Anti-ERP29 monoclonal antibody, clone FQS23096

Antibody Isotype

IgG

Clone

FQS23096

Species Reactivity

Rat; Human

Immunogen

Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) within Human ERp29 aa 200 to the C-terminus (Cysteine residue). The exact sequence is proprietary.Database link: P30040

Conjugate

Application Notes

IHC-P: 1/50 - 1/100; WB: 1/1000 - 1/10000; ICC/IF: 1/50 - 1/100.

Alternative Names

ERP29; endoplasmic reticulum protein 29; C12orf8, chromosome 12 open reading frame 8; endoplasmic reticulum resident protein 29; ERp28; ERp29; ERp31; PDI DB; PDIA9; protein disulfide isomerase family A; member 9; endoplasmic reticulum resident protein 28

Entrez Gene ID

UniProt ID

Antigen Description

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.

Pathway

Protein processing in endoplasmic reticulum, organism-specific biosystem; Protein processing in endoplasmic reticulum, conserved biosystem;