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FA2H encodes a protein that catalyzes the synthesis of 2-hydroxysphingolipids, a subset of sphingolipids that contain 2-hydroxy fatty acids. Additionally we are shipping FA2H Proteins (4) and FA2H Kits (3) and many more products for this protein.
Showing 10 out of 38 products:
Human Polyclonal FA2H Primary Antibody for WB - ABIN265110
Alderson, Walla, Hama: A novel method for the measurement of in vitro fatty acid 2-hydroxylase activity by gas chromatography-mass spectrometry. in Journal of lipid research 2005
Show all 3 references for ABIN265110
Human Polyclonal FA2H Primary Antibody for IHC (p), WB - ABIN650994
Uchida, Hama, Alderson, Douangpanya, Wang, Crumrine, Elias, Holleran: Fatty acid 2-hydroxylase, encoded by FA2H, accounts for differentiation-associated increase in 2-OH ceramides during keratinocyte differentiation. in The Journal of biological chemistry 2007
Novel mutations in FA2H in Arab patients with a clinical spectrum of neurodegeneration and hereditary spastic paraparesis were identified.
Three novel mutations in Chinese patients significantly reduce FA2H enzyme activity leading to hereditary spastic paraplegia.
Induced levels of PPARalpha (show PPARA Antibodies) may be involved in the Delta(9)-THC up-regulation of FA2H in MDA-MB-231 cells.
One heterozygous deletion within 16q22.3-q23.1 including FA2H was observed in two siblings who share symptoms of autism and severe cognitive impairment, axial T2-FLAIR weighted MRI (show C7ORF49 Antibodies) posterior periventricular white matter lesions.
Identification of a novel triple heterozygous mutations in FA2H gene (c.968C>A; c.976G>A; c.688G>A) in a Chinese family with Hereditary Spastic Paraplegia Type 35.
FA2H is a novel (9)-THC-regulated gene, and that (9)-THC induces differentiation signal(s) in poorly differentiated MDA-MB-231 cells.
we report a novel mutation in FA2H gene in two sibs presenting with adult onset complicated spastic paraparesis and thin corpus callosum
This study did not find any mutations in the FA2H gene in patients with neurodegeneration with brain iron accumulation.
a novel homozygous c.270+3A>T mutation altered FA2H function led to a severe phenotype, with clinical features overlapping those in three FA2H-associated disorders
The 2-hydroxylated sphingomyelin (SM) profiles were characterized in blood and fibroblasts from patients harboring a deleterious FA2H mutation.
the importance of the sebaceous glands and a role of specific sebaceous gland or sebum lipids, synthesized by FA2H, in the hair follicle homeostasis
This study provided the first evidence that FA2H has an important function outside of oligodendrocytes in the Central nervous system.
Our study showed that the additional deletion of Fa2h does not obviously affect the phenotype of Cgt (show UGT8 Antibodies)-/- mice. This suggests that HFA-GlcCer and HFA-sphingomyelin do not functionally compensate the loss of HFA-GalCer in Cgt (show UGT8 Antibodies)-/- mice.
Fndings document the novel role of FA2H in adipocyte lipogenesis possibly by modulation of raft fluidity and level of GLUT4 (show SLC2A4 Antibodies).
FA2H is the enzyme responsible for the formation of alpha-hydroxylated ceramide in oligodendrocytes of the mammalian brain.
FA2H is the major fatty acid 2-hydroxylase in brain, and 2-hydroxylation of free fatty acids is the first step in the synthesis of 2-hydroxy galactolipids
This gene encodes a protein that catalyzes the synthesis of 2-hydroxysphingolipids, a subset of sphingolipids that contain 2-hydroxy fatty acids. Sphingolipids play roles in many cellular processes and their structural diversity arises from modification of the hydrophobic ceramide moiety, such as by 2-hydroxylation of the N-acyl chain, and the existence of many different head groups. Mutations in this gene have been associated with leukodystrophy dysmyelinating with spastic paraparesis with or without dystonia.
fatty acid 2-hydroxylase
, fatty acid 2-hydroxylase-like
, fatty acid hydroxylase
, fatty acid alpha-hydroxylase
, fatty acid hydroxylase domain containing 1
, spastic paraplegia 35 (autosomal recessive)
, WD repeat domain 59