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Overview
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F-CHP is labeled with fluorescein for direct fluorescence detection.
• More informative, reliable and convenient than zymography, DQ collagen, SHG, and TEM
• High affinity and unparalleled specificity to collagen with essentially no nonspecific binding
• Applicable to all types of collagen from all species, relying on collagen's secondary structure instead of any defined sequence for binding
• Suitable for both frozen and paraffin-embedded sections with no need for antigen retrieval
• A non-antibody approach with no species restrictions against any co-staining antibody
• Small size (2% of IgG by MW) enabling facile tissue penetration and whole specimen staining without sectioning
• Stable in solution under 4 °C, eliminating the need to aliquot for storage
CHP can slowly self-assemble into the triple helical structure in solution during storage. The trimeric CHP requires a simple heating step prior to usage.Please contact us at for specific academic pricing.
Background
The collagen hybridizing peptide (CHP) is a novel and unique peptide that specifically binds unfolded collagen chains, both in vitro and in vivo.[1,2,3] By sharing the Gly-X-Y repeating sequence of natural collagen, CHP has a strong capability to hybridize with denatured collagen chains by reforming the triple helical structure, in a fashion similar to DNA fragments annealing to complementary DNA strands. CHP is extremely specific: it has negligible affinity to intact collagen molecules due to lack of binding sites, and it is inert towards non-specific binding because of its neutral and hydrophilic nature.
1. Targeting and mimicking collagens via triple helical peptide assemblies. Curr. Opin. Chem. Biol., 2013.
CHP is a powerful histopathology tool which enables straightforward detection of inflammation and tissue damage caused by a large variety of diseases, as well as tissue remodeling during development and aging.[3] CHP robustly visualizes the pericellular matrix turnover caused by proteolytic migration of cancer cells within 3D collagen culture, without the use of synthetic fluorogenic matrices or genetically modified cells.[4] CHP can measure and localize mechanical injury to collagenous tissue at the molecular level.[5] It also enables assessment of collagen denaturation in decellularized extracellular matrix.[6] In addition, CHP can be used to specifically visualize collagen bands in SDS-PAGE gels without the need for western blot.[7]
Specificity: CHP binds to the unfolded triple-helical chains of all collagen types (e.g., I, II, III, IV, etc).[3,7]
2. Targeting collagen strands by photo-triggered triple-helix hybridization. Proc. Natl. Acad. Sci. U.S.A., 2012.
3. In situ imaging of tissue remodeling with collagen hybridizing peptides. ACS Nano, 2017.
4. Visualizing collagen proteolysis by peptide hybridization: From 3D cell culture to in vivo imaging. Biomaterials, 2018.
5. Molecular level detection and localization of mechanical damage in collagen enabled by collagen hybridizing peptides. Nat. Commun., 2017.
6. Molecular assessment of collagen denaturation in decellularized tissues using the collagen hybridizing peptide. Acta Biomater., 2017.
7. Direct detection of collagenous proteins by fluorescently labeled collagen mimetic peptides. Bioconjug. Chem., 2013.
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- Properties
- Applications
- Reference
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Overview