AUP1 (D5M9Q) Rabbit mAb #35055
- WB
- IP
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 42 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
AUP1 (D5M9Q) Rabbit mAb recognizes endogenous levels of total AUP1 protein.
Species Reactivity:
Human, Mouse, Rat
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Bovine
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln320 of human AUP1 protein, long isoform.
Background
Ancient ubiquitous protein 1 (AUP1) is a component of the ER-associated protein degradation (ERAD) machinery responsible for the ubiquitin-mediated degradation of misfolded proteins (1). AUP1 protein contains four conserved domains, with a long, amino-terminal stretch of hydrophobic amino acids followed by an acyltransferase domain (2). Amino-terminal protein sequences direct localization of AUP1 to both the ER and to cytosolic lipid droplets (3). The AUP1 CUE domain binds ubiquitin (4), while the G2BR domain allows for association between AUP1 and E2 conjugating enzyme UBE2G2 (5,6). The presence of these binding domains suggests a central role for AUP1 in the ubiquitination-mediated protein degradation (2). Research studies indicate that AUP1 recruits UBE2G2 to cytosolic lipid droplets, ER-derived organelles that are sites for storage and hydrolysis of neutral lipids. Inhibition of AUP1 protein function results in decreased ubiquitin-mediated degradation of several proteins, including the cholesterol biosynthetic enzyme HMG-CoA-reductase and the cholesterol synthesis regulator INSIG1 (6).
Limited Uses
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