Cat: IPD-X37065

Recombinant Human GALNT10 Protein (HEK293),His

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Analytical Data

  • Gene name

    GALNT10

  • 简介

    GALNT10 protein assumes a crucial role in the initiation of O-linked oligosaccharide biosynthesis, facilitating the transfer of an N-acetyl-D-galactosamine residue to specific serine or threonine residues on protein receptors. With its catalytic activity, GALNT10 demonstrates specificity towards substrates such as Muc5Ac and EA2 peptides, contributing to the intricate process of protein glycosylation and subsequent cellular functions. GALNT10 Protein, Human (HEK293, His) is the recombinant human-derived GALNT10 protein, expressed by HEK293 , with N-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Polypeptide N-acetylgalactosaminyltransferase 10; GalNAc-T10

  • Species

    Human

  • Source

    HEK293

  • Tag

    N-10*His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    Q86SR1-1

  • Expression Region

    T39-N603

  • AA Sequence

    TPGGSGAAVAPAAGQGSHSRQKKTFFLGDGQKLKDWHDKEAIRRDAQRVGNGEQGRPYPMTDAERVDQAYRENGFNIYVSDKISLNRSLPDIRHPNCNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEIVLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHCEANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIPPELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRMEDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDVAVQKKLRSSLNCKSFKWFMTKIAWDLPKFYPPVEPPAAAWGEIRNVGTGLCADTKHGALGSPLRLEGCVRGRGEAAWNNMQVFTFTWREDIRPGDPQHTKKFCFDAISHTSPVTLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRIFMNTCNPSSLTQQWLFEHTNSTVLEKFNRN

  • Protein Length

    Partial

  • Molecular Weight

    70-75 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

GALNT10, a member of the polypeptide N-acetylgalactosaminyltransferase (GALNT) family, plays a crucial role in the O-glycosylation of proteins, a post-translational modification that influences various biological processes, including cell adhesion, signaling, and immune responses. Research has revealed that GALNT10 is involved in the glycosylation of mucins and other glycoproteins, which are essential for maintaining epithelial integrity and function. Abnormal expression or activity of GALNT enzymes, including GALNT10, has been linked to various diseases, particularly cancer, where altered glycosylation patterns can contribute to tumor progression and metastasis. Understanding the functional mechanisms of GALNT10 is vital for elucidating its role in both normal physiological processes and disease states. By studying the recombinant GALNT10 protein, researchers aim to dissect its enzymatic activity, substrate specificity, and regulatory mechanisms. Additionally, investigating GALNT10 may provide insights into potential therapeutic targets for modulating glycosylation processes in diseases characterized by aberrant glycosylation patterns. Overall, the study of GALNT10 is essential for advancing our knowledge of glycosylation biology and its implications in health and disease.

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