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SPTLC2 encodes a long chain base subunit of serine palmitoyltransferase. Zusätzlich bieten wir Ihnen serine Palmitoyltransferase, Long Chain Base Subunit 2 Antikörper (86) und serine Palmitoyltransferase, Long Chain Base Subunit 2 Kits (7) und viele weitere Produktgruppen zu diesem Protein an.
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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.
an increase in transepidermal water loss is an obligatory trigger for the upregulation of serine palmitoyltransferase mRNA expression in human epidermis
Results suggest that functional serine palmitoyltransferase is not a dimer, but a higher organized complex, composed of three distinct subunits (SPTLC1, SPTLC2 and SPTLC3) with a molecular mass of 480 kDa.
discovery of 2 proteins, ssSPTa and ssSPTb, which each interacts with both hLCB1 and hLCB2, suggesting that there are 4 distinct human SPT 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 and Sptlc2, serine palmitoyltransferase long chain base subunit 1/2) 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 gene knockout mice with myeloid cell-specific Sptlc2 haploinsufficiency exhibited significantly less atherosclerosis than controls.
Data show that LCAT activity was significantly higher in long chain base biosynthesis protein 2 (Sptlc2)+/- and sphingomyelin synthase 2 (Sms2)-/- mice, but markedly lower in ApoE-/- and Ldlr-/- mice.
results suggest that Sptlc2-mediated de novo ceramide synthesis is an essential source of C18:0 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 and Sptlc2 interactions are necessary for Serine palmitoyl-CoA transferase (SPT) activity in vivo and SPT activity directly influences plasma sphingolipid levels
The expression and activities of SPT in mouse liver increased significantly following fumonisin B1 treatment.
the proximal 335 bp contain initiator and downstream promoter elements, two proximal GC boxes that stimulate transcription in a cooperative manner, and several additional elements whose activity cannot be accounted for by known factor binding sites
Data show that plasma from Sptlc2 knock-out mice had a significantly stronger potential for promoting cholesterol efflux from macrophages than from wild-type mice because of a greater amount of apoE in the circulation.
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