Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
SPTLC2 encodes a long chain base subunit of serine palmitoyltransferase.
Showing 5 out of 7 products:
2 families had late-onset autosomal dominant HSAN1C caused by a new variant in SPTLC2, c.547C>T, p.(Arg183Trp). The variant changed a conserved amino acid.
The activities of the hLCB2a mutants were measured in the presence of ssSPTa and ssSPTb and was found that all decrease enzyme activity.
Mutations in SPTLC2 are associated with increased deoxySL formation causing hereditary sensory and autonomic neuropathy type 1 (HSANI) in a familial study.
Mutations in the SPTLC2 subunit of serine palmitoyltransferase cause hereditary sensory and autonomic neuropathy type I.
results suggest that SPTLC2 mutations are not a common cause for genetic sensory neuropathies.
Results suggest that functional serine palmitoyltransferase is not a dimer, but a higher organized complex, composed of three distinct subunits (SPTLC1 (Montrer SPTLC1 Protéines), SPTLC2 and SPTLC3 (Montrer SPTLC3 Protéines)) with a molecular mass of 480 kDa.
discovery of 2 proteins, ssSPTa and ssSPTb, which each interacts with both hLCB1 (Montrer SPTLC1 Protéines) and hLCB2, suggesting that there are 4 distinct human SPT (Montrer AGXT Protéines) isozymes.
The expression of SPT2 was stronger in vascular smooth muscle cells and neointima of carotid arteries from knock-out mice compared to wild-type.
Data suggest that overexpression of serine palmitoyltransferase (Sptlc1 (Montrer SPTLC1 Protéines) and Sptlc2, serine palmitoyltransferase long chain base subunit 1 (Montrer SPTLC1 Protéines)/2) to elevate de novo sphingolipid biosynthesis induces autophagy in the liver.
SPTLC2 knockout mice showed decreased ceramide levels in the epidermis, which impaired water-holding capacity and barrier function.
Ldlr (Montrer LDLR Protéines) gene knockout mice with myeloid cell-specific Sptlc2 haploinsufficiency exhibited significantly less atherosclerosis than controls.
Data show that LCAT (Montrer LCAT Protéines) activity was significantly higher in long chain base biosynthesis protein 2 (Sptlc2)+/- and sphingomyelin synthase 2 (Sms2 (Montrer SGMS2 Protéines))-/- mice, but markedly lower in ApoE (Montrer APOE Protéines)-/- and Ldlr (Montrer LDLR Protéines)-/- mice.
results suggest that Sptlc2-mediated de novo ceramide synthesis is an essential source of C18 (Montrer BBS9 Protéines):0 and very long chain, but not of shorter chain, ceramides in the heart
Inflammatory response elicited by lipopolysaccharide increases serine palmitoyltransferase activity via upregulation of Sptlc2 in macrophages.
Deficiency of Sptlc2 induces necrotic lesions in gastrointestinal cells followed by atrophic change of the tissue in short term.
Both Sptlc1 (Montrer SPTLC1 Protéines) and Sptlc2 interactions are necessary for Serine palmitoyl-CoA transferase (SPT (Montrer AGXT Protéines)) activity in vivo and SPT (Montrer AGXT Protéines) activity directly influences plasma sphingolipid levels
The expression and activities of SPT (Montrer AGXT Protéines) in mouse liver increased significantly following fumonisin B1 treatment.
This gene encodes a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal-5-prime-phosphate-dependent condensation of L-serine and palmitoyl-CoA to 3-oxosphinganine. Mutations in this gene were identified in patients with hereditary sensory neuropathy type I.
, SPT 2
, long chain base biosynthesis protein 2a
, serine palmitoyltransferase 2
, serine palmitoyltransferase, subunit II
, serine-palmitoyl-CoA transferase 2
, serine palmitoyltransferase, long chain base subunit 2
, serine palmitoyltransferase 2-like
, long chain base biosynthesis protein 2
, protein-O-mannosyltransferase 2
, Long chain base biosynthesis protein 2
, Long chain base biosynthesis protein 2a
, Serine-palmitoyl-CoA transferase 2