Anti-RLBP1 Antibody Picoband® Fluoro647 Conjugated

Retinaldehyde-binding protein 1 (RLBP1) also known as cellular retinaldehyde-binding protein (CRALBP) is a 36-kD water-soluble protein that in humans is encoded by the RLBP1 gene. The protein encoded by this gene is a 36-kD water-soluble protein which carries 11-cis-retinaldehyde or 11-cis-retinal as physiologic ligands. It may be a functional component of the visual cycle. Mutations of this gene have been associated with severe rod-cone dystrophy, Bothnia dystrophy (nonsyndromic autosomal recessive retinitis pigmentosa) and retinitis punctata albescens.

Cell Type Marker, Developmental Families, Domain Families, Epigenetics and Nuclear Signaling, Neurogenesis, Neurology Process, Neuroscience, Transcription

Multifunctional transcription factor with different regions mediating its different effects. Acts by binding (via its C-terminal domain) to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes. Regulates the expression of specific genes involved in differentiation and survival within a subset of neuronal lineages. It has been shown that activation of some of these genes requires its N-terminal domain, maybe through a neuronal-specific cofactor. Ativates BCL2 expression and protects neuronal cells from apoptosis (via the N-terminal domain) . Induces neuronal process outgrowth and the coordinate expression of genes encoding synaptic proteins. Exerts its major developmental effects in somatosensory neurons and in brainstem nuclei involved in motor control. Stimulates the binding affinity of the nuclear estrogene receptor ESR1 to DNA estrogen response element (ERE), and hence modulates ESR1-induced transcriptional activity. May positively regulate POU4F2 and POU4F3. Regulates dorsal root ganglion sensory neuron specification and axonal projection into the spinal cord. Plays a role in TNFSF11-mediated terminal osteoclast differentiation. Negatively regulates its own expression interacting ly with a highly conserved autoregulatory domain surrounding the transcription initiation site.

1. Bear, J. C., Nemec, T. F., Kennedy, J. C., Marshall, W. H., Power, A. A., Kolonel, V. M., Burke, G. B. Inbreeding in outport Newfoundland. Am. J. Med. Genet. 29: 649-660, 1988. 2. Burstedt, M. S., Sandgren, O., Holmgren, G., Forsman-Semb, K. Bothnia dystrophy caused by mutations in the cellular retinaldehyde-binding protein gene (RLBP1) on chromosome 15q26. Invest. Ophthal. Vis. Sci. 40: 995-1000, 1999. 3. Burstedt, M. S. I., Forsman-Semb, K., Golovleva, I., Janunger, T., Wachtmeister, L., Sandgren, O. Ocular phenotype of Bothnia dystrophy, an autosomal recessive retinitis pigmentosa associated with an R234W mutation in the RLBP1 gene. Arch Ophthal. 119: 260-267, 2001.