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Collagen (COL) peptide (Biotin) Peptide

COL Host: Synthetic BI, IF, IHC, SDS
Pubmed (9 references)
Catalog No. ABIN6952242
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  • Target See all Collagen (COL) products
    Collagen (COL)
    • 3
    Purification tag / Conjugate
    This Collagen peptide is labelled with Biotin.
    BioImaging (BI), Immunofluorescence (IF), Immunohistochemistry (IHC), SDS-PAGE (SDS)
    Collagen Hybridizing Peptide, Biotin Conjugate (B-CHP)
    CHP binds to the unfolded triple-helical chains of all collagen types (e.g., I, II, III, IV, etc)
    The Collagen Hybridizing Peptide (CHP) is a synthetic peptide that can specifically bind to such denatured collagen strands through hydrogen bonding, both in histology, in vivo, and in vitro (3D cell culture). By sharing the structural motif and the Gly-X-Y repeating sequence of natural collagen, CHP has a strong capability to hybridize with denatured collagen strands, in a fashion that is similar to a DNA fragment annealing to its complimentary DNA strand during PCR. CHP is an extremely specific probe for unfolded collagen molecules: it has negligible affinity to intact collagen molecules due to the lack of binding sites, it is also inert towards non-specific binding because of its neutral and hydrophilic nature.

    Collagen is the major building block of all load-bearing tissues including tendon, ligament, cornea, cartilage and bone. It was recently found that unfolding of the collagen triple helix can occur during mechanical damage to connective tissues, and that CHP can specifically detect and localize such mechanically unfolded collagen molecules in situ, enabling understanding of the mechanical behavior and damage mechanism of these tissues at the molecular level.

    Collagen is also one of the most widely used natural scaffold materials for regenerative medicine. The process of harvesting native extracellular matrix (ECM) by removing cells from animal tissues (i.e., decellularization) may alter the collagen structure and negatively affect the mechanical property and regenerative capacity of the ECM materials. CHP enables assessment of the structural integrity of collagen molecules within these processed matrices, and can facilitate optimization of the decellularization protocols. Additionally, CHP can be used in several biochemical assays, such as in-gel Western blot, for identification and quantification of collagen content in a biological sample.

    The collagen hybridizing peptide (CHP) is a novel and unique peptide that specifically binds unfolded collagen chains, both in vitro and in vivo. 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. 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. CHP can measure and localize mechanical injury to collagenous tissue at the molecular level. It also enables assessment of collagen denaturation in decellularized extracellular matrix. In addition, CHP can be used to specifically visualize collagen bands in SDS-PAGE gels without the need for western blot.

    F-CHP is labeled with fluorescein for direct fluorescence detection.
    HPLC, MS, Binding Assay, Histology
    > 95 %
  • Application Notes
    B-CHP provides the flexibility for visualizing damaged collagen using any user-selected fluorophore (e.g., AlexaFluor dyes conjugated streptavidin), or a non-fluorescence method (e.g., through NeutrAvidin-HRP mediated DAB staining).

    In addition, B-CHP and commercial streptavidin-conjugated gold nanoparticles can be used in combination to label unfolded collagen molecules under TEM.

    CHP tends to slowly self-assemble into CHP triple helices in solution during storage. Such CHP trimers have no driving force to hybridize with unfolded collagen strands. Therefore, the trimeric CHP must be dissociated to monomers by heating prior to use. Since the trimerization of CHP takes hours to occur at low μM concentrations, the heat-dissociated CHP can stay as active monomer strands that are available for hybridization with unfolded collagen. A common protocol is heating the CHP solution (after diluting to the desired concentration) to 80 °C in a water bath, and quickly quenching it to room temperature followed by immediate application to target collagen substrates, as described below in detail. A heating block and an ice-water bath may be needed in most applications (not provided).

    • 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

    Reagent Preparation

    Make sure to tap vial down to ensure powder is at the bottom and that it does not fly out upon opening. Dissolve the 0.3 mg of peptide powder in 1 mL of pure water or phosphate-buffered saline (1x PBS), vortex well and centrifuge, to prepare a stock solution containing approximately 100 μM of CHP. Store the stock solution at 4 °C. Dilute the stock solution to assay dependent concentrations upon use. For the 60 μg products, dissolve the powder in 400 μL water or PBS to get a stock solution with a CHP concentration of 50 μM. For the 15 μg samples, dissolve in 100 μL water or PBS for a stock solution with the CHP concentration of 50 μM.

    For Research Use only
  • Format
    PBS, pH 7.4
    4 °C,-20 °C
    Storage Comment
    -20 °C as powder, 4 °C after reconstitution in water
  • Russo, Cavalera, Huang, Su, Hanna, Chen, Shinde, Conway, Graff, Frangogiannis: "Protective Effects of Activated Myofibroblasts in the Pressure-Overloaded Myocardium Are Mediated Through Smad-Dependent Activation of a Matrix-Preserving Program." in: Circulation research, Vol. 124, Issue 8, pp. 1214-1227, (2020) (PubMed).

    Dai, Xing, Xiao, Li, Cao, He, Fang, Periasamy, Oberhozler, Jin, Landers, Wang, Li: "Microfluidic Disc-on-a-Chip Device for Mouse Intervertebral Disc-Pitching a Next-Generation Research Platform To Study Disc Degeneration." in: ACS biomaterials science & engineering, Vol. 5, Issue 4, pp. 2041-2051, (2019) (PubMed).

    Krishnamoorthy, Hoy, Natelson, Torre, Laudier, Iatridis, Illien-Jünger: "Dietary advanced glycation end-product consumption leads to mechanical stiffening of murine intervertebral discs." in: Disease models & mechanisms, Vol. 11, Issue 12, (2019) (PubMed).

    Abramowitz, Paredes, Zhang, Brightwell, Newsom, Kwon, Custodio, Buttar, Farooq, Zaidi, Pai, Pessin, Hawkins, Fry: "Skeletal muscle fibrosis is associated with decreased muscle inflammation and weakness in patients with chronic kidney disease." in: American journal of physiology. Renal physiology, Vol. 315, Issue 6, pp. F1658-F1669, (2019) (PubMed).

    Peck, Brightwell, Johnson, Ireland, Noehren, Fry: "Anterior Cruciate Ligament Tear Promotes Skeletal Muscle Myostatin Expression, Fibrogenic Cell Expansion, and a Decline in Muscle Quality." in: The American journal of sports medicine, Vol. 47, Issue 6, pp. 1385-1395, (2019) (PubMed).

    Kober, Cano, Géraud, Sipilä, Mobasseri, Philippeos, Pisco, Stannard, Martin, Salvador, Santos, Boutros, Rognoni, Watt: "Loxl2 is dispensable for dermal development, homeostasis and tumour stroma formation." in: PLoS ONE, Vol. 13, Issue 6, pp. e0199679, (2018) (PubMed).

    Hwang, San, Turner, White, Faulk, Badylak, Li, Yu: "Molecular assessment of collagen denaturation in decellularized tissues using a collagen hybridizing peptide." in: Acta biomaterialia, Vol. 53, pp. 268-278, (2018) (PubMed).

    Li, Yu: "Targeting and mimicking collagens via triple helical peptide assembly." in: Current opinion in chemical biology, Vol. 17, Issue 6, pp. 968-75, (2014) (PubMed).

    Li, Foss, Summerfield, Doyle, Torok, Dietz, Pomper, Yu: "Targeting collagen strands by photo-triggered triple-helix hybridization." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 109, Issue 37, pp. 14767-72, (2012) (PubMed).

  • Target
    Collagen (COL)
    CG25C, CG4145, CT12803, Cgc25, Cgc25C, Coll, Coll IV, DCg1, Dcg, Dcg1, Dmel\\CG4145, alpha(IV)1/Cg25C, alpha1, cg25C, cg25c, col4a1, gp125, Collagen type IV alpha 1, COLlagen, hypothetical protein, Col4a1, col-17, F59F5.4
    Collagen is the most abundant protein in mammals. It is the major structural component of almost all organs and tissues, providing the framework for cell attachment and growth. Programmed collagen degradation occurs during tissue development, homeostasis and repair. However, excessive collagen degradation is implicated in a variety of diseases, such as cancer, inflammation, and fibrosis.The triple helix is the hallmark protein structure of collagen. During tissue remodeling, the triple helical collagen molecules are degraded by specific proteases (e.g., MMP or cathepsin K) and become unfolded at body temperature.
    Molecular Weight
    3191.44 g/mol
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