A comprehensive review of beta actin antibodies as a Western blot internal control, with detailed discussion about one of most cited anti-beta actin clones: AC-15.
This is a review about beta actin antibodies (mainly as an internal loading control for Western blot), based on 156 published articles as of April 27, 2015 in randomly selected publications that Labome has surveyed systematically. Labome is continuously curating antibodies cited in formal publications. There are numerous publications using beta actin antibodies; our systematic and random sampling ensures that our results and conclusions are representative. This review aims to facilitate Labome visitors in locating the best-suited beta actin antibodies. Beta actin antibodies from different suppliers are linked below or can be searched here. The article also addresses some of commonly asked questions about beta actin antibodies.
Beta actin is one of the most commonly used loading controls for Western blot, in addition to tubulin and GAPDH.
The actin family of proteins are involved in muscle contraction and cytoskeleton structure. Beta and gamma forms are the only two non-muscle members. They play important rules in basic cellular processes, and are expressed in all cell types. Their sequences are highly conserved across species. Beta actin proteins are identical in human, mouse, and chicken.
Beta-actin antibody is the most commonly used loading control for western blot (see Labome's dedicated discussion on loading control for western blot). Table 1 lists the major providers of anti-beta actin antibodies among the publications Labome has surveyed.
|Santa Cruz Biotechnology||25|
The most cited anti-beta actin antibody clone is AC-15. It is cited in 11 publications among a total of 16 publications that indicate a clone or catalog number. Majority of publications do not indicate any clone number or catalog number. The clone AC-15 was used in Western blot in order to study wild type Cas, CasY253F, or Cas118423 , oogenic processes , apoptosis , Barrett's metaplasia , NF-kappaB signaling , retinal axon development , the role of sFLT-1 in the maintenance of the avascular photoreceptor layer in mouse models , a novel phosphoinositide-binding protein in modulating tight junctions and cell migration , rational drug design , synaptic plasticity  and the role for miR-196a in brown adipogenesis .
AC-15 clone was characterized and reported by Dr. J. Victor Small's lab at Institute for molecular biology, Austrian Academy of Sciences in their 1994 publications [13, 14]. AC-15 belongs to subclass IgG1, and was raised in mice against the N-terminal synthetic peptide of beta actin, with the sequence of AcD-D-D-I-A-A-L-V-I-D-N-G-S-G-K coupled to keyhole limpet hemocyanin. The clone specifically targets the beta isoform, with no cross reactivity against the other 5 isoforms of actin family. This clone is available from most antibody suppliers.
- Dr. Mario Gimona, then a Ph.D. student in Dr. Small lab has kindly provided the following account of history about the clone AC-15 to this article.
"While conducting experiments in 1993 at the Weizmann Institute of Science in Rehovot, Israel, I was invited to visit the facilities of BIOMAKOR, a company focusing on the development of monoclonal antibodies. Dr. Harry Langbeheim and Dr. Zeev Lando of BIOMAKOR instructed me on their latest developments that included isoform specific actin antibodies (at that time excellent probes for muscle actins and pan-actin Abs were available, but a beta-isoform specific probe was lacking). I was given the chance to take some of the putative beta actin specific probes (AC 15 and AC 74) back to Salzburg to test the Ab in our then lab in Salzburg.
With the help of Prof. Small and Dr. Alison North in Salzburg, and together with our collaborator, the actin isoform expert Prof. Joel Vandekerckhove from the University of Ghent, Belgium, we characterized the Ab by light and electron microscopy, as well as 1D and 2D Western Blotting (on whole cell lysates and on isoform specific peptides).
The probe demonstrated excellent specificity and worked well in all techniques and fixation methods used.
Dr. Langebheim, Dr. Lando and BIOMAKOR generously granted us the publication of 2 initial papers in 1994 and provided us with a generous supply of the AC-15 Ab for many years.
To my knowledge the company BIOMAKOR later on went to become part of SIGMA. "
Due to the prevalence of anti-actin antibodies in Western blot as a loading control and the prevalence of Western blot analysis in the overall body of literature, this beta-actin clone is likely the mosted cited antibody clone among all antibody clones in literature.
It must be noted that beta-actin is not an appropriate Western blot loading control in some circumstances. At a higher total protein loading level, beta-actin specific antibodies may not be able to detect the differences of protein loading levels . This is likely due to that beta actin is one of the dominant cellular proteins. This problem may not be alleviated by diluting anybody working solution or shortening the incubation time .
In addition, beta actin expression might change during growth and differentiation, or in disease states , or in different tissues and in different portions of same sample tissues . It is important to evaluate the consistency of beta actin expression over, for example, the total protein, among different samples.
Some of the commonly asked questions about beta actin antibody are addressed below.
There are a number of reasons. The first one to check is whether the anti-beta actin antibody is effective. One way to accomplish that is to reduce the dilution of the anti-beta actin antibody, and check to see whether there is still any band at all, and/or try to use anti-beta actin antibodies from high quality suppliers. The second thing to check is whether the anti-beta actin anybody is suitable for Western blot; some of the anti-actin antibodies are good for immunocytochemistry or immunohistochemistry, but not for Western blot. The third thing to check is whether the proteins are transferred evenly from the gel to the membrane. This can be checked through Ponseau S staining. The fourth thing to check is whether beta actin is expressed in the sample tissue or cells; this should happen very rarely, since beta actin is one of most important housekeeping genes for all cell types. In addition, it should be examined whether beta actin is preferentially degraded (an unlikely event). Another thing to be checked is whether the secondary antibody matches is suitable for the anti-beta actin antibody.
This is not advisable. The best approach is to detect the target protein first, then use western blot stripping buffer to remove the target protein antibody and the secondary antibody, and then to incubate with an anti-beta actin antibody. The reason is that it is difficult to adjust the incubation and developing parameters for two different antibodies and it is also difficult to prevent cross-reactivity among different antibodies.
The easy way to find the best diltion is to check any information sheet that usually comes with the product. Another approach is to contact the antibody supplier; the supplier usually has optimized the dilution. Regardless, if the suggested dilution does not work, different dilutions should be tested to find the optimal one.
Multiple experimental procedures may affect this. It could be that the loading solution becomes more sticky, or the transfer is uneven.
Yes. The internal control not only ensures sample loading, but also checks the transfer, incubation, and signal development.
Beta actin can still be used as an internal control. After the detection of the target protein, the blot should be completely stripped and checked for any signal before incubation with a beta actin antibody. Alternatively, another protein can be used as an internal control, such as tubulin or GAPDH.
No. The nucleus may contain some actin, but its level is dynamic and it should not serve as a control. See Labome's detailed discussion on different loading controls for nulear sample controls.
There are several reasons: 1) Secondary antibody may not be very specific; 2) The loading buffer is not effective; 3) The beta actin antibody is not specific; 4) Beta actin is degraded.
A detailed breakdown of the literature analyzed by Labome citing beta-actin antibodies is provided here. It is organized according to the suppliers. Whenever possible, the clonality and host species are also provided.
Santa Cruz Biotechnology goat anti-actin polyclonal antibody [18-20], mouse anti-beta-actin antibody , and rabbit anti-human actin antibody  were used in Western blot. ChIP  and immunoprecipitation  experiments were also cited. Santa Cruz Biotechnology beta-actin was used in Western blot to study activin receptor , hoxd4 gene repression , Id2 , anthracycline chemotherapy , androgen receptor silencing , human telomerase reverse transcriptase , tumor suppressor SMAR1 , Smad1 and p38 kinase , cortical neurons , C3 transferase. , PMA stimulation , B lymphocytes from patients , 293T cells , Faf1 deficiency , adiponectin haploinsufficiency , ILK , Prdx1 , nitric oxide function , BMP-6 , and MMS19 . Santa Cruz Biotechnologies anti-beta-actin antibody was used to explore the regulation of a sexually transferred steroid hormone and a female protein in the oogenesis in the Malaria Mosquito Anopheles gambiae .
Monoclonal Abcam beta-actin antibody was used in western blot to study tumor necrosis factor alpha translation , phosphorylation of claudin-3 at threonine 192 , VHL status , Bmi1 functions , retinal axon development , and the function of sFLT-1 (ab6276) . Abcam actin antibody was also used to study ABCA1 and ABCG1 in human macrophages , HIF-1 stabilization and degradation , melanoma-associated antigens , ubiquitination pathway , and TRiC/CCT functions .
Chemicon monoclonal anti-actin antibody was used in western blot to study heregulin-dependent BRCA1 phosphorylation , polycystin 2 , and human astrocyte . Chemicon anti-actin antibody was used to study NMT1-1 and NMT2-4 siRNA , alpha-synuclein degradation by serine protease neurosin , the role of CDON in regulating tumor cell survival . Oncogene Research Products and Calbiochem (both are now part of EMD Millipore) anti-actin antibodies were used in western blot to study galectin-3 phosphorylation  and interleukin-11 receptor alpha-chain , respectively.
Zymed Laboratories, Ambion, Neomarkers, Biovision (all are now part of Thermo Fisher) anti-actin antibodies were used in western blot to study HER-2 down-regulation , histone demethylases , p130/p107/p105Rb-dependent transcriptional repression , and the regulatory effect of HILDA complex on VEGF-A expression , respectively.
Rockland actin antibody was used in western blot to study the effect of MDM2-dependent inhibition of p53 on EBV growth transformation of B-cell and infected-cell survival .
Novus anti-beta-actin antibody was used for western blot to investigate the roles of MutSalpha and MutLalpha in ATR-Chk1 pathway .
US Biological beta-actin antibody was used in western blot to study Zinc-induced PTEN protein degradation .
Cytoskeleton goat anti-human actin antibody was used in western blot as a loading control to study the effect of P2Y2 nucleotide receptors on alpha-secretase-dependent amyloid precursor protein processing .
The catalog numbers cited among the surveyed articles include A5441 (for AC-15 clone) [2, 9], AC-15 clone [4, 5, 10, 71, 72], AC-74 clone , rabbit anti-actin antibody A5060  and A5316 for ChIP assay . Most of publications citing Sigma beta actin antibodies are for Western blot; a few of them indicate immunoprecipitation [76-79], ELISA , and immunocytochemistry [81-83].
Monoclonal Sigma anti-actin antibodies were used in Western blot to study p53, WAF1, and MDM2 , von Hippel Lindau tumor suppressor , DNA methylation , ULBP5/RAET1G isoforms , iron accumulation , microtubule-associated protein 1S , SHIP , laminins , copper/zinc superoxide dismutase , H2AX , human astrocytoma cell line 1321N1 , Dnmt1 promoter , SRPK1 , Tsc/mTORC1 signaling , VAMP8/Endobrevin , nitric oxide synthase isoforms , Parkinson disease pathology , and Luc and NudC .
Polyclonal Sigma anti-beta-actin antibodies , from rabbit [103-105], were used in Western blot to investigate PR3-mediated p21 cleavage, Cu/Zn-superoxide dismutase mutant-induced motoneuronal cell death, the role for proepithelin in prostate carcinogenesis and the role of IRAK-1 blockade in immuno-tolerance.
Monoclonal ICN Biomedicals anti-actin antibody was used in western blot to study Vav3 , LNCaP and PC-3 cells , and cystatin M . Its antibodies against beta-actin were used to study lin-4 miRNA in C. elegans , and transforming growth factor-beta 1 .
Cell Signaling anti-beta-actin antibodies [158-160], including that from rabbit , were used to perform western blot to investigate ETB and AT1 receptor, ATM-mediated DDR-p53 signaling pathway, androgen receptor signaling and ING1a. Cell Signaling Technologies anti-beta-actin was used to study the mechanism by which de-differentiation confers multidrug resistance  and the role of ALK7 signaling in catecholamine resistance in obesity .
Roche Molecular Biochemicals monoclonal anti-actin antibody was used in western blot as a loading control .
Transduction Laboratories rabbit polyclonal anti-beta-actin antibody was used in western blot to ensure equal loading .
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