Recombinant OST48 protein (His tag)

Recombinant OST48 protein (His tag)

Cat.#: 542307

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Product Information

  • Product Name
    Recombinant OST48 protein (His tag)
  • Documents
  • Description

    This product is a recombinant fragment of the human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit (DDOST 48 kDa subunit), encompassing amino acids 43-427. It is designed for structural and biochemical studies, offering a stable and soluble unit ideal for investigating oligosaccharyl transferase (OST) complex function and N-glycosylation mechanisms.

    The full-length DDOST protein is a critical subunit of the oligosaccharyl transferase (OST) complex, which catalyzes the initial step of protein N-glycosylation by transferring a defined glycan from dolichol-pyrophosphate to asparagine residues within Asn-X-Ser/Thr motifs in nascent polypeptides. This process occurs cotranslationally in the endoplasmic reticulum (ER) membrane, where the OST complex associates with the Sec61 translocon. DDOST is essential for maximal enzyme activity and required for assembling both SST3A- and SS3B-containing OST complexes, playing a key role in cellular protein modification and quality control. The protein is localized to the ER membrane as a single-pass type I membrane protein, underscoring its importance in ER-related functions.

  • Protein name
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
  • Uniprot ID
    P39656
  • Gene Name
    DDOST; KIAA0115; OST48
  • Source/Expression Host
    E. coli
  • Expression Plasmid/cDNA
    DNA encoding 43-427 aa (P39656) were fused with 6His tag.
  • Protein Species
    Human
  • Molecular weight
    Predictes a molecular mass of 44.36 kDa. In SDS-PAGE under reducing conditions, it migrates as an approximately 44 kDa band.
  • Purity
    >89%, by SDS-PAGE with Coomassie Brilliant Blue staining.
  • Activity
    Not tested.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"