Cell Signaling Technology

Product Pathways - Vesicle Trafficking

Sec61A1 (D7Q6V) Rabbit mAb #14868

No. Size Price
14868S 100 µl ( 10 western blots ) ¥3,100.00 现货查询 购买询价
14868 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat, Endogenous 40 Rabbit IgG
IP 1:100

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation,

Specificity / Sensitivity

Sec61A1 (D7Q6V) Rabbit mAb recognizes endogenous levels of total Sec61A1 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg273 of human Sec61A1 protein.

Western blot analysis of extracts from various cell lines using Sec61A1 (D7Q6V) Rabbit mAb.

Immunoprecipitation of Sec61A1 protein from HeLa cell extracts. Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is Sec61A1 (D7Q6V) Rabbit mAb. Western blot analysis was performed using Sec61A1 (D7Q6V) Rabbit mAb.

Background

Sec61 translocon is a channel complex located on the endoplasmic reticulum (ER) membrane to mediate membrane protein insertion into the organelle (1). There are three components in the complex, Sec61A, Sec61B, and Sec61G (2). Sec61A is the main component of the channel on the ER membrane and directly contacts nascent synthesized polypeptide TMD (transmembrane domain) for insertion (3). Sec61G functions in stablizing the channel (3). In addition to TMD insertion, Sec61 translocon has also been shown to be involved in ER calcium leakage (4,5). Both Bip and calmodulin can inhibit this leakage by their interaction with Sec61A (6,7). Sec61B has no obvious function related to target protein ER membrane insertion, but is involved in other vesicle trafficking processes such as EGFR and Her2 trafficking from the cytosol to nucleus (8,9), Gurken trafficking from Golgi to plasma membrane (10), and copper-transporting ATPase membrane distribution (11).

  1. Shao, S. and Hegde, R.S. (2011) Annu Rev Cell Dev Biol 27, 25-56.
  2. Hartmann, E. et al. (1994) Nature 367, 654-7.
  3. Van den Berg, B. et al. (2004) Nature 427, 36-44.
  4. Flourakis, M. et al. (2006) FASEB J 20, 1215-7.
  5. Lang, S. et al. (2001) Channels (Austin) 5, 228-35.
  6. Erdmann, F. et al. (2011) EMBO J 30, 17-31.
  7. Schäuble, N. et al. (2012) EMBO J 31, 3282-96.
  8. Wang, Y.N. et al. (2010) J Biol Chem 285, 38720-9.
  9. Wang, Y.N. et al. (2012) J Biol Chem 287, 16869-79.
  10. Kelkar, A. and Dobberstein, B. (2009) BMC Cell Biol 10, 11.
  11. Abada, P.B. et al. (2012) Mol Pharmacol 82, 510-20.

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