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Search results

1000 results found for “Chitinase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    HDAC8 Human

    Description:

    Histone Deacetylase 8 Human Recombinant

    Histone deacetylase 8, HD8, HDAC8, HDACL1, CDA07, RPD3.

    Product # :

    ENZ-210

    Price :

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    Description

    HDAC8 Human Recombinant produced in Sf9 Baculovirus cells, glycosylated polypeptide chain containing 383 amino acids (1-377) and having a molecular mass of 42.6kDa. HDAC8 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The HDAC8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.

    • Synonyms

      Histone deacetylase 8, HD8, HDAC8, HDACL1, CDA07, RPD3.

    • 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

      MEEPEEPADS GQSLVPVYIY SPEYVSMCDS LAKIPKRASM VHSLIEAYAL HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDDDH PDSIEYGLGY DCPATEGIFD YAAAIGGATI TAAQCLIDGM CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFE RILYVDLDLH HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDGIQDEKY YQICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWQLATLI LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH RIQQILNYIK GNLKHVVHHH HHH.

    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.

    Hdac8 Human
  • View Data Sheet

    Name :

    UBE2L3 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant

    Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    Product # :

    ENZ-342

    Price :

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    Description

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids & having a molecular mass of 17.9 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 50mM HEPES (pH-7.5) 150mM NaCl, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Human Ubquitin-conjugating enzyme 7 (UbcH7) is a ubiquitin-conjugating enzyme (E2) mediating c-fos degradation, transcription factor NF-B maturation, and human papilloma virus-mediated p53 and Myc protein degradation, in vitro. The ubiquitin-conjugating enzymes (E2s) are essential components of the post-translational protein ubiquitination pathway, mediating the transfer of activated ubiquitin to substrate proteins. The human UBE2L1-UBE2L4 gene could potentially encode different isoforms of the UbcH7. UBE2L3 gene, located at chromosome 22q11.2, is the only identical family member with introns and encodes a polypeptide sequence identical to that of UbcH7.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    • 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

      MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD.

    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.

    Ube2L3 Human
  • View Data Sheet

    Name :

    UBE2V2 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2 Variant 2 Human Recombinant

    DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.

    Product # :

    ENZ-550

    Price :

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    • More Info

    Description

    UBE2V2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145 a.a.) and having a molecular mass of 18.5 kDa. The UBE2V2 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2V2 Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2V2 comprises a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes however require the conserved cysteine residue that is vital for the catalytic activity of E2s. UBE2V2 shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product. UBE2V2 participates in the differentiation of monocytes and enterocytes.

    • Synonyms

      DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.

    • 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 MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ ELRRLMMSKE NMKLPQPPEG QTYNN.

    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.

    Ube2V2 Human
  • 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

    Price :

    Quantity :

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

    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.

    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 :

    UFC1 Human

    Description:

    Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant

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

    Product # :

    ENZ-138

    Price :

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      UFC1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

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

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    Ufc1 Human
  • View Data Sheet

    Name :

    GLYAT Human

    Description:

    Glycine-N-Acyltransferase Human Recombinant

    Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.

    Product # :

    ENZ-148

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    Description

    GLYAT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 36.0 kDa.The GLYAT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLYAT protein (0.5mg/ml) is supplied in 20mM Tris-HCl, pH-8, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLYAT is a mitochondrial acyltransferase that conjugates glycine with acyl-CoA substrates in the mitochondria. GLYAT is vital to the detoxification of endogenous and xenobiotic acyl-CoA's.

    • Synonyms

      Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.

    • Physical Appearance

      GLYAT is supplied as a 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 MMLPLQGAQM LQMLEKSLRK SLPASLKVYG TVFHINHGNP FNLKAVVDKW PDFNTVVVCP QEQDMTDDLD HYTNTYQIYS KDPQNCQEFL GSPELINWKQ HLQIQSSQPS LNEAIQNLAA IKSFKVKQTQ RILYMAAETA KELTPFLLKS KILSPSGGKP KAINQEMFKL SSMDVTHAHL VNKFWHFGGN ERSQRFIERC IQTFPTCCLL GPEGTPVCWD LMDQTGEMRM AGTLPEYRLH GLVTYVIYSH AQKLGKLGFP VYSHVDYSNE AMQKMSYTLQ HVPIPRSWNQ WNCVPL.

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    Glyat Human
  • View Data Sheet

    Name :

    UBE2H Human

    Description:

    Ubiquitin-Conjugating Enzyme E2H Human Recombinant

    Ubiquitin-conjugating enzyme E2 H, UbcH2, Ubiquitin carrier protein H, Ubiquitin-conjugating enzyme E2-20K, Ubiquitin-protein ligase H, UBE2H, GID3, UBC8, UBCH.

    Product # :

    ENZ-603

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    Description

    UBE2H Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-183) and having a molecular mass of 23.1kDa.UBE2H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2H solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-conjugating enzyme E2 H (UBE2H) is a member of the ubiquitin-conjugating enzyme family. Protein modification with ubiquitin is a vital cellular apparatus for directing abnormal or short-lived proteins for degradation. Ubiquitination requires at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2H receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2H protein sequence is 100% identical to the mouse homolog and 98% identical to the frog and zebrafish homologs.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 H, UbcH2, Ubiquitin carrier protein H, Ubiquitin-conjugating enzyme E2-20K, Ubiquitin-protein ligase H, UBE2H, GID3, UBC8, UBCH.

    • 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 MGSMSSPSPG KRRMDTDVVK LIESKHEVTI LGGLNEFVVK FYGPQGTPYE GGVWKVRVDL PDKYPFKSPS IGFMNKIFHP NIDEASGTVC LDVINQTWTA LYDLTNIFES FLPQLLAYPN PIDPLNGDAA AMYLHRPEEY KQKIKEYIQK YATEEALKEQ EEGTGDSSSE SSMSDFSEDE AQDMEL.

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    Ube2H Human
  • View Data Sheet

    Name :

    MTHFS Human

    Description:

    5,10-Methenyltetrahydrofolate Synthetase Human Recombinant

    5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.

    Product # :

    ENZ-096

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    Description

    MTHFS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-203a.a.) and having a molecular mass of 25.4 kDa. MTHFS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MTHFS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 5mM DTT and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MTHFS is a cytosolic protein which takes part in the formate metabolic process. MTHFS along with a magnesium cofactor catalyzes the ATP-dependent reaction which reduces 5-formyltetrahydrofolate (5-MTHF) to 5,10-methenyltetrahydrofolate(MTHF). MTHF is the substrate used by MTHFR (methylenetetrahydrofolate reductase) to generate 5-MTHF. In addition, MTHF is a coenzyme used in thymidine biosynthesis by thymidylate synthase (FAD).

    • Synonyms

      5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAAAAVSSAK RSLRGELKQR LRAMSAEERL RQSRVLSQKV IAHSEYQKSK RISIFLSMQD EIETEEIIKD IFQRGKICFI PRYRFQSNHM DMVRIESPEE ISLLPKTSWN IPQPGEGDVR EEALSTGGLD LIFMPGLGFD KHGNRLGRGK GYYDAYLKRC LQHQEVKPYT LALAFKEQIC LQVPVNENDM KVDEVLYEDS STA

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    Mthfs Human
  • View Data Sheet

    Name :

    CKMT3 Human

    Description:

    Creatine Kinase Muscle Type-3 Human Recombinant

    Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.

    Product # :

    CKI-272

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    Description

    CKMT3 Human Recombinant produced in Pichia Pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to MM Isoenzyme in ELISA.The CKMT3 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    Each mg of protein contains 20mM Tris pH-8, 1mM EDTA and 1mM DTT.

    Purity

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

    Biological Activity

    The biological activity measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 500 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 2,000ng/ml.

    More Info

    • Introduction

      The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

    • Synonyms

      Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. Please prevent 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.

    Ckmmitiii Human
  • View Data Sheet

    Name :

    PYGL Human

    Description:

    Phosphorylase, Glycogen, Liver Human Recombinant

    GSD6, Glycogen phosphorylase, liver form.

    Product # :

    ENZ-675

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    Description

    PYGL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 879 amino acids (1-847 a.a) and having a molecular mass of 100.7kDa.PYGL is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PYGL protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.

    • Synonyms

      GSD6, Glycogen phosphorylase, liver form.

    • 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 MGSEFELRRQ ASMAKPLTDQ EKRRQISIRG IVGVENVAEL KKSFNRHLHF TLVKDRNVAT TRDYYFALAH TVRDHLVGRW IRTQQHYYDK CPKRVYYLSL EFYMGRTLQN TMINLGLQNA CDEAIYQLGL DIEELEEIEE DAGLGNGGLG RLAACFLDSM ATLGLAAYGY GIRYEYGIFN QKIRDGWQVE EADDWLRYGN PWEKSRPEFM LPVHFYGKVE HTNTGTKWID TQVVLALPYD TPVPGYMNNT VNTMRLWSAR APNDFNLRDF NVGDYIQAVL DRNLAENISR VLYPNDNFFE GKELRLKQEY FVVAATLQDI IRRFKASKFG STRGAGTVFD AFPDQVAIQL NDTHPALAIP ELMRIFVDIE KLPWSKAWEL TQKTFAYTNH TVLPEALERW PVDLVEKLLP RHLEIIYEIN QKHLDRIVAL FPKDVDRLRR MSLIEEEGSK RINMAHLCIV GSHAVNGVAK IHSDIVKTKV FKDFSELEPD KFQNKTNGIT PRRWLLLCNP GLAELIAEKI GEDYVKDLSQ LTKLHSFLGD DVFLRELAKV KQENKLKFSQ FLETEYKVKI NPSSMFDVQV KRIHEYKRQL LNCLHVITMY NRIKKDPKKL FVPRTVIIGG KAAPGYHMAK MIIKLITSVA DVVNNDPMVG SKLKVIFLEN YRVSLAEKVI PATDLSEQIS TAGTEASGTG NMKFMLNGAL TIGTMDGANV EMAEEAGEEN LFIFGMRIDD VAALDKKGYE AKEYYEALPE LKLVIDQIDN GFFSPKQPDL FKDIINMLFY HDRFKVFADY EAYVKCQDKV SQLYMNPKAW NTMVLKNIAA SGKFSSDRTI KEYAQNIWNV EPSDLKISLS NESNKVNGN.

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    Pygl Human
  • View Data Sheet

    Name :

    FTCD Human

    Description:

    Formiminotransferase Cyclodeaminase Human Recombinant

    Formiminotransferase-cyclodeaminase, FTCD, LCHC1, LC-1.

    Product # :

    ENZ-302

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    Description

    Formiminotransferase Cyclodeaminase Human Recombinant (also called liver cytosol type 1) produced in SF9, is a glycosylated, polypeptide chain having a molecular mass of 59,749 Dalton.The FTCD is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    FTCD is supplied in 16mM HEPES buffer pH-7.6, 240mM sodium chloride, and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Formiminotransferase cyclodeaminase is an enzyme which catalyzes the conversion of formiminoglutamateand tetrahydrofolateinto formiminotetrahydrofolateand glutamate.
      Formiminotransferase cyclodeaminase, a bifunctional enzyme of tetrahydrofolate synthesis, is the target antigen of anti-LC1 (liver cytosol antigen type 1) autoantibodies. Presence of LC1 autoantibodies is a marker for type 2 autoimmune hepatitis (for which anti-LKM 1/cytochrome P450 2D6 autoantibodies are a further marker).
      Serum LC1 autoantibody concentrations appear to fluctuate in parallel with aminotransferase levels, a particularly intriguing observation that suggests a possible role of LC1 autoreactivity in the pathogenic mechanism leading to hepatocyte injury.

    • Synonyms

      Formiminotransferase-cyclodeaminase, FTCD, LCHC1, LC-1.

    • Stability

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

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels, immuno-dot test).

    • coating concentration

      0.35-0.7 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.

    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.

    Ftcd Hunan
  • View Data Sheet

    Name :

    UBE2L3 Human His

    Description:

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant, His Tag

    Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    Product # :

    ENZ-344

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    Description

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.coli is an 18.9 kDa protein containing 162 amino acids.The UBE2L3 protein contains 6xHis tag and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated (1 mg/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.

    More Info

    • Introduction

      Human Ubquitin Conjugating Enzyme 7 (UbcH7) is a class I enzyme which functions in the stress response and the control of transcription factors. The enzyme is ubiquitously expressed with high levels of expression seen in adult muscle. UbcH7 mediates the selective degradation of short-lived and abnormal proteins and is highly homologous to UbcH5. It has been demonstrated to participate in the ubiquitinylation of p53, c-Fos and NF-?B. UbcH7 is one of two E2s (UbcH5 being the other) with which HECT domain proteins interact with UbcH7 being able to efficiently substitute for UbcH5 in E6-AP-dependent ubiquitinylation.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized UBE2L3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2L3 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 UBE2L3 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHAMAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVP
      DNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAEN
      WKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFT
      KKYGEKRPVD.

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    Ube2L3 Human His
  • View Data Sheet

    Name :

    MPI Human

    Description:

    Mannose Phosphate Isomerase Human Recombinant

    Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.

    Product # :

    ENZ-169

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    Description

    MPI Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 382 amino acids (1-362) and having a molecular mass of 41.9 kDa.The MPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MPI solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MPI is a member of the mannose-6-phosphate isomerase type 1 family. Although MPI is expressed in all tissues, it can be found more abundantly in heart, brain and skeletal muscle. Localized to the cytoplasm, MPI exploits zinc as a cofactor and catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate. Mutations in the MPI gene are the cause of carbohydrate-deficient glycoprotein syndrome, type Ib.

    • Synonyms

      Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.

    • 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 MAAPRVFPLS CAVQQYAWGK MGSNSEVARL LASSDPLAQI AEDKPYAELW MGTHPRGDAK ILDNRISQKT LSQWIAENQD SLGSKVKDTF NGNLPFLFKV LSVETPLSIQ AHPNKELAEK LHLQAPQHYP DANHKPEMAI ALTPFQGLCG FRPVEEIVTF LKTAAGNNME DIFGELLLQL HQQYPGDIGC FAIYFLNLLT LKPGEAMFLE ANVPHAYLKG DCVECMACSD NTVRAGLTPK FIDVPTLCEM LSYTPSSSKD RLFLPTRSQE DPYLSIYDPP VPDFTIMKTE VPGSVTEYKV LALDSASILL MVQGTVIAST PTTQTPIPLQ RGGVLFIGAN ESVSLKLTEP KDLLIFRACC LL

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    Mpi Human
  • View Data Sheet

    Name :

    PAP Human

    Description:

    Prostate Acid Phosphatase Human

    Product # :

    ENZ-1171

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    Description

    Human Prostate Acid Phosphatase produced in Pooled human seminal fluid having a molecular mass of approximately 100kD.

    Source

    Pooled human seminal fluid.

    Formulation

    PAP Human is lyophilized (0.2 µm filtered) from 0.02M NH4HCO3.

    Purity

    Greater than 96.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prostatic acid phosphatase, also known as PAP, is an enzyme produced by the prostate. PAP may be found in increased amounts in men with prostate cancer.
      PAP’s physiological function may be associated with the liquefaction process of semen.
      The highest levels of PAP are found in metastasized prostate cancer. Diseases of the bone, such as Paget's disease or hyperparathyroidism, diseases of blood cells (sickle-cell disease) or multiple myeloma or lysosomal storage diseases (Gaucher's disease), will show moderately higher levels.
      Certain medications can cause temporary changes in PAP levels. Manipulation of the prostate gland through rectal exam, biopsy or massage may increase the level.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      PAP Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.

    • Solubility

      It is recommended to reconstitute the lyophilized PAP Human in phosphate buffer containing 0.15M NaCl.

    • Human Virus Test

      Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, Hepatitis C antibodies and Syphilis.

    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.

    Prostate Acid Phosphatase
  • View Data Sheet

    Name :

    PHPT1 Human, Active

    Description:

    Phosphohistidine Phosphatase 1 Human Recombinant, Active

    PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    Product # :

    ENZ-1041

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    Description

    PHPT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-125a.a.) and having a molecular mass of 15.9kDa.PHPT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHPT1 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >120 units/mg, and is defined as the amount of enzyme that hydrolyze 1nmol f p-nitrophenyl phosphate per minute at pH7.5 at 37°C.

    More Info

    • Introduction

      PHPT1 is a member of the Janus protein familyand is 125 amino acid long. PHPT1 appears as a monomer in the cytoplasm and is an EDTA-insensitive phosphohistidine phosphatase. Overexpression of PHPT1 resolts in specific phosphohistidine phosphatase activity towards phosphopeptide I, with no activity detected towards phosphotyrosine, phosphothreonine and phosphoserine peptides.

    • Synonyms

      PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    • 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 MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW ANDGY.

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    Phpt1 Human Active
  • View Data Sheet

    Name :

    KMT5A Human

    Description:

    Lysine Methyltransferase 5A Human Recombinant

    KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.

    Product # :

    ENZ-1080

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    Description

    KMT5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 165 amino acids (195-352 a.a.) and having a molecular mass of 18.9kDa (Migrates at 18-28 kDa on SDS-PAGE under reducing conditions).KMT5A is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KMT5A protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 5mM DTT, 0.2M NaCl, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lysine Methyltransferase 5A (KMT5A) is an enzyme which catalyzes both histones and non-histone proteins. KMT5A contributes to the maintenance of proper higher-order structure of DNA during mitosis. KMT5A takes part in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. KMT5A plays a role as a barrier to prevent cellular senescence through chromatinmediated regulation of senescence-associated metabolic remodeling. KMT5A mediates monomethylation of p53/TP53 at 'Lys-382', which leads to repress p53/TP53-target genes. The loss of KMT5A simultaneously stimulate nucleolar function and retinoblastoma protein-mediated mitochondrial metabolism.

    • Synonyms

      KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.

    • 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

      MKAELQSEER KRIDELIESG KEEGMKIDLI DGKGRGVIAT KQFSRGDFVV EYHGDLIEIT DAKKREALYA QDPSTGCYMY YFQYLSKTYC VDATRETNRL GRLINHSKCG NCQTKLHDID GVPHLILIAS RDIAAGEELL YDYGDRSKAS IEAHPWLKHH HHHHH.

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    Kmt5A Human
  • View Data Sheet

    Name :

    UBE2Z Human

    Description:

    Ubiquitin Conjugating Enzyme E2Z Human Recombinant

    HOYS7, USE1, Ubiquitin-conjugating enzyme E2 Z, E2 ubiquitin-conjugating enzyme Z, Uba6-specific E2 conjugating enzyme 1, Ubiquitin carrier protein Z, Ubiquitin-protein ligase Z, UBE2Z.

    Product # :

    ENZ-804

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    Description

    UBE2Z Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-246a.a) and having a molecular mass of 30.5kDa. UBE2Z is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2Z solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin Conjugating Enzyme E2Z, also known as UBE2z, is a protein coding gene which is a part of the ubiquitin-conjugating enzyme family. UBE2z catalyzes the covalent attachment of ubiquitin to various proteins. UBE2z takes part in in apoptosis regulation and is also a specific substrate for UBA6, not charged with ubiquitin by UBE1.

    • Synonyms

      HOYS7, USE1, Ubiquitin-conjugating enzyme E2 Z, E2 ubiquitin-conjugating enzyme Z, Uba6-specific E2 conjugating enzyme 1, Ubiquitin carrier protein Z, Ubiquitin-protein ligase Z, UBE2Z.

    • 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 MGSMSIYKEP PPGMFVVPDT VDMTKIHALI TGPFDTPYEG GFFLFVFRCP PDYPIHPPRV KLMTTGNNTV RFNPNFYRNG KVCLSILGTW TGPAWSPAQS ISSVLISIQS LMTENPYHNE PGFEQERHPG DSKNYNECIR HETIRVAVCD MMEGKCPCPE PLRGVMEKSF LEYYDFYEVA CKDRLHLQGQ TMQDPFGEKR GHFDYQSLLM RLGLIRQKVL ERLHNENAEM DSDSSSSGTE TDLHGSLRV.

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    Ube2Z Human
  • View Data Sheet

    Name :

    Luciferase Firefly

    Description:

    Luciferin 4-Monooxygenase Firefly Recombinant

    Luciferase-like monooxygenase, LUC, EC 1.13.12.7.

    Product # :

    ENZ-553

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    Description

    Luciferase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-550 a.a.) and having a molecular mass of 62.9kDa.Luciferase is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.

    • Synonyms

      Luciferase-like monooxygenase, LUC, EC 1.13.12.7.

    • 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 MMEDAKNIKK GPAPFYPLED GTAGEQLHKA MKRYALVPGT IAFTDAHIEV DITYAEYFEM SVRLAEAMKR YGLNTNHRIV VCSENSLQFF MPVLGALFIG VAVAPANDIY NERELLNSMG ISQPTVVFVS KKGLQKILNV QKKLPIIQKI IIMDSKTDYQ GFQSMYTFVT SHLPPGFNEY DFVPESFDRD KTIALIMNSS GSTGLPKGVA LPHRTACVRF SHARDPIFGN QIIPDTAILS VVPFHHGFGM FTTLGYLICG FRVVLMYRFE EELFLRSLQD YKIQSALLVP TLFSFFAKST LIDKYDLSNL HEIASGGAPL SKEVGEAVAK RFHLPGIRQG YGLTETTSAI LITPEGDDKP GAVGKVVPFF EAKVVDLDTG KTLGVNQRGE LCVRGPMIMS GYVNNPEATN ALIDKDGWLH SGDIAYWDED EHFFIVDRLK SLIKYKGYQV APAELESILL QHPNIFDAGV AGLPDDDAGE LPAAVVVLEH GKTMTEKEIV DYVASQVTTA KKLRGGVVFV DEVPKGLTGK LDARKIREIL IKAKKGGKIA V.

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    Luciferase Firefly
  • View Data Sheet

    Name :

    Lysostaphin

    Description:

    Lysostaphin Recombinant

    Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    Product # :

    ENZ-269

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    Description

    Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized without any additives.

    Purity

    98% as determined by RP-HPLC.

    Biological Activity

    Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C.  Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.

    More Info

    • Introduction

      Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.

    • Synonyms

      Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.

    • Protein content

      Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.

    • Specific Activity

      Determined to be 3,540 units/mg.

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    Lysostaphin
  • View Data Sheet

    Name :

    ACPP Mouse

    Description:

    Acid Phosphatase Prostate Mouse Recombinant

    acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.

    Product # :

    ENZ-1157

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    Description

    ACPP Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (32-381 aa) and having a molecular mass of 41.3kDa.ACPP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The ACPP solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >80,000 unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37C.

    More Info

    • Introduction

      Prostatic Acid Phosphatase or ACPP is part of a family of proteins called histidine acid phosphatase. ACPP enhances the hydrolyzation of many phosphate monoesters and proteins that are phosphorylated. In order to function best, ACPP needs a range of range of 4-6 pH, furthermore, L(+)-tartrate inhibits ACPP’s catalyzation. This enzyme can act as a lipid phosphatase as well and can inhibit lysophosphatidic acid in seminal plasma.

    • Synonyms

      acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.

    • 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

      KELKFVTLVF RHGDRGPIET FPTDPITESS WPQGFGQLTQ WGMEQHYELG SYIRKRYGRF LNDTYKHDQI YIRSTDVDRT LMSAMTNLAA LFPPEGISIW NPRLLWQPIP VHTVSLSEDR LLYLPFRDCP RFEELKSETL ESEEFLKRLH PYKSFLDTLS SLSGFDDQDL FGIWSKVYDP LFCESVHNFT LPSWATEDAM IKLKELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILKNMK LATQPQKYKK LVMYSAHDTT VSGLQMALDV YNGVLPPYAS CHMMELYHDK GGHFVEMYYR NETQNEPYPL TLPGCTHSCP LEKFAELLDP VISQDWATEC MATSSHQGRN HHHHHH.

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    Acpp Mouse
  • View Data Sheet

    Name :

    UBE2W Human

    Description:

    Ubiquitin Conjugating Enzyme E2W Human Recombinant

    Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.

    Product # :

    ENZ-117

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    Description

    UBE2W produced in E.Coli is a single, non-glycosylated polypeptide chain containing 171 amino acids (1-151 a.a.) and having a molecular mass of 19.5kDa.UBE2W is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2W solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2W receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2W catalyzes monoubiquitination and 'Lys-11'-linked polyubiquitination. UBE2W is broadly expressed, particularly at highest levels in the testis.

    • Synonyms

      Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      UBE2W Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C.

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    Ube2W Human
  • View Data Sheet

    Name :

    DIMT1 Human

    Description:

    DIM1 Dimethyladenosine Transferase 1 Human Recombinant

    Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.

    Product # :

    ENZ-628

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    Description

    DIMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-313) and having a molecular mass of 37.5kDa.DIMT1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DIMT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 30% glycerol, 2mM DTT, 200mM NaCl and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.

    • Synonyms

      Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.

    • 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 MMPKVKSGAI GRRRGRQEQR RELKSAGGLM FNTGIGQHIL KNPLIINSII DKAALRPTDV VLEVGPGTGN MTVKLLEKAK KVVACELDPR LVAELHKRVQ GTPVASKLQV LVGDVLKTDL PFFDTCVANL PYQISSPFVF KLLLHRPFFR CAILMFQREF ALRLVAKPGD KLYCRLSINT QLLARVDHLM KVGKNNFRPP PKVESSVVRI EPKNPPPPIN FQEWDGLVRI TFVRKNKTLS AAFKSSAVQQ LLEKNYRIHC SVHNIIIPED FSIADKIQQI LTSTGFSDKR ARSMDIDDFI RLLHGFNAEG IHFS.

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    Dimt1 Human
  • View Data Sheet

    Name :

    UBE2S Human

    Description:

    Ubiquitin Conjugating Enzyme E2S Human Recombinant

    Ubiquitin-conjugating enzyme E2 S, Ubiquitin-protein ligase S, Ubiquitin carrier protein S, Ubiquitin-conjugating enzyme E2-24 kDa, E2-EPF5, E2-EPF, UBE2S, E2EPF, EPF5.

    Product # :

    ENZ-444

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    Description

    UBE2S Human Recombinant fused with a 36 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 258 amino acids (1-222 a.a.) and having a molecular mass of 27.9kDa.The UBE2S is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2S solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Ubiquitin-conjugating enzyme E2S (UBE2S) belongs to the ubiquitin-conjugating enzyme family. UBE2S is able to form a thiol ester linkage with ubiquitin in a ubiquitin activating enzyme-dependent manner, a typical property of ubiquitin carrier proteins. UBE2S catalyzes the covalent attachment of ubiquitin to other proteins. UBE2S acts as a crucial factor of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by purposely elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, augmenting the degradation of APC/C substrates by the proteasome and promoting mitotic exit. UBE2S also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is nevertheless uncertain whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and consequent degradation of VHL, resulting in an accumulation of HIF1A.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 S, Ubiquitin-protein ligase S, Ubiquitin carrier protein S, Ubiquitin-conjugating enzyme E2-24 kDa, E2-EPF5, E2-EPF, UBE2S, E2EPF, EPF5.

    • 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 KDRWGSMNSN VENLPPHIIR LVYKEVTTLT ADPPDGIKVF PNEEDLTDLQ VTIEGPEGTP YAGGLFRMKL LLGKDFPASP PKGYFLTKIF HPNVGANGEI CVNVLKRDWT AELGIRHVLL TIKCLLIHPN PESALNEEAG RLLLENYEEY AARARLLTEI HGGAGGPSGR AEAGRALASG TEASSTDPGA PGGPGGAEGP MAKKHAGERD KKLAAKKKTD KKRALRRL.

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    Ube2S Human
  • View Data Sheet

    Name :

    DECR2 Human

    Description:

    2,4-Dienoyl CoA Reductase 2 Human Recombinant

    Peroxisomal 2,4-dienoyl-CoA reductase, pDCR, 2,4-dienoyl-CoA reductase 2, DECR2, PDCR, SDR17C1.

    Product # :

    ENZ-211

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    Description

    DECR2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 33.2kDa.DECR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DECR2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peroxisomal 2,4-dienoyl-CoA reductase (DECR2) is an supporting enzyme of beta-oxidation. DECR2 partakes in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. DECR2 catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.

    • Synonyms

      Peroxisomal 2,4-dienoyl-CoA reductase, pDCR, 2,4-dienoyl-CoA reductase 2, DECR2, PDCR, SDR17C1.

    • 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 MGSMAQPPPD VEGDDCLPAY RHLFCPDLLR DKVAFITGGG SGIGFRIAEI FMRHGCHTVI ASRSLPRVLT AARKLAGATG RRCLPLSMDV RAPPAVMAAV DQALKEFGRI DILINCAAGN FLCPAGALSF NAFKTVMDID TSGTFNVSRV LYEKFFRDHG GVIVNITATL GNRGQALQVH AGSAKAAVDA MTRHLAVEWG PQNIRVNSLA PGPISGTEGL RRLGGPQASL STKVTASPLQ RLGNKTEIAH SVLYLASPLA SYVTGAVLVA DGGAWLTFPN GVKGLPDFAS FSAKL.

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    Decr2 Human
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