RBP1 Human
Description
RBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
RBP1 is a small, soluble protein that binds retinol with high affinity. It is primarily found in the cytoplasm of cells and is involved in the intracellular transport of retinol. The protein ensures that retinol is delivered to specific target cells and tissues, where it can be metabolized into active forms such as retinoic acid. Retinoic acid is a potent regulator of gene expression and is involved in numerous developmental and physiological processes .
Human recombinant RBP1 is typically produced using recombinant DNA technology. This involves inserting the gene encoding RBP1 into a suitable expression system, such as Escherichia coli (E. coli) or yeast, which then produces the protein. The recombinant protein is purified to high levels of purity, often exceeding 95%, to ensure its suitability for research and therapeutic applications .
Retinol and its derivatives are vital for maintaining normal vision, immune function, and skin health. RBP1 plays a critical role in delivering retinol to the retina, where it is converted into retinal, a component of the visual pigment rhodopsin. Additionally, RBP1 is involved in the regulation of retinoic acid levels, which are crucial for embryonic development and cellular differentiation .
Alterations in RBP1 expression or function can lead to various health issues. For instance, deficiencies in retinol transport can result in vitamin A deficiency, leading to conditions such as night blindness and an increased risk of infections. Conversely, excessive retinol levels can be toxic and cause hypervitaminosis A. Therefore, understanding the role of RBP1 in retinol metabolism is essential for developing therapeutic strategies for related disorders .
Human recombinant RBP1 is widely used in research to study retinol metabolism, retinoic acid signaling pathways, and their implications in health and disease. It serves as a valuable tool for investigating the molecular mechanisms underlying retinoid-related processes and for developing potential therapeutic interventions .
