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Mouse Anti-ACTA2 Recombinant Antibody (V2-3360) (CBMAB-0077-CN)


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Summary

Host Animal
Mouse
Specificity
Dog, Chicken, Human, Monkey, Mouse, Shark
Clone
V2-3360
Antibody Isotype
IgM
Application
IHC, WB

Basic Information

Immunogen
Dorsal aortae
Specificity
Dog, Chicken, Human, Monkey, Mouse, Shark
Antibody Isotype
IgM
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:5,000-1:50,000
IHC1:1,000-1:2,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4, 0.5% BSA, 50% Glycerol
Preservative
0.02% sodium azide
Concentration
Batch dependent
Purity
>95%, as determined by SDS-PAGE analysis
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Actin, Alpha 2, Smooth Muscle, Aorta
Introduction
Alpha-actin-2 also known as actin, aortic smooth muscle or alpha smooth muscle actin (α-SMA, SMactin, alpha-SM-actin, ASMA) is a protein that in humans is encoded by the ACTA2 gene located on 10q22-q24. Alpha-smooth muscle actin (α-SMA) is commonly used as a marker of myofibroblast formation (Nagamoto et al., 2000).
Entrez Gene ID
Human59
Mouse11475
Chicken423787
Monkey100427024
Dog477587
Shark103180779
UniProt ID
HumanP62736
MouseP62737
ChickenP08023
MonkeyA0A0D9R387
DogF2Z4N0
SharkA0A4W3JU30
Alternative Names
0610041G09Rik; Actvs; SMAalpha; SMalphaA; a-SMA; alphaSMA
Function
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Biological Process
Glomerular mesangial cell development
Mesenchyme migration
Muscle contraction
Positive regulation of gene expression
Positive regulation of transcription, DNA-templated
Regulation of blood pressure
Response to virus
Vascular associated smooth muscle contraction
Cellular Location
Cytoskeleton
Involvement in disease
Aortic aneurysm, familial thoracic 6 (AAT6): A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.
Moyamoya disease 5 (MYMY5): A progressive cerebral angiopathy characterized by bilateral intracranial carotid artery stenosis and telangiectatic vessels in the region of the basal ganglia. The abnormal vessels resemble a 'puff of smoke' (moyamoya) on cerebral angiogram. Affected individuals can develop transient ischemic attacks and/or cerebral infarction, and rupture of the collateral vessels can cause intracranial hemorrhage. Hemiplegia of sudden onset and epileptic seizures constitute the prevailing presentation in childhood, while subarachnoid bleeding occurs more frequently in adults.
Multisystemic smooth muscle dysfunction syndrome (MSMDS): A syndrome characterized by dysfunction of smooth muscle cells throughout the body, leading to aortic and cerebrovascular disease, fixed dilated pupils, hypotonic bladder, malrotation, and hypoperistalsis of the gut and pulmonary hypertension.
PTM
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.
(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. 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.
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For research use only. Not intended for any clinical use.

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