YO Proteins cat. 739 is native canine collagen type I and III, purified from washed dissected canine tissue by partial pepsin digestion in acidic conditions followed by differential salt precipitation. The resulting preparation is a heterotypic I/III blend that mirrors the connective-tissue composition of dermal, vascular and visceral connective tissue in the dog — the same biological pairing found in cat. 223 (porcine), cat. 221 (mouse) and cat. 634 (bovine) — but supplied as the species-matched material veterinary and translational labs need when canine cell biology refuses to read a heterologous substrate.
The species-specificity matters. In a published canine flow-chamber platelet-adhesion assay, canine platelet adhesion was supported by canine collagen at = 200 µg/mL coating, while bovine skin collagen — a common laboratory default — did not support adhesion. That single observation is the strongest single argument for canine collagen as a stocking reagent in any laboratory doing canine platelet, canine fibroblast, canine MSC, or canine wound-healing work.
Cat. 739 is supplied as a lyophilised, salt-free powder for reconstitution in dilute acetic acid (0.5 M, pH 2.5). The preparation is positioned as a coating material for cell-culture studies; as is typical of partial-pepsin I/III preparations, it is not optimised for self-assembled 3-D gel formation. Labs that need a true canine 3-D gel substrate should pair this product with one of the YO atelocollagen 3-D gel formats from a related species; for users who simply need a species-matched 2-D coating, flow-chamber substrate, or ECM background for ELISA / IF immunostaining, cat. 739 is the direct, published-validated reagent.
SPECIFICATIONS
Catalogue number: 739
Product name: Collagen type I and III (canine)
Source: Canine tissue. Collagen extracted from washed dissected tissue into dilute acetic acid after pepsin treatment; type I + III purified by differential salt precipitation
Purity: Canine collagen I and III = 98 %; canine collagen (other types) < 1 %; non-collagen proteins < 0.5 %
Format: Lyophilised, salt-free
Purification: Partial pepsin digestion in acidic conditions, followed by differential salt precipitation
Heterotypic composition: Heterotypic type I / type III blend (the in-vivo connective-tissue pairing)
Package size: 10 mg
Grade: Research use only (not for diagnostic or therapeutic use)
STORAGE / RECONSTITUTION
Reconstitute in 0.5 M acetic acid, pH 2.5. Mix vigorously overnight at +4 °C. A homogeniser may be required to disperse the recalcitrant sediment — this is normal behaviour for high-purity native collagen and does not indicate aggregation damage.
Shipped at ambient temperature.
Lyophilised protein: store up to 2 years at -20 °C.
Reconstituted protein (0.5 M acetic acid, pH 2.5): store up to 1 month at +4 °C.
APPLICATIONS
- Species-matched coating substrate for canine platelet flow-chamber adhesion assays (published — see Cited Use Cases). Cross-species (bovine) collagen does not substitute.
- Coating substrate for canine fibroblast, canine MSC, and canine endothelial-cell 2-D culture and adhesion studies
- Coating substrate for veterinary wound-healing, scar, and dermal-fibrosis research
- ECM background for canine-cell immunofluorescence and ELISA-based adhesion assays
- Reference antigen for the generation, characterisation, and titration of anti-canine collagen I/III antibodies (natural pairing with YO cat. 775 rabbit anti-canine collagen I and III polyclonal antibody)
- Coating substrate for canine osteoblast / osteoclast and orthopaedic-model research
- Substrate for veterinary platelet-function diagnostics development (point-of-care flow assays for canine sepsis, infection-associated thrombocytopathy, and canine perioperative monitoring)
- Comparative-ECM panels alongside the cross-species I/III blends (cat. 634 bovine, cat. 223 porcine, cat. 221 mouse)
- Substrate for canine tumour-stroma and canine mammary-carcinoma matrix studies (where species-matched ECM influences carcinoma-associated fibroblast phenotype)
APPLICATION HIGHLIGHTS — HIGH-VALUE RESEARCH NICHES
- Species-matched canine matrix for veterinary cell-culture, orthopaedic and dermal wound-healing models.
- Heterotypic type I / III blend reproducing native canine connective-tissue and granulation-tissue composition.
- Coating substrate for canine fibroblast, chondrocyte and endothelial adhesion, contraction and migration assays.
- Reference antigen and immunogen for canine collagen Enzyme-Linked Immunosorbent Assay and antibody cross-reactivity panels.
- Comparative-ECM control alongside human, bovine and rodent collagen preparations in translational studies.
- Bulk 10 mg format for collagen gels, sponges and scaffolds in veterinary tissue-engineering research.
REFERENCES
The following peer-reviewed publications use YO Proteins canine collagen type I and III (cat. 739) as the substrate of record.
1. Ferkau A, Gillmann HJ, Mischke R, Calmer S, Ecklebe S, Abid M, Minde JW, Echtermeyer F, Theilmeier G. Infection-associated platelet dysfunction of canine platelets detected in a flow chamber model. BMC Veterinary Research. 2013 Jun 7;9(1):112. PMID 23758817.
Demonstrated that infection / endotoxin exposure produces a canine-platelet adhesion defect detectable in a biochip flow-chamber model coated with the YO Proteins canine collagen I/III preparation. Establishes the substrate for canine perioperative and sepsis-related platelet diagnostics.
2. Ferkau A, Ecklebe S, Jahn K, Calmer S, Theilmeier G, Mischke R. A dynamic flow-chamber-based adhesion assay to assess canine platelet-matrix interactions in vitro. Veterinary Clinical Pathology. 2013 Jun;42(2):150–6. PMID 23627964.
The methods paper that established the species-matched-collagen requirement. Canine platelet adhesion in the flow chamber was supported by = 200 µg/mL canine collagen, whereas bovine skin collagen at the same coating concentration did not support adhesion. Defines the optimised wall shear stress (14 dyn/cm²) and is the single most-cited rationale for stocking species-matched canine collagen in veterinary translational labs.
