beta-Actin Antibody - #T0022

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Product: beta-Actin Antibody
Catalog: T0022
Description: Mouse monoclonal antibody to beta-Actin
Application: WB IHC IF/ICC ELISA
Reactivity: Human, Mouse, Rat, Pig, Zebrafish, Bovine, Sheep, Rabbit, Goat, Guinea pig, Dog, Monkey, Hamster, Duck, Chicken, Fish
Mol.Wt.: 43KD; 42kD(Calculated).
Uniprot: P60709
RRID: AB_2839417

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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 1:10000-1:320000, IHC 1:50-1:200, 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,Pig,Zebrafish,Bovine,Sheep,Rabbit,Goat,Guinea pig,Dog,Monkey,Hamster,Duck,Chicken,Fish
Clonality:
Monoclonal [F929]
Specificity:
beta-Actin Mouse Monoclonal antibody detects endogenous levels of total beta-Actin protein.
RRID:
AB_2839417
Cite Format: Affinity Biosciences Cat# T0022, RRID:AB_2839417.
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.Stable for 24 months from date of receipt. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

ACTB;Actin; cytoplasmic 1; Beta-actin; Beta actin; BRWS1; Actin; beta; Beta cytoskeletal actin; PS1TP5-binding protein 1; PS1TP5BP1;

Immunogens

Immunogen:

Full-length beta-Actin protein of human.

Uniprot:

P60709(ACTB_HUMAN) >>Visit HPA database.

Gene(ID):
ACTB(60)
Description:
beta-Actin is one of six different actin isoforms that have been identified. The actin molecules found in cells of various species and tissues tend to be very similar in their immunological and physical properties. Therefore, Antibodies against beta-Actin are useful as loading controls for Western Blotting. However it should be noted that levels of beta-Actin may not be stable in certain cells. For example, expression of beta-Actin in adipose tissue is very low and therefore it should not be used as loading control for these tissues.
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). Efficient Therapy of Inflammatory Bowel Disease (IBD) with Highly Specific and Durable Targeted Ta2C Modified with Chondroitin Sulfate (TACS). Advanced Materials (PubMed: 37224059) [IF=29.4]

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

Figure 7.TACS relieves inflammation and restores intestinal barrier function. B)WB analysis of COX-2 and iNOS proteins expression in RAW264.7 cells with different treatments.
2). A genetically encoded fluorescent biosensor for detecting itaconate with subcellular resolution in living macrophages. Nature Communications (PubMed: 36333306) [IF=16.6]
3). Prussian Blue Nanoparticles Stabilize SOD1 from Ubiquitination-Proteasome Degradation to Rescue Intervertebral Disc Degeneration. Advanced Science (PubMed: 35128840) [IF=15.1]

Application: WB    Species: Rat    Sample: NP cells

Figure 4 Intracellular molecular mechanism of PBNPs treated NPCs. A) Expression of SIRT1, SIRT3, SOD1, SOD2, GPX1, B‐actin protein from increasing time of H2O2 (0.6 × 10−3%) treated NP cells detected by WB. B) Expression of SIRT1, SIRT3, SOD1, SOD2, GPX1, GPX4, B‐actin protein from gradient concentrations of PBNPs (0.125–2 µg mL−1) treated NP cells detected by WB. C) Expression of SOD1, SOD2, SIRT1, SIRT3, GPX4, MMP3, MMP9, MMP13, COL2AL, B‐actin protein from increasing time of H2O2 (0.6×10−3%) and PBNPs (2 µg mL−1) treated NP cells detected by WB. D) Expression of Sod1, Sod2, Sod3, Gpx1, Gpx2, Gpx3, Sox9, Col1a1, Col2a1, Aggrecan, Pcna, p53, Sirt1, Sirt2, Sirt3, Adamts5, Mmp3, Mmp13, Ifnb1 mRNA from gradient concentrations of PBNPs (0.5, 1, 2 µg mL−1) treated NP cells detected by PCR. Date showed as Fold Change (2‐ΔΔCT). E) Expression of NRF2 protein from increasing time of H2O2 (0.6 × 10−3%) and PBNPs (2 µg mL−1) treated NP cells detected by WB. F) Expression of SOD1, SOD2, SIRT1, GPX4, B‐actin protein from PBNPs (2 µg mL−1), CHX(50 × 10−9 m), MG132(10 × 10−6 m ), Chiq (25 × 10−9 m) treated NP cells detected by WB. G) Co‐IP assay of Flag‐SOD1, Myc‐UBB overexpressed 293T treated with MG132 and PBNPs. IB with Flag and Myc. The first line of WB records to control groups of 293T overexpressed plv‐C and Myc‐UBB treated with MG132. The experiments above were repeated three times.
4). Binding of cellular nucleolin with the viral core RNA G-quadruplex structure suppresses HCV replication. NUCLEIC ACIDS RESEARCH (PubMed: 30462330) [IF=14.9]

Application: WB    Species: human    Sample: hepatoma cell lines

(B) G4 pull-down and Western blot. The fourth lane represents cell lysates directly used for western blot. β-actin was used as an internal control.
5). Breaking the vicious loop between inflammation, oxidative stress and coagulation, a novel anti-thrombus insight of nattokinase by inhibiting LPS-induced inflammation and oxidative stress. Redox Biology (PubMed: 32193146) [IF=11.4]

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

6). Translocator protein 18 kDa regulates retinal neuron apoptosis and pyroptosis in glaucoma. Redox Biology (PubMed: 37120931) [IF=11.4]

Application: WB    Species: Mouse    Sample:

Fig. 6. Ier2 functioned in the ceRNET during ph-IOP induced retinal damage a. Overexpression of miR-1839 and silencing of TSPO can increase the protective effect of Ier2 knockdown on RGCs by further inhibiting ph-IOP-induced cell loss in the GCL, and antagonizing miR-1839 eliminated the retinal protective effect caused by Ier2 knockdown (n = 3 independent experiments), scale bar = 50 μm; b. The number of RBPMS-positive cells can be further increased by the overexpression of miR-1839, and silencing TSPO further increased cell counts while antagonizing miR-1839 promoted the loss of RBPMS-positive cells (n = 3 independent experiments), scale bar = 100 μm; c. Overexpression of miR-1839 and silencing TSPO could further reduce the number of microglia-positive cells, while antagonizing miR-1839 increased the number of microglia-positive cells (n = 3 independent experiments), scale bar = 50 μm; d. As compared with the ph-IOP group, the overexpression of miR-1839 and silencing of TSPO both protected RGCs from pyroptosis, and antagonizing miR-1839 exacerbated ph-IOP-induced pyroptosis (n = 3 independent experiments); e. NLRP3 mRNA expression levels are regulated by Ier2/miR-1839/TSPO.; f. ROS contents can be reduced by the overexpression of miR-1839 and the silencing of TSPO, and antagonizing miR-1839 will further increase ph-IOP-induced retinal ROS accumulation (n = 3 independent experiments); f-k. Ier2/miR-1839/TSPO regulates NLRP3/cleaved -caspase1/N-GSDMD (pyroptosis-related) and cleaved-caspase3 (apoptosis-related) protein expression levels (n = 3 independent experiments); l-m: Ier2/miR-1839/TSPO can regulate the expression levels of IL-18 and IL-1β in the retina (n = 3 independent experiments). ph-IOP: pathologically high IOP; dIer2: Ier2 knockdown; Ago: miR-1839 agomir; Antago: miR-1839 antagomir; dTSPO: silence TSPO; GCL: ganglion cell layer; IPL: inner plexiform layer; INL: inner nuclear layer; OPL: outer plexiform layer; ONL: outer nuclear layer. The comparison was based on ANOVA analysis. P-values of
7). Pathologically high intraocular pressure induces mitochondrial dysfunction through Drp1 and leads to retinal ganglion cell PANoptosis in glaucoma. Redox Biology (PubMed: 36989574) [IF=11.4]
8). Combination therapy of PKCζ and COX-2 inhibitors synergistically suppress melanoma metastasis. Journal of Experimental & Clinical Cancer Research (PubMed: 28865485) [IF=11.3]

Application: WB    Species: mouse    Sample: B16F10

Fig. 5 The expression of p-PKCζ, p-cofilin and COX-2 after combined treatment of J-4 and Celecoxib. (a) Western blotting images of p-cofilin and COX-2 in B16-F10 cells with various treatments for 24 h. (b) Western blotting images of p-cofilin and COX-2 in A375 cells with various treatments for 24 h. (c) Relative mRNA level of PKCζ and COX-2 determined via RT-PCR. (d) The expression of EMT markers, E-Cadherin and Vimentin, and MMP-2/MMP-9 was affected in B16-F10 and A375 cells after various treatments for 24 h. J-4: 25 μM; Celecoxib: 25 μM. * P < 0.05; ** P < 0.01
9). The interaction of YBX1 with G3BP1 promotes renal cell carcinoma cell metastasis via YBX1/G3BP1-SPP1- NF-κB signaling axis. JOURNAL OF EXPERIMENTAL & CLINICAL CANCER RESEARCH (PubMed: 31481087) [IF=11.3]

Application: WB    Species: human    Sample: A498

(b). β-actin was used as loading control, respectively. ACHN and A498 cells stably expressing shYBX1 were subjected to Migration
10). Water-extracted Lonicera japonica polysaccharide attenuates allergic rhinitis by regulating NLRP3-IL-17 signaling axis. Carbohydrate Polymers (PubMed: 36184153) [IF=11.2]
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