Cat: PAX2000-10452

Recombinant Human POMT2 Protein,GST

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Analytical Data

  • Gene name

    POMT2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    A830009D15Rik; AW046274; DKFZp686G10254; Dolichyl phosphate mannose protein mannosyltransferase 2 ; Dolichyl-phosphate-mannose--protein mannosyltransferase 2; FLJ22309; LGMD2N; MDDGA2; MDDGB2; MDDGC2; POMT 2; Pomt2; POMT2_HUMAN; Protein O mannosyltransferase 2; Protein O mannosyltransferase; Protein O-mannosyl-transferase 2; Putative protein O mannosyltransferase; rCG_20643

  • Species

    Human

  • Source

    E. coli

  • Tag

    GST-tag at N-terminal

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9UKY4

  • Expression Region

    1-750 aa

  • AA Sequence

    MPPATGGGLAESELRPRRGRCGPQAARAAGRDVAAEAVARSPKRPAWGSRRFEAVGWWALLALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKYEHHSYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNSCADRPFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFAVHFMVLSKSGPGDGFFSSAFQARLSGNNLHNASIPEHLAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPLDPSFPVEFVRHGDIIRLEHKETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDHINPKLPNISLDVLQPSFPEILLESHMVMIRGNSGLKPKDNEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQRGARLPAEVAGLSQVLLRGGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPLARGIHVAGILSLLLGTAYSFYLFHPLAYGMVGPLAQDPQSPMAGLRWLDSWDF

  • Molecular Weight

    110.6 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

POMT2, or protein O-mannosyltransferase 2, is an enzyme that plays a crucial role in the post-translational modification of proteins through O-mannosylation, a process essential for the proper function of various glycoproteins. Research on POMT2 has gained significant attention due to its involvement in muscular dystrophies and other congenital disorders linked to glycosylation defects. Mutations in the POMT2 gene can lead to disorders like Fukuyama congenital muscular dystrophy and Walker-Warburg syndrome, highlighting the enzyme's importance in muscle and brain development. Understanding the enzymatic mechanisms and structural characteristics of POMT2 through recombinant protein studies can provide insights into its role in cellular processes and disease mechanisms. The production of recombinant POMT2 in various expression systems facilitates biochemical assays and structural analyses, which are essential for identifying the specific substrate interactions and elucidating the functional consequences of genetic mutations. As the field of glycobiology continues to advance, exploring POMT2's biochemical properties and its implications in human health remains a crucial area of investigation, with potential therapeutic applications aimed at correcting glycosylation defects.

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