Beta Actin Antibody Review and FAQs
  1. Mary Johnson Ph. D.
    mary at labome dot com
    Synatom Research, Princeton, New Jersey, United States
last modified : 2013-11-24; original version : 2013-03-21
Cite as
MATER METHODS 2013;3:179
Beta Actin Antibody

This is a review about beta actin antibodies (mainly as an internal loading control for Western blot), based on 147 published articles as of November 25, 2013 in randomly selected publications that Labome surveyed systematically. Labome is continuously curating antibodies cited in formal publications. There are numerous additional publications using beta actin antibodies, our systematic and random selection sampling will ensure that the results and the conclusion based on the survey results are representative. This review is aimed 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.

Beta Actin Antibody Review and FAQs Figure 1
Figure 1. A typical application of beta actin antibody as the Western blot loading control, from [151].
Beta actin

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 as Western blot loading control

Beta-actin antibody is the most commonly used loading control for western blot (see the 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 surveyed.

Santa Cruz Biotechnology 24
Abcam 10
EMD Millipore/Calbiochem7
Cell Signaling4
Thermo Fisher2
Table 1. Major suppliers of beta actin antibodies used in western blot and their numbers of publications among the cohort of publications surveyed by Labome, as of November 25, 2013
Actin antibody clones

The most cited anti-beta actin antibody clone is AC-15. It is cited in six publications among the total of ten 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 [1], oogenic processes [2], apoptosis [3], Barrett's metaplasia [4], NF-kappaB signaling [5] and retinal axon development [6].

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 [7] [8]. 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, a then Ph.D. student in the 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 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 in the literature.

Beta actin may not be a suitable internal loading control for low abundance proteins, or at diseased states

It must be noted that beta-actin is not an appropriate Western blot loading control in some circumstances. At higher total protein loading level, beta actin specific antibodies may not be able to detect the differences of protein loading levels [9]. 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 [9].

In addition, beta actin expression might change during growth and differentiation, or in disease states [10].

Frequently asked questions about beta actin antibody

Some of the commonly asked questions about beta actin antibody are discussed below.

There is no beta actin band during Western blot.

There are a number of reasons. The 1st one to check is whether the anti-beta actin antibody is actually effective. One way is to reduce the dilution of anti-beta actin antibody, and check to see whether there is still any band at all, and try to use anti-beta actin antibodies from high quality suppliers. The 2nd 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 3rd 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 actually 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. or beta actin is preferentially degraded. Another thing to be checked is whether the secondary antibody matches the anti-beta actin antibody.

Can the antibody for the target protein and the antibody for beta actin be incubated together to detect the talk approaching Pennebaker beta actin at the same time?

This is not advisable. The best approach is to detect the target protein 1st, then use western blot stripping buffer to remove the target approaching antibody and the secondary antibody, and then to incubate with anti-beta actin antibody. The reason is that it is difficult to adjust the incubation and developing parameters for 2 different antibodies; and it is also difficult to prevent cross-reactivity among different antibodies.

What is the best dilution for a given anti-beta actin antibody?

The best way is to check that 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 is not working properly, you still need to test different dilutions to find the optimal one.

With different Western blot experiments, the same sample at the same loading volume gave very different beta actin signal intensities.

Multiple experimental procedures may affect this. It could be the loading solution is becoming more sticky, or the transfer is uneven.

Do I still need to do the internal control if the ratio of phosphorylated target protein against the total target protein is obtained?

Yes. The internal control not only ensures the loading, but also checks the transfer, the incubation, and the development.

The target protein has the same molecular weight as the beta actin.

The 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 signal before incubation with beta actin antibody. Alternatively, another protein can be used as an internal control, such as tubulin or GAPDH.

Can I use beta actin as a loading control for nuclear samples?

No. The nucleus may contain some actin, but its level is dynamic, and should not serve as a control. See Labome's detailed discussion on different loading controls.

There are several beta actin positive bands, all of them are smaller than 43 kD.

Several reasons: 1) secondary antibody may not be very specific; 2) the loading buffer is not effective; 3) the primary antibody is not specific; 4) beta actin is degraded.

Detailed Labome survey results

A detailed breakdown of the literature analyzed by Labome citing beta-actin antibodies is provided here, organized according to the suppliers. Whenever possible, the clonality and host species are also provided.

Santa Cruz Biotechnology

Santa Cruz Biotechnology goat anti-actin polyclonal antibody [11] [12] [13], mouse anti-beta-actin antibody [14], and rabbit anti-human actin antibody [15] were used in Western blot. ChIP [16] and immunoprecipitation [17] experiments were also cited. Santa Cruz Biotechnology beta-actin was used in Western blot to the mechanism of activin receptor [18], the hoxd4 gene repression [19], the role of Id2 [20], anthracycline chemotherapy [21], androgen receptor silencing [22], human telomerase reverse transcriptase [23], tumor suppressor SMAR1 [24], Smad1 and p38 kinase [25], cortical neurons [26], C3 transferase. [27], PMA stimulation [28], B lymphocytes from patients [29], 293T cells [30], Faf1 deficiency [31], adiponectin haploinsufficiency [32], ILK [33], Prdx1 [34], nitric oxide function [35], BMP-6 [36], and MMS19 [37].


Monoclonal Abcam beta-actin antibody was used in western blot to study tumor necrosis factor alpha translation [38], phosphorylation of claudin-3 at threonine 192 [39], VHL status [40], Bmi1 functions [41], and retinal axon development. [6]. Abcam actin antibody was also used to ABCA1 and ABCG1 in human macrophages [42], HIF-1 stabilization and degradation [43], melanoma-associated antigens [44], and ubiquitination pathway [45].

EMD Millipore

Chemicon monoclonal anti-actin antibody was used in western blot to study heregulin-dependent BRCA1 phosphorylation [46], polycystin 2 [47], and human astrocyte [48]. Chemicon anti-actin antibody was used to study NMT1-1 and NMT2-4 siRNA [49] and alpha-synuclein degradation by serine protease neurosin [50]. 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 [51] and interleukin-11 receptor alpha-chain [52], respectively.

Thermo Fisher

Zymed Laboratories, Ambion, Neomarkers (all are now part of Thermo Fisher) anti-actin antibodies were used in western blot to study HER-2 down-regulation [53], histone demethylases [54], and p130/p107/p105Rb-dependent transcriptional repression [55], 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 [56].

Novus Bio

Novus anti-beta-actin antibody was used for western blot to investigate the roles of MutSalpha and MutLalpha in the regulation of ATR-Chk1 pathway [57].

US Biological

US Biological beta-actin antibody was used in western blot to study Zinc-induced PTEN protein degradation [58].


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 [59].


The catalog numbers cited include A5441 (for AC-15 clone) [1], AC-15 clone [3] [4] [60] [61], AC-74 clone [62], rabbit anti-actin antibody A5060 [63] and A5316 for ChIP assay [64]. Most of publications citing Sigma beta actin antibodies are for Western blot, a few of them indicate immunoprecipitation [65] [66] [67] [68], ELISA [69], and immunocytochemistry [70] [71] [72].

Monoclonal Sigma anti-actin antibodies were used in Western blot to study p53, WAF1, and MDM2 [73], von Hippel Lindau tumor suppressor [74], DNA methylation [75], ULBP5/RAET1G isoforms [76], iron accumulation [77], microtubule-associated protein 1S [78], SHIP [79], laminins [80], copper/zinc superoxide dismutase [81], H2AX [82], human astrocytoma cell line 1321N1 [83], Dnmt1 promoter [84], SRPK1 [85], Tsc/mTORC1 signaling [86], VAMP8/Endobrevin [87], nitric oxide synthase isoforms [88], Parkinson disease pathology [89], and Luc and NudC [90].

Polyclonal Sigma anti-beta-actin antibodies [91], from rabbit [92] [93] [94], 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.

Other publications cited Sigma anti-beta actin antibodies in western blot include [95] [96] [97] [98] [99] [100] [101] [102] [103] [104] [105] [106] [107] [108] [109] [110] [111] [112] [113] [114] [115] [116] [117] [118] [119] [120] [121] [122] [123] [124] [125] [126] [127] [128] [129] [130] [131] [132] [133] [134] [135] [136] [137].

MP Biochemicals

Monoclonal ICN Biomedicals anti-actin antibody was used in western blot to study Vav3 [138], LNCaP and PC-3 cells [139], and cystatin M [140]. Its antibodies against beta-actin were used to lin-4 miRNA in C. elegans [141], and transforming growth factor-beta 1 [142].

Cell Signaling Technology

Cell Signaling anti-beta-actin antibodies [143] [144] [145], including that from rabbit [146], was used to perform western blot to investigate ETB and AT1 receptor, ATM-mediated DDR-p53 signaling pathway, androgen receptor signaling and ING1a.

Boehringer Mannheim

Boehringer Mannheim actin antibody was used in western blot to study PTEN [147] and EGFR family members in colon and breast cancer cells [148].


DAKO mouse anti-alpha-actin was used in 1:1000 dilution to perform immunohistochemistry [146].


Roche Molecular Biochemicals monoclonal anti-actin antibody was used in western blot as a loading control [149].

BD Bioscience

Transduction Laboratories rabbit polyclonal anti-beta-actin antibody was used in western blot to ensure equal loading [150].

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