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SEC61B Antibody (Center) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession P60468
Clone Names 100528092
Additional Information
Gene ID 10952
Other Names Protein transport protein Sec61 subunit beta, SEC61B
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name SEC61B {ECO:0000303|PubMed:28375157, ECO:0000312|HGNC:HGNC:16993}
Function Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (PubMed:12475939). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (PubMed:12475939). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (PubMed:32820719, PubMed:36261522). The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER (PubMed:19121997).
Cellular Location Endoplasmic reticulum membrane; Single-pass membrane protein
Research Areas
Citations (0)
citation

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Background

The Sec61 complex is the central component of the proteintranslocation apparatus of the endoplasmic reticulum (ER) membrane.Oligomers of the Sec61 complex form a transmembrane channel whereproteins are translocated across and integrated into the ERmembrane. This complex consists of three membrane proteins- alpha,beta, and gamma. This gene encodes the beta-subunit protein. TheSec61 subunits are also observed in the post-ER compartment,suggesting that these proteins can escape the ER and recycle back.There is evidence for multiple polyadenylated sites for thistranscript.

References

Liao, H.J., et al. Cancer Res. 69(15):6179-6183(2009)Wang, B., et al. Cell 133(6):1080-1092(2008)Liao, H.J., et al. Mol. Biol. Cell 18(3):1064-1072(2007)Olsen, J.V., et al. Cell 127(3):635-648(2006)Olsen, J.V., et al. Cell 127(3):635-648(2006)

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$ 277.78
Cat# BP14910c
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