3Helix - Model R-CHP - Collagen Hybridizing Peptide, Cy3 Conjugate
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.
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]
R-CHP is labeled with sulfo-Cyanine3 for direct fluorescence detection.
Specificity: CHP binds to the unfolded triple-helical chains of all collagen types (e.g., I, II, III, IV, etc).[3,7]
Applications: immunofluorescence,[3] cell imaging,[4] SDS-PAGE (in-gel western)[7]
Specification
| Synonyms | R-CHP, collagen mimetic peptide (CMP) |
| Molecular weight | 3191.44 g/mol |
| Purity | 90% by HPLC |
| Conjugate | Single sulfo-Cyanine3 tag per peptide |
| Excitation | 548 nm |
| Emission | 563 nm |
| Content | Purified lyophilized powder |
| Storage | -20 °C as powder, 4 °C after reconstitution in water |
Features
- 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