Recombinant Human beta Actin protein
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Recombinant Human beta Actin protein is a Human Full Length protein, in the 1 to 375 aa range, expressed in Mammalian, with >85%, suitable for SDS-PAGE.
View Alternative Names
Beta-actin, ACTB
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Beta actin contributes to the maintenance of cell shape and is an important player in cell division and muscle contraction. It forms part of a larger actin filaments network often associating with other proteins to form the actin cytoskeleton complex. This complex supports cellular processes such as signaling intracellular trafficking and positioning of organelles. The dynamic polymerization and depolymerization of actin filaments are critical for cellular functions.
Pathways
Beta actin functions in the regulation of important biological pathways such as the Rho/Rac/Cdc42 signaling pathway and the Wnt signaling pathway. These pathways are essential in numerous cellular activities including cell morphology and gene transcription. Beta actin closely interacts with proteins like myosin and tropomyosin which facilitate its role in muscle contraction and cell division and proteins such as Rac and Cdc42 which help govern cytoskeletal dynamics and cellular responses to extracellular stimuli.
Specifications
Form
Liquid
General info
Function
Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed : 25255767, 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). Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
Sequence similarities
Belongs to the actin family.
Post-translational modifications
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.. Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes (PubMed:23673617). Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (PubMed:23673617).. Methylated at His-73 by SETD3 (PubMed:30526847, PubMed:30626964, PubMed:30785395, PubMed:31388018). Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity).. Actin, cytoplasmic 1. N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP.. Actin, cytoplasmic 1, N-terminally processed. N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins (PubMed:29581253). In contrast, filament nucleation by the Arp2/3 complex is not affected (PubMed:29581253).. (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).
Subcellular localisation
Cytoskeleton
Target data
Product promise
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