Cat. # | Size | Qty. | Price |
---|---|---|---|
4759T | 1 Kit (7 x 20 microliters) |
|
Product Includes | Quantity | Applications | Reactivity | MW(kDa) | Isotype |
---|---|---|---|---|---|
BiP (C50B12) Rabbit mAb 3177 | 20 µl |
|
H M | 78 | Rabbit IgG |
Ero1-Lα Antibody 3264 | 20 µl |
|
H | 60 | Rabbit |
ERp44 (D17A6) XP® Rabbit mAb 3798 | 20 µl |
|
H M R Mk | 44 | Rabbit IgG |
ERp57 (G117) Antibody 2881 | 20 µl |
|
H M R | 57 | Rabbit |
ERp72 (D70D12) XP® Rabbit mAb 5033 | 20 µl |
|
H M R Mk | 72 | Rabbit IgG |
Grp94 Antibody 2104 | 20 µl |
|
H M R Mk | 100 | Rabbit |
PDI (C81H6) Rabbit mAb 3501 | 20 µl |
|
H M R Mk | 57 | Rabbit |
Anti-rabbit IgG, HRP-linked Antibody 7074 | 100 µl |
|
Goat |
Product Information
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Gly584 of human BiP, the sequence of human ERp44, the residues surrounding Met279 of human ERp72 protein and the sequence of human PD1. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequences around Gly117 of human ERp57, Met622 of human Grp94 and Leu218 of human Ero1-Lα. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
After their synthesis, secretory proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds (2). Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes the ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange (3). This event is then followed by PDI-catalyzed disulfide bond formation on folding proteins (3). Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum stress proteins 72, 57 and 44 (ERp72, ERp57 and ERp44), constitute the PDI family (4,5,6). The ER also contains a pool of molecular chaperones, including Grp94, to help proteins fold properly. Grp94 is a glucose-regulated protein (7) with sequence homology to Hsp90 (8). BiP is another chaperone whose synthesis is increased when protein folding is disturbed. BiP binds to misfolded proteins to prevent them from forming aggregates and assists in proper refolding (9).
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