Mouse Anti-RDX Recombinant Antibody (CBCNR-367) (CBMAB-R1997-CN)

Mouse

Human

CBCNR-367

IgG1, κ

ELISA, WB, IF, WB

RDX (H47109, aa. 1-583) full-length recombinant protein with GST tag

Human

IgG1, κ

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

1× PBS, pH 7.2

radixin

Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. It is highly similar in sequence to both ezrin and moesin. The radixin gene has been localized by fluorescence in situ hybridization to 11q23. A truncated version representing a pseudogene (RDXP2) was assigned to Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was mapped to 11p by Southern and PCR analyses. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2012]

Radixin; Deafness, Autosomal Recessive 24; DFNB24;

Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.

Biological Process apical protein localizationIEA:Ensembl
Biological Process barbed-end actin filament cappingIEA:Ensembl
Biological Process cellular response to platelet-derived growth factor stimulusIEA:Ensembl
Biological Process cellular response to thyroid hormone stimulusISS:UniProtKB
Biological Process establishment of endothelial barrierManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process establishment of protein localization to plasma membraneISS:UniProtKB
Biological Process negative regulation of adherens junction organizationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of cell sizeManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of GTPase activityManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of homotypic cell-cell adhesionManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of cell migrationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of early endosome to late endosome transportManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process positive regulation of G1/S transition of mitotic cell cycleISS:UniProtKB
Biological Process positive regulation of gene expressionManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process positive regulation of protein catabolic processManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process positive regulation of protein localization to early endosomeManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process protein kinase A signalingISS:UniProtKB
Biological Process protein localization to plasma membraneManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process regulation of actin filament bundle assemblyManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process regulation of cell shapeManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process regulation of cell sizeManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process regulation of GTPase activityManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process regulation of organelle assemblyManual Assertion Based On ExperimentIGI:UniProtKB
Biological Process regulation of Rap protein signal transductionISS:UniProtKB
Biological Process regulation of ruffle assemblyManual Assertion Based On ExperimentIMP:UniProtKB

Cell membrane
Cytoplasm, cytoskeleton
Cleavage furrow
Cell projection, microvillus
Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively.

Deafness, autosomal recessive, 24 (DFNB24):
A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.

Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity).