FABP5 Human
Description
Recombinant Human Epidermal Fatty Acid Binding Protein (FABP-5) is a monomeric, non-glycosylated, polypeptide chain containing 135 amino acids and having a total molecular mass of 15200 Daltons.
Product Specs
Product Science Overview
Epidermal Fatty Acid Binding Protein (E-FABP), also known as FABP5, is a member of the fatty acid-binding protein family. These proteins are small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. The human recombinant form of this protein is produced using recombinant DNA technology, which allows for the expression of the protein in a host organism, such as Escherichia coli .
E-FABP consists of 135 amino acids and has a molecular weight of approximately 15.19 kDa . The protein’s structure includes a lipocalin/cytosolic fatty-acid binding domain, which is crucial for its function in binding and transporting fatty acids . The protein is monomeric and has been crystallized, with its structure determined through X-ray diffraction at a resolution of 2.05Å .
The primary function of E-FABP is to act as an intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids . It plays a significant role in the metabolism and actions of the ligands it binds. E-FABP is involved in various biological processes, including fatty acid uptake, transport, and metabolism . Additionally, it selectively delivers specific fatty acids from the cytosol to the nucleus, where they activate nuclear receptors .
E-FABP is expressed in various tissues, including the skin, where it is involved in epidermal development . It has been identified as being upregulated in psoriasis tissue, suggesting a role in skin-related disorders . The protein is also implicated in glucose metabolic processes, lipid metabolism, and the regulation of cell growth and differentiation .
The recombinant form of E-FABP is valuable for research purposes, as it allows scientists to study the protein’s structure and function in detail. The expression, purification, and crystal structure determination of recombinant human E-FABP have provided insights into its biochemical properties and potential therapeutic applications . For instance, cannabinoids such as THC and CBD have been shown to inhibit keratinocyte proliferation by targeting FABP5, indicating a potential role for cannabinoids in the treatment of psoriasis .
