Product: pan Actin Antibody
Catalog: AF0115
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 45kD; 42kD(Calculated).
Uniprot: P60709 | Q9BYX7 | P63261
RRID: AB_2833265

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Product Info

Source:
Rabbit
Application:
WB: 1:500-1:3000, IHC: 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
Actin-pan antibody detects endogenous levels of total Actin-pan.
RRID:
AB_2833265
Cite Format: Affinity Biosciences Cat# AF0115, RRID:AB_2833265.
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. 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; ACT; ACTBL3; FKSG30; POTE ankyrin domain family member K pseudogene; POTE2delta; POTEK; ACT; ACTB; ACTG; ACTG_HUMAN; actg1; Actin; Actin, cytoplasmic 2; Actin, gamma 1; Actin, gamma 1 propeptide; Actin, gamma; BRWS2; cytoplasmic 2; Cytoskeletal gamma actin; Deafness, autosomal dominant 20; Deafness, autosomal dominant 26; DFNA20; DFNA26; epididymis luminal protein 176; Gamma-actin; HEL-176; N-terminally processed;

Immunogens

Immunogen:

A synthesized peptide derived from human Actin-pan.

Uniprot:
Gene(ID):
Expression:
Q9BYX7 ACTBM_HUMAN:

Expressed in some hepatocellular carcinomas.

Description:
ACT, Actin, cytoplasmic 1
Sequence:
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

MDDDTAVLVIDNGSGMCKAGFAGDDAPQAVFPSIVGRPRHQGMMEGMHQKESYVGKEAQSKRGMLTLKYPMEHGIITNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGFTHTVPIYEGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTTAEQEIVRDIKEKLCYVALDSEQEMAMAASSSSVEKSYELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHKTTFNSIVKSDVDIRKDLYTNTVLSGGTTMYPGIAHRMQKEITALAPSIMKIKIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

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
Xenopus
100
Chicken
100
Rabbit
100
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P60709/Q9BYX7/P63261 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
Site PTM Type Enzyme
M1 Acetylation
E2 Acetylation
S14 Phosphorylation
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
Y69 Phosphorylation
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
Y218 Phosphorylation
T229 Phosphorylation
S233 Phosphorylation
S235 Phosphorylation
K238 Ubiquitination
S239 Phosphorylation
Y240 Phosphorylation
T249 Phosphorylation
S265 Phosphorylation
S271 Phosphorylation
K284 Ubiquitination
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

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.

PTMs:

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.

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
Tissue Specificity:

Expressed in some hepatocellular carcinomas.

Subunit Structure:

Interacts with PFN1 and PFDN1. Does not interact with PFN2.

Family&Domains:

Belongs to the actin family.

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-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.

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.

Methylated at His-73 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-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.

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. Interacts with TWF1, CAPZB, cofilin and profilin.

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). Li Y et al. Interleukin 17A deficiency alleviates fluoride-induced testicular injury by inhibiting the immune response and apoptosis. Chemosphere 2021 Jan;263:128178. (PubMed: 33297146) [IF=5.778]

2). Zhang S et al. Hyperforin Ameliorates Imiquimod-Induced Psoriasis-Like Murine Skin Inflammation by Modulating IL-17A–Producing γδ T Cells. Front Immunol 2021 May 5;12:635076. (PubMed: 34025642) [IF=5.085]

Application: WB    Species: Mice    Sample: γδ T Cells

Figure 8 Hyperforin inhibits phosphorylation of MAPK and STAT3 pathway components in in vitro cultured γδ T cells. (A) Representative images of Western blot. (B–I) quantification of the Western blot data by densitometric analysis and normalization to GAPDH (n = 3 independent experiments). **P < 0.01 vs model group.

3). Li H et al. MicroRNA-181a regulates epithelial-mesenchymal transition by targeting PTEN in drug-resistant lung adenocarcinoma cells. Int J Oncol 2015 Oct;47(4):1379-92 (PubMed: 26323677) [IF=3.899]

Application: WB    Species: human    Sample: A549 cells

Figure 3. A549/DDP and A549/PTX cells showed molecular and morphological changes that were consistent with EMT. (A) microscopy at x200 magnification was used to assess cell morphology. The A549 cells (parental cells) had an epithelioid, rounded cobblestone appearance and there was limited formation of pseudopodia. A549/PTX and A549/DDP cells exhibited a spindle-shaped morphology and an increased formation of pseudopodia, indicating a loss of cell polarity. (B) E-cadherin, β-catenin, vimentin, MMP-2 and MMP-9 which are EMT-related proteins, were assessed in terms of expression levels. EMT-related transcription factors (Snail, Slug, Twist and ZEB1) were measured in A549/PTX and A549/DDP cells using western blot analysis. (C) The expression changes were confirmed at the mRNA level by qRT-PCR. Expression was standardized to the expression of GAPDH and normalized to 1.0 in the parental cells (compared with the parental A549 cells, means ± SEM, n=3, * P<0.05)

Application: WB    Species: human    Sample: A549, A549/PTX or A549/DDP cells

Figure 9.| miR-181a directly targets PTEN by binding to its 3'UTR. (D) Western blots of PTEN are shown for A549, A549/PTX or A549/DDP cells that were non-transfected (blank) or that were transfected with negative control or miR-181a mimic/inhibitor. β-actin was also tested as a loading control. Shown are results that are representative of three independent experiments.

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