Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
PRO-343

Background:

Troponin Complex is a heteromeric protein playing an important role in the regulation of skeletal and cardiac muscle contraction. It consists of three subunits, Troponin I , Troponin T and Troponin C. Each subunit is responsible for part of Troponin Complex function. E.g. Troponin I inhibits ATP-ase activity of acto-myosin. Troponin T and Troponin I are presented in cardiac muscles in different forms than in skeletal muscles.

Physical Appearance:

Sterile Filtered colourless liquid formualtion

Formulation:

0.5 mg/ml glycerol

Stability:

Recombinant Human Cardiac Troponin I-T-C Complex is stable at 10蚓 between 2-7 days ,however, should be stored desiccated below -18蚓.
Please avoid freeze-thaw cycles.

Purity:

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

Dimers and aggregates:

Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

Endotoxin:

Less than 0.1 ng/ug (IEU/ug) of human Troponin I-T-C Complex .

Applications:

1. Immunoassays
2. Western blot

Usage:

This material is offered by ProSpec-TechnoGene for research, laboratory or further evaluation purposes.

Latest Publications:

1. Calcium-dependent changes in the flexibility of the regulatory domain of troponin C in the troponin complex.
J Biol Chem 2005 Jun 10;280(23):21924-32
2. Biology of the troponin complex in cardiac myocytes.
Prog Cardiovasc Dis 2004 Nov-Dec;47(3):159-76
3. Solution structure of the chicken skeletal muscle troponin complex via small-angle neutron and X-ray scattering.
J Mol Biol 2005 Jan 28;345(4):797-815
4. The calcium-induced switch in the troponin complex probed by fluorescent mutants of troponin I.
Eur J Biochem 2003 Jul;270(14):2937-44
5. Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation.
Biochemistry 2003 Jul 1;42(25):7790-800
6. The highly conserved COOH terminus of troponin I forms a Ca2+-modulated allosteric domain in the troponin complex.
Biochemistry 2001 Feb 27;40(8):2623-31