Name: R-CHP | Collagen Hybridizing Peptide, Cy3 Conjugate
Price: 443.00 USD

- Overview
  - R-CHP is labeled with sulfo-Cyanine3 for direct fluorescence detection.
    
    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
    
    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.
    
    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]
    1. Targeting and mimicking collagens via triple helical peptide assemblies. Curr. Opin. Chem. Biol., 2013.
    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.
- Properties
  - Categories
    
    Peptides
    
    Alternative Name
    
    R-CHP, collagen mimetic peptide (CMP)
    
    Molecular Weight
    
    3191.44 g/mol
    
    Appearance
    
    Purified lyophilized powder
    
    Purity
    
    90% by HPLC
    
    Other Properties
    
    Conjugate: Single sulfo-Cyanine3 tag per peptide
    Excitation: 548 nm
    Emission: 563 nm
    
    Storage
    
    -20 °C as powder, 4 °C after reconstitution in water
    
    * For research use only. Not intended or approved for diagnostic or therapeutic use.
- Applications
  - Application
    
    Immunofluorescence; Cell Imaging; SDS-PAGE (In-gel Western)
- Reference
  - 1. Nikolaos Frangogiannis et al., Protective effects of activated myofibroblasts in the pressure-overloaded myocardium are mediated through Smad-dependent activation of a matrix-preserving program. Circulation Research (2019)
    2. Christopher Fry et al., Anterior cruciate ligament tear promotes skeletal muscle myostatin expression, fibrogenic cell expansion, and a decline in muscle quality. The American Journal of Sports Medicine (2019)
    3. Michele Marino et al., Molecular-level collagen damage explains softening and failure of arterial tissues: A quantitative interpretation of CHP data with a novel elasto-damage model. Journal of the Mechanical Behavior of Biomedical Materials (2019)
    4. Jeffery Molkentin et al., An acute immune response underlies the benefit of cardiac adult stem cell therapy. bioRxiv (2019)
    5. Xudong Li et al., Molecular detection and assessment of intervertebral disc degeneration via a collagen hybridizing peptide. ACS Biomaterials Science & Engineering (2019)
    6. Xudong Li et al., Microfluidic disc-on-a-chip device for mouse intervertebral disc—pitching a next-generation research platform to study disc degeneration. ACS Biomaterials Science & Engineering (2019)
    7. Karl Kadler et al., Protection of circadian rhythms by the protein folding chaperone, BiP. The FASEB Journal (2019)
    8. Stephen Weiss et al., Divergent matrix-remodeling strategies distinguish developmental from neoplastic mammary epithelial cell invasion programs. Developmental Cell (2018)
    9. Fiona Watt et al., Fibroblast state switching orchestrates dermal maturation and wound healing. Molecular Systems Biology (2018)
    10. Fiona Watt et al., Loxl2 is dispensable for dermal development, homeostasis and tumour stroma formation. Plos One (2018)
    11. Matthew Abramowitz et al., Skeletal muscle fibrosis is associated with decreased muscle inflammation and weakness in patients with chronic kidney disease. American Journal of Physiology-Renal Physiology (2018)
    12. Kenneth Monson et al., Detection and characterization of molecular-level collagen damage in overstretched cerebral arteries. Acta Biomaterialia (2018)
    13. Spencer Szczesny et al., Fatigue loading of tendon results in collagen kinking and denaturation but does not change local tissue mechanics. Journal of Biomechanics (2018)
    14. Samuel Veres et al., In tendons, differing physiological requirements lead to functionally distinct nanostructures. Scientific Reports (2018)
    15. Svenja Illien-Junger et al., Dietary advanced glycation end-product consumption leads to mechanical stiffening of murine intervertebral discs. Disease Models & Mechanisms (2018)
    16. Mark Banaszak Holl et al., Fatigue failure mechanism of anterior cruciate ligament fracture. (2018)
    17. Themis Kyriakides et al., Decellularized materials derived from TSP2-KO mice promote enhanced neovascularization and integration in diabetic wounds. Biomaterials (2018)
    18. Per Fogelstrand et al., Systematic in vitro comparison of decellularization protocols for blood vessels. Plos One (2018)

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User Guide

R-CHP | Collagen Hybridizing Peptide, Cy3 Conjugate

R-CHP | Collagen Hybridizing Peptide, Cy3 Conjugate

Background

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