Anti-BiP (GRP78) Antibody, arginylated (Nt-Glu19)

Descrição detalhada : 78 kDa glucose-regulated protein (UniProt P11021; also known as BiP, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, GRP-78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein) is encoded by the HSPA5 (also known as GRP78) gene (Gene ID 3309) in human. BiP (GRP78 or heat shock 70 kDa protein 5), calreticulin (CRT), and protein disulphide isomerase (PDI) are ER lumen folding factors that, together with other PTM enzymes, assist the process of newly synthesized proteins before their release from ER. BiP, CRT, and PDI themselves are subject to posttranslational signal peptide removal after their synthesis, exposing E19, E18, and D18 at the newly formed N-terminus, respectively. The N-terminus D and E residues of the mature proteins are permissive to arginine-tRNA-protein transferase 1/ATE1-catalyzed arginylation, forming arginylated mature proteins (R-BiP, R-CRT, R-PDI) with altered cellular localization to allow their participation in non-ER functions. Although only the basal levels of R-CRT and R-PDI, but not R-BiP, are generally detectible in non-stimulated cells, upregulated N-terminal arginylation of all three proteins is observed upon cytosolic dsDNA exposure and proteasomal inhibition, indicating a shared role in innate immune responses to invading microbes. In addition, ER stress induction by thapsigargin treatment synergistically boosts proteasomal inhibition-induced upregulation of cellular levels of R-BiP, R-CRT, and R-PDI, suggesting that ER stress accelerates the supply of ER lumenal BiP, CRT, and DPI for N-terminal arginylation.
Sinónimos : 78 kDa glucose-regulated protein, Nt-Glu19 arginylated, BiP, Nt-Glu19 arginylated, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Nt-Glu19 arginylated, GRP-78, Nt-Glu19 arginylated, Heat shock 70 kDa protein 5, Nt-Glu19 arginylated, Immunogl
Armazenamento : +2°C to +8°C