|Other Names||Alpha-adducin, Erythrocyte adducin subunit alpha, ADD1, ADDA|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP13986b was selected from the C-term region of ADD1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.|
|Cellular Location||Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side|
|Tissue Location||Expressed in all tissues. Found in much higher levels in reticulocytes than the beta subunit|
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Adducins are a family of cytoskeleton proteins encoded bythree genes (alpha, beta, gamma). Adducin is a heterodimericprotein that consists of related subunits, which are produced fromdistinct genes but share a similar structure. Alpha- andbeta-adducin include a protease-resistant N-terminal region and aprotease-sensitive, hydrophilic C-terminal region. Alpha- andgamma-adducins are ubiquitously expressed. In contrast,beta-adducin is expressed at high levels in brain and hematopoietictissues. Adducin binds with high affinity to Ca(2+)/calmodulin andis a substrate for protein kinases A and C. Alternative splicingresults in multiple variants encoding distinct isoforms; however,not all variants have been fully described.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Irvin, M.R., et al. J. Hypertens. 28(10):2076-2083(2010)Schuur, M., et al. J. Neurol. Neurosurg. Psychiatr. (2010) In press :Wang, Y., et al. Diabet. Med. 27(4):376-383(2010)Cross, D.S., et al. BMC Genet. 11, 51 (2010) :
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