Actin protein (>95% pure): rabbit skeletal muscle

Actin protein (>95% pure): rabbit skeletal muscle

Product Uses Include

  • Identification and characterization of muscle actin binding proteins
  • In vitro actin polymerization studies
  • Antibody standard for Western blot analysis

Actin protein has been purified from rabbit skeletal muscle. AKL99 actin is greater than 99% pure and AKL95 is greater than 95% pure. Muscle actin has an approximate molecular weight of 43 kDa. Rabbit muscle actin is supplied as a white lyophilized powder. The lyophilized protein when stored desiccated to < 10% humidity at 4°C is stable for 6 months. When re constituted in distilled water to 10 mg/ml, the protein is in the following buffer: 5 mM Tris-HCl pH 8.0, 0.2 mM CaCl2, 0.2 mM ATP, 5% sucrose, and 1% dextran.

Protein purity is determined by scanning densitometry of Coomassie Blue stained protein on a 12% polyacrylamide gel. AKL99 consists of >99% pure muscle actin while AKL95 is >95% pure (see Figure 1).


Figure 1: Figure 1. Purities of rabbit skeletal muscle actin protein. 100 µg of >99% pure (AKL99) and >95% pure (AKL95) rabbit skeletal muscle actin were run on SDS-PAGE gels and stained with coomassie blue. The arrow indicates actin protein, the arrowhead an α-actinin contaminant (115 kDa). The minor impurities in the purified actins are predominantly actin binding proteins such as α-actinin and gelsolin.

Biological Activity
The biological activity of muscle actinis determined by its ability to efficiently polymerize into filaments (F-actin) in vitro and separate from unpolymerized components in a spin down assay. Stringent quality control ensures that AKL99 produces > 90% F-actin and AKL95 produces > 80% F-actin in this assay.

For product Datasheets and MSDSs please click on the PDF links below.   For additional information, click on the FAQs tab above or contact our Technical Support department at

AuthorTitleJournalYearArticle Link
Peng, Y. H. et al.Dynamic matrices with DNA-encoded viscoelasticity for cell and organoid cultureNature Nanotechnology 2023 18:122023ISSN 1748--3395
Cao, Muqing et al.An actin filament branching surveillance system regulates cell cycle progression, cytokinesis and primary ciliogenesisNature Communications 2023 14:12023ISSN 2041--1723
McGarry, David J. et al.MICAL1 activation by PAK1 mediates actin filament disassemblyCell Reports2022
Lin, Ying H. et al.Site-specific acetyl-mimetic modification of cardiac troponin I modulates myofilament relaxation and calcium sensitivityJournal of Molecular and Cellular Cardiology2020ISSN 1095-8584
Yamada, Yurika et al.Cardiac muscle thin filament structures reveal calcium regulatory mechanismNature Communications2020ISSN 2041-1723
Seervai, Riyad N.H. et al.The Huntingtin-interacting protein SETD2/HYPB is an actin lysine methyltransferaseScience Advances2020ISSN 2375-2548
Schmidt, William et al.Lysine acetylation of F-actin decreases tropomyosin-based inhibition of actomyosin activityThe Journal of biological chemistry2020ISSN 1083--351X
Ravichandran, Akshaya et al.A novel actin binding drug with in vivo efficacyAntimicrobial Agents and Chemotherapy2019ISSN 1098-6596
Gu, Weihong et al.Mono-fullerenols modulating cell stiffness by perturbing actin bundlingNanoscale2018ISSN 2040--3372
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Bertier, Laurence et al.Nanobodies targeting cortactin proline rich, helical and actin binding regions downregulate invadopodium formation and matrix degradation in SCC-61 cancer cellsBiomedicine and Pharmacotherapy2018ISSN 1950-6007
Cui, Jin et al.Leptolyngbyolides, Cytotoxic Macrolides from the Marine Cyanobacterium Leptolyngbya sp.: Isolation, Biological Activity, and Catalytic Asymmetric Total SynthesisChemistry - A European Journal2017ISSN 1521-3765
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Lin, Yi et al.Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain PolymersCell2016ISSN 1097-4172
Lundquist, Mark R. et al.Redox modification of nuclear actin by MICAL-2 regulates SRF signalingCell2014ISSN 1097-4172
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Mohammad, Ibrahim et al.Flightless I is a focal adhesion-associated actin-capping protein that regulates cell migrationThe FASEB Journal2012ISSN 1530--6860
Mohammad, Ibrahim et al.Flightless I is a focal adhesion‐associated actin‐capping protein that regulates cell migrationThe FASEB Journal2012ISSN 0892--6638
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Arora, Pamela D. et al.Gelsolin Mediates Collagen Phagocytosis through a Rac-dependent StepMolecular Biology of the Cell2004ISSN 1059-1524
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Question 1:  What is the best way to store actin proteins to insure maximum stability and shelf-life?

Answer 1:  Cytoskeleton provides all of our actin proteins as lyophilized powders so that they can be shipped at room temperature.  Upon receipt, the lyophilized powders should be stored at 4°C in a sealed container with desiccant.  It is important to monitor the freshness of the desiccant and insure that it continues to absorb moisture to protect the lyophilized actins.  With proper storage, the lyophilized actins are guaranteed to be stable for 6 months from the date of purchase.  Alternatively, actins can be immediately resuspended at the concentration recommended, aliquoted, snap-frozen in liquid nitrogen and stored at -70°C.  The frozen aliquots will be stable for 6 months.  When thawing frozen aliquots, it is important to thaw in a room temperature water bath.


Question 2:  What is the best way to store F-actin after polymerizing?

Answer 2:  G-actin is stable for two days at 4°C and requires a divalent cation, pH 6.5 - 8.0 and ATP for stability.  F-actin is stable and can be stored at 4°C for 1-2 weeks.  F-actin requires ATP (0.2 mM) and Mg2+ (2 mM) for stability and is unstable below pH 6.5 and above pH 8.5.  F-actin is not stable to freezing.  F-actin can be transferred to a variety of buffers (e.g. HEPES, phosphate, etc) without detrimental effects.  We recommend the addition of antibacterial agents such as 100 μg/ml ampicillin and 10 μg/ml chloramphenicol when storing F-actin at 4°C.


If you have any questions concerning this product, please contact our Technical Service department at