epitope corresponding to amino acids 184-230 mapping near the C-terminus of Derlin-1 of human origin
Modification Notes
Degradation in endoplasmic reticulum proteins, also designated Derlins or DERtrins, are crucial for the degradation of misfolded endoplasmic reticulum (ER) luminal proteins. Derlin proteins are multi-pass membrane proteins localizing to the ER. Derlins are involved in transferring misfolded proteins from the ER to the cytosol, where the misfolded proteins are destroyed in an ubiquitin-dependent manner by the proteasome. In the case of cytomegalovirus infection, Derlin-1, as opposed to Derlins-2 and -3, is involved in the export of MHC class I heavy chains from the ER via its interaction with the viral protein US11. Derlins may also be important for cell proliferation. They are widely expressed, but highest levels are primarily detected in spleen, pancreas, lung, liver, thymus and ovary. Derlin-2 is overexpressed in hepatocarcinomas.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Derlin-1 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 184-230 mapping near the C-terminus of Derlin-1 of human origin
Tissue Specificity
epitope corresponding to amino acids 184-230 mapping near the C-terminus of Derlin-1 of human origin
Application
Application
Western blot analysis of Derlin-1 expression in U-937 whole cell lysate.
Application Notes
recommended for detection of Derlin-1 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.