ABS1621
Anti-Lcat Antibody
serum, from rabbit
Synonym(s):
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, Lcat
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
mouse, human
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... LCAT(3931)
General description
Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43; UniProt P16301; also known as Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT) is encoded by the Lcat (also known as AI046659; D8Wsu61e) gene (Gene ID 16816) in murine species. LCAT catalyzes the esterification of cholesterol and phosphatidylcholines (PCs) to cholesteryl esters and lysoPCs on the surface of high and low density lipoproteins (HDLs and LDLs). LCAT reaction is essential for the maturation of nascent HDL particles in plasma, and a genetic deficiency of LCAT results in the near absence of normal HDL particles and the presence of plasma very low density and low density lipoprotein particles of abnormal size and shape. LCAT is initially produced with a 24-aa N-terminal signal peptide, which is later cleaved to form the mature enzyme. LCAT is synthesized in the liver before it is secreted into the plasma.
Immunogen
Recombinant protein corresponding to mouse Lcat.
Application
This Anti-Lcat Antibody is validated for use in Western Blotting for the detection of Lcat .
Western Blotting Analysis: A representative lot detected Lcat in FPLC-fractionated, TCA-precipitated plasma HDL from wild-type mice as well as mice with human apoM and/or A-I transgene (Liu, M., et al. (2014). J Biol Chem. 289(5)2801-2814).
Western Blotting Analysis: A representative lot detected Lcat in plasma from WT and endothelial lipase (EL) knockout mice (Ma, K., et al. (2003). Proc Natl Acad Sci USA. 100(5)2748-2753).
Western Blotting Analysis: A representative lot detected purified murine Lcat and Lcat in plasma samples from human A-I transgenic mice with or without scavenger receptor class B type I (SR-BI) knockout, purified mouse LCAT (Lee, J.Y., et al. (2007). J Lipid Res. 48(5)1052-1061).
Western Blotting Analysis: A representative lot detected Lcat in plasma from WT and endothelial lipase (EL) knockout mice (Ma, K., et al. (2003). Proc Natl Acad Sci USA. 100(5)2748-2753).
Western Blotting Analysis: A representative lot detected purified murine Lcat and Lcat in plasma samples from human A-I transgenic mice with or without scavenger receptor class B type I (SR-BI) knockout, purified mouse LCAT (Lee, J.Y., et al. (2007). J Lipid Res. 48(5)1052-1061).
Quality
Evaluated by Western Blotting in mouse serum.
Western Blotting Analysis: A 1:500 dilution of this antibody detected Lcat in ~2.3 µg of mouse serum.
Western Blotting Analysis: A 1:500 dilution of this antibody detected Lcat in ~2.3 µg of mouse serum.
Target description
~60 kDa observed. Target band size appears larger than the calculated molecular weight (49.7 kDa/preform & 49.0 kDa/mature) due to glycosylation. Uncharacterized band(s) may appear in some lysates.
Other Notes
Concentration: Please refer to lot specific datasheet.
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
Certificates of Analysis (COA)
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Mingxia Liu et al.
The Journal of biological chemistry, 289(5), 2801-2814 (2013-12-10)
Apolipoprotein M (apoM), a lipocalin family member, preferentially associates with plasma HDL and binds plasma sphingosine 1-phosphate (S1P), a signaling molecule active in immune homeostasis and endothelial barrier function. ApoM overexpression in ABCA1-expressing HEK293 cells stimulated larger nascent HDL formation
Functional LCAT deficiency in human apolipoprotein A-I transgenic, SR-BI knockout mice.
Lee, JY; Badeau, RM; Mulya, A; Boudyguina, E; Gebre, AK; Smith, TL; Parks, JS
Journal of Lipid Research null
Endothelial lipase is a major genetic determinant for high-density lipoprotein concentration, structure, and metabolism.
Ma, K; Cilingiroglu, M; Otvos, JD; Ballantyne, CM; Marian, AJ; Chan, L
Proceedings of the National Academy of Sciences of the USA null
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