Browse our anti-Recoverin (RCVRN) Antibodies

Human Recoverin (RCVRN) interaction partners

1. these data confirm the scaffolding function of several cluster-forming residues and point to their critical role in supporting physiological activity of recoverin

2. High RCVRN expression is associated with renal tumors.

3. Crystal Structure of Recoverin with Calcium Ions Bound to Both Functional EF Hands.

4. C39D substitution reduces alpha-helical content, decreases thermal stability and suppresses membrane association.

5. Aberrant hypomethylation of the recoverin gene region, overlapping the promoter up-stream of the first exon and the first exon itself, is involved in the aberrant expression of recoverin in tumor cells.

6. recoverin has a pathological role in cancer-associated retinopathy

7. There are cis-acting elements in the 5' non-coding region of the recoverin gene that are involved in the activation and suppression of gene expression.

8. Human recoverin is expressed in SCLC cells cultured from an anti-recoverin antibody-negative patient with CAR. KK0206 might be important for further research on SCLC related retinopathy.

9. A GRK1 region close to its C-terminus also seemed to be the binding site for S-modulin/recoverin.

Mouse (Murine) Recoverin (RCVRN) interaction partners

1. model supports the hypothesis that recoverin-specific T cell responses are major drivers of autoimmune retinopathy pathogenesis and that IL-10 is an important factor in protection

2. Recoverin is required for rod photoreceptor light adaptation.

3. Rods and cones share the same isoforms of recoverin and GRK1, and photoactivation also triggers a calcium decline in cones

4. recoverin may modulate the decay of light-activated PDE*, which may be responsible for the quickening of response recovery in background light.

5. High anti-recoverin antibody levels were achieved in two mouse models, accompanied by significantly reduced scotopic and photopic responses on the electroretinograms.

6. This is the first demonstration in an intact rod that light accelerates Rh* inactivation and that the Ca(2+)-binding protein recoverin may be required for the light-dependent modulation of Rh* lifetime.

7. recoverin undergoes light-dependent intracellular translocation in mouse rod photoreceptors

Cow (Bovine) Recoverin (RCVRN) interaction partners

1. A novel rhodopsin-kinase-binding site within the C-terminal region of recoverin.

2. (15) N NMR relaxation data suggest that Ca(2+)-free recoverin undergoes millisecond conformational dynamics at particular amide sites throughout the protein.

3. Ca2+-myristoyl switch in the neuronal calcium sensor requires different functions of Ca2+-binding sites

4. Recoverin is a zinc-binding protein

5. Myristoylation changes the calcium dependent conformation of this protein.

6. Recoverin and rhodopsin kinase have roles in a Ca2+-dependent feedback loop in membrane rafts from rod outer segments

7. an interaction surface for the recoverin target rhodopsin kinase is constituted upon Ca2+ binding to the non-acylated mutant

8. Recoverin binds exclusively to an amphipathic peptide at the N terminus of rhodopsin kinase

9. Ca2+/recoverin has a role in regulating rhodopsin mutants associated with retinitis pigmentosa

10. propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity

11. Time-resolved fluorescence shows biexponential fluorescence decay. The slower time constant was affected by Ca2+-induced conformational changes in WT & RecE85Q (disabled EF-hand 2), & not RecE121Q (EF-hand 3 nonfunctional) with a clamped myristoyl group.

12. Properties of the charged carboxy-terminus are consistent with a role of this region as an internal effector region that prolongs the time recoverin stays on the membrane by influencing its Ca2+-sensitivity