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Search results

1000 results found for “Nuclease”

Name

Description

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  • View Data Sheet

    Name :

    AHCY Human, Sf9

    Description:

    Adenosylhomocysteinase Human Recombinant, Sf9

    EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

    Product # :

    ENZ-1034

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    Description

    AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.

    • Synonyms

      EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

    • 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

      ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH H.

    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.

    Ahcy Human Sf9
  • View Data Sheet

    Name :

    DAAO Human, Active

    Description:

    D-Amino Acid Oxidase Human Recombinant, BioActive

    D-Amino Acid Oxidase 2, D-Amino-Acid Oxidase, EC 1.4.3.3, DAMOX, DAAO, EC 1.4.3, OXDA.

    Product # :

    ENZ-1142

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    Description

    DAAO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (1-347) and having a molecular mass of 41.6 kDa. DAAO Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DAAO Human protein (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 20% glycerol & 1mM DTT.

    .

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3.5unit/mg, in which one unit will oxidatively deaminate 1.0 umole of D-alanine to pyruvateper minute at pH 8.5 at 37C, in the presence of catalase.

    Citations

    More Info

    • Introduction

      D-amino-acid oxidase or DAAO is an enzyme that oxidizes D-amino acids to their imino acids form while using FAD (flavin adenine dinucleotide) as a co-factor, resulting in the formation of ammonia & hydrogen peroxide. the enzyme may take part in keeping the balance of acid base in the kidney tissue. Another role is to detoxifying molecules that abolish D-amino acids aggregated while the cell ages.

    • Synonyms

      D-Amino Acid Oxidase 2, D-Amino-Acid Oxidase, EC 1.4.3.3, DAMOX, DAAO, EC 1.4.3, OXDA.

    • 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 MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG LWQPYLSDPN NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE AIPDPSWKDT VLGFRKLTPR ELDMFPDYGY GWFHTSLILE GKNYLQWLTE RLTERGVKFF QRKVESFEEV AREGADVIVN CTGVWAGALQ RDPLLQPGRG QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG IFQLGNWSEL NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL.

    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.

    Daao Enzyme
  • View Data Sheet

    Name :

    ECI1 Human

    Description:

    Enoyl-CoA Delta Isomerase 1 Human Recombinant

    Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.

    Product # :

    ENZ-758

    Price :

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    Description

    ECI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (42-302 a.a.) and having a molecular mass of 31.1kDa. ECI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ECI1 protein solution (0.25mg/ml) 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.

    Citations

    More Info

    • Introduction

      Enoyl-CoA Delta Isomerase 1 (ECI1) is a main mitochondrial enzyme which takes part in beta-oxidation of unsaturated fatty acids. ECI1 is a member of the hydratase/isomerase superfamily. ECI1 catalyzes the transformation of 3-cis and 3-trans-enoyl-CoA esters to the 2-trans-enoylCoA intermediates.

    • Synonyms

      Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.

    • 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 MGSFGSQRVL VEPDAGAGVA VMKFKNPPVN SLSLEFLTEL VISLEKLEND KSFRGVILTS DRPGVFSAGL DLTEMCGRSP AHYAGYWKAV QELWLRLYQS NLVLVSAING ACPAGGCLVA LTCDYRILAD NPRYCIGLNE TQLGIIAPFW LKDTLENTIG HRAAERALQL GLLFPPAEAL QVGIVDQVVP EEQVQSTALS AIAQWMAIPD HARQLTKAMM RKATASRLVT QRDADVQNFV SFISKDSIQK SLQMYLERLK EEKG.

    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.

    Eci1 Human
  • View Data Sheet

    Name :

    HAO1 Human, Active

    Description:

    Hydroxyacid Oxidase 1 Human Recombinant, Active

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

    Product # :

    ENZ-1094

    Price :

    Quantity :

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    • Citations

    Description

    HAO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-370 a.a) and having a molecular mass of 45.0kDa. HAO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3000 pmol/min/ug, and defined as the amount of enzyme that oxidize glyoxylate at pH 8.0 at 25C.

    Citations

    More Info

    • Introduction

      Glycolate oxidase (HAO1) is a part of the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyses the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate by reducing oxygen to hydrogen peroxide. HAO1 is expressed mainly in the liver and pancreas and is most active on twocarbon substrates such as glycolate. HAO1 isthe main cause of hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.

    • Synonyms

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

    • Physical Appearance

      Sterile filtered yellowish solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMLPR LICINDYEQH AKSVLPKSIY DYYRSGANDE ETLADNIAAF SRWKLYPRMLRNVAETDLST SVLGQRVSMP ICVGATAMQR MAHVDGELAT VRACQSLGTG MMLSSWATSS IEEVAEAGPE ALRWLQLYIY KDREVTKKLVRQAEKMGYKA IFVTVDTPYL GNRLDDVRNR FKLPPQLRMK NFETSTLSFS PEENFGDDSG LAAYVAKAID PSISWEDIKW LRRLTSLPIVAKGILRGDDA REAVKHGLNG ILVSNHGARQ LDGVPATIDV LPEIVEAVEG KVEVFLDGGV RKGTDVLKAL ALGAKAVFVG RPIVWGLAFQGEKGVQDVLE ILKEEFRLAM ALSGCQNVKV IDKTLVRKNP LAVSKI.

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

    Hao1 Protein
  • View Data Sheet

    Name :

    PPM1A Human

    Description:

    Protein Phosphatase 1A Alpha Isoform Human Recombinant

    Protein phosphatase 1A, EC 3.1.3.16, Protein phosphatase 2C isoform alpha, PP2C-alpha, IA, PPM1A, PP2CA, MGC9201.

    Product # :

    PKA-222

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    Description

    PPM1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (1-382a.a) and having a molecular mass of 46.6kDa. PPM1A is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPM1A protein solution (1mg/ml) contains 10mM Tris-HCl, pH7.5, 50mM NaCl, 2mM DTT, 1mM MnCl2 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Protein Phosphatase 2C alpha is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding two distinct isoforms have been described.
      Protein phosphatase 2C(PP2C?) is a Mn2+- or Mg2+-dependent protein serine/threonine phosphatase that is essential for regulating cellular stress response in eukaryotes.

    • Synonyms

      Protein phosphatase 1A, EC 3.1.3.16, Protein phosphatase 2C isoform alpha, PP2C-alpha, IA, PPM1A, PP2CA, MGC9201.

    • 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 KDRWILMGAF LDKPKMEKHN AQGQGNGLRY GLSSMQGWRV EMEDAHTAVI GLPSGLESWS FFAVYDGHAG SQVAKYCCEH LLDHITNNQD FKGSAGAPSV ENVKNGIRTG FLEIDEHMRV MSEKKHGADR SGSTAVGVLI SPQHTYFINC GDSRGLLCRN RKVHFFTQDH KPSNPLEKER IQNAGGSVMI QRVNGSLAVS RALGDFDYKC VHGKGPTEQL VSPEPEVHDI ERSEEDDQFI ILACDGIWDV MGNEELCDFV RSRLEVTDDL EKVCNEVVDT CLYKGSRDNM SVILICFPNA PKVSPEAVKK EAELDKYLEC RVEEIIKKQG EGVPDLVHVM RTLASENIPS LPPGGELASK RNVIEAVYNR LNPYKNDDTD STSTDDMW.

    • Unit Definition

      One unit will hydrolyze 1 nanomole of p-nitrophenyl phosphatate (pNPP) per minute at pH 7.5 at 37°C.

    • Specific Activity

      >1,400 U/mg.

    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.

    Ppm1A Human
  • View Data Sheet

    Name :

    PPME1 Antibody

    Description:

    Protein Phosphatase Methylesterase 1, Mouse Anti Human

    Protein phosphatase methylesterase 1, PME-1, FLJ22226, EC 3.1.1.

    Product # :

    ANT-678

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    Citations

    More Info

    • Introduction

      PPME1 catalyzes the demethylation and inactivation of protein phosphatase (PP2A), a multimeric phosphoserine/ threonine protein phosphatase related to growth inhibition and cell cycle arrest. PPME1 can demethylate PP2A catalytic subunit in vitro and okadaic acid treatment can inhibit this reaction. It is conserved from yeast to human and holds a motif found in lipases having a catalytic triad activated serine as their active site nucleophile.

    • Synonyms

      Protein phosphatase methylesterase 1, PME-1, FLJ22226, EC 3.1.1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PPME1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PPME1 amino acids 1-386 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and K light chain.

    • Clone

      PAT29G3AT.

    • Applications

      PPME1 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      PPME1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Ppme1 Antibody
  • View Data Sheet

    Name :

    QPCT Human

    Description:

    Glutaminyl-Peptide Cyclotransferase Human Recombinant

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

    Product # :

    ENZ-912

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glutaminyl-Peptide Cyclotransferase, also known as QPCT is a member of the glutaminyl-peptide cyclotransferase family. QPCT is responsible for the biosynthesis of pyroglutamyl peptides. Furthermore, QPCT is partial against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length following the second residue. QPCT catalyzes N-terminal pyroglutamate formation, also in vitro, it catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      VSPSASAWPE EKNYHQPAIL NSSALRQIAE GTSISEMWQN DLQPLLIERY PGSPGSYAAR QHIMQRIQRL QADWVLEIDT FLSQTPYGYR SFSNIISTLN PTAKRHLVLA CHYDSKYFSH WNNRVFVGAT DSAVPCAMML ELARALDKKL LSLKTVSDSK PDLSLQLIFF DGEEAFLHWS PQDSLYGSRH LAAKMASTPH PPGARGTSQL HGMDLLVLLD LIGAPNPTFP NFFPNSARWF ERLQAIEHEL HELGLLKDHS LEGRYFQNYS YGGVIQDDHI PFLRRGVPVL HLIPSPFPEV WHTMDDNEEN LDESTIDNLN KILQVFVLEY LHLHHHHHH.

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

    Qpct Human
  • View Data Sheet

    Name :

    SARS Nucleocapsid Polyclonal

    Description:

    SARS-Nucleocapsid protein, Polyclonal Antibody

    Product # :

    ANT-180

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    Formulation

    1mg/ml in PBS and 0.02% sodium azide.

    Citations

    More Info

    • Introduction

      SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.
      It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.

    • Stability

      Store at 4°C, stable for 2 weeks. For long-term storage, store at -20°C.

    • Immunogen

      The antibody was developed by immunizing rabbits with synthetic peptides corresponding to amino a.a. 399-411 of putative SARS nucleocapsid (Genbank accession no. YP_009724397.2).

    • Applications

      Western Blot 1:100-1:2000, Immunohistochemistry, Immunocytochemistry/Immunofluorescence 1:10-1:500

    • Isotype

      Rabbit IgG.

    • Type

      Polyclonal Rabbit Antibody.

    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.

    Sars Nucleocapsid Polyclonal Antibody
  • View Data Sheet

    Name :

    Streptokinase

    Description:

    Streptokinase Recombinant

    Streptokinase, SK.

    Product # :

    ENZ-315

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    sds-page

    streptokinase sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Streptokinase is an extracellular metallo-enzymeproduced by beta-haemolytic streptococcusand is used as an effective and cheap clot-dissolving medicationin some cases of myocardial infarction(heart attack) and pulmonary embolism.
      It belongs to a group of medications known as fibrinolytics, and works by activating plasminogenthrough cleavage to produce plasmin.

    • Synonyms

      Streptokinase, SK.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Streptokinase in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IAGPEWLLDR PSVNNSQLVV SVAGTVEGTN QDISLKFFEI DLTSRPAHGG KTEQGLSPKS KLFATDSGAM PHKLEKADLL KAIQEQLIAN VHSNDDYFEV IDFASDATIT DRNGKVYFAD KDGSVTLPIQ PVQEFLLKGH VRVRPYKEKP VQNQAKSVDV EYTVQFTPLN PDDDFRPALK DTKLLKTLAI GDTITSQELL AQAQSILNKN HPGYTIYERD SSIVTHDNDI FRTILPMDQE FTYHVKNREQ AYRINKKSGL NEEINNTDLI SEKYYVLKKG EKPYDPFDRS HLKLFTIKYV DVNTNELLKS EQLLTASERN LDFRDLYDPR DKAKLLYNNL DAFGIMDYTL TGKVEDNHDD TNRIITVYMG KRPEGENASY HLAYDKDRYT EEEREVYSYL RYTGTPIPDN PNDK.

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

    Streptokinase
  • View Data Sheet

    Name :

    ACSF2 Human

    Description:

    Acyl-CoA Synthetase Family Member 2 Human Recombinant

    Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.

    Product # :

    ENZ-919

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    Description

    ACSF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (42-615 a.a) and having a molecular mass of 66.1kDa. ACSF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ACSF2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline pH 7.4 and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Acyl-CoA synthetase family member 2, also known as ACSF2 is a member of the ATP-dependent AMP-binding enzyme family. Acyl-CoA synthetases are a family of enzymes which catalyze the thioesterification of fatty acids with coenzymeA to form activated intermediates, which play a basic part in lipid metabolism as well as homeostasis of lipid-related processes. ACSF2 is required for the complex of lipid synthesis, energy production via beta-oxidation, protein acylation and fatty-acid dependent transcriptional regulation. Moreover, ACSF2 is required for fatty acid import into cells by the process of vectorial acylation.

    • Synonyms

      Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.

    • 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 MGSLSSREVD RMVSTPIGGL SYVQGCTKKH LNSKTVGQCL ETTAQRVPER EALVVLHEDV RLTFAQLKEE VDKAASGLLS IGLCKGDRLG MWGPNSYAWV LMQLATAQAG IILVSVNPAY QAMELEYVLK KVGCKALVFP KQFKTQQYYN VLKQICPEVE NAQPGALKSQ RLPDLTTVIS VDAPLPGTLL LDEVVAAGST RQHLDQLQYN QQFLSCHDPI NIQFTSGTTG SPKGATLSHY NIVNNSNILG ERLKLHEKTP EQLRMILPNP LYHCLGSVAG TMMCLMYGAT LILASPIFNG KKALEAISRE RGTFLYGTPT MFVDILNQPD FSSYDISTMC GGVIAGSPAP PELIRAIINK INMKDLVVAY GTTENSPVTF AHFPEDTVEQ KAESVGRIMP HTEARIMNME AGTLAKLNTP GELCIRGYCV MLGYWGEPQK TEEAVDQDKW YWTGDVATMN EQGFCKIVGR SKDMIIRGGE NIYPAELEDF FHTHPKVQEV QVVGVKDDRM GEEICACIRL KDGEETTVEE IKAFCKGKIS HFKIPKYIVF VTNYPLTISG KIQKFKLREQ MERHLNL.

    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.

    Acsf2 Human
  • View Data Sheet

    Name :

    ALDH1A1 Human

    Description:

    Aldehyde Dehydrogenase 1A1 Human Recombinant

    ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

    Product # :

    ENZ-453

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    Description

    The ALDH1A1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 54.8kDa and containing 501 amino acids (1-501 a.a.).

    Source

    Escherichia Coli.

    Formulation

    The ALDH1A1 protein solution is formulated in 50mM Tris-HCl pH-7.5 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ALDH1A1 is part of the aldehyde dehydrogenases family.
      Aldehyde dehydrogenase is the 2nd protein of the main oxidative pathway of alcohol metabolism. Cytosolic and mitochondrial are 2 main liver isoforms of ALDH that are differentiateed by their electrophoretic mobility, kinetic property, & subcellular localization. The majority of Caucasians have two main isozymes, whereas just about 50% of Orientals have only the cytosolic form, excluding the mitochondrial form. ALDH1A1 is also a member of the group of corneal crystallins that assist the transparency of the cornea.
      (Retinal + NAD+ + H2O = retinoate + NADH).

    • Synonyms

      ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLYKLADLIERDR LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKIGPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN S.

    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.

    Aldh1A1 Human
  • View Data Sheet

    Name :

    DCXR Human

    Description:

    Dicarbonyl/L-Xylulose Reductase Human Recombinant

    DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.

    Product # :

    ENZ-540

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    Description

    DCXR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-244 a.a.) and having a molecular mass of 28 kDa. The DCXR is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCXR Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 50mM NaCl & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DCXR catalyzes the NADPH-dependent reduction of numerous pentoses, tetroses, trioses, alpha-dicarbonyl molecules and L-xylulose. DCXR takes part in the uronate cycle of glucose metabolism. DCXR participates in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thus preventing osmolytic stress from occurring in the renal tubules.

    • Synonyms

      DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.

    • 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 MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE CPGIEPVCVD LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF DRSFEVNLRA VIQVSQIVAR GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC STKGALDMLT KVMALELGPH KIRVNAVNPT VVMTSMGQAT WSDPHKAKTM LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG FWAC.

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    Dcxr Human
  • 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.

    Citations

    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 :

    PLA2G12 Human

    Description:

    Secreted Phospholipase A2-XII Human Recombinant

    Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.

    Product # :

    ENZ-330

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    Description

    Secreted Phospholipase A2-XII Human Recombiannt was produced with N-terminal His-Tag. PLA2G12 His-Tagged Fusion Protein is 20.6 kDa containing 167 amino acid residues of the human secreted phospholipase A2-XII and 16 additional amino acid residues – His-Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.01M Tris buffer pH 8.6.

    Purity

    Greater than 95% as determined by SDS PAGE.

    Citations

    More Info

    • Introduction

      Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
      The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
      This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso- PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
      In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.

    • Synonyms

      Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMQEQA QTTDWRATLK TIRNGVHKID TYLNAALDLL GGEDGLCQYK CSDGSKPFPR YGYKPSPPNG CGSPLFGVHL NIGIPSLTKC CNQHDRCYET CGKSKNDCDE EFQYCLSKIC RDVQKTLGLTQ HVQACETTVE LLFDSVIHLG CKPYLDSQRA ACRCHYEEKT DL

    • Applications

      Western blotting.

    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.

    Pla2G12 Human
  • View Data Sheet

    Name :

    UBE2I Human His

    Description:

    Ubiquitin-Conjugating Enzyme E2I Human Recombinant, His Tag

    SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.

    Product # :

    ENZ-274

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    Description

    Ubiquitin-Conjugating Enzyme E2I Human Recombinant produced in E.coli is a 19.5 kDa protein containing 171 amino acids.The UBE2I protein contains 6xHis tag and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated (1mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.

    Purity

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

    Citations

    More Info

    • Introduction

      Human Ubquitin Conjugating Enzyme 9 (Ubc9) is a member of the E2 family and is specific for the conjugation of SUMO to a variety of target proteins. SUMO conjugation to target proteins is mediated by a different, but analogous, pathway to ubiquitinylation. This E2 is unusual in that it interacts directly with protein substrates that are modified by sumolyation, and may play a role in substrate recognition. Ubc9 can mediate the conjugation of SUMO-1 to a variety of proteins including RanGAP1, I?B?, and PML without the requirement of an E3 ligase.

    • Synonyms

      SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized UBE2I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2I should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized UBE2I in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHAMGTLNMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGT
      MNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFH
      PNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTI
      YCQNRVEYEKRVRAQAKKFAPS.

    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.

    Ube2I Human His
  • View Data Sheet

    Name :

    UROD Human

    Description:

    Uroporphyrinogen Decarboxylase Human Recombinant

    UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.

    Product # :

    ENZ-536

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    Description

    UROD Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 43 kDa. The UROD is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UROD Human solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl, 1mM EDTA & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UROD is the fifth enzyme in the human heme biosynthetic pathway and is in charge for the transfer of uroporphyrinogen to coproporphyrinogen through the deletion of four carboxymethyl side chains. UROD Mutations and deficiency result in 3 autosomal disorders in humans: familial porphyria cutanea tarda (f-PCT), sporadic porphyria cutanea tarda (s-PCT) and hepatoerythropoietic porphyria (HEP).

    • Synonyms

      UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen 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 MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT LQVNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH SRLLRQN.

    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.

    Urod Human
  • View Data Sheet

    Name :

    GSTT1 Human

    Description:

    Glutathione S-Transferase Theta-1 Human Recombinant

    Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.

    Product # :

    ENZ-429

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    Description

    GSTT1 Human Recombinant fused with 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 277 amino acids (1-240 a.a.) and having a molecular mass of 31.5kDa.The GSTT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTT1 solution contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GSTT1 belongs to a superfamily of proteins which catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. GSTT1 is one of the GSTs’ four main classes: alpha, mu, pi and theta (which includes GSTT1 and GSTT2). GSTT1 is involved in activation and detoxification reactions and catalyzes the conjugation of industrial chemicals, such as epoxybutane, ethylene oxides, halomethane with glutathione. GSTT1 is found in erythrocytes, at low levels in the liver as well as in Clara and ciliated cells at the alveolar/bronchiolar junction in the lung.
      The GSTT1 gene is deficient in 38% of the population. The GSTTI enzyme deficiency might influence the individual risk for development of acquired aplastic anemia and acute myeloid leukemia. The presence or absence of the GSTT1 gene is concurrent with GSST1+ (the conjugator) and GSTT1- (the non-conjugator) phenotypes correspondingly. The GSTT1+ phenotype is able to catalyze the glutathione conjugation of dichloromethane. GSTT1-null genotypes are seen as having a higher risk of developing leukoplakia. Germline genetic polymorphism in GSTT1 is linked to breast cancer.

    • Synonyms

      Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.

    • 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 KDRWGSHMGL ELYLDLLSQP CRAVYIFAKK NDIPFELRIV DLIKGQHLSD ACAQVNPLKK VPALKDGDFT LTESVAILLY LTRKYKVPDY WYPQDLQARA RVDEYLAWQH TTLRRSCLRA LWHKVMFPVF LGEPVSPQTL AATLAELDVT LQLLEDKFLQ NKAFLTGPHI SLADLVAITE LMHPVGAGCQ VFEGRPKLAT WRQRVEAAVG EDLFQEAHEV ILKAKDFPPA DPTIKQKLMP WVLAMIR.

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    Gstt1 Human
  • View Data Sheet

    Name :

    PGC Human

    Description:

    Progastricsin-C Human Recombinant

    Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.

    Product # :

    ENZ-966

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    Description

    PGC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (17-388 a.a.) and having a molecular mass of 41.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PGC is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Progastricsin-C (PGC) is an aspartic proteinase which is synthesized in the gastric mucosa as inactive precursors. PGC is a part of the peptidase family A1 and contains a prosegment which is responsible for stabilizing the inactive form and preventing the entrance of the substrate to the active site. PGC is used as a biomarker for various gastric diseases including Helicobacter pylori related gastritis. PGC is also hydrolyzes various proteins.

    • Synonyms

      Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.

    • 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

      AVVKVPLKKF KSIRETMKEK GLLGEFLRTH KYDPAWKYRF GDLSVTYEPM AYMDAAYFGE ISIGTPPQNF LVLFDTGSSN LWVPSVYCQS QACTSHSRFN PSESSTYSTN GQTFSLQYGS GSLTGFFGYD TLTVQSIQVP NQEFGLSENE PGTNFVYAQF DGIMGLAYPA LSVDEATTAM QGMVQEGALT SPVFSVYLSN QQGSSGGAVV FGGVDSSLYT GQIYWAPVTQ ELYWQIGIEE FLIGGQASGW CSEGCQAIVD TGTSLLTVPQ QYMSALLQAT GAQEDEYGQF LVNCNSIQNL PSLTFIINGV EFPLPPSSYI LSNNGYCTVG VEPTYLSSQN GQPLWILGDV FLRSYYSVYD LGNNRVGFAT AALEHHHHHH.

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    Pgc Human
  • View Data Sheet

    Name :

    Dopa Decarboxylase Human

    Description:

    Dopa Decarboxylase Human Recombinant

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

    Product # :

    ENZ-413

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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.

    Citations

    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.

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    Dopa Decarboxylase Human
  • View Data Sheet

    Name :

    CHST5 Human

    Description:

    Carbohydrate Sulfotransferase 5 Human Recombinant

    Carbohydrate sulfotransferase 5, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4, GST4, Intestinal N-acetylglucosamine-6-O-sulfotransferase, I-GlcNAc6ST, Intestinal GlcNAc-6-sulfotransferase, mIGn6ST, N-acetylglucosamine 6-O-sulfotransferase 3, GlcNAc6ST-3, Gn6st-3, Chst5, Gst4.

    Product # :

    ENZ-1165

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    Description

    CHST5 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (27-395 a.a.) and having a molecular mass of 42.9kDa.CHST5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CHST5 protein solution (0.25mg/ml) containing 20% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is greater than 10,000 pmol/min/ug, and is defined as the amount of enzyme that sulfate from PAPS to Nacetyl-D-glucosamine per minute at pH 7.5, at 37˚C.

    Citations

    More Info

    • Introduction

      Carbohydrate Sulfotransferase 5 (CHST5) is a Golgi-embedded enzyme that is found in B cells, T cells and intestinal epithelium and is also mediates sulfation of keratan in cornea. CHST5 is a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine residues of keratan. CHST5 works on the non-reducing terminal GlcNAc of short andlong carbohydrate substrates that have poly-N-acetyllactosamine structures.

    • Synonyms

      Carbohydrate sulfotransferase 5, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4, GST4, Intestinal N-acetylglucosamine-6-O-sulfotransferase, I-GlcNAc6ST, Intestinal GlcNAc-6-sulfotransferase, mIGn6ST, N-acetylglucosamine 6-O-sulfotransferase 3, GlcNAc6ST-3, Gn6st-3, Chst5, Gst4.

    • 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

      ADPEFSRQVP SSPAGLGERV HVLVLSSWRS GSSFVGQLFS QHPDVFYLME PAWHVWDTLS QGSAPALHMA VRDLIRSVFL CDMDVFDAYL PWRRNISDLF QWAVSRALCS PPVCEAFARG NISSEEVCKP LCATRPFGLA QEACSSYSHV VLKEVRFFNL QVLYPLLSDP ALNLRIVHLV RDPRAVLRSR EQTAKALARD NGIVLGTNGT WVEADPRLRV VNEVCRSHVR IAEAALHKPP PFLQDRYRLV RYEDLARDPL TVIRELYAFT GLGLTPQLQT WIHNITHGSG PGARREAFKT TSRDALSVSQ AWRHTLPFAK IRRVQELCGG ALQLLGYRSV HSELEQRDLS LDLLLPRGMD SFKWASSTEK QPESHHHHHH

    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.

    Chst5 Human
  • View Data Sheet

    Name :

    GPX7 Human

    Description:

    Glutathione Peroxidase 7 Human Recombinant

    Glutathione peroxidase 7, glutathione peroxidase 6, GPX6, NPGPx, CL683, GPx-7, GSHPx-7, non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase, FLJ14777, EC 1.11.1.9.

    Product # :

    ENZ-237

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    Description

    GPX7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (20-187) and having a molecular mass of 21.8kDa.GPX7 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPX7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GPX7 is a member of the glutathione peroxidase family. Glutathione peroxidases (GPx) are a family of enzymes with peroxidase activity whose central biological role is to guard the organism from oxidative damage by reducing lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to water.

    • Synonyms

      Glutathione peroxidase 7, glutathione peroxidase 6, GPX6, NPGPx, CL683, GPx-7, GSHPx-7, non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase, FLJ14777, EC 1.11.1.9.

    • 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 MGSHMQQEQD FYDFKAVNIR GKLVSLEKYR GSVSLVVNVA SECGFTDQHY RALQQLQRDL GPHHFNVLAF PCNQFGQQEP DSNKEIESFA RRTYSVSFPM FSKIAVTGTG AHPAFKYLAQ TSGKEPTWNF WKYLVAPDGK VVGAWDPTVS VEEVRPQITA LVRKLILLKR EDL

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    Gpx7 Human
  • View Data Sheet

    Name :

    SARS Nucleocaspid (2-422), HEK

    Description:

    SARS Nucleocaspid (2-422 a.a.), HEK Recombinant

    Product # :

    SARS-024

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    Description

    The HEK293 derived recombinant protein contains the SARS Coronavirus Nucleoprotein, amino acids 2-422 fused to a 6 His tag at N-terminal.

    Source

    HEK293

    Formulation

    SARS Nucleocapsid protein solution is supplied in 0.28M NaCl & 50mM HEPES pH-8.

    Purity

    Protein is >85% pure as determined SDS-PAGE.

    Citations

    More Info

    • Introduction

      SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      SARS nucleoprotein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Purification Method

      Purified by immobilized metal affinity chromatographic technique.

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

    product_image.jpg
  • View Data Sheet

    Name :

    ALDH1A1 Human, Active

    Description:

    Aldehyde Dehydrogenase 1A1 Human Recombinant, Active

    ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

    Product # :

    ENZ-1179

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    Description

    The ALDH1A1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 54.8kDa and containing 501 amino acids (1-501 a.a.).

    Source

    Escherichia Coli.

    Formulation

    The ALDH1A1 protein solution is formulated at 1mg/ml in 50mM Tris-HCl pH-7.5 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    > 700 pmol/min/ug, as determined by the increase of NADH in absorbance at 340nm resulting from the reduction of NAD at pH 8.8 at 37C.                                                                 

    Citations

    More Info

    • Introduction

      ALDH1A1 is part of the aldehyde dehydrogenases family.
      Aldehyde dehydrogenase is the 2nd protein of the main oxidative pathway of alcohol metabolism. Cytosolic and mitochondrial are 2 main liver isoforms of ALDH that are differentiateed by their electrophoretic mobility, kinetic property, & subcellular localization. The majority of Caucasians have two main isozymes, whereas just about 50% of Orientals have only the cytosolic form, excluding the mitochondrial form. ALDH1A1 is also a member of the group of corneal crystallins that assist the transparency of the cornea.
      (Retinal + NAD+ + H2O = retinoate + NADH).

    • Synonyms

      ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLYKLADLIERDR LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKIGPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN S.

    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.

    Aldh1A1 Protein
  • View Data Sheet

    Name :

    NUDT16L1 Human

    Description:

    Nudix Type Motif 16 Like-1 Human Recombinant

    Protein syndesmos, NUDT16-like protein 1, NUDT16L1, SDOS, MGC11275.

    Product # :

    ENZ-079

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    NUDT16L1 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 231 amino acids (1-211 a.a.) and having a molecular mass of 25.5kDa. The NUDT16L1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT16L1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Syndesmos (NUDT16L1) is a cytoplasmic protein which interacts specifically with the cytoplasmic domain of syndecan-4, and co-localizes with syndecan-4 in focal contacts. NUDT16L1 interacts with the focal adhesion adaptor protein paxillin. The binding of NUDT16L1 to paxillin is direct, and these interactions are triggered by the activation of protein kinase C.

    • Synonyms

      Protein syndesmos, NUDT16-like protein 1, NUDT16L1, SDOS, MGC11275.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSTAAVPELK QISRVEAMRL GPGWSHSCHA MLYAANPGQL FGRIPMRFSV LMQMRFDGLL GFPGGFVDRR FWSLEDGLNR VLGLGLGCLR LTEADYLSSH LTEGPHRVVA HLYARQLTLE QLHAVEISAV HSRDHGLEVL GLVRVPLYTQ KDRVGGFPNF LSNAFVSTAK CQLLFALKVL NMMPEEKLVE ALAAATEKQK KALEKLLPAS S.

    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.

    Nudt16L1 Human
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