Product Pathways - Cytoskeletal Signaling
β-Actin (D6A8) Rabbit mAb #8457
|8457L||300 µl (30 western blots)||---||In Stock||---|
|8457S||100 µl (10 western blots)||---||In Stock||---|
|8457P||40 µl (4 western blots)||---||In Stock||---|
|8457||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||45||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IF-IC=Immunofluorescence (Immunocytochemistry), F=Flow Cytometry
* Product-specific protocol.
Specificity / Sensitivity
β-Actin (D6A8) Rabbit mAb recognizes endogenous levels of total β-actin protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human β-actin protein.
Western blot analysis of extracts from various cell lines using β-Actin (D6A8) Rabbit mAb.
Flow cytometric analysis of NIH/3T3 cells using β-Actin (D6A8) Rabbit mAb (blue) compared to concentration matched Rabbit (DA1E) mAb IgG XP® Isotype control #3900 (red). Anti-rabbit IgG (H+L), F(ab')2 Fragment (Alexa Fluor® 647 Conjugate) #4414 was used as a secondary antibody.
Confocal immunofluorescent analysis of HeLa cells using β-Actin (D6A8) Rabbit mAb (green). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
Actin, a ubiquitous eukaryotic protein, is the major component of the cytoskeleton. At least six isoforms are known in mammals. Nonmuscle β- and γ-actin, also known as cytoplasmic actin, are predominantly expressed in nonmuscle cells, controlling cell structure and motility (1). α-cardiac and α-skeletal actin are expressed in striated cardiac and skeletal muscles, respectively; two smooth muscle actins, α- and γ-actin, are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. These actin isoforms regulate the contractile potential of muscle cells (1). Actin exists mainly as a fibrous polymer, F-actin. In response to cytoskeletal reorganizing signals during processes such as cytokinesis, endocytosis, or stress, cofilin promotes fragmentation and depolymerization of F-actin, resulting in an increase in the monomeric globular form, G-actin (2). The ARP2/3 complex stabilizes F-actin fragments and promotes formation of new actin filaments (2). Research studies have shown that actin is hyperphosphorylated in primary breast tumors (3). Cleavage of actin under apoptotic conditions has been observed in vitro and in cardiac and skeletal muscle, as shown in research studies (4-6). Actin cleavage by caspase-3 may accelerate ubiquitin/proteasome-dependent muscle proteolysis (6).
- Herman, I.M. (1993) Curr. Opin. Cell Biol. 5, 48-55.
- Condeelis, J. (2001) Trends Cell Biol. 11, 288-293.
- Lim, Y.P. et al. (2004) Clin. Cancer Res. 10, 3980-3987.
- Kayalar, C. et al. (1996) Proc. Natl. Acad. Sci. USA. 93, 2234-2238.
- Communal, C. et al. (2002) Proc. Natl. Acad. Sci. USA. 99, 6252-6256.
- Du, J. et al. (2004) J. Clin. Invest. 113, 115-123.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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