The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
WB: 1/2000. Predicted molecular weight of non-fusion protein: 29 kDa.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
Proper protein folding and post-translational modifications are essential for secretory protein export out of the endoplasmic reticulum. This task is accomplished by chaperone proteins such as protein disulfide isomerase (PDI), GRP94, and BiP. A recently characterized protein, designated ERp29, is closely related to these chaperone proteins and appears to be upregulated during ER stress conditions. ERp29 is a soluble 259-residue protein that is localized to the lumen of the endoplasmic reticulum in all mammalian cells. Research has shown that there are two primary domains within ERp29. The first is the C-terminal region that is a novel, all helical, fold that is most likely involved with ERp29 retention to the ER. The second is the N-terminal region that resembles that of PDI’s thioredoxin module. The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER.
Endoplasmic reticulum lumenal protein ERp28 antibody
Endoplasmic reticulum protein 29 antibody
Endoplasmic reticulum protein 29 isoform 1 antibody
Endoplasmic reticulum protein ERp29 antibody
Endoplasmic reticulum resident protein 28 antibody
Endoplasmic reticulum resident protein 29 antibody
Endoplasmic reticulum resident protein 31 antibody
Epididymis secretory protein Li 107 antibody
HEL S 107 antibody
Protein disulfide isomerase family A member 9 antibody
Anti-ERp29 antibody images
Western blot - ERp29 antibody - Azide free (ab37850)
Anti-ERp29 antibody (ab37850) at 1/2000 dilution + E. coli-derived fusion protein.
Secondary Goat anti-IgY-HRP at 1/1000
Predicted band size : 29 kDa Observed band size : 75 kDa (why is the actual band size different from the predicted?) Additional bands at : 40 kDa (possible non-specific binding,degradation product),45 kDa (possible non-specific binding,degradation product),60 kDa (possible non-specific binding,degradation product).