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Search results

1000 results found for “endonuclease”

Name

Description

Product #

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  • View Data Sheet

    Name :

    PRCP Human

    Description:

    Prolylcarboxypeptidase Human Recombinant

    Angiotensinase-C, PRCP, Proline Carboxypeptidase.

    Product # :

    ENZ-1178

    Price :

    Quantity :

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    • source
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    • More Info

    Description

    PRCP Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-496 a.a) containing a total of 481 amino acids, having a molecular mass of 54.3 kDa. PRCP is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The PRCP solution (0.25mg/ml) contains 30% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3,000 pmol/min/μg, and is defined as the amount of enzyme that converts 1pmole of Z-ProAla-OH/min. at pH-4 at 25˚C.

    More Info

    • Introduction

      PRCP is a plasma protein which takes part in the cleavage of C-terminal amino acids linked to proline in proteinfor example angiotensin-2 & 3 at acidic pHenvironment rather than at neutral pHwhich exhibit less activity. This cleavage is important since Angiotensin-2 takes part in regulation of blood pressure & electrolyte balance which is essential to hypertension.

    • Synonyms

      Angiotensinase-C, PRCP, Proline Carboxypeptidase.

    • 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

      LRPALRALGS LHLPTNPTSL PAVAKNYSVL YFQQKVDHFG FNTVKTFNQR YLVADKYWKK NGGSILFYTG NEGDIIWFCN NTGFMWDVAE ELKAMLVFAE HRYYGESLPF GDNSFKDSRH LNFLTSEQAL ADFAELIKHL KRTIPGAENQ PVIAIGGSYG GMLAAWFRMK YPHMVVGALA ASAPIWQFED LVPCGVFMKI VTTDFRKSGP HCSESIHRSW DAINRLSNTG SGLQWLTGALHLCSPLTSQD IQHLKDWISE TWVNLAMVDY PYASNFLQPL PAWPIKVVCQ YLKNPNVSDS LLLQNIFQAL NVYYNYSGQV KCLNISETAT SSLGTLGWSY QACTEVVMPF CTNGVDDMFE PHSWNLKELS DDCFQQWGVR PRPSWITTMY GGKNISSHTN IVFSNGELDP WSGGGVTKDI TDTLVAVTIS EGAHHLDLRT KNALDPMSVL LARSLEVRHM KNWIRDFYDS AGKQ 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.

    Prcp Human
  • View Data Sheet

    Name :

    CES1D Mouse

    Description:

    Carboxylesterase 1D Mouse Recombinant

    Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.

    Product # :

    ENZ-1007

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    Description

    CES1D Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 555 amino acids (19-565 a.a) and having a molecular mass of 60.9kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1D is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1D protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 80,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of p-nitrophenyl acetate to pnitrophenol per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      Carboxylesterase 1D, also known as CES1D is part of a big family of carboxylesterases which are responsible for the hydrolysis of ester in addition to amide bonds. CES1D is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity in addition to lesser but detectable neutral cholesteryl ester hydrolase activity. CES1D demonstrates low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics.

    • Synonyms

      Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.

    • 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

      YPSSPPVVNT VKGKVLGKYV NLEGFTQPVA VFLGVPFAKP PLGSLRFAPP QPAEPWSFVK NTTSYPPMCS QDAVGGQVLS ELFTNRKENI PLQFSEDCLY LNIYTPADLT KNSRLPVMVW IHGGGLVVGG ASTYDGLALS AHENVVVVTI QYRLGIWGFF STGDEHSRGN WGHLDQVAALRWVQDNIANF GGNPGSVTIF GESAGGFSVS VLVLSPLAKN LFHRAISESG VSLTAALITT DVKPIAGLVA TLSGCKTTTS AVMVHCLRQK TEDELLETSL KLNLFKLDLL GNPKESYPFL PTVIDGVVLP KAPEEILAEK SFSTVPYIVG INKQEFGWII PTLMGYPLAE GKLDQKTANSLLWKSYPTLK ISENMIPVVA EKYLGGTDDL TKKKDLFQDL MADVVFGVPS VIVSRSHRDA GASTYMYEFE YRPSFVSAMR PKAVIGDHGD EIFSVFGSPF LKDGASEEET NLSKMVMKFW ANFARNGNPN GGGLPHWPEY DQKEGYLKIG ASTQAAQRLK DKEVSFWAEL RAKESAQRPSHREHVELLEH HHHHH.

    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.

    Ces1D Mouse
  • View Data Sheet

    Name :

    HAO1 Human, Active

    Description:

    Hydroxyacid Oxidase 1 Human Recombinant, Active

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

    Product # :

    ENZ-1094

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered yellowish solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Hao1 Protein
  • View Data Sheet

    Name :

    CoV-2 3CL

    Description:

    Coronavirus 2019 3CL Protease Recombinant

    Product # :

    SARS-058

    Price :

    Quantity :

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    • description
    • source
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    • More Info

    Description

    Recombinant Coronavirus 2019 3CL Protease having a Mw of approximately 33.8 kDa was purified from E. coli. The CoV-2 3CL contains 306 amino acids and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    CoV-2 3CL solution contains 5 % Trehalose, 0.02 % Tween-20 and PBS, pH 7.4.

    Purity

    Protein is >98% pure as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    CoV-2 3CL is a cysteine protease that cleaves proteins with sequences including LQ(S/A/G).  The cleavage takes c-terminal to the glutamine residue. 

    More Info

    • Introduction

      The SARS CoV-2 3CL protease (C30 Endopeptidase) derived from human SARS-CoV-2 is a C30-type cysteine protease situated in the NS3 segment. SARS CoV-2 3CL protease biological functionality is needed to process viral polyproteins to functional complete units. SARS CoV-2 3CL protease (main protease) is the core protease protein in CoV and corresponds to non-structural protein 5. SARS CoV-2 3CL cleaves the CoV polyprotein at 11 locations. SARS CoV-2 3CL protease has a cysteine-histidine catalytic dyad at its active site and cleaves a Gln–(Ser/Ala/Gly) peptide bond. SARS CoV-2 3CL protease at position P1 cleaves the bond between the glutamine and serine/alanine/glycine. SARS CoV-2 3CL protease is necessary in the processing of the CoV replicase polyprotein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. CoV-2 3CL is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      SGFRKMAFPS GKVEGCMVQV TCGTTTLNGL WLDDVVYCPR HVICTSEDML NPNYEDLLIR KSNHNFLVQA GNVQLRVIGH SMQNCVLKLK VDTANPKTPK YKFVRIQPGQ TFSVLACYNG SPSGVYQCAM RPNFTIKGSF LNGSCGSVGF NIDYDCVSFC YMHHMELPTG VHAGTDLEGN FYGPFVDRQT AQAAGTDTTI TVNVLAWLYA AVINGDRWFL NRFTTTLNDF NLVAMKYNYE PLTQDHVDIL GPLSAQTGIA VLDMCASLKE LLQNGMNGRT ILGSALLEDE FTPFDVVRQC SGVTFQ

    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.

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  • 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 :

    ACP5 Human, His

    Description:

    Acid Phosphatase-5 Human Recombinant, His Tag

    Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, EC 3.1.3.2, TrATPase, SPENCDI, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TR-AP, TRAP, ACP5.

    Product # :

    ENZ-913

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    Description

    ACP5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (22-325 a.a) and having a molecular mass of 35.1kDa.ACP5 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACP5 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37C.

    More Info

    • Introduction

      Acid Phosphatase-5, also known as ACP5 is a member of the Purple acid phosphatase family. ACP5 is implicated in osteopontin as well as bone sialoprotein dephosphorylation. ACP5 expression appears to increase in certain pathological states for instance Gaucher & Hodgkin diseases, the hairy cell, the B-cell, as well as the T-cell leukemias.

    • Synonyms

      Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, EC 3.1.3.2, TrATPase, SPENCDI, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TR-AP, TRAP, ACP5.

    • 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

      ATPALRFVAV GDWGGVPNAP FHTAREMANA KEIARTVQIL GADFILSLGD NFYFTGVQDI NDKRFQETFE DVFSDRSLRK VPWYVLAGNH DHLGNVSAQI AYSKISKRWN FPSPFYRLHF KIPQTNVSVA IFMLDTVTLC GNSDDFLSQQ PERPRDVKLA RTQLSWLKKQ LAAAREDYVL VAGHYPVWSI AEHGPTHCLV KQLRPLLATY GVTAYLCGHD HNLQYLQDEN GVGYVLSGAG NFMDPSKRHQ RKVPNGYLRF HYGTEDSLGG FAYVEISSKE MTVTYIEASG KSLFKTRLPR RARPHHHHHH.

    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.

    Acp5 Human
  • View Data Sheet

    Name :

    ADK Human, Active

    Description:

    Adenosine Kinase Human Recombinant, Active

    Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase, Testicular Tissue Protein Li 14, EC 2.7.1.

    Product # :

    PKA-108

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    Description

    ADK produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (22-362a.a.) and having a molecular mass of 40.5kDa.ADK is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ADK protein solution (0.5mg/ml) contains 20% glycerol, 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 1mM EDTA & 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 30 pmol/min/ug and is defined as the amount of enzyme that convert 1.0 pmole of adenosine to AMP per minute at pH 7.5 at 37C in a couple system with PK and LDH.

    More Info

    • Introduction

      Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.

    • Synonyms

      Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase, Testicular Tissue Protein Li 14, EC 2.7.1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MRENILFGMG NPLLDISAVV DKDFLDKYSL KPNDQILAED KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA ATFFGCIGID KFGEILKRKA AEAHVDAHYY EQNEQPTGTC AACITGDNRS LIANLAAANC YKKEKHLDLE KNWMLVEKAR
      VCYIAGFFLT VSPESVLKVA HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN ETEAATFARE QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR TGCTFPEKPD
      FH.

    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.

    Adenosine Kinase
  • View Data Sheet

    Name :

    MPO Human

    Description:

    Myeloperoxidase Human

    Myeloperoxidase, EC 1.11.1.7, MPO.

    Product # :

    ENZ-074

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    Description

    MPO is a natural protein having a molecular mass of 150kDa containing 2 subunits each of a heavy chain with 64kDa and a light chain with 13kDa. MPO is isolated from human peripheral blood polymorphonuclear leukocytes.

    Source

    Human peripheral blood polymorphonuclear leukocytes.

    Formulation

    MPO solution is supplied in 20mM HEPES buffer pH-7.5, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myeloperoxidase is an important enzyme used by granulocytes during phagocytic lysis of foreign particles engulfed. In normal tissues and in a variety of myeloproliferative disorders myeloid cells of both neutrophilic and eosinophilic types, at all stages of maturation, exhibit strong cytoplasmic reactivity for MPO. Erythroid precursors, megakaryocytes, lymphoid cells, mast cells, and plasma cells are nonreactive. MPO is not observed in the neoplastic cells of a wide variety of epithelial tumors and sarcomas. MPO is useful in differentiating between myeloid and lymphoid leukemias.

    • Synonyms

      Myeloperoxidase, EC 1.11.1.7, MPO.

    • 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. Avoid multiple 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.

    Mpo Human
  • View Data Sheet

    Name :

    ENHO Human

    Description:

    Energy Homeostasis Associated Human Recombinant

    Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    Product # :

    PRO-1569

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    Description

    ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.

    • Synonyms

      Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.

    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.

    Enho Human
  • View Data Sheet

    Name :

    ST6GAL1 Human, sf9

    Description:

    ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, sf9 Human Recombinant

    ST6 Beta-Galactoside Alpha-2,6-Sialyltransferase 1, ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, ST6Gal I, CMP-N-Acetylneuraminate-Beta-Galactosamide-Alpha-2,6-Sialyltransferase 1,B-Cell Antigen CD75, Alpha 2,6-ST 1, EC 2.4.99.1, ST6GalI, SIAT1, CMP-N-Acetylneuraminate Beta-Galactosamide Alpha-2,6-Sialyltransferase, Sialyltransferase 1 (Beta-Galactoside Alpha-2,6-Sialyltransferase) , ST6 N-Acetylgalactosaminide Alpha-2,6-Sialyltransferase 1, Sialyltransferase 1, ST6N.

    Product # :

    ENZ-950

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    Description

    ST6GAL1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 389 amino acids (27-406 a.a.) and having a molecular mass of 44.6kDa. ST6GAL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ST6GAL1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ST6GAL1 also known as ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, is part of the glycosyltransferase family 29. ST6GAL1 is a type II membrane protein which catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. Furthermore, ST6GAL1 is normally found in the Golgi however it can be proteolytically processed to a soluble form, ST6GAL1 is also involved in the generation of the cell-surface carbohydrate determinants as well differentiation antigens HB-6, CD75, and CD76.

    • Synonyms

      ST6 Beta-Galactoside Alpha-2,6-Sialyltransferase 1, ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, ST6Gal I, CMP-N-Acetylneuraminate-Beta-Galactosamide-Alpha-2,6-Sialyltransferase 1,B-Cell Antigen CD75, Alpha 2,6-ST 1, EC 2.4.99.1, ST6GalI, SIAT1, CMP-N-Acetylneuraminate Beta-Galactosamide Alpha-2,6-Sialyltransferase, Sialyltransferase 1 (Beta-Galactoside Alpha-2,6-Sialyltransferase) , ST6 N-Acetylgalactosaminide Alpha-2,6-Sialyltransferase 1, Sialyltransferase 1, ST6N.

    • 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

      ADPKEKKKGS YYDSFKLQTK EFQVLKSLGK LAMGSDSQSV SSSSTQDPHR GRQTLGSLRG LAKAKPEASF QVWNKDSSSK NLIPRLQKIW KNYLSMNKYK VSYKGPGPGI KFSAEALRCH LRDHVNVSMV EVTDFPFNTS EWEGYLPKES IRTKAGPWGR CAVVSSAGSL KSSQLGREID DHDAVLRFNG APTANFQQDV GTKTTIRLMN SQLVTTEKRF LKDSLYNEGI LIVWDPSVYH SDIPKWYQNP DYNFFNNYKT YRKLHPNQPF YILKPQMPWE LWDILQEISP EEIQPNPPSS GMLGIIIMMT LCDQVDIYEF LPSKRKTDVC YYYQKFFDSA CTMGAYHPLL YEKNLVKHLN QGTDEDIYLL GKATLPGFRT IHCHHHHHH.

    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.

    St6Gal1 Human Sf9
  • View Data Sheet

    Name :

    TGM2 Human

    Description:

    Tissue Transglutaminase Human Recombinant

    Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.

    Product # :

    ENZ-394

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    Description

    Tissue Transglutaminase Human Recombinant produced in E.coli is a non-glycosylated, polypeptide chain having a molecular mass of 78,018 Dalton. tTG is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. By point mutation of the active center the catalytic transglutaminase activity has been eliminated, resulting in increased stability during storage and coating.

    Source

    Escherichia Coli.

    Formulation

    TGM2 is supplied in 16mM HEPES buffer pH-8.0, 400mM NaCl, and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
      Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins.

    • Synonyms

      Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.

    • 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. Avoid multiple 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.

    Tgm2 Human
  • View Data Sheet

    Name :

    CNDP1 Human

    Description:

    CNDP Dipeptidase 1 Human Recombinant

    Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.

    Product # :

    ENZ-927

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    Description

    CNDP1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 489 amino acids (27-507a.a.) and having a molecular mass of 54.9kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CNDP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.

    • Synonyms

      Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.

    • 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

      SPSPPPALLE KVFQYIDLHQ DEFVQTLKEW VAIESDSVQP VPRFRQELFR MMAVAADTLQ RLGARVASVD MGPQQLPDGQ SLPIPPVILA ELGSDPTKGT VCFYGHLDVQ PADRGDGWLT DPYVLTEVDG KLYGRGATDN KGPVLAWINA VSAFRALEQD LPVNIKFIIE GMEEAGSVAL EELVEKEKDR FFSGVDYIVI SDNLWISQRK PAITYGTRGN SYFMVEVKCR DQDFHSGTFG GILHEPMADL VALLGSLVDS SGHILVPGIY DEVVPLTEEE INTYKAIHLD LEEYRNSSRV
      EKFLFDTKEE ILMHLWRYPS LSIHGIEGAF DEPGTKTVIP GRVIGKFSIR LVPHMNVSAV EKQVTRHLED VFSKRNSSNK MVVSMTLGLH PWIANIDDTQ YLAAKRAIRT VFGTEPDMIR DGSTIPIAKM FQEIVHKSVV LIPLGAVDDG EHSQNEKINR WNYIEGTKLF AAFFLEMAQL HLEHHHHHH.

    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.

    Cndp1 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 :

    MGAT2 Human

    Description:

    Mannoside Acetylglucosaminyltransferase 2 Human Recombinant

    Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.

    Product # :

    ENZ-781

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    Description

    MGAT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (30-447a.a) and having a molecular mass of 50kDa. MGAT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MGAT2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mannoside Acetylglucosaminyltransferase 2 (MGAT2) is a golgi enzyme catalyzing an vital step in the conversion of oligomannose to complex N-glycans. MGAT2 enzyme has the characteristic glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. MGAT2 gene mutations may lead to carbohydrate-deficient glycoprotein syndrome, type II.

    • Synonyms

      Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.

    • 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 avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MRQRKNEALA PPLLDAEPAR GAGGRGGDHP SVAVGIRRVS NVSAASLVPA VPQPEADNLT LRYRSLVYQL NFDQTLRNVD KAGTWAPREL VLVVQVHNRP EYLRLLLDSL RKAQGIDNVL VIFSHDFWST EINQLIAGVN FCPVLQVFFP FSIQLYPNEF PGSDPRDCPR DLPKNAALKL GCINAEYPDS FGHYREAKFS QTKHHWWWKL HFVWERVKIL RDYAGLILFL EEDHYLAPDF YHVFKKMWKL KQQECPECDV LSLGTYSASR SFYGMADKVD VKTWKSTEHN MGLALTRNAY QKLIECTDTF CTYDDYNWDW TLQYLTVSCL PKFWKVLVPQ IPRIFHAGDC GMHHKKTCRP STQSAQIESL LNNNKQYMFP ETLTISEKFT VVAISPPRKN GGWGDIRDHE LCKSYRRLQ.

    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.

    Mgat2 Human
  • View Data Sheet

    Name :

    ACOT8 Human

    Description:

    Acyl-CoA Thioesterase 8 Human Recombinant

    Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.

    Product # :

    ENZ-712

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    Description

    ACOT8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-319) and having a molecular mass of 38.3kDa. ACOT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACOT8 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acyl-CoA Thioesterase 8 (ACOT8) is a group of enzymes which catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), granting the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. ACOT8 mediate Nef-induced down-regulation of CD4. ACOT8 contends with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). ACOT8 prefers medium-length fatty acyl-CoAs.

    • Synonyms

      Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.

    • 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 MGSMSSPQAP EDGQGCGDRG DPPGDLRSVL VTTVLNLEPL DEDLFRGRHY WVPAKRLFGG QIVGQALVAA AKSVSEDVHV HSLHCYFVRA GDPKLPVLYQ VERTRTGSSF SVRSVKAVQH GKPIFICQAS FQQAQPSPMQ HQFSMPTVPP PEELLDCETL IDQYLRDPNL QKRYPLALNR IAAQEVPIEI KPVNPSPLSQ LQRMEPKQMF WVRARGYIGE GDMKMHCCVA AYISDYAFLG TALLPHQWQH KVHFMVSLDH SMWFHAPFRA DHWMLYECES PWAGGSRGLV HGRLWRQDGV LAVTCAQEGV IRVKPQVSES 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.

    Acot8 Human
  • View Data Sheet

    Name :

    DMGO

    Description:

    Dimethylglycine Oxidase Recombinant

    DMGO, Dimethylglycine Oxidase.

    Product # :

    ENZ-318

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    Description

    Dimethylglycine oxidase Recombinant originated from Arthrobacter globifomis fused to His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 850 amino acids and having a molecular mass of 92.1 kDa. The DMGO is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Recombinant Dimethylglycine Oxidase solution contains 20mM Tris-HCl pH7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dimethylglycine oxidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative demethylation of dimethylglycine to yield sarcosine, formaldehyde, and hydrogen peroxide. The N-terminal region binds FAD covalently so it is yellowish.

    • Synonyms

      DMGO, Dimethylglycine Oxidase.

    • Physical Appearance

      Sterile filtered liquid formulation 1 mg/ml.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASTPRIVII GAGIVGTNLA DELVTRGWNN ITVLDQGPLN MPGGSTSHAP GLVFQTNPSK TMASFAKYTVEKLLSLTEDG VSCFNQVGGL EVATTETRLA DLKRKLGYAA AWGIEGRLLS PAECQELYPL LDGENILGGL HVPSDGLASA ARAVQLLIKRTESAGVTYRG STTVTGIEQS GGRVTGVQTA DGVIPADIVV SCAGFWGAKI GAMIGMAVPL LPLAHQYVKT TPVPAQQGRN DQPNGARLPILRHQDQDLYY REHGDRYGIG SYAHRPMPVD VDTLGAYAPE TVSEHHMPSR LDFTLEDFLP AWEATKQLLP ALADSEIEDG FNGIFSFTPDGGPLLGESKE LDGFYVAEAV WVTHSAGVAK AMAELLTTGR SETDLGECDI TRFEDVQLTP EYVSETSQQN FVEIYDVLHP LQPRLSPRNLRVSPFHARHK ELGAFFLEAG GWERPYWFEA NAALLKEMPA EWLPPARDAW SGMFSSPIAA AEAWKTRTAV AMYDMTPLKR LEVSGPGALKLLQELTTADL AKKPGAVTYT LLLDHAGGVR SDITVARLSE DTFQLGANGN IDTAYFERAA RHQTQSGSAT DWVQVRDTTG GTCCIGLWGPLARDLVSKVS DDDFTNDGLK YFRAKNVVIG GIPVTAMRLS YVGELGWELY TSADNGQRLW DALWQAGQPF GVIAAGRAAF SSLRLEKGYRSWGTDMTTEH DPFEAGLGFA VKMAKESFIG KGALEGRTEE ASARRLRCLT IDDGRSIVLG KEPVFYKEQA VGYVTSAAYG YTVAKPIAYSYLPGTVSVGD SVDIEYFGRR ITATVTEDPL YDPKMTRLRG.

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    Dimethylglycine Oxidase
  • View Data Sheet

    Name :

    ARSG Human

    Description:

    Arylsulfatase G Human Recombinant

    Arylsulfatase G, ASG, ARSG, KIAA1001, UNQ839/PRO1777.

    Product # :

    ENZ-677

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    Description

    ARSG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 532 amino acids (17-525) and having a molecular mass of 57kDa.ARSG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Arylsulfatase G (ARSG) is a member of the sulfatase enzyme family. Sulfatases are enzymes which hydrolyze sulfate esters from sulfated steroids, carbohydrates, proteoglycans, and glycolipids. Sulfatases are involved in hormone biosynthesis, modulation of cell signaling, and degradation of macromolecules. The ARSG protein exhibits arylsulfatase activity at acidic pH, as is characteristic of lysosomal sulfatases. The Arylsulfatase G enzyme localizes in the lysosomes. ARSG is inhibited by phosphate, which forms a covalent bond with the active site 3-oxoalanine. Arylsulfatase G is widely expressed, having very low expression in the brain, lung, heart and skeletal muscle.

    • Synonyms

      Arylsulfatase G, ASG, ARSG, KIAA1001, UNQ839/PRO1777.

    • 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 MGSGFLYPLV DFCISGKTRG QKPNFVIILA DDMGWGDLGA NWAETKDTAN LDKMASEGMR FVDFHAAAST CSPSRASLLT GRLGLRNGVT RNFAVTSVGG LPLNETTLAE VLQQAGYVTG IIGKWHLGHH GSYHPNFRGF DYYFGIPYSH DMGCTDTPGY NHPPCPACPQ GDGPSRNLQR DCYTDVALPL YENLNIVEQP VNLSSLAQKY AEKATQFIQR ASTSGRPFLL YVALAHMHVP LPVTQLPAAP RGRSLYGAGL WEMDSLVGQI KDKVDHTVKE NTFLWFTGDN GPWAQKCELA GSVGPFTGFW QTRQGGSPAK QTTWEGGHRV PALAYWPGRV PVNVTSTALL SVLDIFPTVV ALAQASLPQG RRFDGVDVSE VLFGRSQPGH RVLFHPNSGA AGEFGALQTV RLERYKAFYI TGGARACDGS TGPELQHKFP LIFNLEDDTA EAVPLERGGA EYQAVLPEVR KVLADVLQDI ANDNISSADY TQDPSVTPCC NPYQIACRCQ AA.

    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.

    Arsg Human
  • View Data Sheet

    Name :

    PAPSS1 Human

    Description:

    3'-Phosphoadenosine 5'-Phosphosulfate Synthase 1 Human Recombinant

    3'-phosphoadenosine 5'-phosphosulfate synthase 1, ATPSK1, PAPSS 1, SK 1, 3-prime-phosphoadenosine 5-prime-phosphosulfate synthase 1, bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1, PAPS synthase 1, Sulfurylase kinase 1, EC 2.7.1.25.

    Product # :

    ENZ-236

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    Description

    PAPSS1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 626 amino acids (24-624) and having a molecular mass of 70.9kDa.PAPSS1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PAPSS1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      PAPSS1 is a bifunctional enzyme with APS kinase and ATP sulfurylase activity. PAPSS1 facilitates two stages in the sulfate activation pathway, yielding 3'-phosphoadenylylsulfate (PAPS). Additionally, PAPSS1 takes part in the biosynthesis of sulfated L-selectin ligands in endothelial cells.

    • Synonyms

      3'-phosphoadenosine 5'-phosphosulfate synthase 1, ATPSK1, PAPSS 1, SK 1, 3-prime-phosphoadenosine 5-prime-phosphosulfate synthase 1, bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1, PAPS synthase 1, Sulfurylase kinase 1, EC 2.7.1.25.

    • 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 MGSHMRATNV TYQAHHVSRN KRGQVVGTRG GFRGCTVWLT GLSGAGKTTV SMALEEYLVC HGIPCYTLDG DNIRQGLNKN LGFSPEDREE NVRRIAEVAK LFADAGLVCI TSFISPYTQD RNNARQIHEG ASLPFFEVFV DAPLHVCEQR DVKGLYKKAR AGEIKGFTGI DSEYEKPEAP ELVLKTDSCD VNDCVQQVVE LLQERDIVPV DASYEVKELY VPENKLHLAK TDAETLPALK INKVDMQWVQ VLAEGWATPL NGFMREREYL QCLHFDCLLD GGVINLSVPI VLTATHEDKE RLDGCTAFAL MYEGRRVAIL RNPEFFEHRK EERCARQWGT TCKNHPYIKM VMEQGDWLIG GDLQVLDRVY WNDGLDQYRL TPTELKQKFK DMNADAVFAF QLRNPVHNGH ALLMQDTHKQ LLERGYRRPV LLLHPLGGWT KDDDVPLMWR MKQHAAVLEE GVLNPETTVV AIFPSPMMYA GPTEVQWHCR ARMVAGANFY IVGRDPAGMP HPETGKDLYE PSHGAKVLTM APGLITLEIV PFRVAAYNKK KKRMDYYDSE HHEDFEFISG TRMRKLAREG QKPPEGFMAP KAWTVLTEYY KSLEKA.

    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.

    Papss1 Human
  • View Data Sheet

    Name :

    CASP2 Human

    Description:

    Caspase 2 Apoptosis-Related Cysteine Peptidase Human Recombinant

    Caspase-2, CASP-2, CASP2, Caspase 2 Apoptosis-Related Cysteine Peptidase, Neural precursor cell expressed developmentally down-regulated protein 2, NEDD-2, Protease ICH-1, ICH1, NEDD2, Caspase-2 subunit p18, Caspase-2 subunit p13, Caspase-2 subunit p12, Caspase 2 isoform 1, PPP1R57.

    Product # :

    ENZ-801

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    Description

    CASP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (348-452) and having a molecular mass of 14.1kDa.CASP2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CASP2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Caspase 2 Apoptosis-Related Cysteine Peptidase (CASP2) is a part of the cysteine-aspartic acid protease (caspase) family. CASP2 takes part in the activation cascade of caspases responsible for apoptosis execution. CASP2 is also responsible for inactivating proteins essential for cell survival. The proteolytic cleavage of CASP2 is induced by a variety of apoptotic stimuli.

    • Synonyms

      Caspase-2, CASP-2, CASP2, Caspase 2 Apoptosis-Related Cysteine Peptidase, Neural precursor cell expressed developmentally down-regulated protein 2, NEDD-2, Protease ICH-1, ICH1, NEDD2, Caspase-2 subunit p18, Caspase-2 subunit p13, Caspase-2 subunit p12, Caspase 2 isoform 1, PPP1R57.

    • 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 MAGKEKLPKM RLPTRSDMIC GYACLKGTAA MRNTKRGSWY IEALAQVFSE RACDMHVADM LVKVNALIKD REGYAPGTEF HRCKEMSEYC STLCRHLYLF PGHPPT.

    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.

    Casp2 Human
  • View Data Sheet

    Name :

    ITPA Human

    Description:

    Inosine Triphosphatase Human Recombinant

    EC 3.6.1.19, C20orf37, dJ794I6.3, HLC14-06-P, ITPase, My049, OK/SW-cl.9, Inosine Triphosphatase, ITPA.

    Product # :

    ENZ-549

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    Description

    ITPA Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids (1-194 a.a.) and having a molecular mass of 23.7 kDa. The ITPA is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ITPA solution (1mg/ml) contains 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ITPA enzyme catalyzes the pyrophosphohydrolysis of both ITP (inosine triphosphate) and dITP (deoxyinosine triphosphate) to IMP (inosine monophosphate) and diphosphate. IMP is exercised as a substrate for purine nucleotide pathways. IMP is phosphorylated to ITP, and ITPA mediates the concentration of ITP in the cell by changing ITP back to IMP. Defects in ITPA result in ITPA deficiency which is thought to be inherited and is characterized by an over-accumulation of ITP in erythocytes, leukocytes and fibroblasts.

    • Synonyms

      EC 3.6.1.19, C20orf37, dJ794I6.3, HLC14-06-P, ITPase, My049, OK/SW-cl.9, Inosine Triphosphatase, ITPA.

    • 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 MMAASLVGKK IVFVTGNAKK LEEVVQILGD KFPCTLVAQK IDLPEYQGEP DEISIQKCQE AVRQVQGPVL VEDTCLCFNA LGGLPGPYIK WFLEKLKPEG LHQLLAGFED KSAYALCTFA LSTGDPSQPV RLFRGRTSGR IVAPRGCQDF GWDPCFQPDG YEQTYAEMPK AEKNAVSHRF RALLELQEYF GSLAA.

    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.

    Itpa Human
  • View Data Sheet

    Name :

    POLR2E Human

    Description:

    Polymerase II Polypeptide E Human Recombinant

    DNA-directed RNA polymerases I, II, and III subunit RPABC1, RNA polymerases I, II, and III subunit ABC1, DNA-directed RNA polymerase II 23 kDa polypeptide, DNA-directed RNA polymerase II subunit E, RPB5 homolog, XAP4, POLR2E, RPB5, RPABC1, hRPB25, hsRPB5.

    Product # :

    ENZ-673

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    Description

    POLR2E Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210) and having a molecular mass of 27.1kDa.POLR2E is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The POLR2E solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      DNA-directed RNA polymerases I, II, and III subunit RPABC1 (POLR2E) is a member of the archaeal RpoH/eukaryotic RPB5 RNA polymerase subunit family. POLR2E being a DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. POLR2E is the 5th largest subunit of RNA polymerase II (the polymerase which is responsible for synthesizing messenger RNA in eukaryotes). The POLR2E subunit is shared by the other 2 DNA-directed RNA polymerases and is present in two-fold molar excess over the other polymerase subunits. An interaction between the POLR2E subunit and a hepatitis virus transactivating protein has been established, suggesting that an interaction between transcriptional activators and the polymerase can occur through the POLR2E subunit.

    • Synonyms

      DNA-directed RNA polymerases I, II, and III subunit RPABC1, RNA polymerases I, II, and III subunit ABC1, DNA-directed RNA polymerase II 23 kDa polypeptide, DNA-directed RNA polymerase II subunit E, RPB5 homolog, XAP4, POLR2E, RPB5, RPABC1, hRPB25, hsRPB5.

    • 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 MGSMDDEEET YRLWKIRKTI MQLCHDRGYL VTQDELDQTL EEFKAQFGDK PSEGRPRRTD LTVLVAHNDD PTDQMFVFFP EEPKVGIKTI KVYCQRMQEE NITRALIVVQ QGMTPSAKQS LVDMAPKYIL EQFLQQELLI NITEHELVPE HVVMTKEEVT
      ELLARYKLRE NQLPRIQAGD PVARYFGIKR GQVVKIIRPS ETAGRYITYR LVQ.

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    Polr2E Human
  • View Data Sheet

    Name :

    ldhA E. coli

    Description:

    Fermentative D-lactate Dehydrogenase, NAD-Dependent E.Coli Recombinant

    D-lactate dehydrogenase, D-LDH, Fermentative lactate dehydrogenase, ldhA, hslI, htpH, b1380, JW1375.

    Product # :

    ENZ-632

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    Description

    ldhA E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1kDa.ldhA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ldhA solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      D-lactate dehydrogenase (ldha) is a member of the D-isomer specific 2-hydroxyacid dehydrogenase family. In enzymology, an ldha (cytochrome) is an enzyme which catalyzes the chemical reaction. Therefore, the 2 substrates of the ldha enzyme are (D)-lactate and ferricytochrome c, whereas its 2 products are pyruvate and ferrocytochrome c.

    • Synonyms

      D-lactate dehydrogenase, D-LDH, Fermentative lactate dehydrogenase, ldhA, hslI, htpH, b1380, JW1375.

    • 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 MGSHMKLAVY STKQYDKKYL QQVNESFGFE LEFFDFLLTE KTAKTANGCE AVCIFVNDDG SRPVLEELKK HGVKYIALRC AGFNNVDLDA AKELGLKVVR VPAYDPEAVA EHAIGMMMTL NRRIHRAYQR TRDANFSLEG LTGFTMYGKT AGVIGTGKIG VAMLRILKGF GMRLLAFDPY PSAAALELGV EYVDLPTLFS ESDVISLHCP LTPENYHLLN EAAFEQMKNG VMIVNTSRGA LIDSQAAIEA LKNQKIGSLG MDVYENERDL FFEDKSNDVI QDDVFRRLSA CHNVLFTGHQ AFLTAEALTS ISQTTLQNLS NLEKGETCPN ELV.

    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.

    Ldha E Coli
  • View Data Sheet

    Name :

    UBE2I Human His

    Description:

    Ubiquitin-Conjugating Enzyme E2I Human Recombinant, His Tag

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

    Product # :

    ENZ-274

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    Quantity :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MHHHHHHAMGTLNMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGT
      MNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFH
      PNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTI
      YCQNRVEYEKRVRAQAKKFAPS.

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

    Ube2I Human His
  • View Data Sheet

    Name :

    UCHL5 Human

    Description:

    Ubiquitin Carboxyl-Terminal Esterase L5 Human Recombinant

    Ubiquitin Carboxyl-terminal Hydrolase L5, UCH37, CGI-70, UCH-L5, INO80R, Ubiquitin thioesterase L5, INO80 complex subunit R, EC 3.4.19.12, Ubiquitin Carboxyl-terminal Esterase L5.

    Product # :

    ENZ-097

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

    Description

    UCHL5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing349 amino acids (1-329a.a.) and having a molecular mass of 39.7kDa.UCHL5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UCHL5 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 5mM DTT, 200mM NaCl, 0.1mM PMSF, 2mM EDTA and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 500 pmole/min/ug. Measured by the hydrolysis of Ubiquitin-AMC at
     pH 8.0, at 37°C.

    More Info

    • Introduction

      UCHL5 is a member of the peptidase C12 family. UCHL5 protein is a protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains, and deubiquitinating enzyme related to the 19S regulatory subunit of the 26S proteasome.

    • Synonyms

      Ubiquitin Carboxyl-terminal Hydrolase L5, UCH37, CGI-70, UCH-L5, INO80R, Ubiquitin thioesterase L5, INO80 complex subunit R, EC 3.4.19.12, Ubiquitin Carboxyl-terminal Esterase L5.

    • 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

      MGSSHHHHHHSSGLVPRGSH MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR QLAEEEPMDT DQGNSMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL KTLAEHQQLI PLVEKAKEKQ NAKKAQETK

    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.

    Uchl5 Human
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