Technical Data
Collagen Type I
Collagen is an inert, rigid protein found predominantly in skin, ligaments, bones and teeth. Its most distinctive attribute, essential to a transmitter of mechanical force, is inelasticity. Its fundamental structural unit is tropo-collagen, a molecular rod about 2600 in length and 15 in diameter and 300,000 molecular weight. In tendons these macromolecules, grouped as collagen fibrils, run parallel to the axis. In skin the fibrils are interlaced and branched.

Suitable for use in ELISA, Western Blot, Immunoprecipitation and Immunohistochemistry. Other applications not tested.

Recommended Dilutions:
ELISA: 1:5000-1:50,000
Western Blot (non-denaturing, non-dissociating):1:1000-1;10,000
Immunoprecipitation: 1:100
Immunohistochemistry: 1:50-1:200
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
50ug-20CBlue IceHumanRabbit
Collagen Type I from human and bovine placenta
Purified by Immunoaffinity chromatography.
Supplied as a liquid in 0.125M sodium borate, 0.075M sodium chloride, 0.005M EDTA, pH 8.0, 0.01% sodium azide.
Recognizes human Collagen Type I. Species Crossreactivity: mouse, rat and bovine. Recognizes most mammalian Type I collagens and has negligible crossreactivity with Type II, III, IV, V or VI collagens. Non-speci c crossreaction of anti-collagen antibodies with other human serum proteins or non-collagen extracellular matrix proteins is negligible. Some class speci c anti-collagens may be speci c for three-dimensional epitopes which may result in diminished reactivity with denatured collagen or formalin- xed, paraf n embedded tissues.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Kasamatsu, S. et al., (2011) Scientific Reports 1, Article number: 164 doi:10.1038/srep00164. 2. Hachiya, A. et al., (2009) Am. J. Pathology 174:401-413. 3. Yokose, U. et al., (2012) J. Investigative Dermatology , (21 June 2012) | doi:10.1038/jid.2012.204. 1. Stefanovic, B, et al. 2002. J. Biol. Chem. 277:19229-18237. 2. Hashimoto, N, et al. 2004. J. Clin. Invest. 113:243-252. 3. Hazra, S, et al. 2004. J. Biol. Chem. 279:11392-11401.