Non-Polymerizing Actin (alpha skeletal muscle actin)
Non-Polymerizing Actin (NP-Actin)
modified skeletal muscle α-actin, rabbit
Cat. #: 8105-01
............................................................................................................................................................................................................................................................
Description
Protein |
Actin (α-Actin) |
Origin |
Skeletal muscle alpha actin, rabbit |
Molecular mass |
42kDa |
Protein description |
Non-Polymerizing Actin is a-skeletal muscle actin (42kD, 375 aa), enzymatically cleaved between Gly42/Val43. As a result of this cleavage an essential monomer-monomer interaction site is inactivated, rendering the actin unpolymerizable in the presence of Ca++ and e.g. 100mM KCl, conditions where normal actin polymerizes. |
Purity |
>99% by scanning densitometry. |
Properties
Form |
Lyophilized, ready-to-use. |
Quantity per unit |
1.0 mg |
Buffer |
2mM Tris-Cl pH 8.2, 0.4mM ATP, 0.5mM DTT, 0.1mM CaCl2, 1mM NaN3 and 0.3% disaccharides, when reconstituted with 1.0 ml ultrapure water to obtain a 1mg/ml solution. |
Related products |
For dilution of G-actin or exchange of ligand buffer into actin compatible buffer, MonoMix (Cat. #.: 5100-0*) may be used. In the absence of nucleators, the polymerization of G-actin is initiated by PolyMix (Cat.#: 5000-0*). |
Purification notes |
Purified from rabbit skeletal muscle, GPC. |
Protein concentration |
Determined by the Biuret method. |
Storage instructions |
Avoid refreezing. NP-Actin stored at –70°C upon arrival will be stable in performance for at least 6 months from the date of purchase. Solubilized G-actin is kept on ice and should be used within 1 week. |
Shipping conditions |
At ambient temperature. Upon delivery store at -70°C. |
Remarks |
For Use in Research only. Not for Use in Human or Veterinary Diagnostical or Therapeutical Applications. |
CAS no. |
51005-14-2 |
Further Information
References
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
References
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
{{.}}
{{/content}}{{{.}}}
{{/content}}