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NEM-Myosin II (rabbit, m. psoas) - 1x200 µg

Cat. #:
8316-01
Shipping:
FedEx Express (Global) FedEx Express (Global) (shipping info)
Quantity:
200 µg



NEM-Myosin II
(Actin Binding Protein)


Cat. #: 8316-01  

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Application

Tethering protein for TIRF microscopy, biochemical assays 



Description

   

Protein

NEM-Myosin

Origin

Skeletal muscle, rabbit

Molecular mass

~480kDa

Protein description

NEM-Myosin II is chemically inactivated fast muscle myosin II from rabbit psoas muscle. Myosin II is a hexameric, actin-binding ATPase with a total molecular weight of 480kD in a head- and-tail conformation.

Myosin II has two identical head domains, where the actin binding sites are localized. It consists of two heavy chains (each 220kD) and four light chains (ELC=essential and RLC= regulatory light chains). 

Actin interaction

Binds to F-actin.



Properties

   

Form

Lyophilized, ready-to-use.

Quantity

1x200 µg

Buffer

500mM KCl, 20mM Imidazole pH 7.0, 2mM DTT and 8% disaccharides, when reconstituted with 200 µl ultrapure water to obtain a 1mg/ml solution.

Purity

>98% by scanning densitometry from Coomassie G-250 stained SDS-Gels.

Purification notes

Purified from rabbit skeletal muscle (m. psoas).

Protein concentration

Determined at OD280 (0.1% = 0.53).

Storage instructions

Upon reconstitution the product is stored on ice. This product can also be stored as a glycerol stock at -20°C. 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.

 





Further Information
 

Product DataSheet

Material and Safety Data Sheet


 


References
 

TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions.

Kim HR, Kwon MS, Lee S, Mun Y, Lee KS, Kim CH, Na BR, Kim BNR, Piragyte I, Lee HS, Jun Y, Jin MS, Hyun YM, Jung HS, Mun JY, Jun CD.

Sci Rep. 2018 Apr 3;8(1):5503. doi: 10.1038/s41598-018-23816-2.

 
 





 
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