Background:   11-cis-retinal, the universal chromophore of the vertebrate retina, is coupled to opsins in both rod and cone photoreceptor cells and is photoisomerized to all-trans-retinal by light. This conversion is inhibited when 11-cis-retinol is in a complex with cellular retinaldehyde-binding protein (CRALBP). CRALBP may play a role in the vertebrate visual process as a substrate-routing protein, influencing the enzymatic partitioning of 11-cis-retinol at a key branch point in the visual cycle. CRALBP is not expressed in photoreceptors and is abundant in the retinal pigment epithelium (RPE) and Muller cells of the neuroretina, where it carries 11-cis-retinol and 11-cis-retinaldehyde. CRALBPL (cellular retinaldehyde-binding protein-like), also known as Retinaldehyde-binding protein 1-like protein 1, contains a CRAL-TRIO domain, which is typically present in lipid-binding SEC14-like proteins. CRALBPL has 45% sequence similarity to a retina and pineal gland-specific protein, CRALBP (cellular retinaldehyde-binding protein), which is likely involved in the visual process and may be implicated in visual diseases.

Description: Rabbit polyclonal to CRALBP

Immunogen: KLH conjugated synthetic peptide derived from CRALBP

Specificity:  ·Reacts with Human, Mouse and Rat.

.·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 36 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.