Anti-Fatty Acid Binding Protein 5/FABP5 Antibody Picoband® Fluoro647 Conjugated

FABP5, Fatty acid-binding protein, epidermal, is a protein that in humans is encoded by the FABP5 gene. This gene encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. It is mapped to 8q21.13. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism.

E3 ubiquitin-protein ligase TRIM21; 52 kDa Ro protein; 52 kDa ribonucleoprotein autoantigen Ro/SS-A; RING finger protein 81; RING-type E3 ubiquitin transferase TRIM21; Ro (SS-A) ; Sjoegren syndrome type A antigen; SS-A; Tripartite motif-containing protein 21; TRIM21; RNF81; RO52; SSA1

A synthetic peptide corresponding to a sequence at the N-terminus of mouse FABP5, which shares 81.2% amino acid (aa) sequence identity with human FABP5.

Cancer, Cardiovascular, Fatty Acid Oxidation, Fatty Acids, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Lipids/Lipoproteins, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Redox Metabolism, Signal Transduction

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF (SKP2) -like complexes. A TRIM21-containing SCF (SKP2) -like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2. Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of IRF3, hence attenuating type I interferon (IFN) -dependent immune responses.

1. Hertzel, A. V., Bernlohr, D. A.Cloning and chromosomal location of the murine keratinocyte lipid-binding protein gene.Gene 221: 235-243, 1998. 2. Siegenthaler, G., Hotz, R., Chatellard-Gruaz, D., Didierjean, L., Hellman, U., Saurat, J. H.Purification and characterization of the human epidermal fatty acid-binding protein: localization during epidermal cell differentiation in vivo and in vitro.Biochem J. 302: 363-371, 1994.