Cat: IPD-X27570

Recombinant Human GALNTL1 Protein (HEK293),His

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Analytical Data

  • Gene name

    GALNTL1

  • 简介

    GALNTL1 protein plays a pivotal role in O-linked oligosaccharide biosynthesis by catalyzing the crucial initial step—the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. This enzymatic activity is fundamental for the glycosylation processes that modulate the structure and function of various proteins, impacting diverse cellular functions. GALNTL1 Protein, Human (HEK293, His) is the recombinant human-derived GALNTL1 protein, expressed by HEK293 , with C-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8N428-1

  • Expression Region

    D27-T558

  • AA Sequence

    DNRAHAASSGGRGAQRAGRRSEQLREDRTIPLIVTGTPSKGFDEKAYLSAKQLKAGEDPYRQHAFNQLESDKLSPDRPIRDTRHYSCPSVSYSSDLPATSVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLLTRIPKVKCLRNDRREGLIRSRVRGADVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKMTRTDPTRPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFRKRHPYNFPEGNALTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNCKSFRWYLENVYPELTVPVKEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLIQQQGKCLAATSTLMSSPGSPVILQMCNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT

  • Protein Length

    Lumenal Domain

  • Molecular Weight

    62-65 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

GALNTL1 (GalNAc-type O-Glycans Transferase-Like 1) is a member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, involved in the initiation of O-glycosylation, a process critical for protein function and stability. O-glycosylation is essential for various biological processes, including cell signaling, adhesion, and differentiation. The GALNTL1 protein plays a unique role in modulating the glycosylation patterns of target proteins, impacting cellular functions such as growth and apoptosis. Research into GALNTL1 has garnered attention due to its potential implications in cancer biology, as altered glycosylation states are often associated with tumor progression and metastasis. Furthermore, GALNTL1 may have therapeutic potential, making it a target for drug development aimed at diseases linked to abnormal glycosylation. Understanding the structure and function of GALNTL1 is crucial for elucidating its role in glycan-mediated processes and for exploring its potential as a biomarker or therapeutic target. Studies focusing on the expression, enzymatic activity, and substrate specificity of GALNTL1 will provide insights into its biological significance and pave the way for novel therapeutic strategies in oncology and beyond.

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