Cat: IPD-X25951

Recombinant Human RPN2/Ribophorin II Protein (HEK293),His

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Analytical Data

  • Gene name

    RPN2/Ribophorin II

  • 简介

    RPN2/riboprotein II is a key subunit of the oligosaccharyltransferase (OST) complex, which catalyzes the initial glycan transfer during co-translational protein N-glycosylation. This critical step occurs in the nascent polypeptide chain and involves the transfer of defined glycans from polyhydroxypyrophosphate to asparagine residues in the Asn-X-Ser/Thr motif. RPN2/Ribophorin II Protein, Human (HEK293, His) is the recombinant human-derived RPN2/Ribophorin II protein, expressed by HEK293 , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2; RIBIIR; RPN-II; RPN2

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P04844

  • Expression Region

    L23-V540

  • AA Sequence

    LTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSSLGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDSSVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSIVEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAIFSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPLTQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIANTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQLVDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYTLYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTV

  • Protein Length

    Lumenal Domain

  • Molecular Weight

    60 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

Ribophorin II (RPN2) is a type I transmembrane protein predominantly found in the endoplasmic reticulum, where it plays a crucial role in the early stages of N-glycosylation of glycoproteins. This glycosylation process is vital for proper protein folding, stability, and function. Research on RPN2 has gained significant interest due to its involvement in various cellular processes and its potential implications in diseases, including cancer and neurodegenerative disorders. Additionally, RPN2 serves as an important component in the ribosome-associated protein complex, influencing protein synthesis and cellular metabolism. Recent advancements in recombinant protein technology have enabled scientists to produce RPN2 in sufficient quantities, facilitating detailed studies on its structure and function. Understanding the molecular mechanisms of RPN2 can provide insights into its role in disease pathology and may lead to the development of novel therapeutic strategies targeting glycosylation pathways. The study of recombinant RPN2 not only enhances our knowledge of cellular biology but also opens up possibilities for biotechnological applications, such as the engineering of glycoproteins for improved therapeutic efficacy.

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