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Search results

1000 results found for “Hepatitis D”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    GPT Human

    Description:

    Glutamic-Pyruvate Transaminase Human Recombinant

    Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    Product # :

    ENZ-192

    Price :

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    Description

    GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

    • Synonyms

      Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS

    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.

    Gpt Human
  • View Data Sheet

    Name :

    GPT Human, His Active

    Description:

    Glutamic-Pyruvate Transaminase, His Tag Active Human Recombinant

    Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    Product # :

    ENZ-1000

    Price :

    Quantity :

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    • source
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    • Citations

    Description

    GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

    • Synonyms

      Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS

    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.

    Gpt Human His Active
  • View Data Sheet

    Name :

    CD14 Human HEK

    Description:

    CD14 Human Recombinant HEK

    Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein, CD14.

    Product # :

    PRO-1642

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
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    • More Info
    • Citations

    Description

    CD14 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 341 amino acids (20-352). CD14 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    CD14 was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, PH 7.4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CD14 (also known lipopolysaccharide (LPS) receptor) is expressed strongly on monocytes and macrophage and weakly on the surface of neutrophils. CD14 is anchored to cells by linkage to glycosylphosphatidylinositol (GPI) and functions as a high affinity receptor for complexes of LPS and LPS binding protein (LBP). Soluble CD14, also binding to LPS, acts at physiological concentration as an LPS agonist and has, at higher concentrations, an LPS antagonizing effect in cell activation. CD14 has been shown to bind apoptotic cells.

    • Synonyms

      Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein, CD14.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CD14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD14 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CD14 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVD
      ADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKIT
      GTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAF
      SCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCA
      ALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKL
      RVLDLSCNRLNRAPQPDELPEVDNLTLDGNPFLVPGTALPHEGSMNSGVVPACVDHHHHHH

    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.

    Cd14 Human Hek
  • View Data Sheet

    Name :

    ID1 Human

    Description:

    Inhibitor of DNA Binding 1 Human Recombinant

    bHLHb24, ID, DNA-binding protein inhibitor ID-1, Class B basic helix-loop-helix protein 24, Inhibitor of DNA binding 1, ID1.

    Product # :

    PRO-1426

    Price :

    Quantity :

    Shipping Method :

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

    Description

    ID1 Human Recombinant produced in E. coli is a single polypeptide chain containing 178 amino acids (1-155) and having a molecular mass of 18.5kDa. ID1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ID1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Inhibitor of DNA Binding 1 (ID1) is a helix-loop-helix protein which can form heterodimers with members of the basic HLH family of transcription factors. ID1 is lacking DNA binding activity and thus can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts. ID1 participates in cell growth, senescence, and differentiation.

    • Synonyms

      bHLHb24, ID, DNA-binding protein inhibitor ID-1, Class B basic helix-loop-helix protein 24, Inhibitor of DNA binding 1, ID1.

    • 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 MGSMKVASGS TATAAAGPSC ALKAGKTASG AGEVVRCLSE QSVAISRCAG GAGARLPALL DEQQVNVLLY DMNGCYSRLK ELVPTLPQNR KVSKVEILQH VIDYIRDLQL ELNSESEVGT PGGRGLPVRA PLSTLNGEIS ALTAEAACVP ADDRILCR.

    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.

    Id1 Human
  • View Data Sheet

    Name :

    ACAD8 Human

    Description:

    Acyl-Coenzyme A Dehydrogenase 8 Human Recombinant

    Acyl-CoA dehydrogenase family member 8 mitochondrial, ACAD-8, Isobutyryl-CoA dehydrogenase, Activator-recruited cofactor 42 kDa component, ARC42, FLJ22590.

    Product # :

    ENZ-294

    Price :

    Quantity :

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    More Info

    • description
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    • More Info
    • Citations

    Description

    ACAD8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 416 amino acids (23-415) and having a molecular mass of 45.1kDa.ACAD8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACAD8 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of ?-oxidationin Fatty acid metabolism.
      Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer formation.

    • Synonyms

      Acyl-CoA dehydrogenase family member 8 mitochondrial, ACAD-8, Isobutyryl-CoA dehydrogenase, Activator-recruited cofactor 42 kDa component, ARC42, FLJ22590.

    • 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 MGSLVQTGHR SLTSCIDPSM GLNEEQKEFQ KVAFDFAARE MAPNMAEWDQ KELFPVDVMR KAAQLGFGGV YIQTDVGGSG LSRLDTSVIF EALATGCTST TAYISIHNMC AWMIDSFGNE EQRHKFCPPL CTMEKFASYC LTEPGSGSDA ASLLTSAKKQ GDHYILNGSK AFISGAGESD IYVVMCRTGG PGPKGISCIV VEKGTPGLSF GKKEKKVGWN SQPTRAVIFE DCAVPVANRI GSEGQGFLIA VRGLNGGRIN IASCSLGAAH ASVILTRDHL NVRKQFGEPL ASNQYLQFTL ADMATRLVAA RLMVRNAAVA LQEERKDAVA LCSMAKLFAT DECFAICNQA LQMHGGYGYL KDYAVQQYVR DSRVHQILEG SNEVMRILIS RSLLQE.

    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.

    Acad8 Human
  • View Data Sheet

    Name :

    ADPRHL2 Human

    Description:

    ADP-Ribosylhydrolase Like 2 Human Recombinant

    Poly(ADP-ribose) glycohydrolase ARH3, ADP-ribosylhydrolase 3, [Protein ADP-ribosylarginine] hydrolase-like protein 2, ADPRHL2, ARH3.

    Product # :

    ENZ-638

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    Description

    ADPRHL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 387 amino acids (1-363) and having a molecular mass of 41.5kDa.ADPRHL2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADPRHL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ADP-ribosylhydrolase like 2 (ADPRHL2) belongs to the ADP-ribosylglycohydrolase family. ADPRHL2 catalyzes the removal of ADP-ribose from ADP-ribosylated proteins. ADPRHL2, which is ubiquitously expressed, uses magnesium as a cofactor to catalyze the hydrolysis of poly (ADP-ribose) that is synthesized after DNA damage. Furthermore, ADPRHL2 has an essential role in the maintenance of normal neuronal cell function. The ADPRHL2 enzyme localizes to the mitochondria, in addition to the nucleus and cytoplasm.

    • Synonyms

      Poly(ADP-ribose) glycohydrolase ARH3, ADP-ribosylhydrolase 3, [Protein ADP-ribosylarginine] hydrolase-like protein 2, ADPRHL2, ARH3.

    • 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 MGSHMAAAAM AAAAGGGAGA ARSLSRFRGC LAGALLGDCV GSFYEAHDTV DLTSVLRHVQ SLEPDPGTPG SERTEALYYT DDTAMARALV QSLLAKEAFD EVDMAHRFAQ EYKKDPDRGY GAGVVTVFKK LLNPKCRDVF EPARAQFNGK GSYGNGGAMR VAGISLAYSS VQDVQKFARL SAQLTHASSL GYNGAILQAL AVHLALQGES SSEHFLKQLL GHMEDLEGDA QSVLDARELG MEERPYSSRL KKIGELLDQA SVTREEVVSE LGNGIAAFES VPTAIYCFLR CMEPDPEIPS AFNSLQRTLI YSISLGGDTD TIATMAGAIA GAYYGMDQVP ESWQQSCEGY EETDILAQSL HRVFQKS.

    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.

    Adprhl2 Human
  • View Data Sheet

    Name :

    SDF2 Human

    Description:

    Stromal Cell-Derived Factor 2 Human Recombinant

    Stromal cell-derived factor 2, SDF-2.

    Product # :

    CHM-028

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    Description

    SDF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (19-211 a.a) and having a molecular mass of 23.7kDa. SDF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SDF2 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.

    Citations

    More Info

    • Introduction

      Stromal Cell-Derived Factor 2 (SDF2) is a secretory protein which is partly similar to the hydrophilic segments of yeast mannosyltransferases. SDF2 protein’s expression is ubiquitous and the gene is rather conserved among mammals. SDF2is a protein-coding gene whose alternative splicing results in coding and non-coding variants.

    • Synonyms

      Stromal cell-derived factor 2, SDF-2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAEL.

    • Background

      What is the molecular weight/Mw of SDF2 HUMAN Protein?
      SDF2 HUMAN Protein has a total Mw of 23.7kDa.

      What is the source or expression system of SDF2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of SDF2 HUMAN Protein?
      SDF2 HUMAN Protein is > 85% pure as determined by SDS-PAGE.

      What is the Biological Activity of SDF2 HUMAN Protein?
      The biological functionality of SDF2 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of SDF2 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAEL.

      What applications can SDF2 HUMAN Protein be used in?
      SDF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for SDF2 HUMAN Protein?
      The endotoxin level is minimal, SDF2 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant SDF2 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of SDF2 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Sdf2 Human
  • View Data Sheet

    Name :

    NQO2 Human

    Description:

    NAD(P)H Dehydrogenase Quinone 2 Human Recombinant

    DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].

    Product # :

    ENZ-515

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    Description

    NQO2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 251amino acids (1-231 a.a.) and having a molecular mass of 28.1 kDa. NQO2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    NQO2 Human solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NQO2 is a flavoprotein that catalyzes the 2-electron reduction of diverse quinones, redox dyes, and the vitamin K menadione. NQO2 mainly uses dihydronicotinamide riboside (NRH) as the electron donor. NQO2 catalyzes the metabolic detoxification of quinones and their derivatives to hydroquinones. This detoxification process protects cells against quinone-induced oxidative stress, cytotoxicity and mutagenicity.

    • Synonyms

      DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].

    • 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 MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNFEPR ATDKDITGTL SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF QFPLYWFSVP AILKGWMDRV LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q.

    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.

    Nqo2 Human
  • View Data Sheet

    Name :

    EMAP II Human

    Description:

    Endothelial-Monocyte Activating Polypeptide II Human Recombinant

    AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

    Product # :

    CYT-607

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    Description

    EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.

    Purity

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

    Biological Activity

    Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

    Citations

    More Info

    • Introduction

      EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.

    • Synonyms

      AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

    • Background

      What is the molecular weight/Mw of EMAP II HUMAN Protein?
      EMAP II HUMAN Protein has a total Mw of 18.3kDa.

      What is the source or expression system of EMAP II HUMAN Protein?
      Escherichia Coli.

      What is the Purity of EMAP II HUMAN Protein?
      EMAP II HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of EMAP II HUMAN Protein?
      Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

      What is the amino acid sequence of EMAP II HUMAN Protein?
      SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

      What applications can EMAP II HUMAN Protein be used in?
      EMAP II HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EMAP II HUMAN Protein?
      The endotoxin level is minimal, EMAP II HUMAN Protein was purified using conventional chromatography techniques

    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.

    Emap Ii
  • View Data Sheet

    Name :

    FAHD1 Human

    Description:

    Fumarylacetoacetate Hydrolase Domain Containing 1 Human Recombinant

    Fumarylacetoacetate hydrolase domain-containing protein 1, YisK-like protein, FAHD1, C16orf36, YISKL, MGC74876, DKFZp566J2046.

    Product # :

    ENZ-067

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    Description

    FAHD1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 244 amino acids (1-224 a.a.) and having a molecular mass of 27kDa. The FAHD1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FAHD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) is a member of the FAH family. FAHD1 is considered to have hydrolase activity and it uses Magnesium and Calcium as cofactors. It seems quite likely that the metal binding sites are involved in an enzymatic activity connected to the catabolism of aromatic amino acids.

    • Synonyms

      Fumarylacetoacetate hydrolase domain-containing protein 1, YisK-like protein, FAHD1, C16orf36, YISKL, MGC74876, DKFZp566J2046.

    • 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 MGIMAASRPL SRFWEWGKNI VCVGRNYADH VREMRSAVLS EPVLFLKPST AYAPEGSPIL MPAYTRNLHH ELELGVVMGK RCRAVPEAAA MDYVGGYALC LDMTARDVQD ECKKKGLPWT LAKSFTASCP VSAFVPKEKI PDPHKLKLWL KVNGELRQEG ETSSMIFSIP YIISYVSKII TLEEGDIILT GTPKGVGPVK ENDEIEAGIH GLVSMTFKVE KPEY.

    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.

    Fahd1 Human
  • View Data Sheet

    Name :

    PDPN Human

    Description:

    Podoplanin Human Recombinant

    Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.

    Product # :

    PRO-626

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    Description

    PDPN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (99-207 a.a) and having a molecular mass of 13.4kDa. PDPN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH7.5 & 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
      PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
      Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors.

    • Synonyms

      Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.

    • 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 MASTGQPEDD TETTGLEGGV AMPGAEDDVV TPGTSEDRYK SGLTTLVATS VNSVTGIRIE DLPTSESTVH AQEQSPSATA SNVATSHSTE KVDGDTQTTV EKDGLSTVTL.

    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.

    Pdpn Human
  • View Data Sheet

    Name :

    PDRG1 Human

    Description:

    p53 and DNA-Damage Regulated 1 Human Recombinant

    p53 and DNA damage-regulated protein 1, PDRG1, C20orf126, PDRG.

    Product # :

    PRO-007

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    Description

    PDRG1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 153 amino acids (1-133 a.a.) and having a molecular mass of 17.6kDa. The PDRG1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PDRG1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PDRG1 is a 133 amino acid protein that localizes to the cytoplasm and belongs to the prefoldin subunit beta family. PDRG1 is expressed primarily in normal testicular tissue, it is functionally induced by ultraviolet light and is thought to have a role in chaperone-mediated protein folding, possibly having a role in cellular degradation. PDRG1 is linked to Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome.

    • Synonyms

      p53 and DNA damage-regulated protein 1, PDRG1, C20orf126, PDRG.

    • 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 MLSPEAERVL RYLVEVEELA EEVLADKRQI VDLDTKRNQN REGLRALQKD LSLSEDVMVC FGNMFIKMPH PETKEMIEKD QDHLDKEIEK LRKQLKVKVN RLFEAQGKPE LKGFNLNPLN QDELKALKVI LKG.

    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.

    Pdrg1 Human
  • View Data Sheet

    Name :

    PECI Human

    Description:

    Peroxisomal D3,D2-Enoyl-CoA Isomerase Human Recombinant

    EC 5.3.3.8, ACBD2, DRS1, HCA88, PECI, Peroxisomal 3,2-trans-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, Delta(3),delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Diazepam-binding inhibitor-related protein 1, DBI-related protein 1, DRS-1, Hepatocellular carcinoma-associated antigen 88, Renal carcinoma antigen NY-REN-1, KIAA0536, dJ1013A10.

    Product # :

    ENZ-531

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    Description

    PECI Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-364 a.a.) and having a molecular mass of 42.3 kDa. The PECI is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PECI Human solution (1mg/ml) containing 20mM Tris-HCl, pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PECI is an enzyme that localized to the peroxisomal matrix and encloses one ACB (acyl-CoA-binding) domain. PECI is expressed abundantly in liver, heart and skeletal muscle. PECI functions to catalyze the isomerization of both 3-cis and 3-trans double bonds into the 2-trans form in an array of enoyl-CoA species. PECI takes part in the beta-oxidation of unsaturated fatty acids.

    • Synonyms

      EC 5.3.3.8, ACBD2, DRS1, HCA88, PECI, Peroxisomal 3,2-trans-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, Delta(3),delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Diazepam-binding inhibitor-related protein 1, DBI-related protein 1, DRS-1, Hepatocellular carcinoma-associated antigen 88, Renal carcinoma antigen NY-REN-1, KIAA0536, dJ1013A10.

    • 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 MNRTAMRASQ KDFENSMNQV KLLKKDPGNE VKLKLYALYK QATEGPCNMP KPGVFDLINK AKWDAWNALG SLPKEAARQN YVDLVSSLSP SLESSSQVEP GTDRKSTGFE TLVVTSEDGI TKIMFNRPKK KNAINTEMYH EIMRALKAAS KDDSIITVLT GNGDYYSSGN DLTNFTDIPP GGVEEKAKNN AVLLREFVGC FIDFPKPLIA VVNGPAVGIS VTLLGLFDAV YASDRATFHT PFSHLGQSPE GCSSYTFPKI MSPAKATEML IFGKKLTAGE ACAQGLVTEV FPDSTFQKEV WTRLKAFAKL PPNALRISKE VIRKREREKL HAVNAEECNV LQGRWLSDEC TNAVVNFLSR KSKL.

    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.

    Peci Human
  • View Data Sheet

    Name :

    TDP1 Human

    Description:

    Tyrosyl-DNA Phosphodiesterase 1 Human Recombinant

    Tyrosyl-DNA phosphodiesterase 1, TDP1 protein, TDP1.

    Product # :

    ENZ-685

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    Description

    TDP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298) and having a molecular mass of 35.8kDa. TDP1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TDP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tyrosyl-DNA phosphodiesterase 1 ( TDP1) is required for repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. TDP1 also detach glycolate from single-stranded DNA having 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks.

    • Synonyms

      Tyrosyl-DNA phosphodiesterase 1, TDP1 protein, TDP1.

    • 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 MSQEGDYGRW TISSSDESEE EKPKPDKPST SSLLCARQGA ANEPRYTCSE AQKAAHKRKI SPVKFSNTDS VLPPKRQKSG SQEDLGWCLS SSDDELQPEM PQKQAEKVVI KKEKDISAPN DGTAQRTENH GAPACHRLKE EEDEYETSGE GQDIWDMLDK GNPFQFYLTR VSGVKPKYNS GALHIKDILS PLFGTLVSSA QFNYCFDVDW LVKQYPPEFR KKPILLVHGD KREAKAHLHA QAKPYENISL CQAKLDIAFG THHTKMMLLL YEEGLRVVIH TSNLIHADWH QKTQGTHL.

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    Tdp1 Human
  • View Data Sheet

    Name :

    FHIT Human

    Description:

    Fragile Histidine Triad Human Recombinant

    EC 3.6.1.29, Dinucleosidetriphosphatase, Bis (5''-adenosyl)-triphosphatase , AP3Aase, AP3A hydrolase, Diadenosine 5'',5''''''-P1,P3-triphosphate hydrolase, FRA3B.

    Product # :

    PRO-828

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    Description

    FHIT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids (1-147 a.a.) and having a molecular mass of 17.9 kDa. FHIT protein is fused to an 8 amino acid His tag at C-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    FHIT Human solution containing 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FHIT enzyme cleaves adenosine 5'' PPP 5'' A to yield AMP and ADP. FHIT gene includees the regular fragile site FRA3B on chromosome 3. Alterations and deletions of the FHIT gene are highly linked to the genesis and establishment of human tumors of the lung, cervix, breast, colon, stomach and pancreas. In normal cells, FHIT functions as a tumor suppressor and physically relates with ubiquitin conjugating enzyme 9.

    • Synonyms

      EC 3.6.1.29, Dinucleosidetriphosphatase, Bis (5''-adenosyl)-triphosphatase , AP3Aase, AP3A hydrolase, Diadenosine 5'',5''''''-P1,P3-triphosphate hydrolase, FRA3B.

    • 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

      MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL RPDEVADLFQ TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL PRKAGDFHRN DSIYEELQKH DKEDFPASWR SEEEMAAEAA ALRVYFQLEH 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.

    Fhit Human
  • View Data Sheet

    Name :

    CD2 Human

    Description:

    CD2 Human Recombinant

    T-cell surface antigen CD2, T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, Erythrocyte receptor, Rosette receptor, CD2 antigen, CD2, T11, SRBC.

    Product # :

    PRO-1337

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    Description

    CD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (25-209 a.a) and having a molecular mass of 23.8kDa.CD2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CD2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CD2 which is also known as E-rosette receptor, T11 and lymphocytefunction antigen-2 (LFA-2) is expressed on T cells, thymocytes, and subset of natural killer cells. Human CD2 functions as the receptor for sheep erythrocytes, human CD58 (LFA-3), and CD15s (Sialyl Lewis X). p56lck, p59fyn, CD3eta and CD3epsilon are tyrosine-phosphorylated after CD2 stimulation. CD2 plays a role in T cell activation, T- or NK-cell-mediated cytolysis, apoptosis in activated peripheral T cells, and regulation of T cell anergy.

    • Synonyms

      T-cell surface antigen CD2, T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, Erythrocyte receptor, Rosette receptor, CD2 antigen, CD2, T11, SRBC.

    • 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 MGSMKEITNA LETWGALGQD INLDIPSFQM SDDIDDIKWE KTSDKKKIAQ FRKEKETFKE KDTYKLFKNG TLKIKHLKTD DQDIYKVSIY DTKGKNVLEK IFDLKIQERV SKPKISWTCI NTTLTCEVMN GTDPELNLYQ DGKHLKLSQR VITHKWTTSL
      SAKFKCTAGN KVSKESSVEP VSCPEKGLD.

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    Cd2 Human
  • 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.

    Citations

    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.

    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 His
  • View Data Sheet

    Name :

    CISD1 Human

    Description:

    CDGSH Iron Sulfur Domain 1 Human Recombinant

    CDGSH Iron Sulfur Domain 1, Chromosome 10 Open Reading Frame 70, CDGSH Iron Sulfur Domain-Containing Protein 1, Zinc Finger CDGSH-Type Domain 1, C10orf70, ZCD1, MitoNEET , MDS029.

    Product # :

    PRO-1221

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    Description

    CISD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 100 amino acids (32-108) and having a molecular mass of 11.4 kDa.CISD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CISD1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CISD1 protein holds a CDGSH iron-sulfur domain and is known to bind a redox-active [2Fe-2S] cluster. CISD1 is restricted to the outer membrane of mitochondria and takes part in oxidation regulation.

    • Synonyms

      CDGSH Iron Sulfur Domain 1, Chromosome 10 Open Reading Frame 70, CDGSH Iron Sulfur Domain-Containing Protein 1, Zinc Finger CDGSH-Type Domain 1, C10orf70, ZCD1, MitoNEET , MDS029.

    • 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 MGSKRFYVKD HRNKAMINLH IQKDNPKIVH AFDMEDLGDK AVYCRCWRSK KFPFCDGAHT KHNEETGDNV GPLIIKKKET

    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.

    Cisd1 Human
  • View Data Sheet

    Name :

    UGT1A1 Human

    Description:

    UDP Glucuronosyltransferase 1 Family Polypeptide A1 Human Recombinant

    UDP Glucuronosyltransferase 1 Family, Polypeptide A1, UGT1, GNT1, UDP Glycosyltransferase 1 Family, Polypeptide A1, Bilirubin-Specific UDPGT Isozyme 1, UDP-Glucuronosyltransferase 1-A, UDP-Glucuronosyltransferase 1A1, EC 2.4.1.17, UDPGT 1-1, BILIQTL1, HUG-BR1, UGT1-01, UGT-1A, UGT1*1, UGT1.1, UGT1A, Bilirubin UDP-Glucuronosyltransferase Isozyme 1, Bilirubin UDP-Glucuronosyltransferase 1-1, UDP-Glucuronosyltransferase 1-1, UDPGT, UDP-glucuronosyltransferase 1-1.

    Product # :

    ENZ-864

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    Description

    UGT1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 488 amino acids (26-490 a.a) and having a molecular mass of 54.7kDa. UGT1A1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UGT1A1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UDP Glucuronosyltransferase 1 Family Polypeptide A1, also known as UGT1A1 has a main importance in the conjugation as well as subsequent elimination of potentially toxic xenobiotics and endogenous compounds. UGT1A1 is also capable of catalyzing glucuronidation of 17beta, 17alpha, 1-hydroxypyrene, 4-methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone.

    • Synonyms

      UDP Glucuronosyltransferase 1 Family, Polypeptide A1, UGT1, GNT1, UDP Glycosyltransferase 1 Family, Polypeptide A1, Bilirubin-Specific UDPGT Isozyme 1, UDP-Glucuronosyltransferase 1-A, UDP-Glucuronosyltransferase 1A1, EC 2.4.1.17, UDPGT 1-1, BILIQTL1, HUG-BR1, UGT1-01, UGT-1A, UGT1*1, UGT1.1, UGT1A, Bilirubin UDP-Glucuronosyltransferase Isozyme 1, Bilirubin UDP-Glucuronosyltransferase 1-1, UDP-Glucuronosyltransferase 1-1, UDPGT, UDP-glucuronosyltransferase 1-1.

    • 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 MGSHAGKILL IPVDGSHWLS MLGAIQQLQQ RGHEIVVLAP DASLYIRDGA FYTLKTYPVP FQREDVKESF VSLGHNVFEN DSFLQRVIKT YKKIKKDSAM LLSGCSHLLH NKELMASLAE SSFDVMLTDP FLPCSPIVAQ YLSLPTVFFL HALPCSLEFE ATQCPNPFSY VPRPLSSHSD HMTFLQRVKN MLIAFSQNFL CDVVYSPYAT LASEFLQREV TVQDLLSSAS VWLFRSDFVK DYPRPIMPNM VFVGGINCLH QNPLSQEFEA YINASGEHGI VVFSLGSMVS EIPEKKAMAI ADALGKIPQT VLWRYTGTRP SNLANNTILV KWLPQNDLLG HPMTRAFITH AGSHGVYESI CNGVPMVMMP LFGDQMDNAK RMETKGAGVT LNVLEMTSED LENALKAVIN DKSYKENIMR LSSLHKDRPV EPLDLAVFWV EFVMRHKGAP HLRPAAHDLT WYQYHSLD.

    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.

    Ugt1A1 Human
  • View Data Sheet

    Name :

    GSTM1 Mouse, His

    Description:

    Glutathione S-Transferase M1 Mouse Recombinant, His Tag

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

    Product # :

    ENZ-456

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    Description

    GSTM1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 28.1kDa. The GTM1 is fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM1 solution contains 20 mM Tris-HCl buffer ( pH8.0), 1mM DTT and 10% glycerol

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is < 11 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Gstm1 Mouse His
  • View Data Sheet

    Name :

    GSTM2 Human

    Description:

    Glutathione S-Transferase MU 2 Human Recombinant

    Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    Product # :

    ENZ-003

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    Description

    GSTM2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 27.9kDa. The GSTM2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol,
    0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    Citations

    More Info

    • Introduction

      Glutathione S-transferase Mu 2 (GSTM2) belongs to the glutathione s-transferase (GST) family of proteins. GSTM2 is a glutathione S-transferase that belongs to the mu class. There are 8 families of GST proteins, specifically: alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have various functions throughout the cell. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are structured in a gene cluster on chromosome 1p13.3 and are proven to be highly polymorphic. These genetic variants can change an individual''s susceptibility to carcinogens and toxins as well as have an effect on the toxicity and efficacy of several drugs.

    • Synonyms

      Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    • 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 MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK.

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    Gstm2 Human
  • View Data Sheet

    Name :

    GSTM3 Human

    Description:

    Glutathione S-Transferase MU 3 Human Recombinant

    Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.

    Product # :

    ENZ-592

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    Description

    GSTM3 Recombinant produced in E. coli is a single polypeptide chain containing 249 amino acids (1-225) and having a molecular mass of 29.1kDa.GSTM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GSTM3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl,
    1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GSTM3 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The mu type of enzymes takes part in the detoxification of electrophilic compounds, including therapeutic drugs, carcinogens, environmental toxins and products of oxidative stress, by conjugation with glutathione.

    • Synonyms

      Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione
      S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.

    • 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 MGSHMSCESS MVLGYWDIRG LAHAIRLLLE FTDTSYEEKR YTCGEAPDYD RSQWLDVKFK LDLDFPNLPY LLDGKNKITQ SNAILRYIAR KHNMCGETEE EKIRVDIIEN QVMDFRTQLI RLCYSSDHEK LKPQYLEELP GQLKQFSMFL GKFSWFAGEK LTFVDFLTYD ILDQNRIFDP KCLDEFPNLK AFMCRFEALE KIAAYLQSDQ FCKMPINNKM AQWGNKPVC

    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.

    Gstm3 Human
  • View Data Sheet

    Name :

    PTRHD1 Human

    Description:

    Peptidyl-TRNA Hydrolase Domain Containing 1 Human Recombinant

    C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.

    Product # :

    ENZ-826

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    Quantity :

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

    Description

    PTRHD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (1-140 a.a) and having a molecular mass of 18.2kDa.PTRHD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTRHD1 protein solution (1mg/ml) containing Phosphate buffer saline (pH 7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Putative peptidyl-tRNA hydrolase PTRHD1 (PTRHD1) is a 140 amino acid protein, which is encoded by a gene located on human chromosome 2p23.3. Chromosome 2 is the second largest human chromosome; it consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. Several genetic diseases are linked to genes on chromosome 2.

    • Synonyms

      C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.

    • 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 MGSMHRGVGP AFRVVRKMAA SGAEPQVLVQ YLVLRKDLSQ APFSWPAGAL VAQACHAATA ALHTHRDHPH TAAYLQELGR MRKVVLEAPD ETTLKELAET LQQKNIDHML WLEQPENIAT CIALRPYPKE EVGQYLKKFR LFK.

    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.

    Ptrhd1 Human
  • View Data Sheet

    Name :

    MAP E.coli

    Description:

    Methionine Aminopeptidase E.Coli Recombinant

    Methionine aminopeptidase, MAP, Peptidase M, map, b0168, JW0163.

    Product # :

    ENZ-123

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    More Info

    • description
    • source
    • formulation
    • purity
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    • Citations

    Description

    MAP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-264 a.a.) and having a molecular mass of 31.5kDa.MAP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAP protein solution (1mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Methionine aminopeptidases and designated peptidase M proteins belong to the M24 family of proteins. MAP protein removes the amino-terminal methionine residue from nascent polypeptides. The active site of MAP contains 2 adjacent divalent metal ions connected by a water molecule or hydroxide ion.

    • Synonyms

      Methionine aminopeptidase, MAP, Peptidase M, map, b0168, JW0163.

    • 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 MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL RKDDTIPAII SHDE.

    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.

    Map Ecoli
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