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Search results

1000 results found for “Syntaxin”

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  • View Data Sheet

    Name :

    IFNW1 Human, HEK

    Description:

    Interferon-Omega 1 Human Recombinant, HEK

    IFN omega-1, IFN alpha-II-1, IFNW1.

    Product # :

    CYT-1225

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    Description

    IFNW1 Human Recombinant is a single, glycosylated, polypeptide chain (22-195 a.a) containing a total of 180 amino acids and having a molecular mass of 20.9 kDa. IFNW1 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The IFNW1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 is ≤0.07 ng/ml, measured  in a cytotoxicity assay using TF-1 human erythroleukemic cells .

    More Info

    • Synonyms

      IFN omega-1, IFN alpha-II-1, IFNW1.

    • 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

      LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.

    • Background

      Interferons, a family of signaling proteins, play a pivotal role in the immune system’s defense against viral infections and other threats. Among these, Interferon W1 (IFNW1), a member of the Type I interferon family, has emerged as a key player in orchestrating antiviral responses and modulating immune reactions. This research embarks on a detailed exploration of the IFNW1 protein, unveiling its structural intricacies, signaling pathways, and its broader implications in immune regulation and disease. By delving into IFNW1, scientists aim to comprehend the nuances of its functions, decipher its interactions within the complex interferon network, and explore its potential applications in therapeutic interventions and beyond.

      Structural Insights into IFNW1:

      IFNW1, like other Type I interferons, exhibits a unique tertiary structure that enables it to interact with specific cell surface receptors. This interaction triggers a cascade of events, leading to the activation of various antiviral genes and immune modulatory pathways. Understanding the structural basis of IFNW1 is crucial for elucidating its binding affinities, biological activities, and its significance in immune responses.

      Signaling Pathways and Antiviral Defense:

      IFNW1 engages with its cognate receptors, initiating Janus kinase (JAK)-Signal Transducer and Activator of Transcription (STAT) signaling pathways. This activation leads to the transcription of interferon-stimulated genes (ISGs) with potent antiviral properties. IFNW1’s ability to induce an antiviral state in infected and neighboring cells is fundamental for restricting viral replication and curtailing the spread of infections. Additionally, IFNW1 plays a role in modulating adaptive immune responses, contributing to the broader immune defense mechanisms.

      IFNW1 in Immunomodulation and Disease:

      Beyond its antiviral functions, IFNW1 is implicated in immunomodulation and disease pathogenesis. Dysregulation of IFNW1 signaling is associated with autoimmune disorders, including lupus and rheumatoid arthritis, highlighting its involvement in immune-related diseases. Moreover, IFNW1 is being explored in cancer immunotherapy, where its ability to modulate the tumor microenvironment and enhance immune surveillance presents opportunities for novel treatment strategies.

      Therapeutic Potential and Future Prospects:

      The unique properties of IFNW1, particularly its role in immune regulation and antiviral defense, position it as a potential therapeutic target. Research efforts are directed towards harnessing its immunomodulatory functions for developing therapies against infectious diseases, autoimmune disorders, and certain cancers. Additionally, understanding IFNW1’s interactions with other components of the immune system opens avenues for innovative approaches in personalized medicine and targeted immunotherapies.

      IFNW1 Protein, as an integral component of the interferon network, stands as a sentinel in the body’s defense against viral invasions and immune dysregulations. Its multifaceted roles in antiviral defense, immune modulation, and disease pathogenesis underscore its significance in biology and medicine. As researchers delve deeper into the intricacies of IFNW1, they pave the way for innovative therapies, immunomodulatory interventions, and a deeper understanding of immune responses. This research not only illuminates the pivotal role of IFNW1 but also holds the promise of transformative advancements in medicine, shaping the future of immunology and disease therapeutics.

      What is the molecular weight/Mw of IFNW1 HUMAN, HEK Protein?
      IFNW1 HUMAN, HEK Protein has a total Mw of 20.9kDa.

      What is the source or expression system of IFNW1 HUMAN, HEK Protein?
      HEK293 Cells.

      What is the Purity of IFNW1 HUMAN, HEK Protein?
      IFNW1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNW1 HUMAN, HEK Protein?
      The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .

      What is the amino acid sequence of IFNW1 HUMAN, HEK Protein?
      LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.

      What applications can IFNW1 HUMAN, HEK Protein be used in?
      IFNW1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNW1 HUMAN, HEK Protein?
      The endotoxin level is minimal, IFNW1 HUMAN, HEK 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.

    Ifn Omega Human
  • View Data Sheet

    Name :

    IL 1 alpha Mouse, His

    Description:

    Interleukin-1 alpha Mouse Recombinant, His Tag

    Interleukin-1 alpha, IL-1 alpha, Il1a.

    Product # :

    CYT-848

    Price :

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    Description

    IL 1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.4kDa.IL 1 alpha is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IL 1 alpha protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.

    • Synonyms

      Interleukin-1 alpha, IL-1 alpha, Il1a.

    • 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 MGSSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQIS.

    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.

    Il 1 Alpha Mouse His
  • View Data Sheet

    Name :

    SRM Human

    Description:

    Spermidine Synthase Human Recombinant

    Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.

    Product # :

    ENZ-027

    Price :

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    Description

    SRM 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 322 amino acids (1-302 a.a.) and having a molecular mass of 36kDa. The SRM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SRM is an enzyme which catalyzes the transfer of the propylamine group from S-adenosylmethioninamine to putrescine in the biosynthesis of spermidine. The polyamines putrescine, spermine and spermidine are ubiquitous polycationic mediators of cell growth and differentiation. The SRM protein is one of four enzymes in the polyamine-biosynthetic pathway and completes the final step of spermidine biosynthesis.

    • Synonyms

      Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.

    • 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 MEPGPDGPAA SGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV VQCEIDEDVI QVSKKFLPGM AIGYSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP AESLFKESYY QLMKTALKED GVLCCQGECQ WLHLDLIKEM RQFCQSLFPV VAYAYCTIPT YPSGQIGFML CSKNPSTNFQ EPVQPLTQQQ VAQMQLKYYN SDVHRAAFVL PEFARKALND VS.

    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.

    Srm Human
  • View Data Sheet

    Name :

    STAMBP Human

    Description:

    STAM Binding Protein Human Recombinant

    STAM-binding protein, Associated molecule with the SH3 domain of STAM, Endosome-associated ubiquitin isopeptidase, AMSH, EC 3.1.2.15, EC 3.4.19, MICCAP.

    Product # :

    PRO-017

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    Description

    STAMBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424) and having a molecular mass of 50kDa. STAMBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STAMBP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE..

    More Info

    • Introduction

      STAM Binding Protein (STAMBP) is a zinc metalloprotease which specifically cleaves Lys-63-linked polyubiquitin chains, however it doesn’t cleave Lys-48-linked polyubiquitin chains. STAMBP has a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. In addition, STAMBP potentiates BMP signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. STAMBP also has a major role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is essential for efficient EGFR degradation but not for its internalization. STAMBP is also involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.

    • Synonyms

      STAM-binding protein, Associated molecule with the SH3 domain of STAM, Endosome-associated ubiquitin isopeptidase, AMSH, EC 3.1.2.15, EC 3.4.19, MICCAP.

    • 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 MGSMSDHGDV SLPPEDRVRA LSQLGSAVEV NEDIPPRRYF RSGVEIIRMA SIYSEEGNIE HAFILYNKYI TLFIEKLPKH RDYKSAVIPE KKDTVKKLKE IAFPKAEELK AELLKRYTKE YTEYNEEKKK EAEELARNMA IQQELEKEKQ RVAQQKQQQL EQEQFHAFEE MIRNQELEKE RLKIVQEFGK VDPGLGGPLV PDLEKPSLDV FPTLTVSSIQ PSDCHTTVRP AKPPVVDRSL KPGALSNSES IPTIDGLRHV VVPGRLCPQF LQLASANTAR GVETCGILCG KLMRNEFTIT HVLIPKQSAG SDYCNTENEE ELFLIQDQQG LITLGWIHTH PTQTAFLSSV DLHTHCSYQM MLPESVAIVC SPKFQETGFF KLTDHGLEEI SSCRQKGFHP HSKDPPLFCS CSHVTVVDRA VTITDLR.

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    Stambp Human
  • View Data Sheet

    Name :

    STAP1 Human

    Description:

    Signal Transducing Adaptor Family Member 1 Human Recombinant

    Signal-transducing adaptor protein 1, STAP-1, BCR downstream-signaling protein 1, Docking protein BRDG1, Stem cell adaptor protein 1, STAP1, BRDG1.

    Product # :

    PRO-1110

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    Description

    STAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 319 amino acids (1-295 a.a) and having a molecular mass of 36.8kDa.STAP1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STAP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Signal-transducing adaptor protein 1 (STAP1) acts as a docking protein which operates downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The STAP1 protein is directly phosphorylated by Tec in vitro where it partakes in a positive feedback loop, increasing Tec activity.

    • Synonyms

      Signal-transducing adaptor protein 1, STAP-1, BCR downstream-signaling protein 1, Docking protein BRDG1, Stem cell adaptor protein 1, STAP1, BRDG1.

    • 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 MGSHMMAKKP PKPAPRRIFQ ERLKITALPL YFEGFLLIKR SGYREYEHYW TELRGTTLFF YTDKKSIIYV DKLDIVDLTC LTEQNSTEKN CAKFTLVLPK EEVQLKTENT ESGEEWRGFI LTVTELSVPQ NVSLLPGQVI KLHEVLEREK KRRIETEQST SVEKEKEPTE DYVDVLNPMP ACFYTVSRKE ATEMLQKNPS LGNMILRPGS DSRNYSITIR QEIDIPRIKH YKVMSVGQNY TIELEKPVTL PNLFSVIDYF VKETRGNLRP FICSTDENTG QEPSMEGRSE KLKKNPHIA.

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    Stap1 Human
  • View Data Sheet

    Name :

    SULT1A2 Human

    Description:

    Sulfotransferase Family, Cytosolic, 1A, Member 2 Human Recombinant

    Sulfotransferase 1A2, ST1A2, Aryl sulfotransferase 2, Phenol sulfotransferase 2, Phenol-sulfating phenol sulfotransferase 2, P-PST 2, SULT1A2, STP2, HAST4, TSPST2.

    Product # :

    ENZ-152

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    Description

    SULT1A2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295 a.a.) and having a molecular mass of 36.4kDa.SULT1A2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SULT1A2 protein solution (1mg/ml) containing 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.

    More Info

    • Introduction

      Sulfotransferase 1A2 (SULT1A2) belongs to the sulfotransferase family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. SULT1A2 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and might thus participate as a modulating factor of cancer risk.

    • Synonyms

      Sulfotransferase 1A2, ST1A2, Aryl sulfotransferase 2, Phenol sulfotransferase 2, Phenol-sulfating phenol sulfotransferase 2, P-PST 2, SULT1A2, STP2, HAST4, TSPST2.

    • 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 MELIQDISRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG TTWVSQILDM IYQGGDLEKC HRAPIFMRVP FLEFKVPGIP SGMETLKNTP APRLLKTHLP LALLPQTLLD QKVKVVYVAR NAKDVAVSYY HFYHMAKVYP HPGTWESFLE KFMAGEVSYG SWYQHVQEWW ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETV DLMVEHTSFK EMKKNPMTNY TTVRREFMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL.

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    Sult1A2 Human
  • View Data Sheet

    Name :

    CCL21 Human

    Description:

    Exodus-2 Human Recombinant (CCL21)

    Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.

    Product # :

    CHM-332

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    Description

    Exodus-2 Human Recombinant produced in E.Coli as a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12219 Dalton. The CCL21 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM Phosphate Buffer, pH 7.4 and 150mM NaCl.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human total lymphocyte population using a concentration range of 10-100ng/ml.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 21 (CCL21) is a small cytokine belonging to the CC chemokine family. This chemokine is also known as 6Ckine (because it has six conserved cysteine residues instead of the four cysteines typical to chemokines), exodus-2, and secondary lymphoid-tissue chemokine (SLC). CCL21 is expressed predominantly in the lymph nodes and, in contrast to other CC chemokines, is chemotactic for lymphocytes. The gene for CCL21 is located on human chromosome 9. CCL21 elicits its effects by binding to a cell surface chemokine receptor known as CCR7.

    • Synonyms

      Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Exodus-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL21 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 Exodus2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SDGGAQDCCL KYSQRKIPAK VVRSYRKQEP SLGCSIPAIL FLPRKRSQAE LCADPKELWV QQLMQHLDKT PSPQKPAQGC RKDRGASKTG KKGKGSKGCR KTERSQTPKG P.

    • Background

      What is the molecular weight/Mw of CCL21 HUMAN Protein?
      CCL21 HUMAN Protein has a total Mw of 12.21kDa.

      What is the source or expression system of CCL21 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL21 HUMAN Protein?
      CCL21 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL21 HUMAN Protein?
      Determined by its ability to chemoattract human total lymphocyte population using a concentration range of 10-100ng/ml.

      What is the amino acid sequence of CCL21 HUMAN Protein?
      SDGGAQDCCL KYSQRKIPAK VVRSYRKQEP SLGCSIPAIL FLPRKRSQAE LCADPKELWV QQLMQHLDKT PSPQKPAQGC RKDRGASKTG KKGKGSKGCR KTERSQTPKG P.

      What applications can CCL21 HUMAN Protein be used in?
      CCL21 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL21 HUMAN Protein?
      The endotoxin level is minimal, CCL21 HUMAN Protein was purified using conventional chromatography techniques.


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    Ccl21 Human
  • View Data Sheet

    Name :

    SUMO3 Human

    Description:

    Small Ubiquitin-Related Modifier 3 Human Recombinant

    SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.

    Product # :

    PRO-267

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    Description

    SUMO3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (1-92a.a.) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).SUMO3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SUMO3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl,1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SUMO3 belongs to the SUMO protein family and operates like ubiquitin. Nevertheless, unlike ubiquitin that targets proteins for degradation, SUMO3 protein takes part in several cellular processes, like nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO3 regulates amyloid beta generation and is crucial in the onset or progression of Alzheimer’s disease.

    • Synonyms

      SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.

    • 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 MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GG

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    Sumo3 Human
  • View Data Sheet

    Name :

    TBCEL Human

    Description:

    Tubulin Folding Cofactor E-Like Human Recombinant

    Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    Product # :

    PRO-030

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    Description

    TBCEL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. The TBCEL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.

    • Synonyms

      Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    • 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 MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.

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    Tbcel Human
  • View Data Sheet

    Name :

    CCNI Human

    Description:

    Cyclin-I Human Recombinant

    Cyclin-I, CCNI, CYC1, CYI.

    Product # :

    PKA-318

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    Description

    CCNI Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 400 amino acids (1-377 a.a) and having a molecular mass of 44.9kDa.CCNI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCN1 is a part of the extremely conserved cyclin family, whose members are characterized by a remarkable periodicity in protein abundance through the cell cycle. Cyclins which function as regulators of CDK kinases, shows the highest similarity with cyclin G. Different cyclins display diverse expression and degradation patterns which contribute to the chronological coordination of every mitotic event. The transcript of CCN1was found to be expressed continually during cell cycle progression.

    • Synonyms

      Cyclin-I, CCNI, CYC1, CYI.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMKFPGPL ENQRLSFLLE KAITREAQMW KVNVRKMPSN QNVSPSQRDE VIQWLAKLKY QFNLYPETFA LASSLLDRFL ATVKAHPKYL SCIAISCFFL AAKTVEEDER IPVLKVLARD SFCGCSSSEI LRMERIILDK LNWDLHTATP LDFLHIFHAI AVSTRPQLLF SLPKLSPSQH LAVLTKQLLH CMACNQLLQF RGSMLALAMV SLEMEKLIPD WLSLTIELLQ KAQMDSSQLI HCRELVAHHL STLQSSLPLN SVYVYRPLKH TLVTCDKGVF RLHPSSVPGP DFSKDNSKPE VPVRGTAAFY HHLPAASGCK QTSTKRKVEE MEVDDFYDGI KRLYNEDNVS ENVGSVCGTD LSRQEGHASP CPPLQPVSVM.

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    Ccni Human
  • View Data Sheet

    Name :

    GCSH Human

    Description:

    Glycine Cleavage System Protein H Human Recombinant

    Glycine cleavage system protein H (aminomethyl carrier), NKH, GCE, Lipoic acid-containing protein, Mitochondrial glycine cleavage system H-protein.

    Product # :

    PRO-973

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    Description

    GCSH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (48-173) and having a molecular mass of 16.4 kDa.GCSH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      There are four mitochondrial proteins composing the enzyme system for cleavage of glycine (glycine cleavage system): P protein, H protein, T protein, and L protein. GCSH is the H protein. GCSH transfers the methylamine group of glycine from the P protein to the T protein. Mutations in this gene results in nonketotic hyperglycinemia (NKH).

    • Synonyms

      Glycine cleavage system protein H (aminomethyl carrier), NKH, GCE, Lipoic acid-containing protein, Mitochondrial glycine cleavage system H-protein.

    • 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 MGSMSVRKFT EKHEWVTTEN GIGTVGISNF AQEALGDVVY CSLPEVGTKL NKQDEFGALE SVKAASELYS PLSGEVTEIN EALAENPGLV NKSCYEDGWL IKMTLSNPSE LDELMSEEAY EKYIKSIEE

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    Gcsh Human
  • View Data Sheet

    Name :

    CDC123 Human

    Description:

    Cell Division Cycle 123 Human Recombinant

    C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    Product # :

    PRO-1463

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    Description

    CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.

    • Synonyms

      C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    • 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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD

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    Cdc123 Human
  • View Data Sheet

    Name :

    CDC26 Human

    Description:

    Cell Division Cycle  26 Human Recombinant

    Anaphase-promoting complex subunit CDC26, Anaphase-promoting complex subunit 12, APC12, Cell division cycle protein 26 homolog, CDC26, ANAPC12, C9orf17.

    Product # :

    PRO-241

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    Description

    CDC26 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-85 a.a) and having a molecular mass of 11.9kDa.CDC26 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDC26 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDC26 is a member of the CDC26 family which arranges progression via mitosis by enhancing cell-cycle regulators with ubiquitin chains. CDC26 is a component of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated E3 ubiquitin ligase which directs progression through mitosis and the G1 phase of the cell cycle. The APC/C complex operates by mediating ubiquitination and subsequent degradation of target proteins.

    • Synonyms

      Anaphase-promoting complex subunit CDC26, Anaphase-promoting complex subunit 12, APC12, Cell division cycle protein 26 homolog, CDC26, ANAPC12, C9orf17.

    • 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 MLRRKPTRLE LKLDDIEEFE NIRKDLETRK KQKEDVEVVG GSDGEGAIGL SSDPKSREQM INDRIGYKPQ PKPNNRSSQF GSLEF.

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    Cdc26 Human
  • View Data Sheet

    Name :

    CDC42 Human

    Description:

    Cell Division Cycle 42 Human Recombinant

    Cell division control protein 42 homolog, G25K GTP-binding protein, CDC42, G25K, CDC42Hs.

    Product # :

    PRO-727

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    Description

    CDC42 Human Recombinant fused with a 15 amino acid T7 tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids (1-188 a.a.) and having a molecular mass of 22.4kDa.The CDC42 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDC42 solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 10% glycerol and 2mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDC42 (Cell division cycle 42 isoform 1) is a small GTPase of the Rho-subfamily that regulates signaling pathways which control various cellular functions including cell morphology, migration, endocytosis and cell cycle progression. CDC42 is a plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In the active state, CDC42 binds to a variety of effector proteins to regulate cellular responses. CDC42 is involved in epithelial cell polarization processes. CDC42 causes the formation of thin, actin-rich surface projections called filopodia. Also, CDC42 regulates actin polymerization through its direct binding to N-WASP (Neural Wiskott-Aldrich syndrome protein), which subsequently activates Arp2/3 complex.
      Loss of CDC42 function raises endocytotic uptake of apical proteins, as well as apical polarity factors such as Crumbs. The product of oncogene Dbl was described to specifically catalyze the dissociation of GDP from CDC42 protein.

    • Synonyms

      Cell division control protein 42 homolog, G25K GTP-binding protein, CDC42, G25K, CDC42Hs.

    • 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

      MASMTGGQQM GRGSHMQTIK CVVVGDGAVG KTCLLISYTT NKFPSEYVPT VFDNYAVTVM IGGEPYTLGL FDTAGQEDYD RLRPLSYPQT DVFLVCFSVV SPSSFENVKE KWVPEITHHC PKTPFLLVGT QIDLRDDPST IEKLAKNKQK PITPETAEKL ARDLKAVKYV ECSALTQKGL KNVFDEAILA ALEPPEPKKS RRC.

    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.

    Cdc42 Human
  • View Data Sheet

    Name :

    PRDX5 Human

    Description:

    Peroxiredoxin-5 Human Recombinant

    Peroxiredoxin-5 mitochondrial, Prx-V, Peroxisomal antioxidant enzyme, Thioredoxin reductase, Thioredoxin peroxidase PMP20, Antioxidant enzyme B166, TPx type VI, Liver tissue 2D-page spot 71B, Alu corepressor 1, PLP, ACR1, B166, PRXV, PMP20, PRDX6, SBBI10, AOEB166, MGC117264, MGC142283, MGC142285, PRDX5.

    Product # :

    ENZ-426

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    Description

    PRDX5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids (53-214 a.a.) and having a molecular mass of 17 kDa.The PRDX5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRDX5 solution contains 20mM HEPES buffer (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be approximately 117-136 pmole/min/µg. The enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX5 and peroxide for 20 min at room temperature. Specific activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25°C for 1 minute.

    More Info

    • Introduction

      PRDX5 belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides with reducing equivalents supplied through the thioredoxin system. PRDX5 has an antioxidant protective function in different tissues under normal conditions and during inflammatory processes. Peroxiredoxin-5 interacts with peroxisome receptor 1 and is involved in intracellular redox signaling. PRDX5 is involved in intracellular redox signaling. Peroxiredoxin-5 is a significant antioxidant protein of lung epithelial cells for its expression in the human lung increases during inflammation. PRDX5 expression is upregulated in osteoarthritis. PRDX5 may be significant in mitochondrial genome stability. Peroxiredoxin-5 has a protective role in human tendon cells against oxidative stress by reducing apoptosis and upholding collagen synthesis.

    • Synonyms

      Peroxiredoxin-5 mitochondrial, Prx-V, Peroxisomal antioxidant enzyme, Thioredoxin reductase, Thioredoxin peroxidase PMP20, Antioxidant enzyme B166, TPx type VI, Liver tissue 2D-page spot 71B, Alu corepressor 1, PLP, ACR1, B166, PRXV, PMP20, PRDX6, SBBI10, AOEB166, MGC117264, MGC142283, MGC142285, PRDX5.

    • 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

      MAPIKVGDAI PAVEVFEGEP GNKVNLAELF KGKKGVLFGV PGAFTPGCSK THLPGFVEQA EALKAKGVQV VACLSVNDAF VTGEWGRAHK AEGKVRLLAD PTGAFGKETD LLLDDSLVSI FGNRRLKRFS MVVQDGIVKA LNVEPDGTGL TCSLAPNIIS QL.

    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.

    Prdx5 Human
  • View Data Sheet

    Name :

    PRDX6 Human

    Description:

    Peroxiredoxin-6 Human Recombinant

    Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.

    Product # :

    ENZ-432

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    Description

    Peroxiredoxin- 6 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 27.1kDa.The Peroxiredoxin-6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Peroxiredoxin-6 solution contains 20mM Tris-HCl buffer (pH8.0) and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >2,000pmol/min/ug was defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for 1minute. 

    More Info

    • Introduction

      Peroxiredoxin 6 (PRDX6) belongs to the thiol-specific antioxidant protein family. PRDX6 is a bifunctional enzyme with 2 distinct active sites. PRDX6 is involved in redox regulation of the cell and can reduce Hydrogen peroxide and short chain organic, fatty acid, and phospholipid hydroperoxides. PRDX6 may have a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Furthermore, PRDX6 eases the oxidative stress and TGF-beta-induced abnormalities of human trabecular meshwork cells. In addition, PRDX6 is necessary for blood vessel integrity in injured skin.
      At acidic pH, PRDX6 binds to reduced phospholipids, however at cytosolic pH PRDX6 binds only to phospholipids that are oxidized which is compatible with the role for PRDX6 in the repair of peroxidized cell membranes. Hydrogen peroxide-mediated hyperoxidation of PRDX6 induces cell cycle arrest at the G2/M transition via up-regulation of iPLA2 activity. Overexpression of PRDX6 is linked to oligodendroglioma.

    • Synonyms

      Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.

    • 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 MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF PIIDDRNREL AILLGMLDPA EKDEKGMPVT ARVVFVFGPD KKLKLSILYP ATTGRNFDEI LRVVISLQLT AEKRVATPVD WKDGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP.

    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.

    Prdx6 Human
  • View Data Sheet

    Name :

    CDKN3 Human

    Description:

    Cyclin-Dependent Kinase Inhibitor 3 Human Recombinant

    Cyclin-dependent kinase inhibitor 3, CDK2-associated dual-specificity phosphatase, Cyclin-dependent kinase interactor 1, Cyclin-dependent kinase-interacting protein 2, Kinase-associated phosphatase, KAP, CDI1, CIP2, KAP1, FLJ25787, MGC70625, CDKN3.

    Product # :

    PKA-336

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    Description

    CDKN3 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 232 amino acids (1-212 a.a.) and having a molecular mass of 25.9kDa. The CDKN3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDKN3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cyclin-dependent kinase inhibitor 3 (CDKN3) is a member of the dual specificity protein phosphatase family. CDKN3 was identified as a cyclin-dependent kinase inhibitor, and was shown to interact with, and dephosphorylate CDK2 kinase, consequently prevent the activation of CDK2 kinase. In addition CDKN3 is important in cell cycle regulation. The CDKN3 gene was reported to be deleted, mutated, or overexpressed in several kinds of cancers.

    • Synonyms

      Cyclin-dependent kinase inhibitor 3, CDK2-associated dual-specificity phosphatase, Cyclin-dependent kinase interactor 1, Cyclin-dependent kinase-interacting protein 2, Kinase-associated phosphatase, KAP, CDI1, CIP2, KAP1, FLJ25787, MGC70625, CDKN3.

    • 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 MKPPSSIQTS EFDSSDEEPI EDEQTPIHIS WLSLSRVNCS QFLGLCALPG CKFKDVRRNV QKDTEELKSC GIQDIFVFCT RGELSKYRVP NLLDLYQQCG IITHHHPIAD GGTPDIASCC EIMEELTTCL KNYRKTLIHC YGGLGRSCLV AACLLLYLSD TISPEQAIDS LRDLRGSGAI QTIKQYNYLH EFRDKLAAHL SSRDSQSRSV SR.

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    Cdkn3 Human
  • View Data Sheet

    Name :

    TTC1 Human

    Description:

    Tetratricopeptide Repeat Domain 1 Human Recombinant

    Tetratricopeptide repeat protein 1, TPR repeat protein 1, TTC1, TPR1.

    Product # :

    PRO-1160

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    Description

    TTC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-292 a.a) and having a molecular mass of 36.1kDa (Molecular weight on SDS-PAGE will appear higher).TTC1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TTC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Tetratricopeptide repeat protein 1 (TTC1) is comprised of 292 amino acids with 3 TPR motifs, such as a Galpha16-binding protein. This interaction is confirmed both in vitro and in transfected mammalian cells, where TTC1 also binds to a number of other Galpha proteins. TTC1 interacts with Ha-Ras especially in its active form. TTC1 also interacts with the GAP domain of NF1.

    • Synonyms

      Tetratricopeptide repeat protein 1, TPR repeat protein 1, TTC1, TPR1.

    • 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 MGSHMGEKSE NCGVPEDLLN GLKVTDTQEA ECAGPPVPDP KNQHSQSKLL RDDEAHLQED QGEEECFHDC SASFEEEPGA DKVENKSNED VNSSELDEEY LIELEKNMSD EEKQKRREES TRLKEEGNEQ FKKGDYIEAE SSYSRALEMC PSCFQKERSI LFSNRAAARM KQDKKEMAIN DCSKAIQLNP SYIRAILRRA ELYEKTDKLD EALEDYKSIL EKDPSIHQAR EACMRLPKQI EERNERLKEE MLGKLKDLGN LVLRPFGLST ENFQIKQDSS TGSYSINFVQ NPNNNR.

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    Ttc1 Human
  • View Data Sheet

    Name :

    UBE2I Human His

    Description:

    Ubiquitin-Conjugating Enzyme E2I Human Recombinant, His Tag

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

    Product # :

    ENZ-274

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

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    • 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 :

    CKBB Human His

    Description:

    Creatine Kinase Brain Human Recombinant, His Tag

    EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.

    Product # :

    CKI-274

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    Description

    CKBB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-381 a.a.) and having a molecular mass of 44.8 kDa. The CKB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CKBB Human solution containing 20mM Trsi pH-8, 1mM DTT, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CKB is a cytoplasmic enzyme that takes part in energy homeostasis. CKB enzyme reversibly catalyzes the transfer of phosphate among ATP and various phosphogens such as creatine phosphate. CKB functions as a homodimer in the brain as well as in different tissues, and as a heterodimer with a similar muscle isozyme in heart. Creatine kinases supply the energy of phosphate hydrolysis essential to drive the normal role of many cellular systems including muscle, tumor and cancer cells.

    • Synonyms

      EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD
      RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.

    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.

    Ckb Human
  • View Data Sheet

    Name :

    UMPS Human

    Description:

    Uridine Monophosphate Synthetase Human Recombinant

    OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.

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    ENZ-663

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    Description

    UMPS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 500 amino acids (1-480 a.a) and having a molecular mass of 54.3kDa.UMPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UMPS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Uridine 5'-monophosphate synthase (UMPS), is a bifunctional enzyme that catalyzes the ultimate two steps of the de novo pyrimidine biosynthetic pathway. UMPS in eukaryotes links the orotate phosphoribosyltransferase and the orotidine-5’-monophosphate (OMP) decarboxylase activities into a single protein. The harmony of these 2 enzymes is assumed to be stabilized the catalytic centers as a result of the low molar concentration of the protein in mammalian cells.mutations in this gene are the reason of inherited orotic aciduria disease.

    • Synonyms

      OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.

    • 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 MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV.

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    Umps Human
  • View Data Sheet

    Name :

    PTGES2 Human

    Description:

    Prostaglandin E Synthase 2 Human Recombinant

    Prostaglandin E synthase 2, Microsomal prostaglandin E synthase 2, mPGES-2, PTGES2, C9orf15, PGES2, GBF1.

    Product # :

    ENZ-136

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    Description

    PTGES2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-186 a.a.) and having a molecular mass of 23.5kDa.PTGES2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTGES2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PTGES2 is a membrane-associated prostaglandin E synthase, which catalyzes the conversion of prostaglandin H2 to prostaglandin E2. Additionally, PTGES2 activates the transcription regulated by a gamma-INF-activated transcription element. PTGES2 is widely expressed- in the heart, including apex, inter-ventricular septum, both atria and ventricles, but not in the aorta. PTGES2 is also expressed in fetal heart. PTGES2 is detected in various regions of the brain: cerebellum; occipital, frontal and parietal lobes. It is also expressed in the lymph nodes, skeletal muscle, kidney and trachea, but not in the thymus or lung. PTGES2 is overexpressed in colorectal cancer.

    • Synonyms

      Prostaglandin E synthase 2, Microsomal prostaglandin E synthase 2, mPGES-2, PTGES2, C9orf15, PGES2, GBF1.

    • 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 MKAVNEQGKE VTEFGNKYWL MLNEKEAQQV YGGKEARTEE MKWRQWADDW LVHLISPNVY RTPTEALASF DYIVREGKFG AVEGAVAKYM GAAAMYLISK RLKSRHRLQD NVREDLYEAA DKWVAAVGKD RPFMGGQKPN LADLAVYGVL RVMEGLDAFD DLMQHTHIQP WYLRVERAIT EASPAH.

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    Ptges2 Human
  • View Data Sheet

    Name :

    CLTB Human

    Description:

    Clathrin, Light Chain B Human Recombinant

    Clathrin light chain B, Lcb, CLTB.

    Product # :

    PRO-1172

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    Description

    CLTB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-211 a.a) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear higher).CLTB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLTB protein solution (1mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 0.2mM PMSF and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Clathrin light chain B (CLTB) is a member of the clathrin light chain family. Clathrin is a protein that has a key role in the formation of coated vesicles. CLTB functions as the key structural component of the lattice-type cytoplasmic face of coated pits and vesicles which capture certain macromolecules during receptor-mediated endocytosis. CLTB forms a triskelion form comprised of 3 clathrin heavy chains and 3 light chains. When the triskelia interact they form a polyhedral pattern which encircles the vesicle. CME (Clathrin-mediated endocytosis) controls numerous cellular physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission.

    • Synonyms

      Clathrin light chain B, Lcb, CLTB.

    • 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 MGSMADDFGF FSSSESGAPE AAEEDPAAAF LAQQESEIAG IENDEGFGAP AGSHAAPAQP GPTSGAGSED MGTTVNGDVF QEANGPADGY AAIAQADRLT QEPESIRKWR EEQRKRLQEL DAASKVTEQE WREKAKKDLE EWNQRQSEQV EKNKINNRAS
      EEAFVKESKE ETPGTEWEKV AQLCDFNPKS SKQCKDVSRL RSVLMSLKQT PLSR.

    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.

    Cltb Human
  • View Data Sheet

    Name :

    GSTA1 Mouse

    Description:

    Glutathione S-Transferase Alpha 1 Mouse Recombinant

    Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.

    Product # :

    ENZ-873

    Price :

    Quantity :

    Shipping Method :

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    More Info

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

    Description

    GSTA1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.a) and having a molecular mass of 28kDa.GSTA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTA1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity is defined as the amount of enzyme that conjugate 1.0 pmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C and is > 4,000 pmol/min/ug.

    More Info

    • Introduction

      Membrane-bound & Cytosolic forms of GST are encoded by 2 separate supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. There are 8 different classes of soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTA1 is found in a cluster mapped to chromosome 6, and is highly expressed in the liver. GSTA1 protects the cells from reactive oxygen species.

    • Synonyms

      Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.

    • 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 MGSMAGKPVL HYFNARGRME CIRWLLAAAG VEFEEKFIQS PEDLEKLKKD GNLMFDQVPM VEIDGMKLAQ TRAILNYIAT KYDLYGKDMK ERALIDMYSE GILDLTEMIG QLVLCPPDQR EAKTALAKDR TKNRYLPAFE KVLKSHGQDY LVGNRLTRVD IHLLEVLLYV EEFDASLLTP FPLLKAFKSR ISSLPNVKKF LQPGSQRKPP MDAKQIQEAR KAFKIQ.

    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.

    Gsta1 Mouse
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