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Search results

1000 results found for “phosphorylase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    UBE2K Human

    Description:

    Ubiquitin-Conjugating Enzyme E2K Human Recombinant

    HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.

    Product # :

    ENZ-339

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    • description
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    Description

    UBE2K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-200a.a.) and having a molecular mass of 26.5kDa.UBE2K is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 50mM NaCl, and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      UBE2K belongs to the ubiquitin-conjugating enzymes family which take part in many cellular processes such as selective protein degradation, DNA repair, cell cycle control, and sporulation. In this mechanism, the ATP-coupled activation and subsequent ligation of ubiquitin are catalyzed by separate enzymes functionally linked by ubiquitin carrier protein UBC1. In addition, UBE2K is involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with amyloid-?, huntingtin, and MHC-heavy chain proteins.

    • Synonyms

      HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMANI AVQRIKREFK EVLKSEETSK NQIKVDLVDE NFTELRGEIA GPPDTPYEGG RYQLEIKIPE TYPFNPPKVR FITKIWHPNI SSVTGAICLD ILKDQWAAAM TLRTVLLSLQ ALLAAAEPDD PQDAVVANQY KQNPEMFKQT ARLWAHVYAG APVSSPEYTK KIENLCAMGF DRNAVIVALS SKSWDVETAT ELLLSN.

    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.

    Ube2K Human
  • View Data Sheet

    Name :

    SURA E.Coli

    Description:

    Chaperone SURA E.Coli Recombinant

    Rotamase surA, Survival protein A.

    Product # :

    ENZ-257

    Price :

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    Description

    SURA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 429 amino acids (21-428 a.a.) and having a molecular weight of 47.3kDa. The SURA is fused to 20 a.a His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SURA 1mg/ml protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 450 nmoles/min/ug, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      SURA is a PPIase enzyme and chaperone of Escherichia coli and other Gram-negative bacteria. SURA is a key player in the biogenesis of beta-barrel outer membrane proteins and is involved in cell envelope homeostasis and cell envelope functions. SURA is necessary for the survival of E.coli in stationary phase and needed for pilus biogenesis.

    • Synonyms

      Rotamase surA, Survival protein A.

    • 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 MAPQVVDKVA AVVNNGVVLE SDVDGLMQSV KLNAAQARQQ LPDDATLRHQ IMERLIMDQI ILQMGQKMGV KISDEQLDQA IANIAKQNNM TLDQMRSRLA YDGLNYNTYR NQIRKEMIIS EVRNNEVRRR ITILPQEVES LAQQVGNQND ASTELNLSHI LIPLPENPTS DQVNEAESQA RAIVDQARNG ADFGKLAIAH SADQQALNGG QMGWGRIQEL PGIFAQALST AKKGDIVGPI RSGVGFHILK VNDLRGESKN ISVTEVHARH ILLKPSPIMT DEQARVKLEQ IAADIKSGKT TFAAAAKEFS QDPGSANQGG DLGWATPDIF DPAFRDALTR LNKGQMSAPV HSSFGWHLIE LLDTRNVDKT DAAQKDRAYR MLMNRKFSEE AASWMQEQRA SAYVKILSN.

    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.

    Sura
  • View Data Sheet

    Name :

    Urease

    Description:

    Urease Recombinant

    Product # :

    ENZ-277

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    The mutant Urease from microorganism source, showing shifted substrate affinity to urea. It was designed wildtype coding gene from microorganism. The subunit structure is very similar to well known microbial urease. Please refer to published literature such as JBC 262, 5963-67 (1987). It is composed of multi-subunits and shows a bit complex protein structure (alpha 2 Beta 4 Gamma 4) as compared to plant urease rUrease is genetically designed unique mutant having shifted high Km to urea, which is suited material to kinetic urea assay with wide measurable range. The enzyme comprises of three different subunits to make complete fully active form, 60.3 kD a subunit, 11.7 kD b subunit and 11.1 kD g subunit respectively.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 370µg Potassium Phosphate and 30µg EDTA Na2.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity was found to be 120U/mg powder.

    More Info

    • Physical Appearance

      Sterile Lyophilized Powder.

    • Stability

      Urease although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Urease in sterile 18MΩ-cm H2O.

    • Unit Definition

      One Unit oxidizes one micromole of NADH per minute at 25°C, at pH 7.6.

    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.

    Urease
  • View Data Sheet

    Name :

    MMP14 Human, His

    Description:

    Matrix Metalloproteinase-14 Human Recombinant, His Tag

    Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 1.

    Product # :

    ENZ-1003

    Price :

    Quantity :

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    • description
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    Description

    MMP14 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 527 amino acids (21-538a.a) and having a molecular mass of 59.9kDa (Molecular size on SDS-PAGE will appear at approximately 35-70kDa). MMP14 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MMP14 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Matrix metalloproteinase-14 (MMP14), is a membrane-anchored zinc-binding endopeptidase which is expressed at the leading edge of different invasive carcinomas and also promotes tumor cell invasion through degradation of the extracellular matrix. MMP14 takes a vital part in extracellular matrix, ECM, remodeling by having the capability to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules for instance CD44 and integrin alpha V. MMP14 is a key enzyme in many physiological as well as pathological processes for example angiogenesis & tumor invasion.

    • Synonyms

      Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 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

      ADLALASLGS AQSSSFSPEA WLQQYGYLPP GDLRTHTQRS PQSLSAAIAA MQKFYGLQVT GKADADTMKA MRRPRCGVPD KFGAEIKANV RRKRYAIQGL KWQHNEITFC IQNYTPKVGE YATYEAIRKA FRVWESATPL RFREVPYAYI REGHEKQADI MIFFAEGFHG DSTPFDGEGG FLAHAYFPGP NIGGDTHFDS AEPWTVRNED LNGNDIFLVA VHELGHALGL EHSSDPSAIM APFYQWMDTE NFVLPDDDRR GIQQLYGGES GFPTKMPPQP RTTSRPSVPD KPKNPTYGPN ICDGNFDTVA MLRGEMFVFK ERWFWRVRNN QVMDGYPMPI GQFWRGLPAS INTAYERKDG KFVFFKGDKH WVFDEASLEP GYPKHIKELG RGLPTDKIDA ALFWMPNGKT YFFRGNKYYR FNEELRAVDS EYPKNIKVWE GIPESPRGSF MGSDEVFTYF YKGNKYWKFN NQKLKVEPGY PKSALRDWMG CPSGGRPDEG TEEETEVIII EVDEEGGGAV SHHHHHH.

    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.

    Mmp14 Human
  • View Data Sheet

    Name :

    MDH2 Human

    Description:

    Malate Dehydrogenase 2 Human Recombinant

    M-MDH, MDH, MOR1.

    Product # :

    ENZ-247

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

      M-MDH, MDH, MOR1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Mdh2 Human
  • View Data Sheet

    Name :

    PPP1R3B Human

    Description:

    Protein Phosphatase 1, Regulatory Subunit 3B Human Recombinant

    Protein phosphatase 1 regulatory subunit 3B, Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, Protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, Protein phosphatase 1 subunit GL, PTG, PPP1R4, PPP1R3B, Protein Phosphatase 1, Regulatory Subunit 3B, GL.

    Product # :

    PRO-1700

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    Description

    PPP1R3B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285) and having a molecular mass of 35.1 kDa.PPP1R3B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPP1R3B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein Phosphatase 1, Regulatory Subunit 3B (PPP1R3B) is the catalytic subunit of the serine/theonine phosphatase, protein phosphatase-1. PPP1R3B, which is expressed both in liver and in skeletal muscle tissue, regulates glycogen synthesis in these tissues. PPP1R3B is involved in type 2 diabetes and maturity-onset diabetes of the young.

    • Synonyms

      Protein phosphatase 1 regulatory subunit 3B, Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, Protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, Protein phosphatase 1 subunit GL, PTG, PPP1R4, PPP1R3B, Protein Phosphatase 1, Regulatory Subunit 3B, GL.

    • 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 MGSMMAVDIE YRYNCMAPSL RQERFAFKIS PKPSKPLRPC IQLSSKNEAS GMVAPAVQEK KVKKRVSFAD NQGLALTMVK VFSEFDDPLD MPFNITELLD NIVSLTTAES ESFVLDFSQP SADYLDFRNR LQADHVCLEN CVLKDKAIAG TVKVQNLAFE KTVKIRMTFD TWKSYTDFPC QYVKDTYAGS DRDTFSFDIS LPEKIQSYER MEFAVYYECN GQTYWDSNRG KNYRIIRAEL KSTQGMTKPH SGPDLGISFD QFGSPRCSYG LFPEWPSYLG YEKLGPYY.

    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.

    Ppp1R3B Human
  • View Data Sheet

    Name :

    PRMT3 Human

    Description:

    Protein Arginine Methyltransferase 3 Human Recombinant

    Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.

    Product # :

    ENZ-848

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    Description

    PRMT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 554 amino acids (1-531 a.a) and having a molecular mass of 62.3kDa.PRMT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRMT3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol, 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRMT3, also known as protein arginine N-methyltransferase 3, is a member of the protein arginine methyltransferase family. PRMT3 catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. PRMT3 operates on 40S ribosomal protein S2 ,rpS2, which is the major in-vivo substrate, additionally PRMT3 is also involved in the proper maturation of the 80S ribosome.

    • Synonyms

      Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.

    • 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 MGSMCSLASG ATGGRGAVEN EEDLPELSDS GDEAAWEDED DADLPHGKQQ TPCLFCNRLF TSAEETFSHC KSEHQFNIDS MVHKHGLEFY GYIKLINFIR LKNPTVEYMN SIYNPVPWEK EEYLKPVLED DLLLQFDVED LYEPVSVPFS YPNGLSENTS VVEKLKHMEA RALSAEAALA RAREDLQKMK QFAQDFVMHT DVRTCSSSTS VIADLQEDED GVYFSSYGHY GIHEEMLKDK IRTESYRDFI YQNPHIFKDK VVLDVGCGTG ILSMFAAKAG AKKVLGVDQS EILYQAMDII RLNKLEDTIT LIKGKIEEVH LPVEKVDVII SEWMGYFLLF ESMLDSVLYA KNKYLAKGGS VYPDICTISL VAVSDVNKHA DRIAFWDDVY GFKMSCMKKA VIPEAVVEVL DPKTLISEPC GIKHIDCHTT SISDLEFSSD FTLKITRTSM CTAIAGYFDI YFEKNCHNRV VFSTGPQSTK THWKQTVFLL EKPFSVKAGE ALKGKVTVHK NKKDPRSLTV TLTLNNSTQT YGLQ

    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.

    Prmt3 Human
  • View Data Sheet

    Name :

    CDC25A Human

    Description:

    Cell Division Cycle 25A Human Recombinant

    M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.

    Product # :

    ENZ-091

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    Description

    CDC25A Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 560 amino acids (1-524 a.a.) and having a molecular mass of 63.2kDa. The CDC25A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDC25A solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 20% glycerol, 0.2M NaCl and 1mM EDTA.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      M-phase inducer phosphatase 1 (CDC25A) belongs to the CDC25 family of phosphatases. CDC25A is essential for progression from G1 to the S phase of the cell cycle. CDC25A activates the cyclin-dependent kinase CDC2 by eliminating 2 phosphate groups. CDC25A is specifically degraded in reaction to DNA damage, which inhibits cells with chromosomal abnormalities from progressing in the course of cell division. CDC25A is an oncogene, though its exact function in oncogenesis has not been determined.

    • Synonyms

      M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.

    • 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 KDRWGSMELG PEPPHRRRLL FACSPPPASQ PVVKALFGAS AAGGLSPVTN LTVTMDQLQG LGSDYEQPLE VKNNSNLQRM GSSESTDSGF CLDSPGPLDS KENLENPMRR IHSLPQKLLG CSPALKRSHS DSLDHDIFQL IDPDENKENE AFEFKKPVRP VSRGCLHSHG LQEGKDLFTQ RQNSAPARML SSNERDSSEP GNFIPLFTPQ SPVTATLSDE DDGFVDLLDG ENLKNEEETP SCMASLWTAP LVMRTTNLDN RCKLFDSPSL CSSSTRSVLK RPERSQEESP PGSTKRRKSM SGASPKESTN PEKAHETLHQ SLSLASSPKG TIENILDNDP RDLIGDFSKG YLFHTVAGKH QDLKYISPEI MASVLNGKFA NLIKEFVIID CRYPYEYEGG HIKGAVNLHM EEEVEDFLLK KPIVPTDGKR VIVVFHCEFS SERGPRMCRY VRERDRLGNE YPKLHYPELY VLKGGYKEFF MKCQSYCEPP SYRPMHHEDF KEDLKKFRTK SRTWAGEKSK REMYSRLKKL.

    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.

    Cdc25A Human
  • View Data Sheet

    Name :

    ACE2 (19-740) Human

    Description:

    Angiotensin Converting Enzyme 2 (19-740 a.a.), Human Recombinant

    Product # :

    ENZ-1122

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    Description

    The CHO derived ACE2 Human recombinant protein contains the extracellular domain amino acids 19-740 fused to Fc tag at C-terminal. ACE2 Protein binds to SARS Coronavirus-2 [ CoV-2019 ] Spike receptor binding domain.

    Source

    CHO Cells

    Formulation

    ACE2 Human protein solution is supplied in 50mM Tris-HCl, pH7.5, and 90mM glycine.

    Purity

    Protein is >95% pure as determined SDS-PAGE.

    Biological Activity

    ACE2 activity was measured by its binding ability in a functional ELISA.

    The immobilized Recombinant Human ACE2 protein binds to SARS CoV2 Spike protein Receptor Binding Domain at 2ug per ml.

    More Info

    • Introduction

      ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      ACE-2 Human Recombinant Protein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Purification Method

      Purified by Protein-G 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.

    Ace 2 Human
  • View Data Sheet

    Name :

    GSK3B Human, sf9

    Description:

    Glycogen synthase kinase-3 beta, sf9 Human Recombinant

    Glycogen synthase kinase-3 beta, GSK-3 beta, Serine/threonine-protein kinase GSK3B.

    Product # :

    PKA-084

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    Description

    GSK3B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (1-420a.a.) and having a molecular mass of 47.5kDa. GSK3B is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GSK3B protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4), 0.5mM PMSF and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GSK3B is a serine-threonine kinase that belongs to the glycogen synthase kinase subfamily. GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation. Polymorphisms in the GSK3B gene have been implicated in modifying risk of Parkinson disease, and studies in mice show that overexpression of the GSK3B gene may be significant to the pathogenesis of Alzheimer disease.

    • Synonyms

      Glycogen synthase kinase-3 beta, GSK-3 beta, Serine/threonine-protein kinase GSK3B.

    • 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

      MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF NFTTQELSSN PPLATILIPP HARIQAAAST PTNATAASDA NTGDRGQTNN AASASASNST 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.

    Gsk3B Human Sf9
  • View Data Sheet

    Name :

    tPA Human

    Description:

    Tissue Plasminogen Activator Human Recombinant

    Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.

    Product # :

    ENZ-263

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    Description

    Tissue Plasminogen Activator Human Recombinant produced in CHO cells is a single, glycosylated polypeptide chain containing 527 amino acids and having a molecular mass of 59008.71 Dalton. tPA is a serine protease enzyme that converts plasminogen to plasmin. The tPA is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells (CHO)

    Formulation

    Each mg of t-PA contains 1.7 gr L-arginine, 0.5 gr phosphoric acid and 4 mg tween 80.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
      This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

    • Synonyms

      Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Enzymatic Activity

      580,000 IU/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.

    T Pa Human
  • View Data Sheet

    Name :

    PPIL2 Human

    Description:

    Cyclophilin-60 Human Recombinant

    CYC4, Cyp-60, CYP60, hCyP-60, Peptidyl-prolyl cis-trans isomerase-like 2, PPIase, Rotamase PPIL2, Cyclophilin-60, Cyclophilin-like protein Cyp-60, PPIL2, MGC787, FLJ39930, MGC33174.

    Product # :

    ENZ-497

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    Description

    PPIL2 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 547 amino acids (1-527 a.a.) and having a molecular mass of 61.6 kDa. The PPIL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPIL2 solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 290 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      PPIL2 is part of the cyclophilin family of peptidylprolyl isomerases which are highly conserved ubiquitous proteins that play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL2 interacts with the proteinase inhibitor eglin c and is localized in the nucleus. PPIL2 increases folding of proteins andcatalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

    • Synonyms

      CYC4, Cyp-60, CYP60, hCyP-60, Peptidyl-prolyl cis-trans isomerase-like 2, PPIase, Rotamase PPIL2, Cyclophilin-60, Cyclophilin-like protein Cyp-60, PPIL2, MGC787, FLJ39930, MGC33174.

    • 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 MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK IIDPDEEKAK QDPSYYLKNT NAETRETLQE YKEFKGDEI LAATMKAPEK KKVDKLNAAH YSTGKVSASF TSTAMVPETT EAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV GKYINPAATE QQRKSPQPVP LSPCPRRSPV GVLGTSAPGS SRLPDDH.

    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.

    Ppil2 Human
  • View Data Sheet

    Name :

    UBA5 Human

    Description:

    Ubiquitin-Like Modifier Activating Enzyme 5 Human Recombinant

    Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.

    Product # :

    ENZ-602

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    Description

    UBA5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-404) and having a molecular mass of 47.4kDa.UBA5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBA5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-like modifier activating enzyme 5 (UBA5) is a member of the ubiquitin-activating E1 family and UBA5 subfamily. Ubiquitin and ubiquitin-like proteins are recognized as covalently conjugated to various cellular substrates by a three-step enzymatic pathway. The ubiquitin-activating enzyme (E1) has a vital role in the first step of ubiquitination pathway to activate ubiquitin or ubiquitin-like proteins. UBA5 activates an ubiquitin-like protein, ubiquitin-fold modifier 1 (Ufm1), by forming a high-energy thioester bond. UBA5 is located primarily in cytoplasm, while it generally localizes to the nucleus in presence of SUMO2.

    • Synonyms

      Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.

    • 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 MGSHMAESVE RLQQRVQELE RELAQERSLQ VPRSGDGGGG RVRIEKMSSE VVDSNPYSRL MALKRMGIVS DYEKIRTFAV AIVGVGGVGS VTAEMLTRCG IGKLLLFDYD KVELANMNRL FFQPHQAGLS KVQAAEHTLR NINPDVLFEV HNYNITTVEN
      FQHFMDRISN GGLEEGKPVD LVLSCVDNFE ARMTINTACN ELGQTWMESG VSENAVSGHI QLIIPGESAC FACAPPLVVA ANIDEKTLKR EGVCAASLPT TMGVVAGILV QNVLKFLLNF GTVSFYLGYN AMQDFFPTMS MKPNPQCDDR NCRKQQEEYK KKVAALPKQE VIQEEEEIIH
      EDNEWGIELV SEVSEEELKN FSGPVPDLPE GITVAYTIPK KQEDSVTELT VEDSGESLED LMAKMKNM.

    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.

    Uba5 Human
  • View Data Sheet

    Name :

    SUOX Human

    Description:

    Sulfite Oxidase Human Recombinant

    Sulfite Oxidase, EC 1.8.3.1, Sulfite oxidase, mitochondrial.

    Product # :

    ENZ-887

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    Description

    SUOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 489 amino acids (80-545 a.a) and having a molecular mass of 53.9kDa. SUOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sulfite oxidase, also known as SUOX is a homodimeric protein localized to the intermembrane space of mitochondria. Each subunit includes a heme domain as well as a molybdopterin-binding domain. The SUOX enzyme catalyzes the oxidation of sulfite to sulfate, the last reaction in the oxidative degradation of the sulfur amino acids cysteine and methionine. In addition, the deficiency of SUOX results in neurological abnormalities which are often fatal at an early age.

    • Synonyms

      Sulfite Oxidase, EC 1.8.3.1, Sulfite oxidase, 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 MGSESTHIYT KEEVSSHTSP ETGIWVTLGS EVFDVTEFVD LHPGGPSKLM LAAGGPLEPF WALYAVHNQS HVRELLAQYK IGELNPEDKV APTVETSDPY ADDPVRHPAL KVNSQRPFNA EPPPELLTEN YITPNPIFFT RNHLPVPNLD PDTYRLHVVG APGGQSLSLS LDDLHNFPRY EITVTLQCAG NRRSEMTQVK EVKGLEWRTG AISTARWAGA RLCDVLAQAG HQLCETEAHV CFEGLDSDPT GTAYGASIPL ARAMDPEAEV LLAYEMNGQP LPRDHGFPVR VVVPGVVGAR HVKWLGRVSV QPEESYSHWQ RRDYKGFSPS VDWETVDFDS APSIQELPVQ SAITEPRDGE TVESGEVTIK GYAWSGGGRA VIRVDVSLDG GLTWQVAKLD GEEQRPRKAW AWRLWQLKAP VPAGQKELNI VCKAVDDGYN VQPDTVAPIW NLRGVLSNAW HRVHVYVSP.

    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.

    Suox 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 :

    MVD Human

    Description:

    Mevalonate Decarboxylase Human Recombinant

    Diphosphomevalonate decarboxylase, Mevalonate (diphospho)decarboxylase, MDDase, Mevalonate pyrophosphate decarboxylase, MVD, MPD, FP17780.

    Product # :

    ENZ-226

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    Description

    MVD Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (1-400) and having a molecular mass of 45.6kDa.MVD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Diphosphomevalonate decarboxylase (MVD) catalyzes the conversion of mevalonate pyrophosphate into isopentenyl pyrophosphate in one of the early steps in cholesterol biosynthesis. MVD decarboxylates and dehydrates its substrate while hydrolyzing ATP. MVD is expressed in the heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta.

    • Synonyms

      Diphosphomevalonate decarboxylase, Mevalonate (diphospho)decarboxylase, MDDase, Mevalonate pyrophosphate decarboxylase, MVD, MPD, FP17780.

    • 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 MASEKPLAAV TCTAPVNIAV IKYWGKRDEE LVLPINSSLS VTLHQDQLKT TTTAVISKDF TEDRIWLNGR EEDVGQPRLQ ACLREIRCLA RKRRNSRDGD PLPSSLSCKV HVASVNNFPT AAGLASSAAG YACLAYTLAR VYGVESDLSE VARRGSGSAC RSLYGGFVEW QMGEQADGKD SIARQVAPES HWPELRVLIL VVSAEKKLTG STVGMRASVE TSPLLRFRAE SVVPARMAEM ARCIRERDFP SFAQLTMKDS NQFHATCLDT FPPISYLNAI SWRIIHLVHR FNAHHGDTKV AYTFDAGPNA VIFTLDDTVA EFVAAVWHGF PPGSNGDTFL KGLQVRPAPL SAELQAALAM EPTPGGVKYI IVTQVGPGPQ ILDDPCAHLL GPDGLPKPAA.

    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.

    Mvd Human
  • View Data Sheet

    Name :

    MAO B Human

    Description:

    Monoamine Oxidase B Human Recombinant

    Amine oxidase [flavin-containing] B, Monoamine oxidase type B, MAO-B, MAOB, MGC26382.

    Product # :

    ENZ-440

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    Description

    MAO-B Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 488 amino acids fragment (2-489) corresponding to the cytoplasmic domain fragment of the mature protein, having a total molecular mass of 59.84kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The MAO-B is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAO-B protein is supplied in 20mM Tris-HCl, pH 8.0, 250mM NaCl, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAO-B is a member of the flavin monoamine oxidase family. MAO-B (Monoamine oxidase B) is a flavin-containing mitochondrial enzyme that catalyzes the oxidative deamination of biogenic and xenobiotic monoamines. MAO-B controls the metabolic degradation of catecholamines and serotonin in neural and other target tissues. MAO-B is located in platelets and in DOPA-secreting neurons in the brain. MAOB and MAOA genes have an imperative function in DOPA degradation. Benzylamine and phenylethylamine are preferentially degraded by MAOB. The MAOB gene is linked to autistic traits, empathy and Asperger syndrome. Amplified levels of MAO B are identified in the brain of Alzheimer’s patients. High phenylethylamine levels in neonates as a result of low MAOB are consistent with phenylketonuria in newborns. Polymorphisms in MAO-B are connected to smoking behavior.

    • Synonyms

      Amine oxidase [flavin-containing] B, Monoamine oxidase type B, MAO-B, MAOB, MGC26382.

    • 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.

    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.

    Mao B Human
  • View Data Sheet

    Name :

    GSTM1 Mouse

    Description:

    Glutathione S-Transferase M1 Mouse Recombinant

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

    Product # :

    ENZ-397

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    Description

    GSTM1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 218 amino acids and having a molecular mass of 25.9 kDa.The GTM1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM1 solution contains PBS pH-7.4 & 5mM glutathione.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is 3 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK.

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    Gstm1 Mouse
  • View Data Sheet

    Name :

    Carbonic Anhydrase II E.coli

    Description:

    Carbonic Anhydrase II E.coli Recombinant

    Carbonic anhydrase 2, Carbonate dehydratase 2, can, cynT2, yadF, b0126, JW0122, Carbonic Anhydrase II.

    Product # :

    ENZ-373

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    Description

    Carbonic anhydrase II is an E.coli Recombinant protein produced in E.Coli containing 240 amino acids (1-220) and having a molecular mass of 27 kDa. Carbonic anhydrase is expressedwith an amino-terminal hexahistidine tag.The Carbonic anhydrase 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Carbonic Anhydrase 2 enzyme is supplied in 20mM Tris pH-8 and 1mM DTT.

    Purity

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

    More Info

    • Introduction

      The enzyme Carbonic anhydrase II having an accession number of NP_414668 is also called carbonate dehydratase which is part of the enzyme family that catalyses rapid inter-conversion of carbon dioxide & water to bicarbonate, carbonic acid and protons (CO2 + H2O ? HCO3? + H+), a reaction that occurs rather slowly in the absence of a catalyst. The majority of carbonic anhydrases enclose a zinc ion in their active site and therefore is classified as metalloenzymes.
      The most important function of Carbonic anhydrase is known to preserve acid-base balance in blood and other tissues, and to help transport carbon dioxide of tissues. Carbonic anhydrases have been found in all kingdoms of life. Carbonic anhydrase has 3 different classes: alpha, beta and gamma which share very little sequence or structural similarity, thus far they all perform the same function and require a zinc ion at the active site. Mammalian carbonic anhydrase is monomeric and belongs to the alpha class. Plant carbonic anhydrase is dimeric and belongs to the beta class.
      Methane-producing bacteria carbonic anhydrase is trimeric and grows in hot springs which forms the gamma class.

    • Synonyms

      Carbonic anhydrase 2, Carbonate dehydratase 2, can, cynT2, yadF, b0126, JW0122, Carbonic Anhydrase II.

    • 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 MKDIDTLISN NALWSKMLVE EDPGFFEKLAQAQKPRFLWI GCSDSRVPAE RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL HIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK.

    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.

    Carbonic Anhydrase Ii
  • View Data Sheet

    Name :

    SPOP Human

    Description:

    Speckle-Type POZ Protein Human Recombinant

    Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    Product # :

    PRO-195

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    Description

    SPOP 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 394 amino acids (1-374 a.a.) and having a molecular mass of 44.3kDa. The SPOP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPOP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 50% glycerol, 0.2M NaCl and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Speckle-type POZ protein (SPOP) belongs to the Tdpoz family containing one N-terminal MATH (Meprin and TRAF homology) domain and one C-terminal BTB/POZ domain. SPOP inhibits IPF1/PDX1 transactivation of established target promoters, may be by recruiting a repressor complex. SPOP is involved in ubiquitinylation and protein degradation as a result of an interaction with CUL-3.

    • Synonyms

      Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    • Physical Appearance

      SPOP is supplied as a 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 MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE
      VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA EAYRSLASAQ CPFLGPPRKR LKQS.

    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.

    Spop Human
  • View Data Sheet

    Name :

    ALDH2 Human

    Description:

    Aldehyde Dehydrogenase-2 Human Recombinant

    ALDM, ALDHI, ALDH-E2, MGC1806, ALDH2, Aldehyde dehydrogenase mitochondrial, ALDH class 2.

    Product # :

    ENZ-401

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    Description

    ALDH2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 501 amino acids (18-517 a.a.) & having a molecular mass of 54.5 kDa. The ALDH2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ALDH2 protein (1mg/ml) contains 20mM Tris-HCl buffer, pH-7.5, 1mM DTT, 1mM EDTA and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity was found to be > 250pmol/min/ug, and was obtained by measuring the increase of NADH in absorbance at 340 nm resulting from the reduction of NAD at pH 8.0 at 25°C.

    More Info

    • Introduction

      ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.

    • Synonyms

      ALDM, ALDHI, ALDH-E2, MGC1806, ALDH2, Aldehyde dehydrogenase mitochondrial, ALDH class 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MSAAATQAVP APNQQPEVFC NQIFINNEWH DAVSRKTFPT VNPSTGEVIC QVAEGDKEDV DKAVKAARAA FQLGSPWRRM DASHRGRLLNRLADLIERDR TYLAALETLD NGKPYVISYL VDLDMVLKCL RYYAGWADKY HGKTIPIDGD FFSYTRHEPV GVCGQIIPWN FPLLMQAWKL GPALATGNVV VMKVAEQTPL TALYVANLIK EAGFPPGVVN IVPGFGPTAG AAIASHEDVD KVAFTGSTEI GRVIQVAAGS SNLKRVTLEL GGKSPNIIMS DADMDWAVEQ AHFALFFNQG QCCCAGSRTF VQEDIYDEFV ERSVARAKSR VVGNPFDSKT EQGPQVDETQ FKKILGYINT GKQEGAKLLC GGGIAADRGY FIQPTVFGDV QDGMTIAKEE IFGPVMQILK FKTIEEVVGR ANNSTYGLAA AVFTKDLDKA NYLSQALQAGTVWVNCYDVF GAQSPFGGYK MSGSGRELGE YGLQAYTEVK TVTVKVPQKN 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.

    Aldh2 Human
  • View Data Sheet

    Name :

    GPX1 Human

    Description:

    Glutathione Peroxidase 1 Human Recombinant

    Glutathione peroxidase 1, GPx-1, GSHPx-1, Cellular glutathione peroxidase, GPX1, GPXD, GSHPX1.

    Product # :

    ENZ-186

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    Description

    GPX1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-203) and having a molecular mass of 24.2kDa.GPX1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GPX1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 30% glycerol and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutathione peroxidase 1 (GPX1) is a member of the glutathione peroxidase family, consisting of 8 identified glutathione peroxidases (Gpx1-8) in humans. Glutathione peroxidase serves in the detoxification of hydrogen peroxide, and is one of the most vital antioxidant enzymes in humans. The GPX1 is a component of the enzymatic antioxidant defense, preventing oxidative damage to DNA, proteins and lipids by detoxifying hydrogen and lipid peroxides which may contribute to prostate cancer development. GPX1 is one of only a small number of proteins known in higher vertebrates to contain selenocysteine, which occurs at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA. Furthermore, the GPX1 protein is characterized in a polyalanine sequence polymorphism in the N-terminal region, which includes 3 alleles with 5, 6 or 7 alanine (ALA) repeats in this sequence. The allele with 5 ALA repeats is significantly linked to breast cancer risk.

    • Synonyms

      Glutathione peroxidase 1, GPx-1, GSHPx-1, Cellular glutathione peroxidase, GPX1, GPXD, GSHPX1.

    • 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 MCAARLAAAA AAAQSVYAFS ARPLAGGEPV SLGSLRGKVL LIENVASLCG TTVRDYTQMN ELQRRLGPRG LVVLGFPCNQ FGHQENAKNE EILNSLKYVR PGGGFEPNFM LFEKCEVNGA GAHPLFAFLR EALPAPSDDA TALMTDPKLI TWSPVCRNDV AWNFEKFLVG PDGVPLRRYS RRFQTIDIEP DIEALLSQGP SCA.

    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.

    Gpx1 Human
  • View Data Sheet

    Name :

    UBE2R2 Human

    Description:

    Ubiquitin Conjugating Enzyme E2R 2 Human Recombinant

    CDC34B, E2-CDC34B, UBC3B, Ubiquitin carrier protein R2, Ubiquitin-conjugating enzyme E2-CDC34B, Ubiquitin-protein ligase R2, Ubiquitin-conjugating enzyme E2 R2, EC 6.3.2.19.

    Product # :

    ENZ-511

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    Description

    UBE2R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 amino acids (1-238 a.a) and having a molecular mass of 29.6kDa (Molecular size on SDS-PAGE will appear higher).UBE2R2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2R2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-conjugating enzyme E2 R2 (UBE2R2) is a member of the ubiquitin-conjugating enzyme family. Protein kinase CK2 is a ubiquitous and pleiotropic Ser/Thr protein kinase implicated in cell growth andtransformation. This protein is a protein similar to the E2 ubiquitin conjugating enzyme UBC3/CDC34. Studies propose that CK2-dependent phosphorylation of this ubiquitin-conjugating enzyme functions by regulating beta-TrCP substrate recognition and induces its interaction with beta-TrCP, enhancing beta-catenin degradation. UBE2R2 receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. UBE2R2 may be implicated in degradation of katenin. Among the diseases associated with UBE2R2 are cblc, and herpes simplex.

    • Synonyms

      CDC34B, E2-CDC34B, UBC3B, Ubiquitin carrier protein R2, Ubiquitin-conjugating enzyme E2-CDC34B, Ubiquitin-protein ligase R2, Ubiquitin-conjugating enzyme E2 R2, EC 6.3.2.19.

    • 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 MGSMAQQQMT SSQKALMLEL KSLQEEPVEG FRITLVDESD LYNWEVAIFG PPNTLYEGGY FKAHIKFPID YPYSPPTFRF LTKMWHPNIY ENGDVCISIL HPPVDDPQSG ELPSERWNPT QNVRTILLSV ISLLNEPNTF SPANVDASVM FRKWRDSKGK DKEYAEIIRK QVSATKAEAE KDGVKVPTTL AEYCIKTKVP SNDNSSDLLY DDLYDDDIDD EDEEEEDADC YDDDDSGNEE 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.

    Ube2R2 Human
  • View Data Sheet

    Name :

    ALDH3A1 Human

    Description:

    Aldehyde Dehydrogenase 3 Family Member A1 Human Recombinant

    Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.

    Product # :

    ENZ-479

    Price :

    Quantity :

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    More Info

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

    Description

    ALDH3A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 473 amino acids (1-453 a.a.) and having a molecular mass of 52.5 kDa. ALDH3A1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ALDH3A1 solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity was found to be < 1 units/ml. Activity was obtained by measuring the increase of NADP in absorbance at 340 nm resulting from the reduction of NAD. 1 unit will oxidize 1umole of acetaldehyde to acetic acid per minute at pH 8 at 25°C in the presence of beta-NAD, potassium and thiols.

    More Info

    • Introduction

      ALDH3A1 is involved in the detoxification of alcohol-derived acetaldehyde. ALDH3A1 participates in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. ALDH3A1 oxidizes aromatic aldehyde substrates and toxic aldehydes. ALDH3A1 forms a cytoplasmic homodimer that oxidizes aromatic and medium-chain saturated and unsaturated aldehyde substrates. ALDH3A1 promotes resistance to UV and 4-hydroxy-2-nonenal-induced oxidative damage in the cornea.

    • Synonyms

      Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA DLHKNEWNAY YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI HSEPLGVVLV IGTWNYPFNL TIQPMVGAIA AGNAVVLKPS ELSENMASLL ATIIPQYLDK DLYPVINGGV PETTELLKER FDHILYTGST GVGKIIMTAA AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS GQTCVAPDYI LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVLPIVCVRSLEE AIQFINQREK PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL PFGGVGNSGM GSYHGKKSFE TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM TQH.

    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.

    Aldh3A1 Human
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