  • View Data Sheet

    Name :

    MMP28 Human

    Description:

    Matrix Metalloproteinase-28 Human Recombinant

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

    Product # :

    ENZ-768

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    Description

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

    Source

    Escherichia Coli.

    Formulation

    The MMP28 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      MMP28, which belongs to the matrix metalloproteinase (MMP) family, takes part in the breakdown of extracellular matrix for both normal physiological processes, such as embryonic development, reproduction and tissue remodeling, and disease processes, like asthma and metastasis. MMP28 is a secreted enzyme which degrades casein. MMP28 participates in tissue homeostasis and in wound repair.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSFAKQGNK WYKQHLSYRL VNWPEHLPEP AVRGAVRAAF QLWSNVSALE FWEAPATGPA DIRLTFFQGD HNDGLGNAFD GPGGALAHAF LPRRGEAHFD QDERWSLSRR RGRNLFVVLA HEIGHTLGLT HSPAPRALMA PYYKRLGRDA LLSWDDVLAV QSLYGKPLGG SVAVQLPGKL FTDFETWDSY SPQGRRPETQ GPKYCHSSFD AITVDRQQQL YIFKGSHFWE VAADGNVSEP RPLQERWVGL PPNIEAAAVS LNDGDFYFFK GGRCWRFRGP KPVWGLPQLC RAGGLPRHPD AALFFPPLRR LILFKGARYY VLARGGLQVE PYYPRSLQDW GGIPEEVSGA LPRPDGSIIF FRDDRYWRLD QAKLQATTSG RWATELPWMG CWHANSGSAL F.

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    Mmp28 Human
  • View Data Sheet

    Name :

    GZMK Human, Sf9

    Description:

    Granzyme-K, Human Recombinant, sf9

    GZMK, TRYP2, Granzyme-K, Granzyme K, Fragmentin-3, Granzyme-3, NK-tryptase-2, NK-Tryp-2.

    Product # :

    ENZ-1031

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    Description

    GZMK Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 247 amino acids (27-264) and having a molecular mass of 26.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GZMK is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GZMK protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

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    • Introduction

      GZMK is a part of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes and natural killer cells have the outstanding ability to bind, recognize and lyse specific target cells. They defend their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens.

    • Synonyms

      GZMK, TRYP2, Granzyme-K, Granzyme K, Fragmentin-3, Granzyme-3, NK-tryptase-2, NK-Tryp-2.

    • 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

      ADPIIGGKEV SPHSRPFMAS IQYGGHHVCG GVLIDPQWVL TAAHCQYRFT KGQSPTVVLG AHSLSKNEAS KQTLEIKKFI PFSRVTSDPQ SNDIMLVKLQ TAAKLNKHVK MLHIRSKTSL RSGTKCKVTG WGATDPDSLR PSDTLREVTV TVLSRKLCNS QSYYNGDPFI TKDMVCAGDA KGQKDSCKGD SGGPLICKGV FHAIVSGGHE CGVATKPGIY TLLTKKYQTW IKSNLVPPHT NHHHHHH.

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    Gzmk Sf9
  • View Data Sheet

    Name :

    TOP1 Bovine

    Description:

    DNA Topoisomerase-I Bovine

    DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.

    Product # :

    ENZ-656

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    Description

    Bovine DNA Topoisomerase-I shows multiple bands between 76-109 KDa and is purified from bovine tissues by proprietary chromatographic techniques.

    Source

    Bovine tissues.

    Formulation

    TOP1 is supplied in 20mM HEPES buffer pH-7.5, 400mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      TOP1 is an important nuclear enzyme that interconverts supercoiled DNA to the necessary topological conformations for standard DNA replication and transcription. TOP1 is the target antigen for TOP1 autoantibodies. TOP1 antibodies are a specific marker in scleroderma patients (specificity 98-100%) and are related with the existence of diffuse skin involvement and pulmonary fibrosis. In human tissues top1 enzyme is primarily synthesized as a protein with a molecular weight of 100-kDa. Most of this precursor is then proteolytically processed to a 70-kDa size, from which the TOP1 antigen has derived its name.

    • Synonyms

      DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative samples) and immunodot test with positive/negative samples.

    • coating concentration

      0.5-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.

    • Applications

      Western blot with anti TOP1 autoantibody positive sample.

    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.

    Top1 Bovine
  • View Data Sheet

    Name :

    NDUFV2 Human

    Description:

    NADH Dehydrogenase Flavoprotein 2 Human Recombinant

    CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    Product # :

    ENZ-743

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    Description

    NDUFV2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (33-249 a.a) and having a molecular mass of 26.1kDa.NDUFV2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NDUFV2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NADH Dehydrogenase Flavoprotein 2 (NDUFV2) is a 24 kDa Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysisthe. NDUFV2 is aslo involved in electron transfer. Mutations in NDUFV2 are implicated in Parkinson's disease, bipolar disorder, schizophrenia, and have been discovered in one case of early onset hypertrophic cardiomyopathy and encephalopathy.

    • Synonyms

      CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    • 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 MGSGAGGALF VHRDTPENNP DTPFDFTPEN YKRIEAIVKN YPEGHKAAAV LPVLDLAQRQ NGWLPISAMN KVAEVLQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK VGETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTAK DIEEIIDELK AGKIPKPGPR SGRFSCEPAG GLTSLTEPPK GPGFGVQAGL.

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    Ndufv2 Human
  • View Data Sheet

    Name :

    G6PD E.Coli

    Description:

    Glucose-6-Phosphate Dehydrogenase E.coli Recombinant

    G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    Product # :

    ENZ-399

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    Description

    G6PD E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 491 amino acids and having a molecular mass of 55.7kDa. The G6PD is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The G6PD protein contains 50mM MES 6.0, 0.1mM PMSF, 2mM EDTA, 0.5mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 70 units/mg obtained by measuring  the increase of beta-NADPH in absorbance at 340 nm resulting from the reduction beta- NADP. One unit oxidizes 1.0 umole D-glucose-6-phosphate to 6-phospho-D-gluconate per min in the presence of beta-NADP at pH 7.4 at 25C.

    More Info

    • Introduction

      G6PD is the rate-limiting enzyme of the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells by maintaining the level of NADPH. G6PD converts glucose-6-phosphate into 6-phosphoglucono-?-lactone and at the same time produces NADPH. The NADPH maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. G6PD deficiency causes acute hemolytic anemia, neonatal jaundice or acute hemolysis. G6PD is a cytosolic enzyme encoded by an X-linked gene whose main function is to produce NADPH, a crucial electron donor in the defense against oxidizing agents and in reductive biosynthetic reactions. G6PD produces pentose sugars for nucleic acid synthesis and is a main producer of NADPH reducing power.

    • Synonyms

      G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    • 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

      MAVTQTAQAC DLVIFGAKGD LARRKLLPSL YQLEKAGQLN PDTRIIGVGR ADWDKAAYTK VVREALETFM KETIDEGLWD TLSARLDFCN LDVNDTAAFS RLGAMLDQKN RITINYFAMP PSTFGAICKG LGEAKLNAKP ARVVMEKPLG TSLATSQEIN DQVGEYFEEC QVYRIDHYLG KETVLNLLAL RFANSLFVNN WDNRTIDHVE ITVAEEVGIE GRWGYFDKAG QMRDMIQNHL LQILCMIAMS PPSDLSADSI RDEKVKVLKS LRRIDRSNVR EKTVRGQYTA GFAQGKKVPG YLEEEGANKS SNTETFVAIR VDIDNWRWAG VPFYLRTGKR LPTKCSEVVV YFKTPELNLF KESWQDLPQN KLTIRLQPDE GVDIQVLNKV PGLDHKHNLQ ITKLDLSYSE TFNQTHLADA YERLLLETMR GIQALFVRRD EVEEAWKWVDSITEAWAMDN DAPKPYQAGT WGPVASVAMI TRDGRSWNEF E.

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    G6Pd
  • View Data Sheet

    Name :

    GSTO2 Human

    Description:

    Glutathione S-Transferase Omega 2 Human Recombinant

    Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.

    Product # :

    ENZ-605

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    Description

    GSTO2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (1-243) and having a molecular mass of 30.6kDa.GSTO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 40% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutathione S-transferase omega 2 (GSTO2) is a member of the GST superfamily. GSTO2 is involved in catalyzing the reaction of glutathione with a broad range of organic compounds to form thioethers, a process which is vital for the metabolism and detoxification of a variety of xenobiotics and carcinogens. GSTO2 displays glutathione-dependent thiol transferase activity. GSTO2 has a high dehydroascorbate reductase activity and may be a factor in the recycling of ascorbic acid. GSTO2 also participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). GSTO2 is expressed in an array of tissues, including the liver, kidney, skeletal muscle and prostate, while the strongest expression is seen in the testis.

    • Synonyms

      Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.

    • 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 MGSMSGDATR TLGKGSQPPG PVPEGLIRIY SMRFCPYSHR TRLVLKAKDI RHEVVNINLR NKPEWYYTKH PFGHIPVLET SQCQLIYESV IACEYLDDAY PGRKLFPYDP YERARQKMLL ELFCKVPHLT KECLVALRCG RECTNLKAAL RQEFSNLEEI
      LEYQNTTFFG GTCISMIDYL LWPWFERLDV YGILDCVSHT PALRLWISAM KWDPTVCALL MDKSIFQGFL NLYFQNNPNA FDFGLC.

    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.

    Gsto2 Human
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