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Search results

1000 results found for “decarboxylase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    UFC1 Human

    Description:

    Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant

    Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.

    Product # :

    ENZ-138

    Price :

    Quantity :

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    Description

    UFC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.6kDa.UFC1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UFC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      UFC1 is a member of the ubiquitin-conjugating enzyme family. UFC1 is an E2-like conjugating enzyme for ubiquitin-fold modifier-1. UFM1 is activated by UBA5 (a novel E1-like enzyme) by forming a high-energy thioester bond. Activated UFM1 is subsequently transferred to its cognate E2-like enzyme, UFC1, in a similar thioester linkage.

    • Synonyms

      Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      UFC1 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 MADEATRRVV SEIPVLKTNA GPRDRELWVQ RLKEEYQSLI RYVENNKNAD NDWFRLESNK EGTRWFGKCW YIHDLLKYEF DIEFDIPITY PTTAPEIAVP ELDGKTAKMY RGGKICLTDH FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLIQKGVIQ HKEKCNQ.

    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.

    Ufc1 Human
  • View Data Sheet

    Name :

    HRP

    Description:

    Horseradish Peroxidase

    Horseradish Peroxidase, HRP, EC 1.11.1.7.

    Product # :

    ENZ-321

    Price :

    Quantity :

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    • description
    • source
    • purity
    • biological activity
    • More Info

    Description

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

    Source

    Root extracts of horseradish.

    Purity

    (A403/A275) = RZ: 3.0.

    Biological Activity

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

    More Info

    • Introduction

      The enzyme horseradish peroxidase, found in horseradish, is used extensively in molecular biologyand in antibody amplification and detection, among other things. For example, "In recent years the technique of marking neurons with the enzyme horseradish peroxidase (HRP) has become a major tool. In its brief history, this method has probably been used by more neurobiologists than have used the Golgi stainsince its discovery in 1870." Horseradish peroxidase is also highly used in techniques such as Western blottingand ELISAs.
      HRP is widely used as an enzymatic label in immunoassays. Usually, the enzyme is coupled to antibodies, lectins or haptens. Coupling to antibodies etc. may be performed through the carbohydrate side chains of the HRP.

    • Synonyms

      Horseradish Peroxidase, HRP, EC 1.11.1.7.

    • Physical Appearance

      Sterile Filtered red-brown lyophilized powder.

    • Stability

      Lyophilized HRP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HRP should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized HRP in sterile 18MΩ-cm H2O not less than 100 µg/ml.

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

    Horseradish Peroxidase
  • View Data Sheet

    Name :

    PRPS2 Human

    Description:

    Phosphoribosyl Pyrophosphate Synthetase 2 Human Recombinant

    Phosphoribosyl Pyrophosphate Synthetase 2, Phosphoribosyl Pyrophosphate Synthase II, Ribose-Phosphate Diphosphokinase 2, EC 2.7.6.1, PRS-II, Ribose-Phosphate Pyrophosphokinase 2, PPRibP Synthetase , PRS II, PPRibP, PRSII, Ribose-phosphate pyrophosphokinase 2.

    Product # :

    PKA-009

    Price :

    Quantity :

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    • description
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    Description

    PRPS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a) and having a molecular mass of 37.4kDa. PRPS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    PRPS2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoribosyl Pyrophosphate Synthetase 2, also known as PRPS2 is a member of the ribose-phosphate pyrophosphokinase family. PRPS2 catalyzes the synthesis of 5-phosphoribosyl 1-pyrophosphate from ATP and D-ribose 5-phosphate.

    • Synonyms

      Phosphoribosyl Pyrophosphate Synthetase 2, Phosphoribosyl Pyrophosphate Synthase II, Ribose-Phosphate Diphosphokinase 2, EC 2.7.6.1, PRS-II, Ribose-Phosphate Pyrophosphokinase 2, PPRibP Synthetase , PRS II, PPRibP, PRSII, Ribose-phosphate pyrophosphokinase 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 MGSMPNIVLF SGSSHQDLSQ RVADRLGLEL GKVVTKKFSN QETSVEIGES VRGEDVYIIQ SGCGEINDNL MELLIMINAC KIASSSRVTA VIPCFPYARQ DKKDKVGESR APISAKLVAN MLSVAGADHI ITMDLHASQI QGFFDIPVDN LYAEPAVLQW IRENIAEWKN CIIVSPDAGG AKRVTSIADR LNVEFALIHK ERKKANEVDR MVLVGDVKDR VAILVDDMAD TCGTICHAAD KLLSAGATKV YAILTHGIFS GPAISRINNA AFEAVVVTNT IPQEDKMKHC TKIQVIDISM ILAEAIRRTH NGESVSYLFS HVPL.

    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.

    Prps2 Human
  • View Data Sheet

    Name :

    ADI1 Human

    Description:

    Acireductone Dioxygenase 1 Human Recombinant

    APL1, ARD, FLJ10913, HMFT1638, MTCBP-1, SIPL, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, Acireductone dioxygenase, Fe-ARD, Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1, Submergence-induced protein-like factor.

    Product # :

    ENZ-700

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    • More Info

    Description

    ADI1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-179 a.a.) and having a molecular mass of 25.6kDa. ADI1 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ADI1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acireductone dioxygenase 1 (ADI1) is a part of the acireductone dioxygenase family of metal-binding enzymes, which are involved in methionine salvage. ADI1 regulates mRNA processing in the nucleus, and carries out different functions depending on its localization. Related pseudogenes have been defined on chromosomes 8 and 20. ADI1 down-regulates cell migration arbitrated by MMP14.

    • Synonyms

      APL1, ARD, FLJ10913, HMFT1638, MTCBP-1, SIPL, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, Acireductone dioxygenase, Fe-ARD, Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1, Submergence-induced protein-like factor.

    • 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 KDRWGSSMVL AWYMDDAPGD PRQPHRPDPG RPVGLEQLRR LGVLYWKLDA DKYENDPELE KIRRERNYSW MDIITICKDK LPNYEEKIKM FYEEHLHLDD EIRYILDGSG YFDVRDKEDQ WIRIFMEKGD MVTLPAGIYH RFTVDEKNYT KAMRLFVGEP VWTAYNRPAD HFEARGQYVK FLAQTA.

    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.

    Adi1 Human
  • View Data Sheet

    Name :

    ENO1 Human

    Description:

    Enolase-1 Human Recombinant

    NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    Product # :

    ENZ-452

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    • biological activity
    • More Info

    Description

    The ENO1 Human Recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 47.1kDa and containing 434 amino acids (1-434 a.a.).

    Source

    Escherichia Coli.

    Formulation

    The ENO1 protein solution (1mg/ml) is formulated in 20mM Tris-HCl pH-7.5 1mM MgSO4 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20,000pmol/min/ug, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.

    More Info

    • Introduction

      ENO1 is a homodimeric soluble protein that encodes a smaller monomeric structural lens protein, tau-crystallin. ENO1 is a glycolytic enzyme expressed in mainly all tissues. ENO1 isoenzyme full length protein is found in the cytoplasm. The shorter protein is formed from another translation start that is restricted to the nucleus, and binds to a component in the c-myc promoter. ENO1 is involved in anaerobic metabolism under hypoxic conditions and plays a role as a cell surface plasminogen receptor during tissue invasion. Irregular expression of Enolase-1 is linked with tumor progression in several cases of breast and lung cancer. Enolase-1 is as an auto antigen associated with Hashimoto's encephalopathy and severe asthma. ENO1 is the target protein of serum anti-endothelial antibody in Behcet's disease.

    • Synonyms

      NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    • 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

      MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK AKFAGRNFRN PLAK.

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    Eno1 Human
  • View Data Sheet

    Name :

    BHMT Human

    Description:

    Betaine Homocysteine S-Methyltransferase Human Recombinant

    BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.

    Product # :

    ENZ-292

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    Description

    Betaine Homocysteine S-Methyltransferase Human Recombinant fused to His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 443 amino acids (21-236) and having a molecular mass of 49.2 kDa. The BHMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BHMT solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Betaine-homocysteine methyltransferase (BHMT) is a cytosolic enzyme that catalyzes the conversion of betaine and homocysteine to dimethylglycine and methionine, respectively. BHMT displays differential expression in a model of liver cirrhosis.

    • Synonyms

      BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.

    • Physical Appearance

      Sterile Filtered clear colorless solution 1 mg/ml.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMPP VGGKKAKKGI LERLNAGEIV IGDGGFVFAL EKRGYVKAGP WTPEAAVEHP EAVRQLHREF LRAGSNVMQT FTFYASEDKL ENRGNYVLEK ISGQEVNEAA CDIARQVADE GDALVAGGVS QTPSYLSCKS ETEVKKVFLQ QLEVFMKKNV DFLIAEYFEH VEEAVWAVET LIASGKPVAA TMCIGPEGDL HGVPPGECAV RLVKAGASII GVNCHFDPTI SLKTVKLMKE GLEAARLKAH LMSQPLAYHT PDCNKQGFIDLPEFPFGLEP RVATRWDIQK YAREAYNLGV RYIGGCCGFE PYHIRAIAEE LAPERGFLPPASEKHGSWGS GLDMHTKPWV RARARKEYWE NLRIASGRPY NPSMSKPDGW GVTKGTAELM QQKEATTEQQ LKELFEKQKF KSQ.

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    Bhmt Human
  • View Data Sheet

    Name :

    GCLM Human

    Description:

    Glutamate-Cysteine Ligase, Modifier Subunit Human Recombinant

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

    Product # :

    ENZ-636

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamate-cysteine ligase (GCLM) is the first rate limiting enzyme of glutathione synthesis. The GCLM enzyme is comprised of 2 subunits, a heavy catalytic subunit and a light regulatory subunit. GCLM deficiency is associated with some forms of hemolytic anemia.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMGTDSR AAKALLARAR TLHLQTGNLL NWGRLRKKCP STHSEELHDC IQKTLNEWSS QINPDLVREF PDVLECTVSH AVEKINPDER EEMKVSAKLF IVESNSSSST RSAVDMACSV LGVAQLDSVI IASPPIEDGV NLSLEHLQPY WEELENLVQS KKIVAIGTSD LDKTQLEQLY QWAQVKPNSN QVNLASCCVM PPDLTAFAKQ FDIQLLTHND PKELLSEASF QEALQESIPD IQAHEWVPLW LLRYSVIVKS RGIIKSKGYI LQAKRRGS.

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    Gclm Human
  • View Data Sheet

    Name :

    PPA2 Human

    Description:

    Pyrophosphatase-2 Human Recombinant

    PPA2, Pyrophosphatase-2, Inorganic pyrophosphatase 2, mitochondrial, PPase 2, Pyrophosphatase SID6-306, Pyrophosphate phospho-hydrolase 2, HSPC124, Pyrophosphatase (inorganic) 2, SID6-306, Inorganic pyrophosphatase 2, mitochondrial isoform 1.

    Product # :

    ENZ-815

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    Description

    PPA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (33-334 a.a) and having a molecular mass of 37.1kDa.PPA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PPA2 shares great imagination with members of the inorganic pyrophosphatase (PPase) family. PPA2 is localized to the mitochondrion and owns the signature sequence necessary for the catalytic activity of PPase. PPases catalyze the hydrolysis of pyrophosphate to inorganic phosphate, which is vital for the phosphate metabolism of cells.

    • Synonyms

      PPA2, Pyrophosphatase-2, Inorganic pyrophosphatase 2, mitochondrial, PPase 2, Pyrophosphatase SID6-306, Pyrophosphate phospho-hydrolase 2, HSPC124, Pyrophosphatase (inorganic) 2, SID6-306, Inorganic pyrophosphatase 2, mitochondrial isoform 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 MGSALYHTEE RGQPCSQNYR LFFKNVTGHY ISPFHDIPLK VNSKEENGIP MKKARNDEYE NLFNMIVEIP RWTNAKMEIA TKEPMNPIKQ YVKDGKLRYV ANIFPYKGYI WNYGTLPQTW EDPHEKDKST NCFGDNDPID VCEIGSKILS CGEVIHVKIL GILALIDEGE TDWKLIAINA NDPEASKFHD IDDVKKFKPG YLEATLNWFR LYKVPDGKPE NQFAFNGEFK NKAFALEVIK STHQCWKALL MKKCNGGAIN CTNVQISDSP FRCTQEEARS LVESVSSSPN KESNEEEQVW HFLGK.

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    Ppa2 Human
  • View Data Sheet

    Name :

    LCAT Human

    Description:

    Lecithin-Cholesterol Acyltransferase Human Recombinant

    Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    Product # :

    ENZ-380

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    Description

    LCAT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 441 amino acids (25-440) which includes a 25 amino acid His Tag fused at N-terminus and having a total molecular mass of 49.8 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCAT protein solution (0.5mg/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

      LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.

    • Synonyms

      Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    • 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 MGSHMFWLLN VLFPPHTTPK AELSNHTRPV ILVPGCLGNQ LEAKLDKPDV VNWMCYRKTE DFFTIWLDLN MFLPLGVDCW IDNTRVVYNR SSGLVSNAPG VQIRVPGFGK TYSVEYLDSS KLAGYLHTLV QNLVNNGYVR DETVRAAPYD WRLEPGQQEE YYRKLAGLVE EMHAAYGKPV FLIGHSLGCL HLLYFLLRQP QAWKDRFIDG FISLGAPWGG SIKPMLVLAS GDNQGIPIMS SIKLKEEQRI TTTSPWMFPS RMAWPEDHVF ISTPSFNYTG RDFQRFFADL HFEEGWYMWL QSRDLLAGLP APGVEVYCLY GVGLPTPRTY IYDHGFPYTD PVGVLYEDGD DTVATRSTEL CGLWQGRQPQ PVHLLPLHGI QHLNMVFSNL TLEHINAILL GAYRQGPPAS PTASPEPPPP E.

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    Lcat Human
  • View Data Sheet

    Name :

    EPHX1 Human

    Description:

    Epoxide Hydrolase 1 Microsomal Human Recombinant

    Epoxide hydrolase 1, microsomal (xenobiotic), MEH, EPHX, EPOX, Epoxide hydratase, Microsomal epoxide hydrolase.

    Product # :

    ENZ-773

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    Description

    EPHX1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 451 amino acids (21-455a.a) and having a molecular mass of 52.2kDa. EPHX1 is fused to a 16 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EPHX1 solution (0.25mg/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

      Epoxide Hydrolase 1 Microsomal (EPHX1) is a vital biotransformation enzyme which transfers epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase plays a role in both activation and detoxification of epoxides. Mutations in EPHX1 trigger preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.

    • Synonyms

      Epoxide hydrolase 1, microsomal (xenobiotic), MEH, EPHX, EPOX, Epoxide hydratase, Microsomal epoxide hydrolase.

    • 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

      MASMTGGQQM GRGSHMRDKE ETLPLEDGWW GPGTRSAARE DDSIRPFKVE TSDEEIHDLH QRIDKFRFTP PLEDSCFHYG FNSNYLKKVI SYWRNEFDWK KQVEILNRYP HFKTKIEGLD IHFIHVKPPQ LPAGHTPKPL LMVHGWPGSF YEFYKIIPLL TDPKNHGLSD EHVFEVICPS IPGYGFSEAS SKKGFNSVAT ARIFYKLMLR LGFQEFYIQG GDWGSLICTN MAQLVPSHVK GLHLNMALVL SNFSTLTLLL GQRFGRFLGL TERDVELLYP VKEKVFYSLM RESGYMHIQC TKPDTVGSAL NDSPVGLAAY ILEKFSTWTN TEFRYLEDGG LERKFSLDDL LTNVMLYWTT GTIISSQRFY KENLGQGWMT QKHERMKVYV PTGFSAFPFE LLHTPEKWVR FKYPKLISYS YMVRGGHFAA FEEPELLAQD IRKFLSVLER Q.

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    Ephx1 Human
  • View Data Sheet

    Name :

    METTL21A Human

    Description:

    Methyltransferase Like 21A Human Recombinant

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

    Product # :

    ENZ-718

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    Description

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

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      METTL21A, which is a part of the methyltransferase superfamily, is a Protein-lysine methyltransferase that in vitro methylates HSPA1, HSPA5 and HSPA8.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSTDRKVAL EFLKSNVQAN LPPHIQTKTV VKELTWGQNL GSFSPGEFDL ILGADIIYLE ETFTDLLQTL EHLCSNHSVI LLACRIRYER DNNFLAMLER QFTVRKVHYD PEKDVHIYEA QKRNQKEDL.

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    Mettl21A Human
  • View Data Sheet

    Name :

    ENO2 Mouse

    Description:

    Enolase-2 Mouse Recombinant

    AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.

    Product # :

    ENZ-1028

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    Description

    ENO2 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (1-434) and having a molecular mass of 49.7kDa.ENO2 is fused to a 23 amino acid His-tag at N-terminus& purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ENO2 solution (1mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 10,000 pmol/min/µg, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.

    More Info

    • Introduction

      Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.

    • Synonyms

      AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSIEKIW AREILDSRGN PTVEVDLYTA KGLFRAAVPS GASTGIYEAL ELRDGDKQRY LGKGVLKAVD HINSRIAPAL ISSGISVVEQ EKLDNLMLEL DGTENKSKFG ANAILGVSLA VCKAGAAERD LPLYRHIAQL AGNSDLILPV PAFNVINGGS HAGNKLAMQE FMILPVGAES FRDAMRLGAE VYHTLKGVIK DKYGKDATNV GDEGGFAPNI LENSEALELV KEAIDKAGYT EKMVIGMDVA ASEFYRDGKY DLDFKSPADP SRYITGDQLG ALYQDFVRNY PVVSIEDPFD QDDWAAWSKF TANVGIQIVG DDLTVTNPKR IERAVEEKAC NCLLLKVNQI GSVTEAIQAC KLAQENGWGV MVSHRSGETE DTFIADLVVG LCTGQIKTGA PCRSERLAKY NQLMRIEEEL GDEARFAGHN FRNPSVL.

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    Eno2 Mouse
  • View Data Sheet

    Name :

    TDO2 Human

    Description:

    Tryptophan 2,3-Dioxygenase Human Recombinant

    Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.

    Product # :

    ENZ-081

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    Description

    TDO2 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 426 amino acids (1-406 a.a.) and having a molecular mass of 50kDa. The TDO2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TDO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TDO2 is a ferrous heme enzyme that catalyzes the first and rate-limiting step in the kynurenine pathway which is the major pathway of tryptophan metabolism. TDO2 integrates oxygen into the indole moiety of tryptophan. TDO2 has broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin.

    • Synonyms

      Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.

    • 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 MSGCPFLGNN FGYTFKKLPV EGSEEDKSQT GVNRASKGGL IYGNYLHLEK VLNAQELQSE TKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VVSRMHRVSV ILKLLVQQFS ILETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQN MRVPYNRRHY RDNFKGEENE LLLKSEQEKT LLELVEAWLE RTPGLEPHGF NFWGKLEKNI TRGLEEEFIR IQAKEESEEK EEQVAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYRALQ GALMIYFYRE EPRFQVPFQL LTSLMDIDSL MTKWRYNHVC MVHRMLGSKA GTGGSSGYHY LRSTVSDRYK VFVDLFNLST YLIPRHWIPK MNPTIHKFLY TAEYCDSSYF SSDESD.

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    Tdo2 Human
  • View Data Sheet

    Name :

    CDO1 Human

    Description:

    Cysteine Dioxygenase Human Recombinant

    Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.

    Product # :

    ENZ-449

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    Description

    CDO1 Human Recombinant fused with a 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-170 a.a.) and having a molecular mass of 23.9kDa.The CDO1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDO1 solution contains 20mM Tris buffer(pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDO1 (Cysteine dioxygenase) is a mammalian non-heme iron enzyme that initiates a number of significant metabolic pathways associated with pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate) by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels. CDO1 is highly expressed in the liver and placenta. On the other hand CDO1 has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells.

    • Synonyms

      Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.

    • 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 KDRWGSHMEQ TEVLKPRTLA DLIRILHQLF AGDEVNVEEV QAIMEAYESD PTEWAMYAKF DQYRYTRNLV DQGNGKFNLM ILCWGEGHGS SIHDHTNSHC FLKMLQGNLK ETLFAWPDKK SNEMVKKSER VLRENQCAYI NDSVGLHRVE NISHTEPAVS LHLYSPPFDT CHAFDQR.

    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.

    Cdo1 Human
  • View Data Sheet

    Name :

    Uricase

    Description:

    Urate Oxidase Recombinant

    Urate Oxidase, Uricase, Urate Oxygen, Oxidoreductase, UOX, UO, EC 1.7.3.

    Product # :

    ENZ-312

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    Description

    Urate Oxidase Recombinant produced in E.Coli is a tetrameric, non-glycosylated polypeptide chain containing 302 amino acids, having a molecular formula of C1523H2383N417O462S7 and a molecular mass of 34,247 Dalton.The cDNA coding for urate-oxidase was cloned from a strain of Aspergillus flavus . The monomer protein has no intra- or inter-disulfide bridges.

    Source

    Escherichia Coli.

    Formulation

    Each 1.5mg Uricase contains 5mg sucrose, 25mg glycine, 0.1mg Tween-80, 13.6 mg Na2HPO4*12H20 and 0.33 mg NaH2PO4*2H20.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 10U/mg.
    One Unit oxidizes one micromole of uric acid per minute at 25°C, at pH 8.5.

    More Info

    • Introduction

      Urate oxidase catalyzes the enzymatic oxidation (degrades) of uric acid into allantoin, an inactive and soluble metabolite, which is 5 to 10 fold more soluble than uric acid . Urate oxidase is an enzyme of the purine breakdown pathway that catalyses the oxidation of uric acid to allantoin. Uricase is present in numerous diverse organisms, but not in higher primates including human. Hyperuricaemia is most commonly associated with gout and also occurs in mammalians with malignancy, especially those with lymphoid malignancies due to rapid cell turnover and an increased rate of purine metabolism. Uricase is effective in the prevention and treatment of hyperuricaemia in mammalians with malignancy and in those who have undergone transplantation. It appears to act rapidly, safely and induces a more dramatic decrease in plasma levels of uric acid.

    • Synonyms

      Urate Oxidase, Uricase, Urate Oxygen, Oxidoreductase, UOX, UO, EC 1.7.3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Urate Oxidase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Uricase should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      We highly recommend reconstituting the lyophilized Uricase in 50mM borate buffer containing 0.001%Triton X-100 and 1.0mM EDTA, pH 8.5 for activity assay.

    • Amino Acid Sequence

      msavkaaryg kdnvrvykvh kdektgvqtv yemtvcvlle geietsytka dnsvivatds ikntiyitak qnpvtppelf gsilgthfie kynhihaahv nivchrwtrm didgkphphs firdseekrn vqvdvvegkg idiksslsgl tvlkstnsqf wgflrdeytt lketwdrils tdvdatwqwk nfsglqevrs hvpkfdatwa tarevtlktf aednsasvqa tmykmaeqil arqqlietve yslpnkhyfe idlswhkglq ntgknaevfa pqsdpnglik ctvgrsslks kl.

    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.

    Urate Oxidase
  • View Data Sheet

    Name :

    SULT2A1 Human

    Description:

    Sulfotransferase Family, Cytosolic, 2A, Member 1 Human Recombinant

    Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.

    Product # :

    ENZ-141

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    Description

    SULT2A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (1-285a.a) and having a molecular mass of 35.9kDa.SULT2A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SULT2A1 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SULT2A1 is a member fo the sulfotransferase family. SULT2A1 is primarily expressed in liver and adrenal tissues, and to a lesser extent in kidney. SULT2A1 catalyzes the 3'-phosphoadenosine 5'-phosphosulfate-dependent sulfation of an extensive selection of steroids in human liver and adrenal tissues, and in addition is responsible for a larg number of the sulfation of bile acids in human liver.

    • Synonyms

      Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.

    • 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 MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL AEILCLMHSK GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL PIQLFPKSFF SSKAKVIYLM RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF EWFCQGTVLY GSWFDHIHGW MPMREEKNFL LLSYEELKQD TGRTIEKICQ FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV DKAQLLRKGV SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE

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    Sult2A1 Human
  • View Data Sheet

    Name :

    UBE2E3 Human

    Description:

    Ubiquitin Conjugating Enzyme E2E3 Human Recombinant

    UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.

    Product # :

    ENZ-906

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    Description

    UBE2E3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-207 a.a) and having a molecular mass of 25.3kDa.UBE2E3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2E3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2E3 or Ubiquitin-conjugating enzyme E2 E3 is part of the E2 ubiquitinconjugating enzyme family. UBE2E3 is needed for the destruction of mitotic cyclins and for cell cycle progression. The ubiquitination process covalently attaches to a short protein of 76 amino acids called ubiquitin, to a lysine residue on the target protein. When a protein has been tagged with one ubiquitin molecule, other rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein which grants passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.

    • Synonyms

      UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.

    • 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 MGSMSSDRQR SDDESPSTSS GSSDADQRDP AAPEPEEQEE RKPSATQQKK NTKLSSKTTA KLSTSAKRIQ KELAEITLDP PPNCSAGPKG DNIYEWRSTI LGPPGSVYEG GVFFLDITFS SDYPFKPPKV TFRTRIYHCN INSQGVICLD ILKDNWSPAL TISKVLLSIC SLLTDCNPAD PLVGSIATQY LTNRAEHDRI ARQWTKRYAT.

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    Ube2E3 Human
  • View Data Sheet

    Name :

    NTH E.Coli

    Description:

    Endonuclease-III E.Coli Recombinant

    DNA-(apurinic or apyrimidinic site) lyase, b1633, JW1625.

    Product # :

    ENZ-132

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    Description

    NTH E.Coli Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 231 amino acids (1-211a.a.) and having a molecular mass of 25.7kDa. The NTH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NTH solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT, 0.1mM PMSF and 40% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Endonuclease III (nth) is a DNA repair enzyme which has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases numerous damaged pyrimidines from DNA by cleaving the N-glycosidic bond and leaving an AP (apurinic/apyrimidinic) site. This AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, thus leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

    • Synonyms

      DNA-(apurinic or apyrimidinic site) lyase, b1633, JW1625.

    • 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 MNKAKRLEIL TRLRENNPHP TTELNFSSPF ELLIAVLLSA QATDVSVNKA TAKLYPVANT PAAMLELGVE GVKTYIKTIG LYNSKAENII KTCRILLEQH NGEVPEDRAA LEALPGVGRK TANVVLNTAF GWPTIAVDTH IFRVCNRTQF APGKNVEQVE EKLLKVVPAE FKVDCHHWLI LHGRYTCIAR KPRCGSCIIE DLCEYKEKVD I.

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    Nth Ecoli
  • View Data Sheet

    Name :

    PON1 Human, HEK

    Description:

    Paraoxonase-1 Human Recombinant, HEK

    Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5

    Product # :

    ENZ-1154

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    Description

    PON1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (16-355 a.a) containing a total of 346 amino acids, having a molecular mass of 39.0kDa. PON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The PON1 solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500 pmol/min/ug. Defined by the amount of enzyme that  hydrolyzes 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37˚C.

    More Info

    • Introduction

      Paraoxonase-1 or PON1 is part of the paraoxonase group of proteins. PON1 is an enzyme, responsible to the toxic metabolites of a different of organophosphorus insecticides hydrolyzation. Furthermore, PON1 is a dominant anti-atherosclerotic part of HDL. The enzyme needs PPAR-gamma for activation, leading to synthesis and release of paraoxonase 1 from the liver tissue, resulting in atherosclerosis reduction. PON1 has many qualities for atheroprotective through inflammatory lipid peroxides metabolism. This enzyme can hydrolyze a large number of substrates, for example cyclic carbonates, lactones, nerve gases etc.

    • Synonyms

      Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5

    • 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

      LFRNHQSSYQ TRLNALREVQ PVELPNCNLV KGIETGSEDL EILPNGLAFI SSGLKYPGIK SFNPNSPGKI LLMDLNEEDP TVLELGITGS KFDVSSFNPH GISTFTDEDN AMYLLVVNHP DAKSTVELFK FQEEEKSLLH LKTIRHKLLP NLNDIVAVGP EHFYGTNDHY FLDPYLQSWE MYLGLAWSYV VYYSPSEVRV VAEGFDFANG INISPDGKYV YIAELLAHKI HVYEKHANWT LTPLKSLDFN TLVDNISVDP ETGDLWVGCH PNGMKIFFYD SENPPASEVL RIQNILTEEP KVTQVYAENG TVLQGSTVAS VYKGKLLIGT VFHKALYCEL HHHHHH

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

    Pon1 Enzyme
  • View Data Sheet

    Name :

    GDA Human, His

    Description:

    Guanine Deaminase Human Recombinant, His Tag

    CYPIN, GUANASE, NEDASIN, Guanine aminase, Guanine aminohydrolase, GAH, p51-nedasin.

    Product # :

    ENZ-682

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    Description

    GDA Human Recombinant produced in E. coli is a single polypeptide chain containing 477 amino acids (1-454) and having a molecular mass of 53kDa. GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDA solution (1mg/1ml) contains 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

      GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

    • Synonyms

      CYPIN, GUANASE, NEDASIN, Guanine aminase, Guanine aminohydrolase, GAH, p51-nedasin.

    • 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 MGSMCAAQMP PLAHIFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE ASQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHASQ YSFAGSSIDL PLLEWLTKYT FPAEHRFQNI DFAEEVYTRV VRRTLKNGTT TACYFATIHT DSSLLLADIT DKFGQRAFVG KVCMDLNDTF PEYKETTEES IKETERFVSE MLQKNYSRVK PIVTPRFSLS CSETLMGELG NIAKTRDLHI QSHISENRDE VEAVKNLYPS YKNYTSVYDK NNLLTNKTVM AHGCYLSAEE LNVFHERGAS IAHCPNSNLS LSSGFLNVLE VLKHEVKIGL GTDVAGGYSY SMLDAIRRAV MVSNILLINK VNEKSLTLKE VFRLATLGGS QALGLDGEIG NFEVGKEFDA ILINPKASDS PIDLFYGDFF GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.

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    Gda Human
  • View Data Sheet

    Name :

    OGG1 Mouse

    Description:

    8-Oxoguanine DNA Glycosylase Mouse Recombinant

    HMMH, HOGG1, MUTM, OGH1, AP lyase, OGG1, 8-Oxoguanine DNA Glycosylase, OGG1.

    Product # :

    ENZ-1048

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    Description

    OGG1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a) and having a molecular mass of 41.3kDa. OGG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OGG1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3 to the lesion.

    • Synonyms

      HMMH, HOGG1, MUTM, OGH1, AP lyase, OGG1, 8-Oxoguanine DNA Glycosylase, OGG1.

    • 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 MGSMLFRSWL PSSMRHRTLS SSPALWASIP CPRSELRLDL VLASGQSFRW KEQSPAHWSG VLADQVWTLT QTEDQLYCTV YRGDDSQVSR PTLEELETLH KYFQLDVSLA QLYSHWASVD SHFQRVAQKF QGVRLLRQDP TECLFSFICS SNNNIARITG MVERLCQAFG PRLIQLDDVT YHGFPNLHAL AGPEAETHLR KLGLGYRARY VRASAKAILE EQGGPAWLQQ LRVAPYEEAH KALCTLPGVG AKVADCICLM ALDKPQAVPV DVHVWQIAHR DYGWHPKTSQ AKGPSPLANK ELGNFFRNLW GPYAGWAQAV LFSADLRQPS LSREPPAKRK KGSKRPEG.

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    Ogg1 Mouse
  • 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

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

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

    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 :

    DPP4 Human

    Description:

    Dipeptidyl-Peptidase 4 Human Recombinant

    CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

    Product # :

    ENZ-375

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    Description

    DPPIV Human Recombinant produced in Insect cells is a single, glycosylated polypeptide chain containing 737 amino acids (39-766) and having a molecular mass of 85.4kDa.DPPIV is fused to a 6 His Tag at C-terminus and purified using conventional chromatography techniques.

    Source

    Insect cells.

    Formulation

    DPP4 is formulated in 20mM Tris-HCl buffer pH-8, 100mM NaCl, 1mM EDTA and 10% glycerol.

    Purity

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

    Biological Activity

    >200 Units/mg.

    More Info

    • Introduction

      DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.

    • Synonyms

      CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPSRKTYTL TDYLKNTYRL KLYSLRWISD HEYLYKQENN ILVFNAEYGN SSVFLENSTF DEFGHSINDY SISPDGQFIL LEYNYVKQWR HSYTASYDIY DLNKRQLITE ERIPNNTQWV TWSPVGHKLA YVWNNDIYVK IEPNLPSYRI TWTGKEDIIY NGITDWVYEE EVFSAYSALW WSPNGTFLAY AQFNDTEVPL IEYSFYSDES LQYPKTVRVP YPKAGAVNPT VKFFVVNTDS LSSVTNATSI QITAPASMLI GDHYLCDVTW ATQERISLQW LRRIQNYSVM DICDYDESSG RWNCLVARQH IEMSTTGWVG RFRPSEPHFT LDGNSFYKII SNEEGYRHIC YFQIDKKDCT FITKGTWEVI GIEALTSDYL YYISNEYKGM PGGRNLYKIQ LSDYTKVTCL SCELNPERCQ YYSVSFSKEA KYYQLRCSGP GLPLYTLHSS VNDKGLRVLE DNSALDKMLQ NVQMPSKKLD FIILNETKFW YQMILPPHFD KSKKYPLLLD VYAGPCSQKA DTVFRLNWAT YLASTENIIV ASFDGRGSGY QGDKIMHAIN RRLGTFEVED QIEAARQFSK MGFVDNKRIA IWGWSYGGYV TSMVLGSGSG VFKCGIAVAP VSRWEYYDSV YTERYMGLPT PEDNLDHYRN STVMSRAENF KQVEYLLIHG TADDNVHFQQ SAQISKALVD VGVDFQAMWY TDEDHGIASS TAHQHIYTHM SHFIKQCFSL PHHHHHH.

    • Unit Definition

      One unit will hydrolyze 1 umole of p-nitroaniline per minute at pH8.0 at 37°C using 1mM of Gly-Pro p-nitroanilde as a substrate.

    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.

    Dpp4 Human
  • View Data Sheet

    Name :

    OSGEP Human

    Description:

    O-Sialoglycoprotein Endopeptidase Human Recombinant

    O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.

    Product # :

    ENZ-821

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    OSGEP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-335 a.a) and having a molecular mass of 38.8kDa. OSGEP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSGEP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      O-Sialoglycoprotein Endopeptidase, also known as OSGEP is a member of the KAE1 / TsaD family. OSGEP is essential for the formation of threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs which read codons beginning with adenine. OSGEP take a direct catalytic part in the above reaction, however other proteins of the complex are required to fulfill this activity.

    • Synonyms

      O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.

    • 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 MGSMPAVLGF EGSANKIGVG VVRDGKVLAN PRRTYVTPPG TGFLPGDTAR HHRAVILDLL QEALTESGLT SQDIDCIAYT KGPGMGAPLV SVAVVARTVA QLWNKPLVGV NHCIGHIEMG RLITGATSPT VLYVSGGNTQ VIAYSEHRYR IFGETIDIAV GNCLDRFARV LKISNDPSPG YNIEQMAKRG KKLVELPYTV KGMDVSFSGI LSFIEDVAHR MLATGECTPE DLCFSLQETV FAMLVEITER AMAHCGSQEA LIVGGVGCNV RLQEMMATMC QERGARLFAT DERFCIDNGA MIAQAGWEMF RAGHRTPLSD SGVTQRYRTD EVEVTWRD.

    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.

    Osgep Human
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