ATTO550-Actin for TIRFM (alpha-Actin, skeletal muscle rabbit) - 5x100µg
ATTO550-Actin for TIRFM
Superresolution-optimized fluorescent rabbit skeletal muscle α-actin; lysine-labelled with ATTO550.
Applications
| Applications | Superresolution-optimized, polymerization-competent fluorescent rabbit skeletal muscle α-actin for TIRFM, high- and super-resolution fluorescence microscopy, filament tracking, fluorescence spectroscopy and biochemical actin assays. |
Description
| Product name | ATTO550-Actin for TIRFM |
| Protein | Rabbit skeletal muscle α-actin. |
| Molecular mass | 42 kDa. |
| Product description | ATTO550-Actin for TIRFM is chemically modified rabbit skeletal muscle G-actin carrying covalently attached ATTO550 fluorescent groups on lysine residues. Rabbit skeletal muscle actin is a single-chain polypeptide of approximately 42 kDa consisting of 375 amino acids. The product is prepared as a superresolution-optimized fluorescent actin probe with an adjusted degree of labelling to support bright fluorescence detection while preserving the polymerization properties of native G-actin. It is designed for TIRF microscopy and other fluorescence-based actin assays requiring polymerization-competent labelled actin. |
| Fluorophore | ATTO550. |
| Spectral properties | Excitation maximum: 554 nm; emission maximum: 576 nm. |
| Labelling chemistry | ATTO550 is covalently attached to lysine residues of rabbit skeletal muscle G-actin. |
| Degree of labelling | This product is supplied with an optimized degree of labelling (DOL) of approximately 0.3 to support superresolution and TIRF microscopy applications. |
| Overview | Superresolution-optimized fluorescent rabbit skeletal muscle α-actin; ATTO550-labelled on lysine residues; polymerization-competent; suitable for TIRFM, high- and super-resolution fluorescence microscopy, filament tracking and biochemical actin assays; supplied lyophilized in actin-compatible buffer; 5 × 100 µg package variant. |
Properties
| Form | Lyophilized, ready-to-use after reconstitution. |
| Quantity per unit | 5 × 100 µg. |
| Reconstitution | Reconstitute each 100 µg tube with 100 µl ultrapure water to obtain a 1 mg/ml ATTO550-Actin solution. |
| Buffer | 2 mM Tris-HCl pH 8.2, 0.4 mM ATP, 0.5 mM DTT, 0.1 mM CaCl2 and 0.3% disaccharides after reconstitution with ultrapure water to obtain a 1 mg/ml solution. |
| Purity | >99% by scanning densitometry. |
| Purification notes | Purified from rabbit skeletal muscle. |
| Protein concentration | Determined by UV absorbance at 290 nm (A290 = 0.63 for 1 mg/ml actin) with fluorophore-specific correction factor applied. |
| Storage instructions | ATTO550-Actin stored at −70 °C upon arrival will be stable in performance for at least 6 months from the date of purchase. The solubilized product should be kept protected from light and on ice and used within 1 week. Avoid refreezing of actin. |
| Shipping conditions | At ambient temperature. Upon delivery store at −70 °C. |
| Remarks | For research use only. Not for use in human or veterinary diagnostic or therapeutic applications. |
| CAS no. | |
Proteins and buffers from Hypermol® are prepared with ultrapure reagents in Milli-Q™ water, as described in our publications.
Further Information
Product DataSheet
Download product datasheet for ATTO550-Actin for TIRFM.
Material and Safety Data Sheet
MSDS / SDS document for ATTO-labelled skeletal muscle actin products.
Protein Sequence on NCBI
Reference sequence information for rabbit skeletal muscle actin.
Hide ATTO dyes & spectral properties
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ATTO dyes – spectral overview (λex / λem)
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References
| Reference | Phosphoinositides regulate force-independent interactions between talin, vinculin, and actin. Kelley CF, Litschel T, Schumacher S, Dedden D, Schwille P, Mizuno N. eLife. 2020;9:e56110. Published 2020 Jul 13. doi:10.7554/eLife.56110. |
| Reference | Kank2 activates talin, reduces force transduction across integrins and induces central adhesion formation. Sun Z, Tseng HY, Tan S, Senger F, Kurzawa L, Dedden D, Mizuno N, Wasik AA, Thery M, Dunn AR, Fässler R. Nat Cell Biol. 2016 Sep;18(9):941-53. doi:10.1038/ncb3402. |
