Product Pathways - Cytoskeletal Signaling
Phospho-Talin (Ser425) Antibody #5426
|W||H M R Mk||Endogenous||270||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-Talin (Ser425) Antibody detects endogenous levels of talin protein only when phosphorylated at Ser425.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser425 of human talin protein. Antibodies are purified using protein A and peptide affinity chromatography.
Focal adhesions connect the cytoskeleton with the extracellular matrix (ECM), a complex structure of secreted macromolecules that surrounds mammalian organs and tissues. Integrins clustered on the extracellular side of focal adhesions signal from the ECM to intracellular protein complexes, which in turn signal to the actin cytoskeleton to regulate the tension needed for cell motility. Internal signals also converge on focal adhesions to regulate integrin affinity and avidity. Signaling through focal adhesions regulates cell adhesion, migration, proliferation, apoptosis and gene expression, and impacts cellular processes such as development, wound healing, immune response, invasion, metastasis and angiogenesis (reviewed in 1-3). Talin is a large, multidomain focal adhesion protein that interacts with the intracellular domains of integrins and other focal adhesion proteins. Talin is involved in the formation of focal adhesions and in linking focal adhesions to the actin cytoskeleton (4). The interaction between talin and integrins increases the affinity between integrin and both insoluble and soluble ECM proteins (5,6).
Phosphorylation of talin at Ser425 was discovered using mass spectrometry. This site is a potential substrate of CDK5 (7).
- Burridge, K. et al. (1988) Annu Rev Cell Biol 4, 487-525.
- Calderwood, D.A. et al. (2000) J Biol Chem 275, 22607-10.
- ffrench-Constant, C. and Colognato, H. (2004) Trends Cell Biol 14, 678-86.
- Nayal, A. et al. (2004) Curr Opin Cell Biol 16, 94-8.
- Tanentzapf, G. and Brown, N.H. (2006) Nat Cell Biol 8, 601-6.
- Tadokoro, S. et al. (2003) Science 302, 103-6.
- Ratnikov, B. et al. (2005) J Cell Sci 118, 4921-3.
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