Key features and details
- Rabbit polyclonal to LCLAT1
- Suitable for: IHC-P
- Reacts with: Human
- Isotype: IgG
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage bufferpH: 7.20
Preservative: 0.02% Sodium azide
Constituents: 40% Glycerol, 59% PBS
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab122197 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||1/200 - 1/500. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.|
FunctionAcyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages.
Tissue specificityExpressed at higher level in heart, kidney and pancreas than in brain, spleen, liver, lung, small intestine and placenta.
PathwayPhospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Sequence similaritiesBelongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
DomainThe HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Cellular localizationEndoplasmic reticulum membrane.
- Information by UniProt
- 1-acylglycerol-3-phosphate O-acyltransferase 8 antibody
- 1-AGP acyltransferase 8 antibody
- 1-AGPAT 8 antibody
ab122197 has not yet been referenced specifically in any publications.