Anti-FABP5

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Fatty acid binding protein 5 (psoriasis-associated) is a protein that in humans is encoded by the FABP5 gene, also known as PAFABP, EFABP, E-FABP, KFABP, PA-FABP, and Epidermal-type fatty acid-binding protein. It is a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. The cDNA encodes a 135-amino acid protein with molecular weight 15,164. This gene encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. It is though that FABPs roles include fatty acid uptake, transport, and metabolism. Kaczocha et al.(2009) identified FABP5 and FABP7 as cytosolic proteins that transport AEA from the plasma membrane to subcellular fatty acid amide hydrolase, where it is hydrolyzed and inactivated. FABP3 did not show this specific transport function. Protein function: Intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids, that regulate the metabolism and actions of the ligands they bind (PubMed:8608126, PubMed:12540600). In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors. Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta, which promotes proliferation and survival (PubMed:17512406). May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling (PubMed:29531087). Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (PubMed:29440395). May be involved in keratinocyte differentiation. [The UniProt Consortium]