Actin Filament Regulation Immunocytochemistry Kit

Background:
Actin is a major cytoskeletal protein involved in diverse cellular functions including cell motility, adhesion, and morphology. Six different actin isoforms have been identified in vertebrates. There are four α isoforms: skeletal, cardiac, and two smooth muscle (enteric and aortic) actins, along with two cytoplasmic actins (β and γ). Actin exists in two principal forms, globular monomeric (G) actin, and filamentous polymeric (F) actin. The assembly and disassembly of actin filaments, and also their organization into functional networks, is regulated by a variety of actin-binding proteins (ABPs). Phosphorylation may also be important for regulating actin assembly and interaction with ABPs. In Dictyostelium, phosphorylation of Tyr-53 occurs in response to cell stress and this phosphorylation may alter actin polymerization. In B cells, SHP-1 tyrosine dephosphorylation of actin leads to actin filament depolymerization following BCR stimulation.

Background References
Wulf, E. et al. (1979) Proc. Nat. Acad. of Sci.(USA). 76:4498.
Faulstich, H. et al. (1983) Exp. Cell Res. 144:73.
Faulstich, H. et al. (1988) J. Muscle Res. Cell Motility. 9:370.
Jungbluth, A. et al. (1995) FEBS Let. 375:87.
Baba, T. et al. (2003) J. Immunol. 170: 3762.
Winder, S.J. et al. (2005) J. Cell Sci. 118:651.
Liu, X. et al. (2006) Proc Nat Acad Sci U S A. 103(37):13694.

Buffer/Storage:
Mouse monoclonal, rabbit polyclonal, and secondary reagents are supplied in phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.

Product References:
AM2021 Dutta, P et al. (2014) J Neurochem. 130(3):360 WB: rat brain
AM2021 Muirhead, G et al. (2014) J Mol Neurosci. 53(1):125 WB: rat brain
AM2021 Pritchard, AJ et al. (2014) PLoS One. 9(6):e99444 WB: mouse splenocytes