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SPTLC2 encodes a long chain base subunit of serine palmitoyltransferase. Additionally we are shipping serine Palmitoyltransferase, Long Chain Base Subunit 2 Kits (4) and serine Palmitoyltransferase, Long Chain Base Subunit 2 Proteins (4) and many more products for this protein.
Showing 10 out of 74 products:
Human Polyclonal SPTLC2 Primary Antibody for WB - ABIN1881828
Rotthier, Auer-Grumbach, Janssens, Baets, Penno, Almeida-Souza, Van Hoof, Jacobs, De Vriendt, Schlotter-Weigel, Löscher, Vondráček, Seeman: Mutations in the SPTLC2 subunit of serine palmitoyltransferase cause hereditary sensory and autonomic neuropathy type I. in American journal of human genetics 2010
Show all 5 references for ABIN1881828
Human Polyclonal SPTLC2 Primary Antibody for EIA, WB - ABIN357774
Stachowitz, Alessandrini, Abeck, Ring, Behrendt: Permeability barrier disruption increases the level of serine palmitoyltransferase in human epidermis. in The Journal of investigative dermatology 2002
Show all 5 references for ABIN357774
Chicken Polyclonal SPTLC2 Primary Antibody for WB - ABIN2783451
Hornemann, Wei, von Eckardstein: Is the mammalian serine palmitoyltransferase a high-molecular-mass complex? in The Biochemical journal 2007
Human Polyclonal SPTLC2 Primary Antibody for ELISA, WB - ABIN564104
Wang, Robinet, Smith, Gulshan: ORMDL orosomucoid-like proteins are degraded by free-cholesterol-loading-induced autophagy. in Proceedings of the National Academy of Sciences of the United States of America 2015
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 (show SPTLC1 Antibodies) and Sptlc2, serine palmitoyltransferase long chain base subunit 1 (show SPTLC1 Antibodies)/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 (show LDLR Antibodies) gene knockout mice with myeloid cell-specific Sptlc2 haploinsufficiency exhibited significantly less atherosclerosis than controls.
Data show that LCAT (show LCAT Antibodies) activity was significantly higher in long chain base biosynthesis protein 2 (Sptlc2)+/- and sphingomyelin synthase 2 (Sms2 (show SGMS2 Antibodies))-/- mice, but markedly lower in ApoE (show APOE Antibodies)-/- and Ldlr (show LDLR Antibodies)-/- mice.
results suggest that Sptlc2-mediated de novo ceramide synthesis is an essential source of C18 (show BBS9 Antibodies):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 (show SPTLC1 Antibodies) and Sptlc2 interactions are necessary for Serine palmitoyl-CoA transferase (SPT (show AGXT Antibodies)) activity in vivo and SPT (show AGXT Antibodies) activity directly influences plasma sphingolipid levels
The expression and activities of SPT (show AGXT Antibodies) in mouse liver increased significantly following fumonisin B1 treatment.
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 (show SPTLC1 Antibodies), SPTLC2 and SPTLC3 (show SPTLC3 Antibodies)) with a molecular mass of 480 kDa.
discovery of 2 proteins, ssSPTa and ssSPTb, which each interacts with both hLCB1 (show SPTLC1 Antibodies) and hLCB2, suggesting that there are 4 distinct human SPT (show AGXT Antibodies) isozymes.
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.
serine palmitoyltransferase, long chain base subunit 2
, serine palmitoyltransferase 2-like
, sublingual parotid tongue-2 salivary protein
, LCB 2
, Long chain base biosynthesis protein 2
, Long chain base biosynthesis protein 2a
, SPT 2
, Serine-palmitoyl-CoA transferase 2
, serine palmitoyltransferase 2
, long chain base biosynthesis protein 2a
, serine palmitoyltransferase, subunit II
, serine-palmitoyl-CoA transferase 2
, long chain base biosynthesis protein 2
, protein-O-mannosyltransferase 2