CapZ (skeletal muscle, native) - 25 µg
Cap Z (capping protein)
(Actin Binding Protein)
Description
| Protein | Cap Z, Capping protein (skeletal muscle isoform) |
| Origin | Skeletal muscle, rabbit |
| Molecular mass | 66 kDa |
| Protein description | The subunits of the heterodimeric capping protein CapZ possess a molecular mass of 34 kDa (α1 subunit) and 32 kDa (β2 subunit). CapZ binds with high affinity in a Ca++-independent manner to the barbed end of actin filaments (1:1000 M/M). |
| Actin interaction | Ca++-insensitive barbed end capping protein. Kd actin binding = >1 nM (barbed end). |
Properties
| Form | Lyophilized, ready-to-use. |
| Quantity per unit | 25 µg |
| Buffer | 100 mM KCl, 20 mM Hepes pH 7.4, 1 mM DTT and 3% disaccharides, when reconstituted with 25 µl ultrapure water to obtain a 1.0 mg/ml solution. |
| Purity & Activity | Purity: >92% by scanning densitometry from Coomassie G-250 stained SDS-Gels. Capping activity: F-actin (Cat.#: 8101) containing 20% pyrene actin (Cat.#: 8112) was incubated with CapZ and diluted below the critical concentration. Depolymerisation was followed by fluorometry and compared to an actin reference without CapZ. Complete capping was obtained at a molar ratio of 1 : 1000 (CapZ : Actin). All proteins were used as supplied, i.e. without dialysis. G-Actin stock solutions were pre-spun 1 h, 100.000xg, 4°C. |
| Purification notes | CapZ has been finally purified by gel filtration on a Superdex 75 column. |
| Protein concentration | Determined by OD280 (0.1% = 1.234). |
| Storage instructions | CapZ stored at −70 °C upon arrival will be stable in performance for at least 6 months from the date of purchase. The solubilized protein is kept on ice and should be stored at -20°C in glycerol or CryoProtect (Cat.#: 6011-01). Avoid repeated freeze / thaw cycles. |
| 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. | |
Proteins and buffers from Hypermol® are made of the ultrapure reagents in Milli-Q™ water, as described in our publications.
Further Information
Product DataSheet
Material and Safety Data Sheet
Sequence on NCBI (alpha-1 SU)
Sequence on NCBI (beta-2 SU)
Structure on NCBI (PDB ID: 1IZN)
References
Myosin-II activity generates a dynamic steady state with continuous actin turnover in a minimal actin cortex
Sonal, Kristina A. Ganzinger, Sven K. Vogel, Jonas Mücksch, Philipp Blumhardt and Petra Schwille.
bioRxiv preprint first posted online May 2, 2018; doi: 10.1101/312512
Crystal structure of capz: structural basis for actin filament barbed end capping.
Yamashita A, Maeda K, Maeda Y.
EMBO J. (2003) 22:1529.
