ACTB;Actin; cytoplasmic 1; Beta-actin; Beta actin; BRWS1; Actin; beta; Beta cytoskeletal actin; PS1TP5-binding protein 1; PS1TP5BP1;
WB: 1:3000-1:10000, IHC: 1:200, IF/ICC: 1:200
*The optimal dilutions should be determined by the end user.
Human, Mouse, Rat, Pig, Zebrafish, Bovine, Sheep, Rabbit, Goat, Guinea pig, Dog, Monkey, Hamster, Chicken, Fish
Mouse
Monoclonal
F929
Affinity-chromatography.
beta-Actin Mouse Monoclonal antibody detects endogenous levels of total beta-Actin protein.
AB_2839417
Please cite this product as: Affinity Biosciences Cat# T0022, RRID:AB_2839417.
Liquid
1mg/ml
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 24 months from date of receipt.
Full-length beta-Actin protein of human.
>>Visit The Human Protein Atlas
ACTB
Observed Mol.Wt.: 43kD.
Predicted Mol.Wt.: 42kDa(Calculated)..
Cytoplasm > cytoskeleton. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
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.
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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.
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.
Cytoplasm>Cytoskeleton. Nucleus.
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
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.
Belongs to the actin family.
· 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 > Tight junction.(View pathway)
· Cellular Processes > Cellular community - eukaryotes > Adherens 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: Viral > Influenza A.
· Human Diseases > Infectious diseases: Bacterial > Shigellosis.
· Human Diseases > Infectious diseases: Bacterial > Vibrio cholerae infection.
· Human Diseases > Infectious diseases: Bacterial > Salmonella infection.
· Human Diseases > Cardiovascular diseases > Viral myocarditis.
· Human Diseases > Cardiovascular diseases > Hypertrophic cardiomyopathy (HCM).
· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.
· Human Diseases > Cardiovascular diseases > Dilated cardiomyopathy (DCM).
· Human Diseases > Cardiovascular diseases > Arrhythmogenic right ventricular cardiomyopathy (ARVC).
· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.(View pathway)
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Organismal Systems > Endocrine system > Oxytocin signaling pathway.
· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.(View pathway)
· Organismal Systems > Digestive system > Gastric acid secretion.
· Organismal Systems > Immune system > Leukocyte transendothelial migration.(View pathway)
· Organismal Systems > Immune system > Platelet activation.(View pathway)
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.
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
Application: WB Species:mouse; Sample:Not available
Figure 7. FCN-A promoted the M1 polarization of BMDMs through a TLR4/MyD88-dependent pathway in vitro. (a) The protein expressions of the purified GST-FCN-A and GST were determined by SDS-PAGE. (b) The extracted membrane proteins from RAW264.7 cells were incubated with the purified GST-FCN-A or GST proteins. Co-IP analysis of the interaction between TLR4 of macrophage and GST-FCN-A was performed by using anti-TLR4. Rabbit IgG was used as a negative control in co-IP. (c, e) BMDMs, isolated from WT, TLR4-/- or MyD88-/- mice, were stimulated with FCN-A (10g/mL) for 24 h, then the expressions of iNOS and Arg-1 from BMDMs were examined by Western blot analysis. (d, f) The levels of pro-inflammatory cytokines IL-1in cell lysates, and secreted IL-6, TNF- were detected by ELISA. (g, h) Western blot analysis of p-IRAK1, p-p65, p-ERK1/2, and p-JNK in the BMDM lysates of TLR4-/-, MyD88-/- or WT after stimulation with FCN-A for 0-45 min. In d and f, values are mean ± [SEM] from three independent experiments.
Application: WB Species:human; Sample:Not available
Fig. 3 Knockdown of Rictor inhibits melanoma cells proliferation and blocked the cell cycle in G2/M phase. (A) Cell viability of A375 and MUM-2B cells after Rictor knockdown evaluated by MTT assay (*P < 0.05, **P < 0.01). (B) Cell cycle of A375 and MUM-2B cells after Rictor knockdown examined by FCM. (C) The expression of p-CDK2 and p-Histone H3 induced by knockdown of Rictor.
Application: WB Species:rat; Sample:rat hippocampus
Fig. 7 a Western blot analysis demonstrates levels of TNF-a and IL-1b in the hippocampus of rats at 12, 24, and 48 h following TBI or sham operation (n = 5/group). b Densitometry of the TNF-a and IL-1b band correlated to the b-actin band. The bars represent the mean ± SE (n = 5/group). The results demonstrated that a significant increase of TNF-a and IL-1b expression in the TBI group (*p\0.01 vs. sham group), and treatment with TAK-242 significantly downregulated the level of TNF-a and IL-1b protein expression at 12, 24, and 48 h following TBI (# p\0.05 vs. TBI group). TNF-a, tumor necrosis factor-a; IL-1b, interleukin-1b
Application: WB Species:human; Sample:BGC-823 cell
Figure 4. Overexpression of FOXQ1 in BGC-823 cell line resulted in EMT and increased invasiveness. To determine whether FOXQ1 promotes the EMT to increase cell invasion, the expression levels of FOXQ1, E-cadherin and vimentin were detected via western blotting and qRT-PCR. The results revealed that FOXQ1 could increase EMT, which decreased E-cadherin expression and increased vimentin expression (* P
Application: WB Species:human; Sample:Not available
Figure 2. Co-culture with TAMs induces EMT in GC cells. (A) The EMT markers in MKN45 and MKN74 cells were analyzed using western blotting after being co-cultured with THP-1 cells. (B and C) The EMT markers in MKN45 and MKN74 cells were analyzed by RT-PCR after being co-cultured with THP-1 cells; * P
Application: WB Species:rat; Sample:Not available
FIGURE 4 Effects of BPA on the hypothalamic GnRH protein expression in female rats on PND35. (a) Depicted representative bands of GnRH in different groups.
Application: WB Species:human; Sample:human gastric cancer
Fig. 6. MiR-1271 inhibited gastric cancer cell migration, invasion, and epithelial-mesenchymal transition. (A) Overexpression of miR-1271 could inhibit MGC-803 cell migration and invasion, whereas its downregulation in SGC-7901 cells increased the cell migration and invasion processes. (B) Western blots showed that overexpression of miR-1271 could upregulate E-cadherin and downregulate N-cadherin and vimentin expression in MGC-803 cells, whereas its downregulation had the opposite effect in SGC- 7901 cells. Three independent experiments were conducted. *P < 0.05, **P < 0.01.
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
T0022-BP
(Blocking peptide available as T0022-BP)
$350/1mg.
Tips: For phospho antibody, we provide phospho peptide(0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.
Site | PTM Type | Enzyme | Source |
---|---|---|---|
M1 | Acetylation | Uniprot | |
D2 | Acetylation | Uniprot | |
S14 | Phosphorylation | Uniprot | |
C17 | S-Nitrosylation | Uniprot | |
K18 | Methylation | Uniprot | |
K18 | Ubiquitination | Uniprot | |
S33 | Phosphorylation | Uniprot | |
K50 | Acetylation | Uniprot | |
K50 | Methylation | Uniprot | |
K50 | Ubiquitination | Uniprot | |
S52 | Phosphorylation | Uniprot | |
Y53 | Phosphorylation | Uniprot | |
S60 | Phosphorylation | Uniprot | |
K61 | Acetylation | Uniprot | |
K61 | Sumoylation | Uniprot | |
K61 | Ubiquitination | Uniprot | |
T66 | Phosphorylation | Uniprot | |
K68 | Methylation | Uniprot | |
K68 | Sumoylation | Uniprot | |
Y69 | Phosphorylation | Uniprot | |
H73 | Methylation | Uniprot | |
T77 | Phosphorylation | Uniprot | |
K84 | Methylation | Uniprot | |
K84 | Sumoylation | Uniprot | |
K84 | Ubiquitination | Uniprot | |
T89 | Phosphorylation | Uniprot | |
Y91 | Phosphorylation | Uniprot | |
T106 | Phosphorylation | Uniprot | |
K113 | Acetylation | Uniprot | |
K113 | Sumoylation | Uniprot | |
K113 | Ubiquitination | Uniprot | |
T120 | Phosphorylation | Uniprot | |
Y143 | Phosphorylation | Uniprot | |
S155 | Phosphorylation | Uniprot | |
T160 | Phosphorylation | Uniprot | |
T162 | Phosphorylation | Uniprot | |
Y166 | Phosphorylation | Uniprot | |
Y169 | Phosphorylation | Uniprot | |
T186 | Phosphorylation | Uniprot | |
Y188 | Phosphorylation | Uniprot | |
K191 | Acetylation | Uniprot | |
K191 | Methylation | Uniprot | |
K191 | Ubiquitination | Uniprot | |
T194 | Phosphorylation | Uniprot | |
Y198 | Phosphorylation | Uniprot | |
S199 | Phosphorylation | Uniprot | |
T201 | Phosphorylation | Uniprot | |
T202 | Phosphorylation | Uniprot | |
T203 | Phosphorylation | Uniprot | |
K213 | Acetylation | Uniprot | |
K213 | Ubiquitination | Uniprot | |
K215 | Ubiquitination | Uniprot | |
C217 | S-Nitrosylation | Uniprot | |
Y218 | Phosphorylation | Uniprot | |
T229 | Phosphorylation | Uniprot | |
S233 | Phosphorylation | Uniprot | |
S235 | Phosphorylation | Uniprot | |
K238 | Ubiquitination | Uniprot | |
S239 | Phosphorylation | Uniprot | |
Y240 | Phosphorylation | Uniprot | |
T249 | Phosphorylation | Uniprot | |
C257 | S-Nitrosylation | Uniprot | |
S265 | Phosphorylation | Uniprot | |
S271 | Phosphorylation | Uniprot | |
C272 | S-Nitrosylation | Uniprot | |
K284 | Sumoylation | Uniprot | |
K284 | Ubiquitination | Uniprot | |
C285 | S-Nitrosylation | Uniprot | |
K291 | Sumoylation | Uniprot | |
K291 | Ubiquitination | Uniprot | |
Y294 | Phosphorylation | Uniprot | |
T297 | Phosphorylation | Uniprot | |
S300 | Phosphorylation | Uniprot | |
T303 | Phosphorylation | Uniprot | |
T304 | Phosphorylation | Uniprot | |
Y306 | Phosphorylation | Uniprot | |
K315 | Acetylation | Uniprot | |
K315 | Sumoylation | Uniprot | |
K315 | Ubiquitination | Uniprot | |
T318 | Phosphorylation | Uniprot | |
S323 | Phosphorylation | Uniprot | |
T324 | Phosphorylation | Uniprot | |
K326 | Acetylation | Uniprot | |
K326 | Methylation | Uniprot | |
K326 | Sumoylation | Uniprot | |
K326 | Ubiquitination | Uniprot | |
K328 | Acetylation | Uniprot | |
K328 | Sumoylation | Uniprot | |
K328 | Ubiquitination | Uniprot | |
K336 | Sumoylation | Uniprot | |
S348 | Phosphorylation | Uniprot | |
K359 | Ubiquitination | Uniprot | |
Y362 | Phosphorylation | Uniprot | |
S365 | Phosphorylation | Uniprot | |
S368 | Phosphorylation | Uniprot | |
K373 | Ubiquitination | Uniprot | |
C374 | S-Nitrosylation | Uniprot |