Actin Monomers (from rabbit skeletal muscle alpha actin) - 2.0mg
Monomeric Actin (G-Actin)
freshly prepared from rabbit skeletal muscle α-actin
Cat. #: 8101-G
Description
| Protein | Actin (α-Actin) – Actin monomers (G-Actin) |
| Origin | Skeletal muscle alpha actin, rabbit |
| Molecular mass | 42 kDa |
| Protein description | Freshly prepared actin monomers are shipped on ice by overnight express, ready to start your assays tomorrow. G-Actin prepared from rabbit skeletal muscle is a single chain polypeptide with a molecular weight of 42 kDa (375 amino acids). G-Actin from Hypermol® is column purified (>99% purity) and pre-centrifuged at 100,000 × g for 3 h. Fresh G-actin is made exclusively for you prior to shipping. It is also possible to customize the polymerization conditions according to your demands. Please contact Customer Service: cusserv@hypermol.com. |
| Purity | >99% by scanning densitometry. |
Proteins and buffers from Hypermol® are made of the ultrapure reagents in Milli-Q™ water, as described in our publications.
Properties
| Form | Liquid |
| Quantity & Concentration | 2.0 mg at 2 mg/ml (for other quantities see above). |
| Buffer | 2 mM Trizma, 0.4mM ATP, 0.5 mM DTT, 0.1 mM CaCl2, pH 8.2. |
| Availability / Manufacturing time | 2–4 days. |
| Purification notes | Purified from rabbit skeletal muscle, GPC. |
| Protein concentration | Determined at A280; 1 mg/ml = 0.63. |
| Storage instructions | G-Actin is kept on ice and should be used within 1 week if kept on ice and avoidance of contamination. MonoMix (50 ml) is the G-actin buffer shipped with the product to dilute the actin or actin ligands. Do not freeze. |
| Shipping conditions | Wet ice |
| Remarks | For Use in Research only. Not for Use in Human or Veterinary Diagnostical or Therapeutical Applications. |
| CAS no. | 51005-14-2 |
Proteins and buffers from Hypermol® are made of the ultrapure reagents in Milli-Q™ water, as described in our publications.
Further Information
References
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): 8330–8337.
Rosin, Christopher, Paul Hendrik Schummel and Robert S. C. Winter.
Physical Chemistry Chemical Physics (PCCP) 17(13) (2015): 8330–8337.
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.
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.
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.
