|Application ||WB, IHC-P, ICC, E, IP, IHC-Fr|
|Dilution||ICC (1:1000-1:10000), IHC-Fr (1:1000-1:10000), IHC-P (2.5 µg/ml), WB (1:1000-1:6000) ,|
|Other Names||B-cell receptor-associated protein 31, BCR-associated protein 31, Bap31, 6C6-AG tumor-associated antigen, Protein CDM, p28, BCAP31, BAP31, DXS1357E|
|Target/Specificity||Recognizes an epitope (aa 230-246) encompassing a caspase recognition site and the ER-homing motif (KKEE), present at the C-terminus of human, primate, bovine and hamster BAP31. Does not recognize mouse and rat BAP31.|
|Reconstitution & Storage||+4°C or -20°C, Avoid repeated freezing and thawing.|
|Precautions||BCAP31 / BAP31 Antibody (clone CC-1) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins. May be involved in CASP8- mediated apoptosis.|
|Cellular Location||Endoplasmic reticulum membrane; Multi- pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Note=May shuttle between the ER and the intermediate compartment/cis-Golgi complex|
|Tissue Location||Ubiquitous. Highly expressed in neurons and discrete endocrine cells.|
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Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins. May be involved in CASP8- mediated apoptosis.
Mosser J.,et al.Genomics 22:469-471(1994).
Li E.,et al.Eur. J. Biochem. 238:631-638(1996).
Adachi T.,et al.EMBO J. 15:1534-1541(1996).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Ross M.T.,et al.Nature 434:325-337(2005).
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