beta Actin Antibody - AF7018
-
- Product Name
- beta Actin Antibody
-
- Catalog No.
- AF7018
-
- Source
- Rabbit
-
- Application
- WB,IHC,IF/ICC
-
- Reactivity:
- Human, Mouse, Rat, Pig, Zebrafish, Dog, Monkey, Fish
-
- Prediction:
- Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Chicken(100%), Xenopus(100%)
-
- UniProt
-
- Mol.Wt.
- 43kDa
-
- Concentration
- 1mg/ml
Product Information
Alternative Names:Expand▼
ACTB; Actin; cytoplasmic 1; Beta-actin; Beta actin; BRWS1; β actin;b actin; Actin beta; Beta cytoskeletal actin; PS1TP5-binding protein 1; PS1TP5BP1;
Applications:
WB 1:3000-1:20000, IHC 1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
Reactivity:
Human, Mouse, Rat, Pig, Zebrafish, Dog, Monkey, Fish
Predicted Reactivity:
Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Chicken(100%), Xenopus(100%)
Source:
Rabbit
Clonality:
Polyclonal
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Specificity:
Beta actin antibody detects endogenous levels of total Beta actin.
Format:
Liquid
Concentration:
1mg/ml
Storage Condition and Buffer:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
Immunogen Information
Immunogen:
A synthesized peptide derived from human Beta actin.
Uniprot:
>>Visit The Human Protein Atlas
Gene id:
Molecular Weight:
Observed Mol.Wt.: 43kDa.
Predicted Mol.Wt.: 42kDa.
Subcellular Location:
Cytoplasm > cytoskeleton. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Description:
Actin, a ubiquitous eukaryotic protein, is the major component of the cytoskeleton. At least six isoforms are known in mammals. Nonmuscle β- and γ-actin, also known as cytoplasmic actin, are predominantly expressed in nonmuscle cells, controlling cell structure and motility.
Sequence:
10 20 30 40 50
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG
160 170 180 190 200
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF
210 220 230 240 250
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI
260 270 280 290 300
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Background
Function:
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Post-translational Modifications:
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 (By similarity).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.(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 (PubMed:19015515). 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 (PubMed:26228148).
Subcellular Location:
Cytoskeleton;
Subunit Structure:
Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). 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 DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (PubMed:11687588).
Similarity:
Belongs to the actin family.
Research Fields
Research Fields:
· Cellular Processes > Transport and catabolism > Phagosome.(View pathway)
· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.(View pathway)
· Cellular Processes > Cellular community - eukaryotes > Tight junction.(View pathway)
· Cellular Processes > Cell growth and death > Apoptosis.(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 > Hippo signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Rap1 signaling pathway.(View pathway)
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.(View pathway)
· Human Diseases > Cardiovascular diseases > Arrhythmogenic right ventricular cardiomyopathy (ARVC).
· Human Diseases > Cardiovascular diseases > Dilated cardiomyopathy (DCM).
· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.
· Human Diseases > Cardiovascular diseases > Hypertrophic cardiomyopathy (HCM).
· Human Diseases > Cardiovascular diseases > Viral myocarditis.
· Human Diseases > Infectious diseases: Bacterial > Salmonella infection.
· Human Diseases > Infectious diseases: Bacterial > Vibrio cholerae infection.
· Human Diseases > Infectious diseases: Bacterial > Shigellosis.
· Human Diseases > Infectious diseases: Viral > Influenza A.
· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.
· Organismal Systems > Immune system > Platelet activation.(View pathway)
· Organismal Systems > Immune system > Leukocyte transendothelial migration.(View pathway)
· Organismal Systems > Digestive system > Gastric acid secretion.
· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.(View pathway)
· Organismal Systems > Endocrine system > Oxytocin signaling pathway.
Protocols & Troubleshooting
Reference Citations:
Application: WB Species:mouse; Sample:Not available
Figure 5. Down regulation of Tcf12 accelerate and potentiate bone repair in vivo. (A‐B) Quantification of Alp activity at day 14 in U‐0126 and LDN‐193189 treated shTcf12 and scrambled groups.
Application: WB Species:human; Sample:Not available
FIGURE 3 miR-506 down-regulated MDR1/P-gp expression in HCT116-OxR. A, The mRNA level of MDR1 was decreased after transfection with the miR-506 mimic of the relative chemoresistant genes as demonstrated by qRT-PCR. B, The protein level of MDR1 was decreased after transfection with the miR-506 mimic of the relative chemoresistant proteins as demonstrated by Western blot. C, Expression of P-gp detected by immunofluorescence staining.HCT116-OxR-miR-506 cells showed low levels of fluorescent staining of P-gp, whereas maximal staining of P-gp was observed in HCT116-OxR cells, readily distinguished from background. Zoom: 200×. *P<.05)
Application: WB Species:human; Sample:breast cancer
Application: WB Species:human; Sample:Not available
Fig. 2. Effects of CsA on emodin-induced apoptosis. The cells were treated with emodin for 48 h in the presence or absence of CsA (5mM), then assays were performed. (A) Analysis of apoptosis by nuclear condensation. The Hoechst 33342 staining showed typical apoptotic morphology changes after emodin treatment. The images were acquired by inverted fluorescence microscopy. (B) Analysis of apoptosis by Annexin V/PI double-staining assay. (C) Determination of Cyto-C level in mitochondria and cytosol by western blots. b-actin and VDAC1 were used as internal control.
Application: WB Species:mouse; Sample:Not available
Fig. 6. Role of MRP1 on lead-induced mitochondrial toxicity. (A) Expression of MRP1 in the mitochondria of Sertoli cells with various concentrations of lead acetate. (B) Expression of MRP1 in the mitochondria of Sertoli cells with continuous time exposure to lead acetate (20mM). (C) Expression of MRP1 in the mitochondria of the TM4 cells and MRP1()TM4 cells. (D) Transport activity of MRP1 in the mitochondria of the TM4 cells and MRP1()TM4 cells. (E) The accumulation of lead in the mitochondria of TM4 cells and MRP1()TM4 cells. Data represent mean SD of at least three independent experiments (*P < 0.05, **P < 0.01 vs. control).
Application: WB Species:human; Sample:Not available
Figure 2. Crocetin induces cell cycle arrest and influences PCNA, p21, and p53 expression in RPE cells. (A) Cells were harvested after treatment with or without 50 and 100 μM crocetin for 24 h. DNA was stained with PI for flow cytometric analysis. The number of cells in G1 phase was significantly increased in the crocetin-treated group compared with that in the untreated group. (B) Cells were treated or without with 50, 100 and 200 μM crocetin for 48 h. Western blot analysis was used to evaluated the expression of PCNA, p21, p53 and the housekeeping protein β-actin. *P< 0.05 vs 0 μM crocetin, **P< 0.01 vs 0 μM crocetin. The data are presented as the mean ± S.D. (n = 3/group).
Application: WB Species:human; Sample:Not available
(C) miR-93-5p overexpression suppressed and increased E-cadherin and N-cadherin expression, respectively. The opposite result was observed in response to miR-93-5p downregulation.
Application: WB Species:Not available; Sample:Not available
Application: WB Species:human; Sample:Not available
Application: WB Species:Not available; Sample:Not available
Application: WB Species:human; Sample:Not available
Application: WB Species:rat; Sample:rat
LTG decreased Aβ1–42 and phosphorylated tau protein levels in the ipsilateral hippocampus of MCAO rats. (a) Immunoblotting photographs of Aβ1–42, Tau-5, and AT8. (b–d) Quantitative analysis of immunoreactivity of Aβ1–42 (b), Tau-5 (c), and AT8 (d). (e) Immunofluorescence of the hippocampal CA1 zone for AT8. Scale bar=50 μm. *Means sham versus another group, *P<0.05, **P< 0.01, ***P<0.001; † LTG 20 versus vehicle, † P<0.05, †††P<0.001; ‡ LTG 40 versus vehicle, ‡‡P< 0.01, ‡‡‡P
Application: WB Species:Not available; Sample:Not available
Application: WB Species:human; Sample:HGC27
Figure 4 CUL4A and NF-κB were overexpressed in GC tissues. Notes: (A) Representative images of gastric tumor tissues showing concordant positive staining of CUL4A and NF-κB in the same sample (200×). (B) Western blot analysis of CUL4A and NF-κB expressions in three paired primary GC and adjacent noncancerous tissue samples. These three patients were all diagnosed stage III. (C) CUL4A expression scores and NF-κB expression scores in 50 GC samples revealed that CUL4A expression positively correlated with NF-κB expression via correlation analysis
Submit Review
Catalog Number :
AF7018-BP
(Blocking peptide available as AF7018-BP)
Price/Size :
$200/1mg.
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).
Function :
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.
Format and storage :
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.
Precautions :
This product is for research use only. Not for use in diagnostic or therapeutic procedures.
P60709 as Substrate
| 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 |
