alpha SMA Antibody - #BF9212

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Product: alpha SMA Antibody
Catalog: BF9212
Description: Mouse monoclonal antibody to alpha SMA
Application: WB IF/ICC IP ELISA
Reactivity: Human, Mouse, Rat
Mol.Wt.: 42kDa; 42kD(Calculated).
Uniprot: P62736
RRID: AB_2839428

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 50ul $150 In stock
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 200ul $350 In stock
 1ml $1200 In stock

Lead Time: Same day delivery

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Related Downloads
MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Mouse
Application:
WB 1:1000-10000, IP 1:200, IF/ICC 1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Monoclonal [AFB7535]
Specificity:
The α Skeletal Muslce Actin mouse monoclonal antibody can recognize endogenous α Skeletal Muslce Actin proteins.
RRID:
AB_2839428
Cite Format: Affinity Biosciences Cat# BF9212, RRID:AB_2839428.
Conjugate:
Unconjugated.
Purification:
affinity purification.
Storage:
1mg/ml in PBS, pH 7.4. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

a actin; AAT6; ACTA_HUMAN; ACTA2; Actin alpha 2 smooth muscle aorta; Actin aortic smooth muscle; Actin; aortic smooth muscle; ACTSA; ACTVS; Alpha 2 actin; Alpha actin 2; Alpha cardiac actin; Alpha-actin-2; Cell growth inhibiting gene 46 protein; Cell growth-inhibiting gene 46 protein; GIG46; Growth inhibiting gene 46; MYMY5; Sarcomeric Actin;

Immunogens

Immunogen:

A Mouse monoclonal antibody is prepared by immunizing recombinant protein.

Uniprot:

P62736(ACTA_HUMAN) >>Visit HPA database.

Gene(ID):
ACTA2(59)
Description:
Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1 gene. Actin alpha 1 which is expressed in skeletal muscle is one of six different actin isoforms which have been identified. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus
Sequence:
MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF

PTMs - P62736 As Substrate

Site PTM Type Enzyme
E3 Acetylation
S35 Phosphorylation
K52 Acetylation
K52 Methylation
K52 Ubiquitination
S54 Phosphorylation
Y55 Phosphorylation
S62 Phosphorylation
K63 Acetylation
K63 Sumoylation
K63 Ubiquitination
T68 Phosphorylation
K70 Acetylation
K70 Methylation
K70 Ubiquitination
Y71 Phosphorylation
T79 Phosphorylation
K86 Acetylation
K86 Methylation
S91 Phosphorylation
Y93 Phosphorylation
R97 Methylation
K115 Acetylation
K115 Ubiquitination
T128 Phosphorylation
Y145 Phosphorylation
T151 Phosphorylation
S157 Phosphorylation
Y168 Phosphorylation
Y171 Phosphorylation
T188 Phosphorylation
Y190 Phosphorylation
K193 Acetylation
K193 Methylation
K193 Ubiquitination
T196 Phosphorylation
R198 Methylation
Y200 Phosphorylation
S201 Phosphorylation
T204 Phosphorylation
K215 Acetylation
K215 Ubiquitination
K217 Acetylation
K217 Methylation
C219 S-Nitrosylation
Y220 Phosphorylation
S235 Phosphorylation
S236 Phosphorylation
S237 Phosphorylation
K240 Ubiquitination
S241 Phosphorylation
Y242 Phosphorylation
T251 Phosphorylation
C259 S-Nitrosylation
T262 Phosphorylation
S267 Phosphorylation
T280 Phosphorylation
Y281 Phosphorylation
S283 Phosphorylation
C287 S-Nitrosylation
K293 Ubiquitination
Y296 Phosphorylation
T305 Phosphorylation
T306 Phosphorylation
Y308 Phosphorylation
K317 Acetylation
K317 Sumoylation
K317 Ubiquitination
T320 Phosphorylation
S325 Phosphorylation
T326 Phosphorylation
K328 Acetylation
K328 Methylation
K328 Sumoylation
K328 Ubiquitination
K330 Acetylation
K330 Sumoylation
K330 Ubiquitination
K338 Sumoylation
S350 Phosphorylation
Y364 Phosphorylation
S370 Phosphorylation
K375 Ubiquitination
C376 S-Nitrosylation

Research Backgrounds

Function:

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

PTMs:

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.

Subcellular Location:

Cytoplasm>Cytoskeleton.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

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 4 others.

Family&Domains:

Belongs to the actin family.

Research Fields

· Environmental Information Processing > Signal transduction > Apelin signaling pathway.   (View pathway)

· Organismal Systems > Circulatory system > Vascular smooth muscle contraction.   (View pathway)

· Organismal Systems > Endocrine system > Relaxin signaling pathway.

References

1). Injectable hydrogel with dual-sensitive behavior for targeted delivery of oncostatin M to improve cardiac restoration after myocardial infarction. Journal of Materials Chemistry B, 2022 (PubMed: 35997155) [IF=7.0]
2). Sequential targeting biomimetic nano platform for enhanced mild photothermal therapy and chemotherapy of tumor. Computational and structural biotechnology journal, 2023 (PubMed: 37181660) [IF=6.0]
3). Ellagic Acid Attenuates BLM-Induced Pulmonary Fibrosis via Inhibiting Wnt Signaling Pathway. Frontiers in Pharmacology, 2021 (PubMed: 33912053) [IF=5.6]

Application: IHC    Species: mice    Sample: lung tissue

FIGURE 6 Ellagic acid attenuates BLM-induced fibroblasts activation and ECM accumulation in vivo. The mice were treated with Ellagic acid (10 mg/kg, 20 mg/kg) from day 7–13 after administrating BLM (A) Immunohistochemistry was used to analyze the expression levels of α-SMA, Col1 and Fn (n = 3). Quantitative analysis was shown beside. Scale bars: 50 μm (B–C) The expression levels of α-SMA and Col1 were detected by immunofluorescence in lung sections. The analyses of mean gray value were shown beside. Scale bars: 50 μm (D) Lung homogenization was used to analysis the α-SMA, LC3-II/I and p-mTOR (S2248), mTOR expression levels by Western blot (n = 6). Densitometric analyses were shown beside. Data in (A,D) are means ± Standard Error of Mean, *p < 0.05, **p < 0.01, ***p < 0.001, and NS: nonsignificant (one-way ANOVA). β-tubulin was used as a loading control.

Application: WB    Species: mice    Sample: lung tissue

FIGURE 6 Ellagic acid attenuates BLM-induced fibroblasts activation and ECM accumulation in vivo. The mice were treated with Ellagic acid (10 mg/kg, 20 mg/kg) from day 7–13 after administrating BLM (A) Immunohistochemistry was used to analyze the expression levels of α-SMA, Col1 and Fn (n = 3). Quantitative analysis was shown beside. Scale bars: 50 μm (B–C) The expression levels of α-SMA and Col1 were detected by immunofluorescence in lung sections. The analyses of mean gray value were shown beside. Scale bars: 50 μm (D) Lung homogenization was used to analysis the α-SMA, LC3-II/I and p-mTOR (S2248), mTOR expression levels by Western blot (n = 6). Densitometric analyses were shown beside. Data in (A,D) are means ± Standard Error of Mean, *p < 0.05, **p < 0.01, ***p < 0.001, and NS: nonsignificant (one-way ANOVA). β-tubulin was used as a loading control.

Application: IF/ICC    Species: mouse    Sample: Lung

FIGURE 6 | (B–C) The expression levels of α-SMA and Col1 were detected by immunofluorescence in lung sections. The analyses of mean gray value were shown beside.
4). Regorafenib-Attenuated, Bleomycin-Induced Pulmonary Fibrosis by Inhibiting the TGF-β1 Signaling Pathway. International Journal of Molecular Sciences, 2021 (PubMed: 33671452) [IF=5.6]

Application: WB    Species: Mouse    Sample: Mouse lung fibroblast (Mlg) or NaCl-primary pulmonary fibroblast (PPF) cells

Figure 2. Regorafenib suppresses transforming growth factor (TGF)-β1-induced activation, extracellular matrix (ECM) accumulation, and the migration of pulmonary fibroblasts. (A,B) Mouse lung fibroblast (Mlg) or NaCl-primary pulmonary fibroblast (PPF) cells were exposed to TGF-β1(5 ng/mL) and/or regorafenib (RG) (2 µM, 4 µM) for 24 h to detect the expression levels of α-SMA and Col 1 by Western blotting. Densitometric analyses are shown; (C) Mlg cells were exposed to TGF-β1 (5 ng/mL) and/or RG (2 µM, 4 µM) for 24 h, and quantitative real-time PCR was used to detect the mRNA levels of α-SMA, Col 1a, and Fn; (D) RG (2 µM, 4 µM) was exposed to Mlg cells for 24 h, and the α-SMA expression level was detected by immunofluorescence. Relative pixels intensity is shown. Scale bars: 50 µm; (E) Mlg cells were treated with TGF- β1 and/or RG (2 µM, 4 µM) for 0, 12, 24, or 36 h. Distance analyses are shown below. Scale bars: 100 µm; (F) The PPF cells isolated from NaCl-treated and BLM-treated mice were incubated RG (2 µM, 4 µM) for a series of time points (0, 12, 24, 36 h). Distance analyses are shown below. Scale bars: 100 µm; Data in (A–F) are means ± standard error of mean (SEM), and β-tubulin was used as a loading control. ### p < 0.001, ** p < 0.01, *** p < 0.001 (one-way ANOVA), NS: not significant.

Application: IHC    Species: mice    Sample: lung tissue

Figure 1. Regorafenib attenuated bleomycin (BLM)-induced pulmonary fibrosis in mice. (A) Regorafenib (15 mg/kg, 30 mg/kg) and nintedanib (100 mg/kg) were given orally once a day from days 7–13 after BLM treatment, lungs were harvested at day 14, and body weight loss was measured every day; (B) Percentages of surviving mice were plotted from days 7–14 after bleomycin treatment; (C) Representative images of hematoxylin–eosin (H&E) and Masson staining of lung tissue sections. Scale bars: 50 µM; (D) Percentages of fibrotic area in lung tissues; (E) Hydroxyproline contents in right lung tissues; (F) Immunohistochemistry of lung sections was used to analyze the expression levels of α-smooth muscle actin (α-SMA), collagen 1 (Col 1), and fibronectin (Fn). Quantitative analysis is shown below. Scale bars: 50 µm; (G–L) Pulmonary function parameters, such as forced vital capacity (FVC), forced expiratory volume in 0.1 s (FEV0.1), forced expiratory volume in 0.3 s (FEV0.3), expiratory resistance (Re), inspiratory resistance (Ri), and dynamic compliance (Cydn). Data in (A,B) and (D–L) are means ± standard error of mean (SEM), n = 6; # p < 0.05, ## p < 0.01, ### p < 0.001, * p < 0.05, ** p < 0.01, *** p < 0.001 (one-way ANOVA), NS: not significant.
5). Protective effect of remdesivir against pulmonary fibrosis in mice. Frontiers in Pharmacology, 2021 (PubMed: 34512328) [IF=5.6]

Application: WB    Species: Mice    Sample: lung tissues

FIGURE 5 Remdesivir attenuates TGF-β1-induced activation of lung fibroblasts. (A) NIH-3T3 cells were co-treated with TGF-β1 (5 ng ml−1) and Remdesivir (12.5, 25, 50 μM) for 24 h. mRNA levels of α-SMA, Fibronectin and Collagen I were tested by RT-PCR in NIH-3T3 cells (B) NIH-3T3 cells were co-treated with TGF-β1 (5 ng ml−1) and Remdesivir (12.5, 25, 50 μM) for 24 h. α-SMA and Fibronectin were assessed using western blot, GAPDH was used as the internal control (C) PPF cells were co-treated with TGF-β1 (5 ng ml−1) and Remdesivir (12.5, 25, 50 μM) for 24 h. α-SMA and Fibronectin were assessed using western blot, β-tubulin was used as the internal control (D) Immunofluorescence staining of α-SMA were performed on NIH-3T3 cells treated with/without TGF-β1 (5 ng ml−1) and/or Remdesivir (12.5, 25, 50 μM) for 24 h. Data was noted as the means ± SD, n = 3. *p < 0.05, **p < 0.01, ***p < 0.001, **** p < 0.0001.
6). Natural product mogrol attenuates bleomycin-induced pulmonary fibrosis development through promoting AMPK activation. Journal of Functional Foods, 2021 [IF=5.6]

Application: WB    Species: Mouse    Sample: MLE-12 cells

Fig. 1. . Regulation of natural compound mogrol on the EMT in TGF-β1 mediated alveolar epithelial cells MLE-12. Mouse MLE-12 cells were treated with or without TGF-β1 (10 ng/ml) in the absence or presence of mogrol for 48 h. (a) Chemical structure of mogrol. (b) Effects of mogrol (0.1–100 μM) on the proliferation MLE-12 cells were measured by MTT assays. (c-f) Protein expressions of α-SMA, Col I, Vimentin and E-cadherin in MLE-12 cells treated with/without TGF-β1 were detected by western blotting analysis. Data are presented as mean ± SD (n = 5). *p < 0.05, **p < 0.01, ***p < 0.001. NS, non-significant.
7). Activation of AMPK signalling by Metformin: Implication an important molecular mechanism for protecting against mice silicosis via inhibited endothelial cell-to-mesenchymal transition by regulating oxidative stress and apoptosis. International Immunopharmacology, 2023 (PubMed: 37192555) [IF=5.6]
8). Exosome‑encapsulated miR‑26a attenuates aldosterone‑induced tubulointerstitial fibrosis by inhibiting the CTGF/SMAD3 signaling pathway. International Journal of Molecular Medicine, 2023 (PubMed: 36524378) [IF=5.4]

Application: WB    Species: Mice    Sample: kidneys

Figure 1 miR-26a expression is downregulated in the kidneys of ALD-induced mice. (A) Representative images of Masson's trichrome stained kidney tissues of mice in the sham and ALD groups. Scale bar, 50 µm. (B) RT-qPCR analysis of miR-26a expression levels in the kidney tissues of mice in the sham and ALD groups; U6 was used for normalization. (C) RT-qPCR analysis of collagen I, α-SMA and LCN2 mRNA expression levels in the kidney tissues of mice from the sham and ALD groups; β-actin was used for normalization. (D) Representative western blotting images and semi-quantitative analysis of E-cadherin, collagen I, α-SMA, CTGF and LCN2 protein expression levels in the kidney tissue of mice in the sham and ALD groups. (E) Immunohistochemical analysis of E-cadherin (green), α-SMA (red) and fibronectin (green) in the kidney tissue of mice in the sham and ALD groups; DAPI (blue) was used to stain the nuclei. Scale bar, 50 µm. Data are presented as the mean ± SD; n=5 mice/group; *P<0.05 vs. sham. α-SMA, α-smooth muscle actin2; CTGF, connective tissue growth factor; LCN2, lipocalin; RT-qPCR, reverse transcription-quantitative PCR.

Application: IF/ICC    Species: Mice    Sample: kidneys

Figure 1 miR-26a expression is downregulated in the kidneys of ALD-induced mice. (A) Representative images of Masson's trichrome stained kidney tissues of mice in the sham and ALD groups. Scale bar, 50 µm. (B) RT-qPCR analysis of miR-26a expression levels in the kidney tissues of mice in the sham and ALD groups; U6 was used for normalization. (C) RT-qPCR analysis of collagen I, α-SMA and LCN2 mRNA expression levels in the kidney tissues of mice from the sham and ALD groups; β-actin was used for normalization. (D) Representative western blotting images and semi-quantitative analysis of E-cadherin, collagen I, α-SMA, CTGF and LCN2 protein expression levels in the kidney tissue of mice in the sham and ALD groups. (E) Immunohistochemical analysis of E-cadherin (green), α-SMA (red) and fibronectin (green) in the kidney tissue of mice in the sham and ALD groups; DAPI (blue) was used to stain the nuclei. Scale bar, 50 µm. Data are presented as the mean ± SD; n=5 mice/group; *P<0.05 vs. sham. α-SMA, α-smooth muscle actin2; CTGF, connective tissue growth factor; LCN2, lipocalin; RT-qPCR, reverse transcription-quantitative PCR.
9). Cancer-associated fibroblasts-derived FMO2 as a biomarker of macrophage infiltration and prognosis in epithelial ovarian cancer. Gynecologic Oncology, 2022 (PubMed: 36114029) [IF=4.7]
10). Efficacy of anti-programmed cell death protein 1 monoclonal antibody combined with bevacizumab and/or Pseudomonas aeruginosa injection in transplanted tumor of mouse forestomach carcinoma cell gastric cancer in mice and its mechanism in regulating tumor immune microenvironment. Clinical and experimental immunology, 2023 (PubMed: 37392409) [IF=4.6]
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