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AB134555

Recombinant Human alpha smooth muscle Actin protein (His tag N-Terminus)

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(1 Publication)

Recombinant Human alpha smooth muscle Actin protein (His tag N-Terminus) is a Human Full Length protein, in the 3 to 377 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

ACTSA, ACTVS, GIG46, ACTA2, Alpha-actin-2, Cell growth-inhibiting gene 46 protein

1 Images
SDS-PAGE - Recombinant Human alpha smooth muscle Actin protein (His tag N-Terminus) (AB134555)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human alpha smooth muscle Actin protein (His tag N-Terminus) (AB134555)

15% SDS-PAGE analysis of 3 µg ab134555.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

P62736

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl

storage-buffer

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Reactivity data

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

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSHMEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF","proteinLength":"Full Length","predictedMolecularWeight":"44.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":377,"aminoAcidStart":3,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P62736","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

Alpha smooth muscle actin (α-SMA) also known as ACTA2 is an actin isoform with a specific role in the contractile function of smooth muscle cells. The molecular weight of α-SMA is approximately 42 kDa. This protein is expressed widely in vascular smooth muscle cells the peritoneal lining and myofibroblasts. It often serves as a marker for these cell types. The expression of α-SMA is critical for the mechanical attributes of cells contributing to the rigidity and contractility of tissues where it is present.
Biological function summary

Alpha smooth muscle actin aids in maintaining the structural integrity of tissues by forming part of the actin cytoskeleton an important element in cellular support. It exists in high concentration in stress fibers contributing to cellular movements and shape maintenance. These actions are essential in various dynamic cellular processes such as cell migration and adhesion. Alpha smooth muscle actin does not typically form complexes but it associates with other components of the actin cytoskeleton to ensure cell stability and function.

Pathways

Alpha smooth muscle actin functions significantly within the TGF-beta signaling pathway which influences cell proliferation differentiation and apoptosis. It interacts closely with proteins such as myosin to facilitate cellular contractility and motility. Additionally α-SMA plays a part in the RhoA/Rho kinase (ROCK) pathway connecting with regulators of actin filament organization. These pathways are essential for modulation of smooth muscle contraction and actin filament assembly contributing to vascular development and wound healing.

Alpha smooth muscle actin is importantly involved in fibrotic diseases and vascular diseases like arteriosclerosis. Increased expression of α-SMA is often observed in fibrotic tissues contributing to pathogenesis due to excessive extracellular matrix deposition. In the context of vascular disorders overexpression of α-SMA can lead to abnormal vascular remodeling often seen in diseases like hypertension. Interactions with proteins such as fibronectin and collagens facilitate these pathological changes highlighting the importance of α-SMA in disease development.
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Specifications

Form

Liquid

Additional notes

ab134555 is purified using conventional chromatography techniques.

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General info

Function

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Sequence similarities

Belongs to the actin family.

Post-translational modifications

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.. Methylated at His-75 by SETD3.. Actin, aortic smooth muscle, intermediate form. N-terminal cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP.. (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).

Subcellular localisation

Cytoskeleton

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Product protocols

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Target data

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
See full target information ACTA2
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

eLife 7: PubMed30260317

2018

α-actinin accounts for the bioactivity of actin preparations in inducing STAT target genes in .

Applications

Unspecified application

Species

Unspecified reactive species

Oliver Gordon,Conor M Henry,Naren Srinivasan,Susan Ahrens,Anna Franz,Safia Deddouche,Probir Chakravarty,David Phillips,Roger George,Svend Kjaer,David Frith,Ambrosius P Snijders,Rita S Valente,Carolina J Simoes da Silva,Luis Teixeira,Barry Thompson,Marc S Dionne,Will Wood,Caetano Reis e Sousa
View all publications
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