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RRBP1 encodes a ribosome-binding protein of the endoplasmic reticulum (ER) membrane. Additionally we are shipping RRBP1 Antibodies (49) and RRBP1 Kits (4) and many more products for this protein.
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High RRBP1 expression facilitates colorectal cancer progression and predicts an unfavourable post-operative prognosis.
Data indicate that p180 (show MLL Proteins) is required for the efficient targeting of placental alkaline phosphatase (ALPP (show ALP Proteins)) mRNA to the endoplasmic reticulum (ER).
RRBP1 could alleviate ER stress and help cancer cell survive
p180 (show MLL Proteins) is concentrated in ER sheets by interacting with polysomes and may play a role in ER morphology.
p180 (show MLL Proteins) promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.
A novel function of p180 (show MLL Proteins)-abundant endoplasmic reticulum on the trans-Golgi network expansion, both of which are highly developed in various professional secretory cells.
p180 (show MLL Proteins) plays crucial roles in enhancing collagen biosynthesis at the entry site of the secretory compartments by a novel mechanism that mainly involves facilitating ribosome association on the ER.
Results identify the ribosome receptor, p180, as a binding partner of the kinesin heavy chain isoform KIF5B.
These data suggest that p180 (show MLL Proteins) mediates interactions between the endoplasmic reticulum and microtubules mainly through the novel microtubule-binding and -bundling domain MTB (show NCAPG2 Proteins)-1.
over-expression of p180R failed to increase secretory pathway proteins calnexin (show CANX Proteins), SEC61beta, and calreticulin (show CALR Proteins), or ribosome biogenesis
This gene encodes a ribosome-binding protein of the endoplasmic reticulum (ER) membrane. Studies suggest that this gene plays a role in ER proliferation, secretory pathways and secretory cell differentiation, and mediation of ER-microtubule interactions. Alternative splicing has been observed and protein isoforms are characterized by regions of N-terminal decapeptide and C-terminal heptad repeats. Splicing of the tandem repeats results in variations in ribosome-binding affinity and secretory function. The full-length nature of variants which differ in repeat length has not been determined. Pseudogenes of this gene have been identified on chromosomes 3 and 7, and RRBP1 has been excluded as a candidate gene in the cause of Alagille syndrome, the result of a mutation in a nearby gene on chromosome 20p12.
180 kDa ribosome receptor homolog
, ES/130-related protein
, ribosome binding protein 1 homolog 180kDa (dog)
, ribosome receptor protein
, ribosome-binding protein 1
, 180 kDa ribosome receptor
, ribosome receptor