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β-Actin (E4D9Z) Mouse mAb

β-Actin (E4D9Z) Mouse mAb #58169

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Supporting Data

REACTIVITY	H M R
SENSITIVITY	Endogenous
MW (kDa)	45
Source/Isotype	Mouse IgG2a

Application Key:

WB-Western Blotting
IF-Immunofluorescence
F-Flow Cytometry

Species Cross-Reactivity Key:

H-Human
M-Mouse
R-Rat

Product Information

Product Usage Information

Application	Dilution
Western Blotting	1:1000
Immunofluorescence (Immunocytochemistry)	1:400
Flow Cytometry (Fixed/Permeabilized)	1:50

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

β-Actin (E4D9Z) Mouse mAb 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

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala7 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).

Database Links

UniProt ID: P60709

Entrez-Gene Id: 60

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