|Application ||WB, IHC, E|
|Other Accession||NP_061167, 8923911|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||Predicted: 50 kDa; Observed: 48 kDa|
|Application Notes||LANCL2 antibody can be used for the detection of LANCL2 by Western blot at 1 - 2 µg/mL. Antibody can also be used for immunohistochemistry starting at 5 µg/mL.|
|Target/Specificity||LANCL2; LANCL2 antibody is human, mouse and rat reactive.|
|Reconstitution & Storage||LANCL2 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.|
|Precautions||LANCL2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes.|
|Cellular Location||Nucleus. Cytoplasm. Cell membrane Note=Localizes to the juxta-nuclear vesicles (PubMed:16979580) Associates with the cortical actin cytoskeleton (PubMed:16979580) Cholesterol depletion by methyl-beta-cyclodextrin causes partial dissociation from the cell membrane in vitro and an enhanced cell detachment from the matrix in vivo (PubMed:16979580). Membrane- association is important for the increased cellular sensitivity to an anticancer drug (adriamycin) (PubMed:16979580)|
|Tissue Location||Expressed in brain and testis.|
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Provided below are standard protocols that you may find useful for product applications.
LANCL2 (LanC-like protein 2), also known as TASP (testis-specific adriamycin sensitivity protein) or GPR69B, is a 450 amino acid member of the LanC-like protein family (1). It is expressed highly in brain and testis and localized to the nucleus, cytoplasm and cell membrane (2,3). LANCL2 is necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes (3,4).
Mayer H, Pongratz M, and Prohaska R. Molecular cloning, characterization, and tissue-specific expression of human LANCL2, a novel member of the LanC-like protein family. DNA Seq. 2001; 12:161-6.
Sturla L, Fresia C, Guida L, et al. Binding of abscisic acid to human LANCL2. Biochem. Biophys. Res. Commun. 2011; 415:390-5.
Landlinger C, Salzer U, and Prohaska R. Myristoylation of human LanC-like protein 2 (LANCL2) is essential for the interaction with the plasma membrane and the increase in cellular sensitivity to adriamycin. Biochim. Biophys. Acta. 2006; 1758:1759-67.
Zeng M, van der Donk WA, Chen J. Lanthionine synthetase C-like protein 2 (LanCL2) is a novel regulator of Akt. Mol. Biol. Cell 2014; 25:3954-61.
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