beta-Actin Antibody - #BF0198

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Product: beta-Actin Antibody
Catalog: BF0198
Description: Mouse monoclonal antibody to beta-Actin
Application: WB IF/ICC ELISA FACS
Reactivity: Human, Mouse, Rat, Monkey, Hamster
Mol.Wt.: 43KD; 42kD(Calculated).
Uniprot: P60709
RRID: AB_2833667

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

Product Info

Source:
Mouse
Application:
ELISA 1:10000, WB 1:500-1:2000, IF/ICC 1:200-1:1000, FCM 1:200-1:400
*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,Monkey,Hamster
Clonality:
Monoclonal [AFB1643]
Specificity:
beta-Actin antibody detects endogenous levels of total beta-Actin.
RRID:
AB_2833667
Cite Format: Affinity Biosciences Cat# BF0198, RRID:AB_2833667.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

A26C1A; A26C1B; ACTB; ACTB_HUMAN; Actin beta; Actin cytoplasmic 1; Actin, cytoplasmic 1, N-terminally processed; Actx; b actin; Beta cytoskeletal actin; Beta-actin; BRWS1; E430023M04Rik; MGC128179; PS1TP5 binding protein 1; PS1TP5BP1;

Immunogens

Immunogen:

Purified recombinant fragment of human beta-Actin expressed in E. Coli.

Uniprot:

P60709(ACTB_HUMAN) >>Visit HPA database.

Gene(ID):
ACTB(60)
Description:
Beta-actin (PS1TP5-binding protein 1), also known as ACTB, PS1TP5BP1. Entrez Protein NP_001092. It is one of six different actin proteins. Actin, a ubiquitous eukaryotic protein, is the major component of the cytoskeleton.Actins are highly conserved proteins that are involved in various types of cell motility, structure, and integrity. Actin is ubiquitously expressed in all eukaryotic cells. This actin is a major constituent of the contractile apparatus and one of the two nonmuscle cytoskeletal actins.
Sequence:
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

PTMs - P60709 As Substrate

Site PTM Type Enzyme
M1 Acetylation
D2 Acetylation
S14 Phosphorylation
C17 S-Nitrosylation
K18 Methylation
K18 Ubiquitination
S33 Phosphorylation
K50 Acetylation
K50 Methylation
K50 Ubiquitination
S52 Phosphorylation
Y53 Phosphorylation
S60 Phosphorylation
K61 Acetylation
K61 Sumoylation
K61 Ubiquitination
T66 Phosphorylation
K68 Methylation
K68 Sumoylation
Y69 Phosphorylation
H73 Methylation
T77 Phosphorylation
K84 Methylation
K84 Sumoylation
K84 Ubiquitination
T89 Phosphorylation
Y91 Phosphorylation
T106 Phosphorylation
K113 Acetylation
K113 Sumoylation
K113 Ubiquitination
T120 Phosphorylation
Y143 Phosphorylation
S155 Phosphorylation
T160 Phosphorylation
T162 Phosphorylation
Y166 Phosphorylation
Y169 Phosphorylation
T186 Phosphorylation
Y188 Phosphorylation
K191 Acetylation
K191 Methylation
K191 Ubiquitination
T194 Phosphorylation
Y198 Phosphorylation
S199 Phosphorylation
T201 Phosphorylation
T202 Phosphorylation
T203 Phosphorylation
K213 Acetylation
K213 Ubiquitination
K215 Ubiquitination
C217 S-Nitrosylation
Y218 Phosphorylation
T229 Phosphorylation
S233 Phosphorylation
S235 Phosphorylation
K238 Ubiquitination
S239 Phosphorylation
Y240 Phosphorylation
T249 Phosphorylation
C257 S-Nitrosylation
S265 Phosphorylation
S271 Phosphorylation
C272 S-Nitrosylation
K284 Sumoylation
K284 Ubiquitination
C285 S-Nitrosylation
K291 Sumoylation
K291 Ubiquitination
Y294 Phosphorylation
T297 Phosphorylation
S300 Phosphorylation
T303 Phosphorylation
T304 Phosphorylation
Y306 Phosphorylation
K315 Acetylation
K315 Sumoylation
K315 Ubiquitination
T318 Phosphorylation
S323 Phosphorylation
T324 Phosphorylation
K326 Acetylation
K326 Methylation
K326 Sumoylation
K326 Ubiquitination
K328 Acetylation
K328 Sumoylation
K328 Ubiquitination
K336 Sumoylation
S348 Phosphorylation
K359 Ubiquitination
Y362 Phosphorylation
S365 Phosphorylation
S368 Phosphorylation
K373 Ubiquitination
C374 S-Nitrosylation

Research Backgrounds

Function:

Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA.

PTMs:

ISGylated.

Oxidation of Met-44 and Met-47 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 promote actin repolymerization.

Monomethylation at Lys-84 (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-73 by SETD3. Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity).

N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins. In contrast, filament nucleation by the Arp2/3 complex is not affected.

(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-50 of one monomer and Glu-270 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. Nucleus.
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

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. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM. Interacts with TBC1D21 (By similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes. Interacts with FAM107A.

Family&Domains:

Belongs to the actin family.

Research Fields

· Cellular Processes > Transport and catabolism > Phagosome.   (View pathway)

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Adherens junction.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Tight junction.   (View pathway)

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Environmental Information Processing > Signal transduction > Rap1 signaling pathway.   (View pathway)

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

· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.

· Human Diseases > Infectious diseases: Bacterial > Vibrio cholerae infection.

· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.

· Human Diseases > Infectious diseases: Bacterial > Shigellosis.

· Human Diseases > Infectious diseases: Bacterial > Salmonella infection.

· Human Diseases > Infectious diseases: Viral > Influenza A.

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.   (View pathway)

· Human Diseases > Cardiovascular diseases > Hypertrophic cardiomyopathy (HCM).

· Human Diseases > Cardiovascular diseases > Arrhythmogenic right ventricular cardiomyopathy (ARVC).

· Human Diseases > Cardiovascular diseases > Dilated cardiomyopathy (DCM).

· Human Diseases > Cardiovascular diseases > Viral myocarditis.

· Organismal Systems > Immune system > Platelet activation.   (View pathway)

· Organismal Systems > Immune system > Leukocyte transendothelial migration.   (View pathway)

· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Oxytocin signaling pathway.

· Organismal Systems > Digestive system > Gastric acid secretion.

References

1). Crocetin Alleviates Ovariectomy-Induced Metabolic Dysfunction through Regulating Estrogen Receptor β. Journal of agricultural and food chemistry, 2021 (PubMed: 34851635) [IF=5.7]
2). JNK signaling pathway mediates acetaminophen-induced hepatotoxicity accompanied by changes of glutathione S-transferase A1 content and expression. Frontiers in Pharmacology, 2019 (PubMed: 31620005) [IF=5.6]

Application: WB    Species: mouse    Sample: liver

FIGURE 2 | Activation of JNK signaling pathway under different dosages of APAP.(E) Western blot analyses of total tissue lysate for p-ASK1, ASK1, p-MKK4, MKK4, and β-actin (loading control). Values represented as means ± SD, n = 3. *Represents statistical differences caused by APAP. #Represents statistical differences caused by SP600125 under 150 mg·kg−1 APAP;§Represents statistical differences caused by SP600125 under 175 mg·kg−1 APAP. 0.05 > P > 0.01 (*, #, §). P < 0.01 (**, §§).
3). Effect of (R)-salbutamol on the switch of phenotype and metabolic pattern in LPS-induced macrophage cells. JOURNAL OF CELLULAR AND MOLECULAR MEDICINE, 2020 (PubMed: 31680470) [IF=5.3]

Application: WB    Species: Mouse    Sample: RAW 264.7 cells

Figure 3 Effects of (R)‐salbutamol on LPS‐induced NO production and the expression of iNOS in RAW264.7 macrophages. A, Representative images of control cells, LPS‐induced cells, LPS‐induced cells pretreated with (R)‐salbutamol and LPS‐induced cells pretreated with ICI‐118551 labelled with the fluorescent NO indicator DAF‐FM DA (indicated by red arrows) for 30 min. Images were captured by a confocal microscope. B, Fluorescence quantification of NO was performed on digitalized images using ZEN 2011 Image Solution software (scale bars, 100 μm). C, Graph showing the content of NO2 − in the cell supernatants of control cells, LPS‐induced cells, LPS‐induced cells pretreated with (R)‐salbutamol and LPS‐induced cells pretreated with ICI‐118551 using Griess reagent. D,E, iNOS protein and mRNA expressions in control cells, LPS‐induced cells, LPS‐induced cells pretreated with (R)‐salbutamol and LPS‐induced cells pretreated with ICI‐118551 as quantified using Western blotting and qPCR. Data are presented as the mean ± SD. ** P < .01, * P < .05; ns, not significant

Application: WB    Species: Mice    Sample: RAW264.7 cells

Figure 3 Effects of (R)‐salbutamol on LPS‐induced NO production and the expression of iNOS in RAW264.7 macrophages. A, Representative images of control cells, LPS‐induced cells, LPS‐induced cells pretreated with (R)‐salbutamol and LPS‐induced cells pretreated with ICI‐118551 labelled with the fluorescent NO indicator DAF‐FM DA (indicated by red arrows) for 30 min. Images were captured by a confocal microscope. B, Fluorescence quantification of NO was performed on digitalized images using ZEN 2011 Image Solution software (scale bars, 100 μm). C, Graph showing the content of NO2 − in the cell supernatants of control cells, LPS‐induced cells, LPS‐induced cells pretreated with (R)‐salbutamol and LPS‐induced cells pretreated with ICI‐118551 using Griess reagent. D,E, iNOS protein and mRNA expressions in control cells, LPS‐induced cells, LPS‐induced cells pretreated with (R)‐salbutamol and LPS‐induced cells pretreated with ICI‐118551 as quantified using Western blotting and qPCR. Data are presented as the mean ± SD. ** P < .01, * P < .05; ns, not significant
4). Human colon carcinogenesis is associated with increased interleukin-17-driven inflammatory responses. Drug Design Development and Therapy, 2015 (PubMed: 25834404) [IF=4.7]

Application: WB    Species:    Sample:

5). Low miR-936-mediated upregulation of Pim-3 drives sorafenib resistance in liver cancer through ferroptosis inhibition by activating the ANKRD18A/Src/NRF2 pathway. Frontiers in oncology, 2024 (PubMed: 39507762) [IF=4.7]
6). Novel Anti-Enterovirus A71 Compounds Discovered by Repositioning Antivirals from the Open-Source MMV Pandemic Response Box. Pharmaceuticals (Basel, Switzerland), 2024 (PubMed: 38931452) [IF=4.6]
7). Bi-phasic effect of gelatin in myogenesis and skeletal muscle regeneration. Disease Models & Mechanisms, 2021 (PubMed: 34821368) [IF=4.0]

Application: WB    Species: Mouse    Sample:

Fig. 4.Linear and bell-shaped dose response of reactive oxygen species (ROS) and the antioxidant system to gelatin. (A,B) Flow cytometry analysis (A) and quantification (B) of cells stained with 2′,7′-dichlorodihydrofluorescein diacetate (DCFH-DA; DCF) (ROS indicator). Count (y-axis in A) indicates cell counts (n=3). (C) Production of specific ROS: O2−, ·OH and H2O2 (n=3). (D) Activities of antioxidases: superoxide dismutase (SOD), glutathione peroxidase (GSH-PX) and catalase (CAT) (n=3). (E,F) Western blots (E) and quantification (F) of NOX2 and NOX4 in the cells cultured on gelatin-coated dishes at 90% confluence (n=3). β-Actin is used as a loading control. (G) Quantification of MitoSOX+ cells obtained by flow cytometry (n=3). (H) Flow cytometry analysis of the cells treated with diphenyliodonium (DPI; 0.5 μM, NOX2 inhibitor) and rotenone (ROT; 10 μM, an inhibitor of mitochondrial respiratory complex I) (n=3). Significance was determined by unpaired two-tailed Student's t-test with Welch's correction (B-D,F-G) and one-way ANOVA with Tukey's post-hoc test (H).
8). Ginger Extract Decreases Susceptibility to Dextran Sulfate Sodium-Induced Colitis in Mice Following Early Antibiotic Exposure. Frontiers in Medicine, 2022 (PubMed: 35071260) [IF=3.9]

Application: WB    Species: Mouse    Sample:

Figure 3 Ginger improves the intestinal barrier function of mice with DSS-induced colitis exposed to AZT in early life. (A) TJ morphology (magnification, ×8000): (a) CTR group; (b) MOD group; (c) AZT group; and (d) GIN group. Arrows, TJ; arrow heads, desmosome. (B) Representative images of immunofluorescence of ZO-1 in colon sections. (C) Western blot analysis of claudin-1 and ZO-1 expression in colon tissue. (D) and (E) Relative levels of claudin-1 and ZO-1 (n = 4). ***p < 0.01 vs. MOD group; ###p < 0.01 vs. AZT group.
9). Secretory Carrier Membrane Protein 3 Interacts with 3A Viral Protein of Enterovirus and Participates in Viral Replication. Microbiology spectrum, 2021 (PubMed: 34378951) [IF=3.7]

Application: WB    Species: Human    Sample:

FIG 3 Effects of SCAMP3 knockdown or knockout on EV-A71 replication. (A) Effect of SCAMP3 knockdown on EV-A71/4643 RNA levels. SF268 cells were transfected with NC siRNA or siRNA against SCAMP3. Cells were mock infected or infected with EV-A71/4643 at an MOI of 10 2 days after transfection. Total RNA was extracted and viral RNA levels were determined by quantitative RT-qPCR. (B) Effect of SCAMP3 knockdown on EV-A71/4643 viral 3D, 3CD, and P3 protein levels. SF268 cells were transfected with NC siRNA or siRNA against SCAMP3. Cells were mock infected or infected with EV-A71/4643 at an MOI of 10 2 days after transfection. Total cell lysates were examined by Western blotting. (C) Effect of SCAMP3 knockdown on EV-A71/4643 viral growth. SF268 cells were transfected with NC siRNA or siRNA against SCAMP3. Cells were mock infected or infected with EV-A71 at an MOI of 10 2 days after transfection. Viruses were harvested at different time points postinfection and assayed by plaque formation with RD cells. (D) Effect of SCAMP3 knockdown on EV-A71-3A4-FLAG RNA levels. RD cells were transfected with NC siRNA or siRNA against SCAMP3. Cells were mock infected or infected with EV-A71-3A4-FLAG at an MOI of 20 2 days after transfection. Total RNA was extracted and viral RNA levels were determined by RT-qPCR. (E) Effect of SCAMP3 knockdown on EV-A71-3A4-FLAG viral 3D protein levels. RD cells were transfected with NC siRNA or siRNA against SCAMP3. Cells were mock infected or infected with EV-A71-3A4-FLAG at an MOI of 20 2 days after transfection. Total cell lysates were examined by Western blotting. (F) Effect of SCAMP3 knockdown on EV-A71-3A4-FLAG viral growth. RD cells were transfected with NC siRNA or siRNA against SCAMP3. Cells were mock infected or infected with EV-A71-3A4-FLAG at an MOI of 20 2 days after transfection. Viruses were harvested at different time points postinfection and assayed by plaque formation with RD cells. (G) Effect of SCAMP3 knockout on EV-A71 RNA levels. Scramble or SCAMP3 KO RD cells were mock infected or infected with EV-A71-3A4-FLAG at an MOI of 20. Total RNA was extracted and viral RNA levels were determined by RT-qPCR. (H) Effect of SCAMP3 knockout on EV-A71-3A4-FLAG viral 3D, 3CD, and P3 protein levels. Scramble or SCAMP3 KO RD Cells were mock infected or infected with EV-A71-3A4-FLAG at an MOI of 20. Total cell lysates were examined by Western blotting. (I) Effect of SCAMP3 knockout on EV-A71-3A4-FLAG viral growth. Scramble or SCAMP3 KO RD Cells were mock infected or infected with EV-A71-3A4-FLAG at an MOI of 20. Viruses were harvested at different time points postinfection and assayed by plaque formation with RD cells.
10). Qi-dan-di-huang decoction alleviates diabetic nephropathy by inhibiting the NF-kappaB pathway. Frontiers in Bioscience-Landmark, 2019 (PubMed: 31136992) [IF=3.3]
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