For immunochemical detection of MBOAT4
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MBOAT4 Polyclonal Antibody

Item No. 18614

Technical Information
Synonyms
  • Ghrelin O-Acyltransferase
  • GOAT
  • Membrane-bound O-Acyltransferase Domain-containing Protein 4
Immunogen
Synthetic peptide from the internal intracellular region of human MBOAT4
500 µl of peptide affinity-purified polyclonal antibody
Storage Buffer
TBS, pH 7.4, with 50% glycerol, 0.1% BSA, and 0.02% sodium azide
Host
Rabbit
Applications
FC and IF
Species Reactivity
(+) Human; other species not tested
UniProt Accession №
Q96T53
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Membrane bound O-acyl transferases (MBOATs) are a group of conserved, multiple transmembrane spanning enzymes involved in many biological functions including lipid biosynthesis, embryogenesis, nutrient sensing, and membrane lipid remodeling. This group of proteins is associated with pathologies such as diabetes, obesity, atherosclerosis, and Alzheimer’s disease.1 MBOAT4 is responsible for the octanoylination of ghrelin at serine 3, and can use a number of fatty acids as substrates including octanoic acid, decanoic acid, and tetradecanoic acid.2 Increases in the expression of MBOAT4 are dependent on preproghrelin expression during insulin-induced adipogenesis.3 Cayman's MBOAT4 Polyclonal Antibody detects MBOAT in MCF-7 and RT-4 cells by flow cytometry and immunofluorescence in human samples.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Chang, C.C.Y., Sun, J., and Chang, T.Y. Membrane-bound O-acyltransferases (MBOATs). Front. Biol. 6(3), 177-182 (2011).

    2. Gutierrez, J.A., Solenberg, P.J., Perkins, D.R., et alGhrelin octanoylation mediated by an orphan lipid transferase. Proc. Natl. Acad. Sci. USA 105(17), 6320-6325 (2008).

    3. Gurriarán-Rodríguez, U., Al-Massadi, O., Crujeiras, A.B., et alPreproghrelin expression is a key target for insulin action on adipogenesis. J. Endocrinol. 210(2), (2011).