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Render Timestamp: 2024-11-25T11:37:04.155Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-04-05 20:22:12.840
Product last modified at: 2024-06-27T13:36:13.023Z
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PDP - Template Name: Blocking Peptide
PDP - Template ID: *******6db2f4c

β-Actin Blocking Peptide #1025

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    Product Information

    Product Usage Information

    Use as a blocking reagent to evaluate the specificity of antibody reactivity in dot blot protocols.

    Storage

    Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA and 5% glycerol. 1% DMSO. Store at –20°C.

    Product Description

    This peptide is used to specifically block β-Actin (13E5) Rabbit mAb #4970 by dot blot.

    Quality Control

    The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide blocks beta-Actin (13E5) Rabbit mAb #4970 by dot blot.

    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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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