The RP2 Polyclonal Antibody (PAC04414) is a valuable tool for researchers studying RP2, a protein involved in ciliary function and linked to genetic disorders like retinitis pigmentosa. This antibody, generated in rabbits, shows high reactivity with human samples and is validated for use in various applications, including Western blotting.RP2 is a key player in regulating cilia structure and function, making it essential for processes like vision and cellular signaling. Mutations in the RP2 gene can lead to ciliary dysfunction, resulting in vision impairment and other health issues.
By targeting RP2 with this antibody, researchers can elucidate its role in cilia biology and potentially uncover new therapeutic strategies for ciliopathies and related conditions.Overall, the RP2 Polyclonal Antibody offers a reliable tool for investigating the function and dysfunction of RP2, ultimately advancing our understanding of ciliary biology and disease mechanisms. Its specificity and sensitivity make it a valuable asset for research in genetics, ophthalmology, and cell biology.
Immunohistochemistry of paraffin-embedded human kidney tissue using PACO44414 at dilution of 1:100.
Immunofluorescent analysis of Hela cells using PACO44414 at dilution of 1:100 and Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
Background:
Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins.
Synonyms:
Protein XRP2, RP2
UniProt Protein Function:
RP2: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. Defects in RP2 are the cause of retinitis pigmentosa type 2 (RP2); also known as X-linked retinitis pigmentosa 2 (XLRP-2). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Belongs to the TBCC family.Protein type: ChaperoneChromosomal Location of Human Ortholog: Xp11.3Cellular Component: centriole; Golgi apparatus; cytoplasm; plasma membrane; cytoplasmic vesicleMolecular Function: protein binding; GTP binding; unfolded protein binding; nucleoside diphosphate kinase activity; actin binding; GTPase activator activity; ATP bindingBiological Process: GTP biosynthetic process; CTP biosynthetic process; protein transport; protein folding; visual perception; organelle organization and biogenesis; UTP biosynthetic process; cell morphogenesis; nucleoside diphosphate phosphorylation; cytoskeleton organization and biogenesis; post-Golgi vesicle-mediated transport; post-chaperonin tubulin folding pathway; positive regulation of GTPase activityDisease: Retinitis Pigmentosa 2
UniProt Protein Details:
NCBI Summary:
The RP2 locus has been implicated as one cause of X-linked retinitis pigmentosa. The predicted gene product shows homology with human cofactor C, a protein involved in the ultimate step of beta-tubulin folding. Progressive retinal degeneration may therefore be due to the accumulation of incorrectly-folded photoreceptor or neuron-specific tubulin isoforms followed by progressive cell death [provided by RefSeq, Jul 2008]
