Cat: IPD-X36679

Recombinant Human GALNT3 Protein (HEK293),His

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Analytical Data

  • Gene name

    GALNT3

  • 简介

    GALNT3 Protein initiates O-linked oligosaccharide biosynthesis by transferring an N-acetyl-D-galactosamine residue to serine or threonine on protein receptors, including HIV envelope glycoproteins (gp120), EA2, MUC2, MUC1A, MUC5AC, and possibly fibronectin. GALNT3 also glycosylates FGF23 in vivo. GALNT3 Protein, Human (HEK293, His) is the recombinant human-derived GALNT3 protein, expressed by HEK293 , with C-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Polypeptide N-acetylgalactosaminyltransferase 3; Polypeptide GalNAc transferase 3; GalNAc-T3; pp-GaNTase 3; Protein-UDP acetylgalactosaminyltransferase 3; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3; HFTC; HHS

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q14435-1

  • Expression Region

    Q38-D633

  • AA Sequence

    QREVSVQYSKEESRMERNMKNKNKMLDLMLEAVNNIKDAMPKMQIGAPVRQNIDAGERPCLQGYYTAAELKPVLDRPPQDSNAPGASGKAFKTTNLSVEEQKEKERGEAKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKRCPPLPTTSVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDEYLHDKLDEYVKQFSIVKIVRQRERKGLITARLLGATVATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFNKPSPYGSNHNRGNFDWSLSFGWESLPDHEKQRRKDETYPIKTPTFAGGLFSISKEYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSKSPHSFPKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIVKQKAFGDLSKRFEIKHRLQCKNFTWYLNNIYPEVYVPDLNPVISGYIKSVGQPLCLDVGENNQGGKPLIMYTCHGLGGNQYFEYSAQHEIRHNIQKELCLHAAQGLVQLKACTYKGHKTVVTGEQIWEIQKDQLLYNPFLKMCLSANGEHPSLVSCNPSDPLQKWILSQND

  • Protein Length

    Lumenal Domain

  • Molecular Weight

    80.0 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

GALNT3 (UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase 3) is an enzyme belonging to the GALNT family, which plays a crucial role in the initiation of O-glycosylation, a post-translational modification that affects protein stability, localization, and function. GALNT3 is particularly significant in the context of various biological processes, including cell signaling, tissue development, and the regulation of biomolecules such as hormones and growth factors. Mutations in the GALNT3 gene have been linked to distinct pathological conditions, notably a rare disorder called familial hyperphosphatemic tumoral calcinosis, characterized by ectopic mineralization and disrupted phosphate homeostasis. Research on recombinant GALNT3 proteins aims to elucidate their functional mechanisms and interactions within the glycosylation pathways. Understanding GALNT3's role can provide insights into disease mechanisms and potential therapeutic interventions. As the field progresses, studies focusing on the structural and functional aspects of GALNT3 may reveal new avenues for addressing related disorders and enhancing our knowledge of glycosylation's impacts on human health.

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