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AB235730

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

Key facts

Purity

>85% SDS-PAGE

Expression system

Mammalian

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P60709

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF","proteinLength":"Full Length","predictedMolecularWeight":"41.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":375,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Mammalian","accessionNumber":"P60709","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Beta actin also known as beta cytoplasmic actin plays a central role in cell structure and motility. It is part of the actin protein family and is widely expressed in eukaryotic cells. The molecular weight of beta actin is approximately 42 kDa. It contributes to the formation of the cytoskeleton and participates in various cellular processes including movement and stability. Actin is abundant in all cell types providing structural integrity and flexibility.
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.

Beta actin has links to cancers and muscular dystrophies. Aberrations in actin dynamics can result in tumor cell migration and metastasis making it a component of interest in cancer research. Additionally mutations or dysregulation in actin-associated proteins may contribute to muscular dystrophies affecting muscle function and strength. Beta actin's interactions with proteins like dystrophin involved in maintaining muscle integrity further highlight its relevance in both biological functions and disease contexts.

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

Product protocols

Target data

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).
See full target information ACTB

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