Non-Muscle CapZ Heterodimer is a high-affinity actin filament capping protein essential for cytoskeletal organization and cellular dynamics. This heterodimeric protein consists of two subunits:
• α1-subunit (34 kDa)
• β2-subunit (32 kDa)
CapZ binds with nanomolar affinity to the barbed ends of actin filaments in a Ca2+-independent manner, effectively regulating actin filament growth and turnover. By capping the fast-growing barbed end, CapZ prevents the addition or dissociation of actin monomers, ensuring precise filament length control and stabilization.
150 mM NaCl, 20 mM Hepes pH 7.4, 1 mM DTT and 5% sucrose, when reconstituted with 1.0 ml ultrapure water to obtain a 1.0 mg/ml solution.
Purity & Activity
Purity: >94% 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
The alpha-1 SU is untagged, while the beta-2 SU contains a His-tag. Using anti-His antibodies, the protein can be identified by suited immunological techniques.
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.