Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
host | mouse |
isotype | IgG1 |
clonality | monoclonal |
concentration | 1 mg/mL |
applications | ICC/IF, IHC, WB |
reactivity | cow, human, mouse, pig, rat |
available sizes | 1 mg, 100 µg, 25 µg |
mouse anti-Actin (pan) monoclonal antibody (5J11) 7047
$100.00 – $2,600.00
Antibody summary
- Mouse monoclonal to Actin (pan)
- Suitable for: WB, ICC/IF, IHC
- Reacts with: human, mouse, rat, cow, pig
- Isotype: IgG1
- 100 µg, 25 µg, 1 mg
mouse anti-Actin (pan) monoclonal antibody (5J11) 7047
target relevance |
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Actin, a highly conserved protein, is widely recognized as an essential loading control in scientific research, particularly in the field of cell biology and molecular biology. As a structural component of the cytoskeleton, actin is present in virtually all eukaryotic cells. Actin participates in many important cellular processes, including muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape. Many of these processes are mediated by extensive and intimate interactions of actin with cellular membranes. Its ubiquitous expression and relatively stable levels make it an ideal reference protein for normalizing protein loading in Western blotting and other protein analysis techniques. Actin' abundance and consistent expression ensure that its quantity remains relatively constant across different experimental conditions and sample variations. Actin isoforms are distinct variants of the actin protein found in eukaryotic cells, and they play crucial roles in various cellular processes. One of the primary differences between actin isoforms lies in their tissue-specific distribution. For instance, skeletal muscle cells predominantly express the α-actin isoform, while smooth muscle cells mainly contain the γ-actin isoform. These tissue-specific distributions are essential for the specialized functions of muscle cells. Moreover, actin isoforms can also differ in their post-translational modifications. For example, γ-actin is more prone to undergo acetylation than α-actin. Additionally, actin isoforms can exhibit variations in their kinetic properties, such as rates of polymerization and depolymerization, which can influence their roles in processes like cell motility or cytoskeletal stability. Furthermore, some actin isoforms may interact with different binding partners or regulatory proteins, further diversifying their functions within the cell. These differences in tissue distribution, post-translational modifications, kinetic properties, and protein interactions contribute to the versatility and specificity of actin isoforms in various cellular processes and underline their importance in maintaining cellular structure and function. This antibody recognizes multiple actin isoforms and can be used as a loading control when run alongside proteins of interest with different and resolvable molecular weights and ideally in combination with antibodies of same host and when using a secondary antibody. Click for more on: loading controls and Actin |
Protein names Actin, alpha skeletal muscle (EC 3.6.4.-) (Alpha-actin-1) [Cleaved into: Actin, alpha skeletal muscle, intermediate form] |
Gene names ACTA1, ACTA2, ACTB, ACTG1, ACTC1,ACTA1 ACTA2 ACTB ACTG1 ACTC1 |
Protein family Actin family |
Mass 42051Da |
Function Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. |
Catalytic activity Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence=; |
Subellular location Cytoplasm, cytoskeleton. |
Structure Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Interacts with alpha-actinin (By similarity). Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X (By similarity). Interacts with TTID (PubMed:10958653). Interacts (via its C-terminus) with USP25; the interaction occurs for all USP25 isoforms but is strongest for isoform USP25m in muscle differentiating cells (PubMed:16501887). |
Post-translational modification Oxidation of Met-46 and Met-49 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 promotes actin repolymerization. ; Monomethylation at Lys-86 (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. ; [Actin, alpha skeletal muscle, intermediate form]: N-terminal cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP. ; Methylated at His-75 by SETD3. ; (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-52 of one monomer and Glu-272 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). |
Involvement in disease Nemaline myopathy 3 (NEM3) [MIM:161800]: A form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. Note=The disease is caused by variants affecting the gene represented in this entry.; Myopathy, actin, congenital, with excess of thin myofilaments (MPCETM) [MIM:161800]: A congenital muscular disorder characterized at histological level by areas of sarcoplasm devoid of normal myofibrils and mitochondria, and replaced with dense masses of thin filaments. Central cores, rods, ragged red fibers, and necrosis are absent. Note=The disease is caused by variants affecting the gene represented in this entry.; Myopathy, congenital, with fiber-type disproportion (CFTD) [MIM:255310]: A genetically heterogeneous disorder in which there is relative hypotrophy of type 1 muscle fibers compared to type 2 fibers on skeletal muscle biopsy. However, these findings are not specific and can be found in many different myopathic and neuropathic conditions. Note=The disease is caused by variants affecting the gene represented in this entry.; Myopathy, scapulohumeroperoneal (SHPM) [MIM:616852]: An autosomal dominant muscular disorder characterized by progressive muscle weakness with initial scapulo-humeral-peroneal and distal distribution. Over time, muscle weakness progresses to proximal muscle groups. Clinical characteristics include scapular winging, mild lower facial weakness, foot drop due to foot eversion and dorsiflexion weakness, and selective muscle atrophy. Age at onset and disease progression are variable. Note=The disease is caused by variants affecting the gene represented in this entry. |
Target Relevance information above includes information from UniProt accession: PANACT |
The UniProt Consortium |
Publications
pmid | title | authors | citation |
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37310811 | Oncostatin-M and OSM-Receptor Feed-Forward Activation of MAPK Induces Separable Stem-like and Mesenchymal Programs | Polak KL, Tamagno I, Parameswaran N, Smigiel J, Chan ER, Yuan X, Rios B, Jackson MW. | Mol Cancer Res. 2023 Sep 1;21(9):975-990. doi: 10.1158/1541-7786.MCR-22-0715. |
33839158 | The C99 domain of the amyloid precursor protein resides in the disordered membrane phase | Capone R, Tiwari A, Hadziselimovic A, Peskova Y, Hutchison JM, Sanders CR, Kenworthy AK. | J Biol Chem. 2021 Jan-Jun;296:100652. doi: 10.1016/j.jbc.2021.100652. Epub 2021 Apr 9. |
33175436 | Neuron-specific cilia loss differentially alters locomotor responses to amphetamine in mice | Ramos C, Roberts JB, Jasso KR, Ten Eyck TW, Everett T, Pozo P, Setlow B, McIntyre JC. | J Neurosci Res. 2021 Mar;99(3):827-842. doi: 10.1002/jnr.24755. Epub 2020 Nov 11. |
29321224 | Reconsidering an active role for G-actin in cytoskeletal regulation | Skruber K, Read TA, Vitriol EA. | J Cell Sci. 2018 Jan 10;131(1):jcs203760. doi: 10.1242/jcs.203760. |
27133808 | Unravelling the Actin Cytoskeleton: A New Competitive Edge? | Davidson AJ, Wood W. | Trends Cell Biol. 2016 Aug;26(8):569-576. doi: 10.1016/j.tcb.2016.04.001. Epub 2016 Apr 25. |
relevant to this product |
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Western blot IHC ICC |
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