Non-Polymerizing Actin ATTO488 (alpha skeletal muscle actin)
Non-Polymerizing Actin ATTO488
Fluorescent non-polymerizing rabbit skeletal muscle α-actin; lysine-labelled with ATTO488.
Applications
| Applications | Fluorescent non-polymerizing actin for optical research techniques investigating the G-actin state, G-actin-ligand studies in the presence of Ca2+ and KCl, and actin-based biochemical assays where a defined non-polymerizing actin probe is required. |
Description
| Product name | Non-Polymerizing Actin ATTO488 |
| Protein | Rabbit skeletal muscle α-actin. |
| Molecular mass | 42 kDa. |
| Product description | Non-Polymerizing Actin ATTO488 is fluorescently labelled rabbit skeletal muscle α-actin. The actin is enzymatically cleaved between Gly42 and Val43. This cleavage inactivates an essential monomer-monomer interaction site and renders the actin non-polymerizing in the presence of Ca2+ and, for example, 100 mM KCl, conditions under which normal actin polymerizes. ATTO488-conjugated non-polymerizing actin is suitable for optical research techniques used to investigate the G-actin state of the protein. It is a useful probe for G-actin-ligand studies in the presence of Ca2+ and KCl. The product remains polymerizable in the presence of Mg2+, with a critical concentration of 3 µM at the barbed end, allowing research on the F-actin state. Actin-compatible buffers preserve the structural integrity of non-polymerizing actin. Its cleavage products of approximately 36 kDa and 6 kDa are only obtained under denaturing conditions, for example by SDS-PAGE. |
| Fluorophore | ATTO488. |
| Spectral properties | Excitation maximum: 500 nm; emission maximum: 520 nm. |
| Labelling chemistry | ATTO488-labelled non-polymerizing rabbit skeletal muscle α-actin. |
| Overview | Fluorescent non-polymerizing rabbit skeletal muscle α-actin; ATTO488-labelled; enzymatically cleaved between Gly42 and Val43; suitable for optical G-actin-state investigations, G-actin-ligand studies and actin-based biochemical workflows; supplied lyophilized in actin-compatible buffer; 50 µg package variant. |
Properties
| Form | Lyophilized, ready-to-use after reconstitution. |
| Quantity per unit | 50 µg. |
| Buffer | 2 mM Tris-HCl pH 8.2, 0.4 mM ATP, 0.5 mM DTT, 0.1 mM CaCl2, 1 mM NaN3 and 0.3% disaccharides after reconstitution with ultrapure water to obtain a 1 mg/ml solution. |
| Purity | >99% by scanning densitometry. |
| Related products | For dilution of G-actin or exchange of ligand buffer into actin-compatible buffer, MonoMix may be used. In the absence of nucleators, polymerization of G-actin is initiated by PolyMix. |
| Purification notes | Purified from rabbit skeletal muscle by GPC. |
| 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 | Non-Polymerizing Actin stored at −70 °C upon arrival will be stable in performance for at least 6 months from the date of purchase. Solubilized actin should be kept on ice and used within 1 week. Avoid refreezing. |
| 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. | 51005-14-2. |
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 Non-Polymerizing Actin ATTO488.
Material and Safety Data Sheet
MSDS / SDS document for 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)
Hover/tap a dye to see details incl. possible excitation source.
References
| Reference | The actin/actin interactions involving the N-terminus of the DNase-I-binding loop are crucial for stabilization of the actin filament. Khaitlina SY, Moraczewska J, Strzelecka-Gołaszewska H. Eur J Biochem. 1993 Dec 15;218(3):911-20. doi: 10.1111/j.1432-1033.1993.tb18447.x. PMID: 8281943. |
