Product: alpha-SMA Antibody
Catalog: AF1032
Description: Rabbit polyclonal antibody to alpha-SMA
Application: WB IHC IF/ICC IP
Reactivity: Human, Mouse, Rat, Bovine
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 45 KD; 42kD(Calculated).
Uniprot: P62736
RRID: AB_2835329

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:1000, IHC 1:50-1:500, IF/ICC: 1:200, IP 1:100
*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,Bovine
Prediction:
Pig(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%)
Clonality:
Polyclonal
Specificity:
alpha-SMA Antibody detects endogenous levels of total alpha-SMA.
RRID:
AB_2835329
Cite Format: Affinity Biosciences Cat# AF1032, RRID:AB_2835329.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Stable for 15 months from date of receipt. 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:
Uniprot:
Gene(ID):
Description:
Defects in ACTA2 are the cause of aortic aneurysm familial thoracic type 6 (AAT6) [MIM:611788]. AATs are characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. They are 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.
Sequence:
MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Chicken
100
Rabbit
100
Xenopus
75
Zebrafish
63
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

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). Yi M et al. The construction, expression, and enhanced anti-tumor activity of YM101: a bispecific antibody simultaneously targeting TGF-β and PD-L1. Journal of Hematology & Oncology 2021 Feb 16;14(1):27 (PubMed: 33593403) [IF=28.5]

Application: IHC    Species: Human    Sample:

Fig. 10 Immunohistochemical staining to evaluate the activity of carcinoma-associated fibroblast, the status of mediated epithelial-mesenchymal transition of cancer cells, as well as the proliferation and apoptosis of cancer cells. a H&E staining. b Anti-α-SMA staining. c Picrosirius red staining. d Anti-E-cadherin staining. e Anti-Vimentin staining. f Anti-Ki-67 staining. g Anti-PCNA staining. h Anti-cleaved-Caspase 3. For quantitative analysis, the integral optical density (IOD) of values the IHC stainings were calculated. *p 

2). Li X et al. Upregulation of BCL-2 by acridone derivative through gene promoter i-motif for alleviating liver damage of NAFLD/NASH. NUCLEIC ACIDS RESEARCH 2020 Jul 25;gkaa615. (PubMed: 32710621) [IF=14.9]

Application: WB    Species: mouse    Sample: liver

Figure 7. Effect of A22 on ameliorating apoptosis, ER stress, inflammation, metabolic syndrome, and fibrogenesis in HF diet-fed mice. (A) Effect of A22 on BCL-2 gene transcription. (B) Effect of A22 on BAX gene transcription. (C) Effect of A22 on expressions of apoptosis-related proteins in liver. The extracted proteins from the liver were immunoblotted with specific antibodies, and quantified based on the loading control of ACTIN. (D) Effect of A22 on ER stress. The UPR proteins (IRE-1, PERK, elF-2 and CHOP) were analyzed by using western Blot. (E) Effect of A22 on expressions of inflammatory factors. (F) Effect of A22 on expressions of fibrogenic proteins.

3). Cheng X et al. pH‐Triggered Size‐Tunable Silver Nanoparticles: Targeted Aggregation for Effective Bacterial Infection Therapy. Small 2022 Jun;18(22):e2200915. (PubMed: 35499191) [IF=13.3]

4). A novel UV-curable extravascular stent to prevent restenosis of venous grafts. Composites Part B: Engineering [IF=13.1]

5). Tu J et al. Nintedanib enhances the efficacy of PD-L1 blockade by upregulating MHC-I and PD-L1 expression in tumor cells. Theranostics 2022 Jan 1;12(2):747-766. (PubMed: 34976211) [IF=12.4]

Application: IF/ICC    Species: Mice    Sample: tumor tissue

Figure 2 Image analysis of tumor tissue stained with different stains. (A) Images of tumor tissue stained with hematoxylin-eosin (HE), Ki67, and TUNEL. Quantitative analysis of the (B) Ki67 positive area and (C) TUNEL positive area. (D) Immunofluorescence (IF) images of CD31 and α-SMA in LLC tumor tissue. The quantitative analysis of the (E) CD31+ vessel area and (F) α-SMA+/ CD31+ vessel area. The green scale bar is 100 µm, the white and black scale bar is 200 µm, and the yellow scale bar is 1000 µm.

6). Sun J et al. The long non-coding RNA PFI protects against pulmonary fibrosis by interacting with splicing regulator SRSF1. CELL DEATH AND DIFFERENTIATION 2021 Oct;28(10):2916-2930. (PubMed: 33981019) [IF=12.4]

Application: WB    Species: Mice    Sample: fibrogenesis

Fig. 1 Knockdown of lncRNA PFI results in fibrogenesis of MLFs. A qRT-PCR analysis showed six upregulated and two downregulated lncRNAs in BLM-treated mice compared to saline-treated mice. B LncRNA NONMMUT060091, which we named lncRNA pulmonary fibrosis inhibitor (lncRNA PFI), was dramatically reduced in TGF-β1-treated mouse lung fibroblasts (MLFs). C, D qRT-PCR assays of relative lncRNA PFI, collagen 1α1, collagen 3α1, Fn1, CTGF, and ACTA2 expression in MLFs treated with SSi-PFI or SSi-NC. E Western blots demonstrated markedly increased expression of fibrosis-related proteins Fn1, Collagen I, and α-SMA in SSi-PFI transfected MLFs. F Immunofluorescence staining of α-SMA suggested acceleration of the fibroblast-myofibroblast transition after silencing of lncRNA PFI; bar = 20 μm; n = 5 independent experiments. G EdU fluorescent staining indicated that lncRNA PFI inhibition promoted the proliferation of MLFs; bar = 50 μm. H A wound healing assay showed that the suppression of lncRNA PFI facilitated MLFs migration; bar = 200 μm. *P < 0.05; **P < 0.01. MLFs mouse lung fibroblasts, SSi-PFI PFI smart silencer, SSi-NC negative control smart silencer.

Application: IF/ICC    Species: Mice    Sample: fibrogenesis

Fig. 1 Knockdown of lncRNA PFI results in fibrogenesis of MLFs. A qRT-PCR analysis showed six upregulated and two downregulated lncRNAs in BLM-treated mice compared to saline-treated mice. B LncRNA NONMMUT060091, which we named lncRNA pulmonary fibrosis inhibitor (lncRNA PFI), was dramatically reduced in TGF-β1-treated mouse lung fibroblasts (MLFs). C, D qRT-PCR assays of relative lncRNA PFI, collagen 1α1, collagen 3α1, Fn1, CTGF, and ACTA2 expression in MLFs treated with SSi-PFI or SSi-NC. E Western blots demonstrated markedly increased expression of fibrosis-related proteins Fn1, Collagen I, and α-SMA in SSi-PFI transfected MLFs. F Immunofluorescence staining of α-SMA suggested acceleration of the fibroblast-myofibroblast transition after silencing of lncRNA PFI; bar = 20 μm; n = 5 independent experiments. G EdU fluorescent staining indicated that lncRNA PFI inhibition promoted the proliferation of MLFs; bar = 50 μm. H A wound healing assay showed that the suppression of lncRNA PFI facilitated MLFs migration; bar = 200 μm. *P < 0.05; **P < 0.01. MLFs mouse lung fibroblasts, SSi-PFI PFI smart silencer, SSi-NC negative control smart silencer.

7). Li et al. Irinotecan/scFv co-loaded liposomes coaction on tumor cells and CAFs for enhanced colorectal cancer therapy. Journal of Nanobiotechnology 2021 Dec 14;19(1):421. (PubMed: 34906155) [IF=10.2]

Application: WB    Species: Mice    Sample:

Fig. 2 Analysis of cell proliferation and migration. Viability of a CT-26 cells and b co-cultured cells (ratio of CT-26 to NIH 3T3 cells was 1:2) after incubation with different formulations at different concentrations for 48 h. c Migration experiment after different formulations treatment for 24 h. Scale bar, 100 μm. d Cell migration percentage. e Western blot analysis of FAP and α-SMA expression levels and f quantification data. **P < 0.01, ***P < 0.001

8). Gong L et al. CD44‐targeting Drug Delivery System of Exosomes Loading Forsythiaside A Combats Liver Fibrosis via Regulating NLRP3‐mediated Pyroptosis. Advanced Healthcare Materials 2023 Jan 5;e2202228. (PubMed: 36603210) [IF=10.0]

9). Cuiping Qi et al. Co-Delivery of Curcumin and Capsaicin by Dual-Targeting Liposomes for Inhibition of aHSC-Induced Drug Resistance and Metastasis. ACS Applied Materials & Interfaces 2021 Apr 14;13(14):16019-16035. (PubMed: 33819006) [IF=9.5]

Application: IHC    Species: Mice    Sample: tumor tissue

Figure 8. In vivo antitumor effect in the H22+m-HSC tumor-bearing mice. (a) Treatment schedule. (b) Body weight. (c) Photographs of tumors. (d) Tumor growth curve. (e) Tumor inhibition rates. (f) H&E staining images. (g) Masson’s staining assay. (h) Immunohistochemistry assay of αSMA protein. (i) Microvessel density assay. Data are given as mean ± SD (n = 4). *P < 0.05, **P < 0.01, ***P < 0.001.

10). Huang D et al. Crosstalk between PML and p53 in response to TGF-β1: A new mechanism of cardiac fibroblast activation. International Journal of Biological Sciences 2023 Jan 22;19(3):994-1006. (PubMed: 36778116) [IF=9.2]

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