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FABP5 encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. Additionally we are shipping FABP5 Antibodies (51) and FABP5 Kits (6) and many more products for this protein.
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Using a yeast two-hybrid screen, immunoprecipitation, microscale thermophoresis analysis and cellular fractionation, we discovered that Fabp5 interacts with the calnexin (show CANX Proteins) cytoplasmic C-tail domain at the endoplasmic reticulum. These observations identify Fabp5 as a previously unrecognized calnexin (show CANX Proteins) binding partner.
Following infection with Listeria monocytogenes, we observed similar clonal expansion, contraction and formation of memory CD8 (show CD8A PLURAL_@39278@) T cells in WT and E-FABP (show FABP5L1 PLURAL_@39278@)-/- mice. Analysis of Listeria-specific CD4 (show CD4 PLURAL_@39278@) T cells revealed no defect in the expansion, contraction, and formation of memory CD4 (show CD4 PLURAL_@39278@) T cells in E-FABP (show FABP5L1 PLURAL_@39278@)-/- mice. Our data demonstrate that E-FABP (show FABP5L1 PLURAL_@39278@) is dispensable for antigen-specific T cell response following bacterial infection.
Genetic deletion of fatty acid-binding protein 5 (FABP5) in mice reduces uptake of exogenous docosahexaenoic acid (DHA) into brain endothelial cells and brain capillaries and reduces brain parenchymal levels of endogenous DHA. Therefore, FABP5 in the brain endothelial cell is a crucial contributor to the brain levels of DHA. Critically, lowered brain DHA levels in FABP5(-/-) mice occurred in tandem with cognitive deficits
the balance between FABP4 (show FABP4 PLURAL_@39278@) and FABP5 in endothelial cells may be important in regulation of angiogenic versus quiescent phenotypes in blood vessels.
Mice lacking FABP5 and FABP7 (show FABP7 Proteins), which exhibit highest affinities for endocannabinoids, possessed elevated levels of the endocannabinoid anandamide and the related N-acylethanolamines palmitoylethanolamide and oleoylethanolamide.
These studies show, for the first time, a correlation between FABP5 and EGFR (show EGFR Proteins) in enhancing TNBC metastasis through a novel mechanism
loss of FABP5 promotes a more anti-inflammatory response.
Circulating levels of GIP (show GIP PLURAL_@39278@) were significantly decreased in FABP5-deficient mice.
The frameshift and missense mutations in FABP3 (show FABP3 Proteins), FABP5, and FABP7 (show FABP7 Proteins) genes have been identified in schizophrenia and autism spectrum disorder in humans and in mouse behavioral studies.
FABP5 contributes to the development of Diet-induced obesity in a gastric inhibitory polypeptide (show GIP Proteins)-dependent manner.
A high expression ratio between FABP5 and CRABPII (show CRABP2 Proteins) may be related to CP tumor recurrence and ATRA could be a potential therapeutic agent for CP chemotherapy.
Data suggest that antinociceptive agent SBFI-26 binds at a portal site as well as at the canonical site in the substrate pocket of FABP5 and FABP7 (show FABP7 Proteins); only the S form of SBFI-26 binds to both FABP5 and FABP7 (show FABP7 Proteins) in their co-crystal structures; SBFI-26 induces conformational changes in FABP5 and FABP7 (show FABP7 Proteins).
secreted FABP4 (show FABP4 PLURAL_@39278@) and FABP5 from adipocytes as adipokines differentially affect transcriptional and metabolic regulation in ADSC near adipocytes
FABP5 plays an important role in the carcinogenesis and metastasis of cervical cancer, and FABP5 may be a novel predictor for prognostic assessment of cervical cancer patients.
FABP5 promoted VEGF (show VEGFA PLURAL_@39278@) expression and angiogenesis through PPARgamma (show PPARG PLURAL_@39278@) which was activated by fatty acids transported by FABP5.
FABP5 is associated with increased subclinical atherosclerosis
Long chain fatty acids suppress the oncogenic properties of FABP5-expressing carcinoma cells in cultured cells.
silencing of Sp1 (show PSG1 Proteins), c-Myc (show MYC Proteins) or FABP5 expression led to a significant decrease in cell proliferation, indicating that up-regulation of FABP5 expression by Sp1 (show PSG1 Proteins) and c-Myc (show MYC Proteins) is critical for the proliferation of prostate cancer cells
FABP5 may contribute to the airway remodeling and inflammation in asthma by fine-tuning the levels of CysLTs, which induce VEGF production.
This gene encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs may play roles in fatty acid uptake, transport, and metabolism. Polymorphisms in this gene are associated with type 2 diabetes. The human genome contains many pseudogenes similar to this locus.
epidermal-type fatty acid-binding protein
, epithelial fatty acid-binding protein
, fatty acid-binding protein, epidermal
, keratinocyte lipid-binding protein
, psoriasis-associated fatty acid-binding protein homolog
, fatty acid binding protein 5
, differentiation-associated lipid-binding protein LP2
, epidermal fatty acid-binding protein
, fatty acid-binding protein 5
, cutaneous fatty acid-binding protein