|
TEL: +32 16 58 90 45
Fax :+ 32 16 50 90 45
GENTAUR Europe
tel+32 2 732 5688
fax+32 2 732 4414
Av.
de l' Armée 68
B-1040 BRUSSELS
BELGIUM
GENTAUR France
tel 01 43 25
01 50
fax01 43 25
01 60
9, rue
Lagrange
75005 PARIS
FRANCE
GENTAUR Italy
tel 02 36 00
65 93
fax 02 36 00
65 94
20135 MILANO
ITALY
GENTAUR Germany
tel +49 241
6085 13140
fax +49 241
6085 33033
Forckenbeckstraße 6,
D-52074
Aachen
GERMANY
| |
For USA call : 888-892-8408
|
Product Code |
Product Name |
Price |
|
Specialty Proteins |
|
|
304 |
I270™ AFM Reference |
€350.00 |
Product information
|
Specialty Proteins |
|
|
I270™ AFM Reference Protein |
| |
I27O™ is a recombinant polyprotein composed
of eight (8) repeats of the Ig 27 domain of human titin. The protein is
used as a reference and calibrator for force extension experiments using
atomic force microscopes. Single molecule measurements give up to eight saw
tooth force-extension curves with the following specifications: |
|
|
|
| |
Parameter |
Value |
|
|
Distance between peaks |
24.1 ± 0.34 nm |
|
|
Force Peaks |
204 ± 26 pN |
|
|
Persistence Length |
0.39 ± 0.07 nm |
|
|
Contour Length (per domain) |
28.4 ± 0.3 nm |
|
|
|
|
| |
I27OÔ
is supplied as a ready-to-use solution. The protein concentration is
0.5-2.0 mg/ml in phosphate buffered saline pH 7.3. To use, dilute the
protein to 100 mg/ml
in buffered saline and absorb to freshly prepared gold AFM coverslips.
Secure the coverslips to the retractable stage of the AFM instrument and
perform force extension measurements. The force-extension relationships for
the I27O polyprotein
are measured using
a single axis atomic force microscope. Single proteins are fully extended
by retracting the sample holder away from the AFM tip. Stretching of the
I27 polyprotein
should result in a
force-extension curve with peaks that varied randomly in amplitude with an
average value of ~200 pN and an average distance between each peak of ~24 nm
(see table above). Between 25% and 50% of the measurements should yield
unfolding curves for all eight domains. Collect data on 20 or more single
molecule full-length extensions and calculate the values for the distance
between peaks, the magnitude of the force peaks, the persistence length and
the contour length for each domain. |
|
