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Mouse Anti-ACTC1 Recombinant Antibody (V2-179583) (CBMAB-A0901-YC)

Provided herein is a Mouse monoclonal antibody against Human Actin, Alpha, Cardiac Muscle 1. The antibody can be used for immunoassay techniques, such as ELISA, IHC-Fr, WB.
See all ACTC1 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Goat, Rabbit, Rat, Pig, Zebrafish, Cattle
Clone
V2-179583
Antibody Isotype
IgG1
Application
ELISA, IHC-Fr, WB

Basic Information

Immunogen
Derived by fusion of NS0 Mouse myeloma cells with spleen cells from a BALB/c Mouse immunized with a peptide comprising the N-terminal nonapeptide of Actin Alpha 1 Cardiac Muscle with an acetylated N-terminus (Ac-DDEETTALVC-COOH) coupled to keyhole limpet hemocyanin through the cysteine residue.
Specificity
Human, Goat, Rabbit, Rat, Pig, Zebrafish, Cattle
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
ELISA1:100-1:2,000
IF(ICC)1:10-1:500
IHC1:100-1:1,000
WB1:1,000-1:5,000

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

Format
Liquid
Buffer
PBS, pH7.2
Preservative
0.09% sodium azide
Concentration
1 mg/ml
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, Cardiac Muscle 1
Introduction
Actins are highly conserved proteins that are involved in various types of cell motility. 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 four others. The prot
Entrez Gene ID
Human70
Goat102170606
Rabbit100340339
Mouse11464
Rat29275
Pig100152267
Zebrafish407658
UniProt ID
HumanP68032
GoatA0A452DQU2
RabbitG1STB6
MouseP68033
RatP68035
PigB6VNT8
ZebrafishB6VNT8
Alternative Names
Actin, Alpha, Cardiac Muscle 1; ACTC; Actin, Alpha Cardiac Muscle 1; Actin, Alpha, Cardiac Muscle; Alpha-Cardiac Actin; CMD1R; CMH11; LVNC4; ASD5;
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
Actin filament-based movement
Actin filament organization
Actin-myosin filament sliding
Actomyosin structure organization
Cardiac muscle contraction
Cardiac muscle tissue morphogenesis
Cardiac myofibril assembly
Heart contraction
Mesenchyme migration
Muscle filament sliding
Positive regulation of gene expression
Response to drug
Response to ethanol
Skeletal muscle thin filament assembly
Cellular Location
Cytoskeleton
Involvement in disease
Cardiomyopathy, dilated 1R (CMD1R): A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Cardiomyopathy, familial hypertrophic 11 (CMH11): A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
Atrial septal defect 5 (ASD5): A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria.
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.

Suresh, R., Picard, D., Lo, R., Beaulieu, J., Remke, M., & Diaz, R. J. (2021). Expression of cell type incongruent alpha-cardiac actin 1 subunit in medulloblastoma reveals a novel mechanism for cancer cell survival and control of migration. Neuro-Oncology Advances.

Frank, D., Rangrez, A. Y., Friedrich, C., Dittmann, S., Stallmeyer, B., Yadav, P., ... & Schulze-Bahr, E. (2019). Cardiac α-actin (ACTC1) gene mutation causes atrial-septal defects associated with late-onset dilated cardiomyopathy. Circulation: Genomic and Precision Medicine, 12(8), e002491.

Rangrez, A. Y., Kilian, L., Stiebeling, K., Dittmann, S., Schulze-Bahr, E., Frey, N., & Frank, D. (2019). A cardiac α-actin (ACTC1) p. Gly247Asp mutation inhibits SRF-signaling in vitro in neonatal rat cardiomyocytes. Biochemical and biophysical research communications, 518(3), 500-505.

Wanibuchi, M., Ohtaki, S., Ookawa, S., Kataoka-Sasaki, Y., Sasaki, M., Oka, S., ... & Honmou, O. (2018). Actin, alpha, cardiac muscle 1 (ACTC1) knockdown inhibits the migration of glioblastoma cells in vitro. Journal of the neurological sciences, 392, 117-121.

Smith, J. G., Owen, T., Bhagwan, J. R., Mosqueira, D., Scott, E., Mannhardt, I., ... & Denning, C. (2018). Isogenic pairs of hiPSC-CMs with hypertrophic cardiomyopathy/LVNC-associated ACTC1 E99K mutation unveil differential functional deficits. Stem cell reports, 11(5), 1226-1243.

Cheung, A. S., de Rooy, C., Levinger, I., Rana, K., Clarke, M. V., How, J. M., ... & Grossmann, M. (2017). Actin alpha cardiac muscle 1 gene expression is upregulated in the skeletal muscle of men undergoing androgen deprivation therapy for prostate cancer. The Journal of steroid biochemistry and molecular biology, 174, 56-64.

Boutilier, J. K., Taylor, R. L., Ram, R., McNamara, E., Nguyen, Q., Goullée, H., ... & Nowak, K. J. (2017). Variable cardiac α-actin (Actc1) expression in early adult skeletal muscle correlates with promoter methylation. Biochimica et Biophysica Acta (BBA)-Gene Regulatory Mechanisms, 1860(10), 1025-1036.

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For research use only. Not intended for any clinical use.

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