β-Actin (D6A8) Rabbit mAb (BSA and Azide Free) #19069
- WB
- IF
- F
Supporting Data
| REACTIVITY | H M R Mk Dm Z |
| SENSITIVITY | Endogenous |
| MW (kDa) | 45 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
- Dm-D. melanogaster
- Z-Zebrafish
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
β-Actin (D6A8) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total β-actin protein. Due to the high sequence identity between the cytoplasmic actin isoforms, β-actin and cytoplasmic γ-actin, this antibody may cross-react with cytoplasmic γ-actin. It does not cross-react with α-skeletal, α-cardiac, α-vascular smooth, or γ-enteric smooth muscle isoforms.
Species Reactivity:
Human, Mouse, Rat, Monkey, D. melanogaster, Zebrafish
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Hamster, Chicken, Bovine, Pig
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.
Background
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 ubiquitously expressed, controlling cell structure and motility (1). While all actin isoforms are highly homologous, cytoplasmic β- and γ-actin protein sequences differ by only four biochemically similar amino acids (2). For this reason, antibodies raised to β-actin may cross-react with γ-actin, and vice versa. 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 (3). The ARP2/3 complex stabilizes F-actin fragments and promotes formation of new actin filaments (3). Research studies have shown that actin is hyperphosphorylated in primary breast tumors (4). Cleavage of actin under apoptotic conditions has been observed in vitro and in cardiac and skeletal muscle, as shown in research studies (5-7). Actin cleavage by caspase-3 may accelerate ubiquitin/proteasome-dependent muscle proteolysis (7).
- Herman, I.M. (1993) Curr. Opin. Cell Biol. 5, 48-55.
- Perrin, B.J. and Ervasti, J.M. (2010) Cytoskeleton (Hoboken) 67, 630-4.
- Condeelis, J. (2001) Trends Cell Biol 11, 288-93.
- Lim, Y.P. et al. (2004) Clin Cancer Res 10, 3980-7.
- Kayalar, C. et al. (1996) Proc Natl Acad Sci U S A 93, 2234-8.
- Communal, C. et al. (2002) Proc Natl Acad Sci U S A 99, 6252-6.
- Du, J. et al. (2004) J Clin Invest 113, 115-23.
Limited Uses
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