RCVRN Mouse

Recoverin Mouse Recombinant
Cat. No.
BT11772
Source
Escherichia Coli.
Synonyms

RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.

Appearance
Sterile filtered colorless solution.
Purity

Greater than 90.0% as determined by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recoverin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202a.a.) and having a molecular mass of 25.8kDa. Recoverin Mouse is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.   

Product Specs

Introduction
Recoverin, a member of the neuronal calcium sensor family, is a 23kDa protein found in retinal photoreceptor cells. This protein, involved in intracellular signal transduction, exhibits heterogeneous acylation and calcium-binding properties. Its structure consists of four EF-hands, two of which bind to calcium ions. Upon calcium binding, the acyl group is extruded from a hydrophobic cleft within the protein. This extrusion triggers the translocation of recoverin from its soluble form to the disc membrane. Functionally, recoverin is involved in regulating the phototransduction cascade's termination in the retina. It achieves this by inhibiting the phosphorylation of photo-activated rhodopsin. Recoverin's role in inhibiting rhodopsin kinase, an enzyme that regulates rhodopsin phosphorylation, is crucial. By modulating rhodopsin phosphorylation, recoverin influences the eye's ability to adapt to light exposure and recover from it. In clinical contexts, recoverin serves as a detectable serological protein marker. Its presence is observed in patients diagnosed with cancer-associated retinopathy, a paraneoplastic syndrome.
Description
Recombinant Recoverin Mouse, produced in E. coli, is a single, non-glycosylated polypeptide chain. This protein comprises 225 amino acids (1-202a.a.) with a molecular weight of 25.8 kDa. The recombinant protein is engineered with a 23 amino acid His-tag fused at its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The protein is supplied at a concentration of 1mg/ml in a buffer consisting of Phosphate Buffered Saline (pH 7.4), 10% glycerol, and 1mM DTT.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To ensure long-term stability, adding a carrier protein like HSA or BSA (0.1%) is advisable. It's important to avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is determined to be greater than 90% based on SDS-PAGE analysis.
Synonyms

RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMGNSKSG ALSKEILEEL QLNTKFTEEE LSAWYQSFLK ECPSGRITRQ EFESIYSKFF PDSDPKAYAQ HVFRSFDANS DGTLDFKEYV IALHMTTAGK PTQKLEWAFS LYDVDGNGTI SKNEVLEIVM AIFKMIKPED VKLLPDDENT PEKRAEKIWA FFGKKEDDKL TEEEFIEGTL ANKEILRLIQ FEPQKVKERI KEKKQ.

Product Science Overview

Introduction

Recoverin is a low molecular-weight, neuronal calcium sensor (NCS) protein primarily located in the photoreceptor outer segments of the vertebrate retina . It plays a crucial role in the recovery phase of visual excitation and adaptation to background light . This article delves into the historical background, structure, function, and significance of Recoverin, particularly focusing on the mouse recombinant version.

Historical Background

The discovery of Recoverin dates back to 1989 when P. Philippov’s group from M.V. Lomonosov Moscow State University developed a method for purifying visual G-protein transducin and other G-proteins . During this process, they identified an unknown protein with an apparent molecular weight of 26 kDa, which they named "p26" . This protein was later found to be specific to the retina, particularly the photoreceptor layer, and was capable of binding calcium ions (Ca²⁺) due to its EF-hand type calcium-binding sites . The protein was subsequently renamed “Recoverin” due to its role in photoreceptor recovery .

Structure

Recoverin contains several EF-hand type Ca²⁺-binding sites, which are crucial for its function . The binding of calcium to these sites induces a conformational change in the protein, enabling it to interact with other molecules . Recoverin also undergoes N-terminal myristoylation, a lipid modification that facilitates its attachment to cellular membranes .

Function

Recoverin plays a pivotal role in the visual cycle by acting as a calcium sensor . In the dark, calcium-bound Recoverin inhibits G-protein-coupled receptor kinase (GRK), preventing the phosphorylation of rhodopsin, a visual receptor . This inhibition is lifted when light reduces intracellular calcium levels, allowing GRK to phosphorylate rhodopsin and initiate the recovery phase of visual excitation . Recoverin’s ability to bind to phospholipid membranes further enhances its regulatory functions .

Significance

Recoverin is not only essential for normal visual function but also serves as a marker for evaluating the differentiation of pluripotent stem cells into rod and cone photoreceptors or cone bipolar cells . Additionally, Recoverin is classified as a cancer-retina antigen due to its aberrant expression in tumors of the lung and other tissues . This makes it a valuable tool in both basic research and clinical diagnostics.

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