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]
F-CHP is labeled with fluorescein 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 | F-CHP, collagen mimetic peptide (CMP) |
Molecular weight | 2952.01 g/mol |
Purity | 95% by HPLC |
Conjugate | Single fluorescein tag per peptide |
Excitation | 494 nm |
Emission | 512 nm |
Content | Purified lyophilized powder |
Storage | -20 °C as powder, 4 °C after reconstitution in water |
Features
For research use only. Not intended or approved for diagnostic or therapeutic use.
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