Overview
- Species: Bovine
- Additional Attributes: 3D Hydrogels, Coating, Collagen, Extracellular Matrix
- Specific Attributes: Atelocollagen/pepsin treatment, steril, Type I
- Features:3 mg/ml
PureCol®, Bovine Collagen
Cat.-Nr.: 5005-100ML
Description
PureCol® collagen (bovine collagen, atelocollagen) is known as the standard of all collagens for purity (>99.9% collagen content), functionality, and the most native-like collagen available. PureCol® is isolated from bovine hides sourced from the only controlled, closed herd in the United States. Advanced BioMatrix’s manufacturing processes comply with stringent quality standards that have proven to yield unsurpassed lot-to-lot consistency.
PureCol® collagen is approximately 97% Type I atelocollagen with the remainder being comprised of Type III collagen. PureCol® collagen is supplied at approximately a 3 mg/ml concentration. The concentration for each specific lot is provided on a Certificate of Analysis that is available with the purchase of each product. PureCol® is soluble atelocollagen in 0.01 N HCI, therefore, the pH is 2. PureCol® collagen is ideal for coating of surfaces, providing preparation of thin layers for culturing cells, or use as a solid gel.
PureCol® collagen is provided in a user-friendly packaging for use and storage. PureCol® is sterile filtered and is supplied as a ready to use solution.
For extensive users of this product: The PureCol® collagen is available in a 1.000 ml unit, too. (please contact us)
Summary of available bovine collagen type I products:
| atelo-collagen | telo-collagen | Concentration [mg/ml] |
| PureCol | TeloCol-3 | 3 |
| Nutragen | TeloCol-6 | 6 |
| FibriCol | TeloCol-10 | 10 |
For an overview of Type I Collagen (Atelocollagen & Telocollagen) products (click)
SUPPLIER:
Advanced BioMatrix
STATUS:
In Stock
SIZE:
100 ml
Bovine collagen, PureCol® is available in 100 ml and 1.000 ml.
References
- Sorensen, Jacob R., et al. "An altered response in macrophage phenotype following damage in aged human skeletal muscle: implications for skeletal muscle repair." The FASEB Journal(2019): fj-201900519R.
- Colaço, E., et al. "Hierarchical Collagen-Hydroxyapatite Nanostructures Designed Through Layer-by-Layer Assembly of Crystal-Decorated Fibrils." , Hierarchical Collagen-Hydroxyapatite Nanostructures Designed Through Layer-by-Layer Assembly of Crystal-Decorated Fibrils (May 13, 2019)(2019).
- Schwerdtfeger, Luke A., et al. "Human colon function ex vivo: Dependence on oxygen and sensitivity to antibiotic." PloS one5 (2019): e0217170.
- Cardoso, Ana, et al. "MiR-144 overexpression as a promising therapeutic strategy to overcome glioblastoma cell invasiveness and resistance to chemotherapy." Human molecular genetics(2019).
- Steele, Hannah E., et al. "Mechanotransduction of mitochondrial AMPK and its distinct role in flow-induced breast cancer cell migration." Biochemical and biophysical research communications2 (2019): 524-529.
- Gehwolf, Renate, et al. "Global Responses of Il-1β-Primed 3D Tendon Constructs to Treatment with Pulsed Electromagnetic Fields." Cells5 (2019): 399.
- Alexander, Frank, Sebastian Eggert, and Dorielle Price. "Label-Free Monitoring of 3D Tissue Models via Electrical Impedance Spectroscopy." (2019): 1-24.
- Matysik-Woźniak, Anna, et al. "Examination of Kynurenine Toxicity on Corneal and Conjunctival Epithelium: In vitro and in vivo Studies." Ophthalmic research(2019): 1-12.
- Compton, Clayton, et al. "Reconstitution of the Ventricular Endocardium Within Acellular Hearts." Regenerative Engineering and Translational Medicine(2019): 1-11.
- Müller, A. L., et al. "4. Identification of miR-301a in Primary Human Atrial Fibroblasts and Bone Marrow-Derived Mesenchymal Progenitor Cells to Attenuate Endogenous Differentiation into Pro-Fibrotic Cells." Differentiation of Primary Human Pro-Fibrotic Mesenchymal Cells Influenced by Extracellular Matrix Environment Determined by Micro-RNA Expression(2018): 130.
- Doblinger, Nina, et al. "Impact of hydroxyethyl starch and modified fluid gelatin on granulocyte phenotype and function." Transfusion(2019).
- Elisabeth, et al. "Pro-Inflammatory Responses in Human Bronchial Epithelial Cells Induced by Spores and Hyphal Fragments of Common Damp Indoor Molds." International journal of environmental research and public health6 (2019): 1085.
- Dodmane, Puttappa R., et al. "Biphasic changes in airway epithelial cell EGF receptor binding and phosphorylation induced by components of hogbarn dust." Experimental lung research10 (2018): 443-454.
- McClellan, Alyce, et al. "A novel mechanism for the protection of embryonic stem cell derived tenocytes from inflammatory cytokine interleukin 1 beta." Scientific reports9 (2019).
- Wang, Weiling, et al. "Aquaporin-3 deficiency slows cyst enlargement in experimental mouse models of autosomal dominant polycystic kidney disease." The FASEB Journal(2019): fj-201801338RRR.
- Teo, Jye Yng, et al. "Surface tethering of stem cells with H2O2-responsive anti-oxidizing colloidal particles for protection against oxidation-induced death." Biomaterials201 (2019): 1-15.
- Gehwolf, Renate, et al. "3D-Embedded Cell Cultures to Study Tendon Biology." (2019): 1-11.
FAQs
How is the purity of the PureCol® determined ?
The purity of PureCol® collagen is determined by SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis in conjunction with bacterial collagenase sensitivity and silver staining techniques with a method sensitivity of 99.9%. It was found that PureCol® collagen is 95 to 98% Type I collagen and the remainder being comprised of Type III collagen.
SDS polyacrylamide gel electrophoresis demonstrates the presence of alpha, beta and gamma components in an appropriate ratio of approximately 40:30:30, respectively. PureCol® collagen is a native collagen as judged by polarimetry and trypsin sensitivity although the product does contain a low percentage of collagen fragments or shortened helices.
Conclusion: With the test method sensitivity of 99.9% (SDS-PAGE gel electrophoresis in conjunction with bacterial collagenase sensitivity and silver staining techniques) and no other proteins present in the preparation, it can be concluded that the purity of the PureCol® collagen is 99.9%.
What is the differnce between Vitrogen and PureCol® ?
There is no difference. Vitrogen was the old tradename, and PureCol® is the new tradename.
What is the viscosity of PureCol® ?
The viscosity of PureCol® is ~32 cp.
How you determine the collagen concentration ?
We primarily use the Biuret method, but we also use BCA, AAA, and hydroxyl-proline assays.
Is my collagen okay, if it was frozen, or left at room temperature ?
– Collagen solutions that are frozen tend to have issues forming 3D hydrogels, and will likely not work. The solutions should still be good for 2D coatings.
– Collagen solutions that are left out at room temperature for extended periods of time may show signs of degradation, which will affect the formation of 3D hydrogels. It is likely still fine for 2D coatings.
Our recommendation is this: If you are using the product directly for a publication, we highly suggest buying a new bottle if the one you have was compromised.
PureCol®, Bovine Collagen, lyoph.