CRABP1 Human

CRABP1 is structurally similar to cellular retinol-binding proteins but is unique in its specific binding to retinoic acid. The protein is composed of 137 amino acids and has a molecular weight of approximately 15 kDa. It is primarily located in the cytoplasm and cytosol of cells .

The primary function of CRABP1 is to bind retinoic acid and transport it to the nucleus. Once in the nucleus, retinoic acid interacts with retinoic acid receptors (RARs) and retinoid X receptors (RXRs), which regulate the transcription of genes involved in cell growth and differentiation .

CRABP1 is constitutively expressed in various tissues, including the thyroid gland, caudate nucleus, and spleen . It is believed to play a significant role in retinoic acid-mediated differentiation and proliferation processes. Unlike its closely related counterpart, CRABP2, CRABP1 has distinct functions within the cell .

Alterations in the expression of CRABP1 have been associated with several diseases, including teratocarcinoma and acute promyelocytic leukemia . The protein’s ability to regulate retinoic acid levels makes it a potential target for therapeutic interventions in conditions where retinoic acid signaling is disrupted.

Recombinant CRABP1 is produced using recombinant DNA technology, which involves inserting the CRABP1 gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the protein for research and therapeutic purposes. Human recombinant CRABP1 retains the same structural and functional properties as the naturally occurring protein, making it a valuable tool in studying retinoic acid signaling pathways and developing retinoid-based therapies.

Recombinant CRABP1 is widely used in biochemical and pharmacological research to study its role in retinoic acid metabolism and its potential as a therapeutic target. It is also utilized in the development of assays to screen for compounds that can modulate retinoic acid signaling.