CapZ-α Antibody (C-1): sc-374303

CapZ-α Antibody (C-1) is a mouse monoclonal IgG1 antibody that detects CapZ-α in mouse, rat, and human samples through various applications including western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and enzyme-linked immunosorbent assay (ELISA). CapZ-α, also known as F-Actin-capping protein subunit alpha-1, is a crucial 286 amino acid component of the F-Actin capping protein complex, which plays a vital role in regulating actin dynamics by binding to the fast-growing barbed ends of actin filaments. This binding prevents the addition or loss of actin monomers, thereby stabilizing the filament structure and influencing cellular processes such as motility, shape, and division. CapZ-α forms a heterodimer with a beta subunit to facilitate actin polymerization nucleation without severing existing filaments. CapZ-α has been shown to interact with the S-100 β chain, a signaling molecule implicated in the calcium-sensitive assembly of intermediate filaments, linking CapZ-α to critical pathways in neurodegenerative diseases such as Alzheimer′s. Anti-CapZ-α antibody (C-1) serves as an invaluable tool for researchers studying actin dynamics and its implications in various biological processes and diseases.

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CapZ-α Antibody (C-1) References:

1. Tuberous sclerosis genes regulate cellular 14-3-3 protein levels.  |  Hengstschläger, M., et al. 2003. Biochem Biophys Res Commun. 312: 676-83. PMID: 14680818
2. S100A8 is identified as a biomarker of HPV18-infected oral squamous cell carcinomas by suppression subtraction hybridization, clinical proteomics analysis, and immunohistochemistry staining.  |  Lo, WY., et al. 2007. J Proteome Res. 6: 2143-51. PMID: 17451265
3. Evolutionary conservation of the WASH complex, an actin polymerization machine involved in endosomal fission.  |  Derivery, E. and Gautreau, A. 2010. Commun Integr Biol. 3: 227-30. PMID: 20714399
4. Disease causing mutations in inverted formin 2 regulate its binding to G-actin, F-actin capping protein (CapZ α-1) and profilin 2.  |  Rollason, R., et al. 2016. Biosci Rep. 36: e00302. PMID: 26764407
5. Mechanosignaling pathways alter muscle structure and function by post-translational modification of existing sarcomeric proteins to optimize energy usage.  |  Russell, B. and Solís, C. 2021. J Muscle Res Cell Motil. 42: 367-380. PMID: 33595762
6. NcRNA-regulated CAPZA1 associated with prognostic and immunological effects across lung adenocarcinoma.  |  Qin, T., et al. 2022. Front Oncol. 12: 1025192. PMID: 36686785
7. Characterization of S-100b binding epitopes. Identification of a novel target, the actin capping protein, CapZ.  |  Ivanenkov, VV., et al. 1995. J Biol Chem. 270: 14651-8. PMID: 7540176
8. Interaction of S100a0 protein with the actin capping protein, CapZ: characterization of a putative S100a0 binding site in CapZ alpha-subunit.  |  Ivanenkov, VV., et al. 1996. Biochem Biophys Res Commun. 221: 46-50. PMID: 8660341
9. Identification of the binding site on S100B protein for the actin capping protein CapZ.  |  Kilby, PM., et al. 1997. Protein Sci. 6: 2494-503. PMID: 9416599
10. Hydrophobic residues in the C-terminal region of S100A1 are essential for target protein binding but not for dimerization.  |  Osterloh, D., et al. 1998. Cell Calcium. 24: 137-51. PMID: 9803314

The preferred CapZ-α antibody is CapZ-α Antibody (H-9): sc-374302.