RRBP1 (ribosome binding protein 1) is a membrane protein that localizes to endoplasmic reticulum (ER). It is also found in cytoplasm and nucleus. This protein is composed of 1410 amino acids, a transmembrane domain in its hydrophobic N-terminal, a highly conserved tandem repeat which functions as the ribosome-binding domain, and the C-terminal which contains an acidic coiled-coil domain.
Synonyms: Anti-180 kDa ribosome receptor homolog antibody produced in rabbit; Anti-ES/130-related protein antibody produced in rabbit; Anti-Ribosome receptor protein antibody produced in rabbit; Anti-Ribosome-binding protein 1 antibody produced in rabbit
Storage: -20C
Application: Anti-RRBP1 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org). Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: RRBP1 (ribosome binding protein 1) is a key ribosome binding protein and plays essential role in the translocation of naïve proteins across the membrane of endoplasmic reticulum (ER). It is essential for the terminal differentiation of secretory tissues, and for the production of pro-collagen in secretory tissues. It also functions as the interacting partner of the motor protein KIF5B (kinesin family member 5B), which is up-regulated in several cancer cell lines. RRBP1 protein is highly expressed in breast cancer (BC) cells and might have potential as a BC marker. This protein is essential for the ER-localization of bulk poly(A) and of certain mRNAs such as, placental alkaline phosphatase and calreticulin. Up-regulation of this protein promotes the progression of colorectal cancer, and functions as a predictor of poor outcome in post-operative cases. In secretory cells, RRBP1-rich ER is responsible for the expansion of trans-Golgi network following the secretion of activated collagen.
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