Actin (rabbit skeletal muscle alpha actin) 4x250µg
alpha-actin from skeletal muscle, rabbit
Cat. #: 8101-01
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Description
|
|
Protein |
Actin (α-Actin) |
Origin |
Skeletal muscle, rabbit |
Molecular mass |
42kDa |
Protein description |
Actin from rabbit skeletal muscle is a single chain polypeptide with a molecular weight of 42kD consisting of 375 amino acids. It is characterized by binding to ATP/ADP (ATPase function) and the binding sites for divalent cations, that strongly contribute to the stabilization of actin. |
Purity |
>99% by scanning densitometry. |
Properties
|
|
Form |
Lyophilized, ready-to-use. |
Quantity per unit |
4x250 µg |
Buffer |
2mM Tris-Cl pH 8.2, 0.4mM ATP, 0.5mM DTT, 0.1mM CaCl2, 1mM NaN3and 0.3% disaccharides, when reconstituted with 0.25ml 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 |
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. Avoid refreezing. |
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
Cosolvent and crowding effects on the polymerization kinetics of actin.
Rosin, Christopher, Paul Hendrik Schummel and Robert S. C. Winter.
Physical chemistry chemical physics : PCCP 17 13 (2015): 8330-7.
Exploring the stability limits of actin and its suprastructures.
Rosin C, Erlkamp M, Ecken JV, Raunser S, Winter R.
Biophys J. 2014 Dec 16;107(12):2982-2992. doi: 10.1016/j.bpj.2014.11.006.
Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau.
Cabrales Fontela Y, Kadavath H, Biernat J, Riedel D, Mandelkow E, Zweckstetter M.
Nat Commun. 2017 Dec 7;8(1):1981. doi: 10.1038/s41467-017-02230-8.
Cosolvent and crowding effects on the polymerization kinetics of actin.
Rosin, Christopher, Paul Hendrik Schummel and Robert S. C. Winter.
Physical chemistry chemical physics : PCCP 17 13 (2015): 8330-7.
Exploring the stability limits of actin and its suprastructures.
Rosin C, Erlkamp M, Ecken JV, Raunser S, Winter R.
Biophys J. 2014 Dec 16;107(12):2982-2992. doi: 10.1016/j.bpj.2014.11.006.
Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau.
Cabrales Fontela Y, Kadavath H, Biernat J, Riedel D, Mandelkow E, Zweckstetter M.
Nat Commun. 2017 Dec 7;8(1):1981. doi: 10.1038/s41467-017-02230-8.
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