ARG56833
anti-beta Actin antibody (HRP)
anti-beta Actin antibody (HRP) for Western blot and Hamster,Human,Monkey,Mouse,Plant,Rat
Controls and Markers antibody; Signaling Transduction antibody; Loading Control antibody; Cytochrome-C fractionation Study antibody; Inflammation Study antibody; Tag Internal Control antibody
Overview
Product Description | HRP-conjugated Mouse Monoclonal antibody recognizes beta Actin |
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Tested Reactivity | Hu, Ms, Rat, Hm, Mk, Plnt |
Tested Application | WB |
Specificity | This antibody detects endogenous levels of beta-actin and does not cross-react with related proteins. |
Host | Mouse |
Clonality | Monoclonal |
Isotype | IgG2b |
Target Name | beta Actin |
Antigen Species | Human |
Immunogen | Purified recombinant Human beta Actin protein fragments. |
Conjugation | HRP |
Alternate Names | PS1TP5BP1; BRWS1; Actin, cytoplasmic 1; Beta-actin |
Application Instructions
Application Suggestion |
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Application Note | * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. |
Properties
Form | Liquid |
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Purification | Affinity purification. |
Buffer | PBS (pH 7.4), 50% Glycerol and 0.1 mg/ml BSA. |
Stabilizer | 50% Glycerol and 0.1 mg/ml BSA |
Concentration | 0.2 mg/ml |
Storage Instruction | Aliquot and store in the dark at 2-8°C. Keep protected from prolonged exposure to light. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. |
Note | For laboratory research only, not for drug, diagnostic or other use. |
Bioinformation
Database Links | |
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Gene Symbol | ACTB |
Gene Full Name | actin, beta |
Background | Beta actin is one of six different actin proteins. Actins are highly conserved proteins that are involved in cell motility, structure, integrity, and intercellular signaling. The encoded protein is a major constituent of the contractile apparatus and one of the two nonmuscle cytoskeletal actins that are ubiquitously expressed. Mutations in this gene cause Baraitser-Winter syndrome 1, which is characterized by intellectual disability with a distinctive facial appearance in human patients. Numerous pseudogenes of this gene have been identified throughout the human genome. [provided by RefSeq, Aug 2017] |
Function | Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:29581253). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947). [UniProt] |
Research Area | Controls and Markers antibody; Signaling Transduction antibody; Loading Control antibody; Cytochrome-C fractionation Study antibody; Inflammation Study antibody; Tag Internal Control antibody |
Calculated MW | 42 kDa |
PTM | ISGylated. Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization (By similarity). Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. (Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-50 of one monomer and Glu-270 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148). |