Anti-Cone Arrestin Antibody

Evaluated by Western Blotting in Mouse Retina tissue lysate. Western Blotting Analysis: A 1:500 dilution of this antibody detected Arrestin-C in Mouse Retina tissue lysate.

Anti-Cone Arrestin , Cat. No. AB15282, is a rabbit polyclonal antibody that detects Arrestin-C and is tested for use in Western Blotting and Immunohistochemistry (Paraffin).

Research Category
Neuroscience

Research Sub Category
Sensory & PNS

Tested Applications Immunohistochemistry (Paraffin) Analysis: A 1:250 dilution from a representative lot detected Cone Arrestin in mouse cerebellum, rat retina, and mouse retina tissue sections. Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user

This rabbit polyclonal antibody detects Arrestin-C. It targets an epitope within 12 amino acids from the C-terminal region.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Arrestin-C (UniProt: Q9EQP6; also known as Cone arrestin, cArr, Retinal cone arrestin-3) is encoded by the Arr3 gene (Gene ID: 170735) in murine species. Arrestins are a superfamily of multi-functional proteins that regulate signaling and trafficking of the majority of G-protein-coupled receptors (GPCRs), as well as sub-cellular localization and activity of many other signaling proteins. Arrestin-C, a disulfide-linked, homodimeric protein, is predominantly found in inner and outer segments, and the inner plexiform regions of the retina. It is expressed in cone photoreceptors and pinealocytes and may contribute to the shut-off mechanisms associated with high acuity color vision. Arrestin-C is an elongated two-domain molecule with overall fold and key inter-domain interactions that hold the free protein in the basal conformation similar to the other subtypes. Several structural elements are reported to contribute to arrestin binding. The C-terminal acidic region serves as a regulatory role in controlling arrestin binding selectivity toward the phosphorylated and activated form of a receptor. The basic N-terminal domain directly participates in receptor interaction and serves a regulatory role via intramolecular interaction with the C-terminal acidic region. Also, two centrally localized domains are directly involved in determining receptor binding specificity and selectivity. Mutations in ARR3 gene in humans have been linked to X-lined myopia 26 that is characterized by typical tigroid fundus changes commonly seen in early onset high myopia. (Ref.: Gurevich, VV., et al. (2018). Protein Cell. 9; 986-1003; Xiao, X., et al. (2016). Mol. Vis. 22; 1257-1266).

Target molecular weight ~50 kDa observed. 41.92 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Epitope: C-terminus

KLH-conjugated linear peptide corresponding to 12 amino acids from the C-terminal region of mouse Cone Arrestin.

Concentration: Please refer to lot specific datasheet.

ImmunoAffinity Purified

Purified rabbit polyclonal antibody in buffer containing 0.02 M phosphate buffer, pH 7.6, 0.25 M NaCl, and 0.1% sodium azide.

Recommended storage: +2°C to +8°C.

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