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Recombinant human VPS35 protein

Cat:P04678

Summary:

【Derived From】: E.coli
【Endotoxin】: Not measured
【Amino Acid】: 1-350aa
【Purity】: ≥85% by SDS-PAGE.
【Name】: VPS35
【Full Name】: vacuolar protein sorting 35 homolog (S. cerevisiae)
【Uniprot】: Q96QK1
【Gene ID】: 55737
【Species Reactivity】: Human Mouse (Bovine ZebraFish)
【Mol Mass】: 40kDa
【Application】: Immunology research
【Purification】: NI-NTA affinity purification
【Bioactive】: N0
【Tag】: With a 6×His tag at the N/C-terminus.
【Concentration】: 1mg/ml by SDS-PAGE.

Store:

【Reconstitution】: Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water.)
【Storage】: Reconstituted protein solution can be stored at 4-7℃ for 1-2 weeks, stored at < -20℃ for 1 year.
【Formulation】: Powder: Lyophilized from a 0.2 μm filtered solution of 2-8M Urea, 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0.

Background:

Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma m

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