Anti-ERp29 Antibody (4M884) is a Rabbit antibody targeting ERp29. Anti-ERp29 Antibody (4M884) can be used in FCM, ICC/IF, IF, IHC-Fr, IHC-P, WB.

IgG

4M884

Human,Mouse,Rat

1. 25 ug total protein per lane of various lysates (see on figure) probed with ERp29 monoclonal antibody, unconjugated (TMAB-05684) at 1: 1000 dilution and 4°C overnight incubation. Followed by conjugated secondary antibody incubation at r. T. for 60 min.
2. The HepG2 (H) cells were fixed with 4% PFA (10 min at r. T.) and then permeabilized with 90% ice-cold methanol for 20 min at -20℃, the cells then were incubated in 5% BSA to block non-specific protein-protein interactions (30 min at r. T.), followed by secondary antibody incubation for 40 min at room temperature. Primary Antibody (green): Rabbit Anti-ERp29 antibody (TMAB-05684, 1: 100); Isotype Control (orange): Rabbit IgG. Blank control (black): PBS. Acquisition of 20,000 events was performed.

FCM=1:50-100; ICC/IF=1:50-200; IF=1:50-200; IHC-Fr=1:100-200; IHC-P=1:100-200; WB=1:500-2000

Monoclonal

A synthesized peptide: human ERp29

Human

ERP29

Endoplasmic reticulum resident protein 29

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.