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.
Applications:Suitable for use in ELISA and Western Blot.
Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Aliquots are stable for 12 months after receipt.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：100ug
Host：rabbit
Source Antibody：human
Grade：Affinity Purified
Purity：Purified by Protein G affinity chromatography.
Form：Supplied as a liquid in 0.01M PBS, pH 7.4, 0.03% Proclin 300, 50% glycerol. Labeled with Biotin
Specificity：Human, Ms, Rat, Cow, Dog, Gpig, Hm
Isotype：IgG
Calc Applications Abbrev：E WB
Calc Crossreactivity：Hu Rt
Immunogen：Recombinant human Endoplasmic reticulum resident protein 29 protein
