RBP3 Human
Escherichia Coli.
RBP3, IRBP, Retinol-binding protein 3, Interphotoreceptor retinoid-binding protein, Interstitial retinol-binding protein.
Greater than 95.0% as determined by SDS-PAGE.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
RBP3 Human Recombinant (321-630a.a) produced in E.Coli is a single, non-glycosylated Polypeptide chain. RBP3 is fused to a 6 a.a His tag at N-terminal and is purified by proprietary chromatographic techniques.
Product Specs
Retinol-binding proteins (RBPs) are essential for transporting retinol and retinoic acid, crucial for embryonic development. These proteins ensure proper retinol levels, preventing complications like embryo mortality or malformations. RBPs are found in the uterus, embryo, and extraembryonic tissues of various mammals, including cows, sheep, and pigs, highlighting their role in successful pregnancies.
This product is a recombinant human RBP3 protein, specifically the 321-630a.a fragment, produced in E. coli bacteria. It's a single, non-glycosylated polypeptide chain with a 6-amino acid Histidine tag at the N-terminus. The protein is purified using proprietary chromatographic techniques.
The lyophilized RBP3 is provided in a 0.2µM solution of phosphate-buffered saline (PBS) at pH 7.4.
Reconstitute the lyophilized RBP3 in sterile distilled water to a concentration of at least 100µg/ml. This solution can be further diluted with other aqueous solutions as needed.
Lyophilized RBP3 can be stored at room temperature for up to 3 weeks. For long-term storage, keep it desiccated below -18°C. After reconstitution, store the RBP3 solution at 4°C for 2-7 days. For longer storage, freeze it below -18°C. Avoid repeated freezing and thawing cycles.
The purity of this product is greater than 95.0% as assessed by SDS-PAGE analysis.
RBP3, IRBP, Retinol-binding protein 3, Interphotoreceptor retinoid-binding protein, Interstitial retinol-binding protein.
Escherichia Coli.
Product Science Overview
Retinol Binding Protein-3 (RBP3), also known as Interphotoreceptor Retinoid-Binding Protein (IRBP), is a large glycoprotein primarily found in the interphotoreceptor matrix of the retina. It plays a crucial role in the visual process by transporting retinoids between the retinal pigment epithelium (RPE) and the photoreceptor cells .
The human RBP3 gene is located on chromosome 10 and spans approximately 9.5 kilobase pairs. It consists of four exons separated by three introns. The gene is transcribed into an mRNA of about 4.3 kilobases, which is then translated and processed into a glycosylated protein with a molecular weight of 135,000 Da .
The amino acid sequence of RBP3 can be divided into four contiguous homology domains, each with 33-38% identity. This suggests that the gene underwent a series of duplication events. Interestingly, the boundaries of these domains are not defined by exon-intron junctions .
RBP3 is essential for the visual cycle. It binds and transports retinoids, which are vital for the regeneration of the visual pigment rhodopsin. This process is critical for vision, especially in low-light conditions. The protein’s ability to bind retinoids ensures that these molecules are efficiently transported between the RPE and photoreceptors, facilitating the visual cycle .
Human recombinant RBP3 is typically produced using recombinant DNA technology. The gene encoding RBP3 is cloned into an expression vector, which is then introduced into a suitable host cell, such as E. coli or mammalian cells. The host cells express the protein, which is subsequently purified using various chromatographic techniques to obtain a high-purity product .
RBP3 undergoes several post-translational modifications, including glycosylation, which are essential for its stability and function. Analytical techniques such as mass spectrometry, X-ray crystallography, and nuclear magnetic resonance (NMR) spectroscopy are used to study the protein’s structure and interactions with retinoids. These analyses provide insights into the protein’s binding sites and its mechanism of action .
