Collagen Peptides Research Compound
Research Use Only
This product is intended for laboratory research purposes only. It is not intended for human or veterinary use, food, cosmetic, household, or agricultural applications. Not for human consumption.
Overview
Collagen peptides (hydrolyzed collagen) are bioactive peptides derived from the enzymatic hydrolysis of native collagen protein. Our collagen peptides are sourced from bovine hides and contain primarily Type I and Type III collagen—the most abundant collagen types in human skin, tendons, ligaments, and bones. The hydrolysis process breaks down the large collagen molecules into smaller peptides (2-6 kDa) with enhanced bioavailability for research applications.
Molecular Characteristics
| Property | Value |
|---|---|
| Source | Bovine (grass-fed) |
| Collagen Types | Type I (90%), Type III (10%) |
| Molecular Weight | 2000-6000 Da (average) |
| Hydrolysis | Enzymatic |
| Protein Content | ≥95% |
| Hydroxyproline | ~12% |
| Storage | Room temperature, sealed |
Amino Acid Profile
| Amino Acid | Content |
|---|---|
| Glycine | ~33% |
| Proline | ~12% |
| Hydroxyproline | ~12% |
| Glutamic Acid | ~10% |
| Alanine | ~8% |
| Arginine | ~8% |
| Other | ~17% |
Mechanism of Action
Collagen peptides provide bioactive fragments for tissue research:
Peptide Absorption
- Small molecular weight enables absorption
- Peptide transport mechanisms (PepT1)
- Distribution to target tissues
- Accumulation in skin, cartilage, bone
Fibroblast Stimulation
- Enhanced fibroblast proliferation
- Increased collagen synthesis
- ECM production stimulation
- Growth factor interactions
Bioactive Sequences
- Gly-Pro-Hyp tripeptides
- Pro-Hyp dipeptides
- Specific sequences with receptor activity
- MMP inhibition potential
Research Applications
Skin Research
- Dermal collagen synthesis
- Skin elasticity studies
- Photoaging models
- Wound healing research
Joint & Cartilage
- Chondrocyte function
- Cartilage matrix synthesis
- Osteoarthritis models
- Joint health biomarkers
Bone Research
- Osteoblast differentiation
- Bone matrix formation
- Calcium metabolism
- Osteoporosis studies
Bioavailability Studies
- Peptide absorption kinetics
- Tissue distribution
- Metabolite identification
- Dose-response relationships
Available Formats
| Size | Format | Catalog Code |
|---|---|---|
| 100g | Powder | COL-100 |
| 500g | Powder | COL-500 |
| 1kg | Powder | COL-1000 |
Handling & Storage
- Store in cool, dry place
- Keep container tightly sealed
- Stable at room temperature for 2+ years
- Protect from moisture
- Highly soluble in cold water
- Neutral taste and odor
Quality Specifications
- Protein Content: ≥95%
- Appearance: White to off-white powder
- Solubility: Instantly soluble in water
- Ash: Less than 2%
- Moisture: Less than 8%
- Heavy Metals: Less than 10 ppm
- Microbiological: Meets USP standards
- Certificate of Analysis provided
Collagen Type Comparison
| Type | Primary Location | Function |
|---|---|---|
| Type I | Skin, bone, tendon | Tensile strength |
| Type II | Cartilage | Compression resistance |
| Type III | Skin, blood vessels | Elasticity, support |
| Type IV | Basement membrane | Structural support |
References
- Asserin J, et al. "The effect of oral collagen peptide supplementation on skin moisture and the dermal collagen network." J Cosmet Dermatol. 2015.
- Shigemura Y, et al. "Dose-dependent changes in the levels of free and peptide forms of hydroxyproline in human plasma after collagen hydrolysate ingestion." Food Chem. 2014.
- Moskowitz RW. "Role of collagen hydrolysate in bone and joint disease." Semin Arthritis Rheum. 2000.