CapZ (skeletal muscle, native) - 25 µg
Cap Z (capping protein)
Cat. #: 8320-01
(Actin Binding Protein)
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Description
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|
Protein |
Cap Z, Capping protein (skeletal muscle isoform) |
Origin |
skeletal muscle, rabbit |
Molecular mass |
66kDa |
Protein description |
The subunits of the heterodimeric capping protein CapZ possess a molecular mass of 34kDa (alpha 1-subunit) and 32kDa (beta 2-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 = >1nM (barbed end) . |
Properties
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|
Form |
Lyophilized, ready-to-use. |
Quantity per unit |
25µg |
Buffer |
100mM KCl, 20mM Hepes pH 7.4, 1mM DTT and 3% dissachardies, 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. |
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 is 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. |
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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: https://dx.doi.org/10.1101/312512
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: https://dx.doi.org/10.1101/312512
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