β-Actin (13E5) Rabbit mAb (Alexa Fluor® 594 Conjugate) #9470
- IF
Supporting Data
| REACTIVITY | H M R Mk B Pg |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
- B-Bovine
- Pg-Pig
Product Information
Product Description
Product Usage Information
| Application | Dilution |
|---|---|
| Immunofluorescence (Immunocytochemistry) | 1:100 - 1:400 |
Storage
Protocol
Specificity / Sensitivity
β-Actin (13E5) Rabbit mAb (Alexa Fluor® 594 Conjugate) detects endogenous levels of total β-actin protein. Depsite the high sequence identity between the cytoplasmic actin isoforms, β-actin and cytoplasmic γ-actin, β-Actin (13E5) Rabbit mAb (Alexa Fluor® 594 Conjugate) #9470 does not cross-react with cytoplasmic γ-actin, or any other actin isoforms.
Species Reactivity:
Human, Mouse, Rat, Monkey, Bovine, Pig
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, Dog, Horse, Rabbit
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).
Limited Uses
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