Fibricol

Manufactured by Advanced BioMatrix

Sourced in United States

FibriCol is a collagen-based matrix material designed for use in a variety of cell culture and tissue engineering applications. It is composed of native type I collagen extracted from bovine sources. FibriCol provides a natural extracellular matrix environment to support cell attachment, proliferation, and differentiation.

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Lab products found in correlation

8 protocols using fibricol

Preparation of Collagen-Agarose-Gelatin Hydrogels

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To prepare the stock solutions, agarose (low gelling temperature, Sigma-Aldrich, St. Louis, United States of America) was mixed with distilled water and sterilized in the autoclave. Before use it was reheated to 70°C and maintained at 40°C. Gelatin (IMAGEL LA, Gelita AG, Eberbach, Germany) was mixed with distilled water in a 40°C water bath and sterile filtered using a cellulose acetate 0.2 µm syringe filter (VWR, Radnor, United States of America). Gelatin stock was warmed to 37°C before use. Sterile bovine collagen type I (FibriCol, Advanced Biomatrix, Carlsbad, United States of America) was stored cold until use.
Seven hydrogel blends were prepared directly before use by mixing stock solutions of agarose, gelatin and bovine collagen I in the order listed in Table 3. The gels containing collagen were neutralized with 1M NaOH solution (Sigma-Aldrich, St. Louis, United States of America). For experiments containing HepG2 cells, 175 µl of DMEM were replaced by a HepG2 stock suspension with a final concentration of 1 × 10⁶ cells/ml.

Fritschen A., Acedo Mestre M., Scholpp S, & Blaeser A. (2023). Influence of the physico-chemical bioink composition on the printability and cell biological properties in 3D-bioprinting of a liver tumor cell line. Frontiers in Bioengineering and Biotechnology, 11, 1093101.

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Agarose-Collagen Hydrogel Blend

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The final agarose concentration of 5 mg/mL hydrogel blend was achieved by diluting an agarose stock solution (22 mg/mL, low gelling temperature, Sigma-Aldrich) followed by storage at 45°C. The type l collagen solution was prepared from 4 mL collagen stock (9.9 mg/mL, FibriCol, Advanced BioMatrix), 500 µL 10x DMEM (Thermo Fischer Scientific), 500 µL DMEM (Gibco) and 100 µL 1 M NaOH (Sigma-Aldrich). The corresponding cells for the co-cultures were added to the collagen solution. Finally, the agarose solution was added and the hydrogel was molded into a 24-well plate. Polymerization was induced by incubation for 10 min at 4°C.

Kniebs C., Kreimendahl F., Köpf M., Fischer H., Jockenhoevel S, & Thiebes A.L. (2019). Influence of Different Cell Types and Sources on Pre-Vascularisation in Fibrin and Agarose–Collagen Gels. Organogenesis, 16(1), 14-26.

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Collagen Type I Hydrogel Preparation

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All following steps were carried out on ice to halt polymerization of the collagen. 50 µl of 10x PBS (Gibco, Thermo Fisher Scientific, cat 70011-044) was added to of 400 µl of bovine collagen type-1 (10 mg/mL FibriCol; Advanced BioMatrix, San Diego, CA, USA, cat 5133) and gently mixed. Subsequently, pH was set to 7.4 using 48.6 µl of 0.1M NaOH and checked. The collagen was then diluted 1:1 with medium to achieve a final collagen concentration of 4 mg/mL for vessel-on-a chip or 3D collagen experiments.

Kempers L., Sprenkeler E.G., van Steen A.C., van Buul J.D, & Kuijpers T.W. (2021). Defective Neutrophil Transendothelial Migration and Lateral Motility in ARPC1B Deficiency Under Flow Conditions. Frontiers in Immunology, 12, 678030.

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Collagen Density Modulates Dendritic Cell Migration

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Matrix densities ranging from 1.7 mg/ml to 5.6 mg/ml were obtained by using different bovine collagen stock solutions (PureCol, Nutragen, Fibricol; all AdvancedBioMatrix) and dilutions, mixed in 1 × minimum essential medium eagle (MEM, Sigma) and 0.4% sodium bicarbonate (Sigma) with 3 × 10⁵ cells in R10 at a 2:1 ratio (as described previously^{40 (link)}). Collagen–cell mixtures were casted in custom-made migration chambers. After 45 min. polymerization of collagen fibres at 37 °C and 5% CO₂, gels were overlaid with 100 μl CCL19 (R&D Systems, 0.6 μg/ml). DC migration was recorded with time-lapse video microscopy and analysed by a custom-made tracking tool. Inhomogeneous collagen gels with spiked regions of higher collagen density were obtained by polymerizing a higher concentrated collagen mixture first (5.6 mg/ml), followed by cutting with a razor blade into very small pieces, and subsequent addition of the more-concentrated collagen gel pieces into a polymerizing mixture of lower-concentration collagen.

Renkawitz J., Kopf A., Stopp J., de Vries I., Driscoll M.K., Merrin J., Hauschild R., Welf E.S., Danuser G., Fiolka R, & Sixt M. (2019). Nuclear positioning facilitates amoeboid migration along the path of least resistance. Nature, 568(7753), 546-550.

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In Vitro Angiogenesis Assay

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FibriCol^® (10 mg/mL) and Glycosil^® were obtained from Advanced BioMatrix (San Diego, CA). pCMV3-VEGF-A plasmids were acquired from Sino Biological (Wayne, PA). Following the manufacturer’s protocols, pCMV3-VEGF-A plasmids were amplified in MAX Efficiency^™ DH5α competent Escherichia coli (Thermo Fisher, Waltham, MA) and purified using a Qiagen Maxiprep Kit (Germantown, MD). Murine recombinant VEGF-A was obtained from Pepro Tech. (Cranbury, NJ). CellTiter 96^® Aqueous One Solution Cell Proliferation Assay (MTS) was purchased from Promega (Madison, WI). Geltrex^™ and Calcein-AM were acquired from ThermoFisher (Waltham, MA). Alexa Fluor^® 555-conjugated Rabbit IgG-CD31 polyclonal antibody (PECAM-1) and Alexa Fluor^® 555-conjugated Rabbit IgG Isotype Control were purchased from Bioss Antibodies Inc. (Woburn, MA). Mouse IgG2a monoclonal α-SMA-FITC antibody and mouse IgG2a-FITC antibody were obtained from Sigma-Aldrich (St. Louis, MO).

Miles S.A., Rezai A.R., Salazar-González J.F., Vander Meyden M., Stevens R.H., Logan D.M., Mitsuyasu R.T., Taga T., Hirano T, & Kishimoto T. (1990). AIDS Kaposi sarcoma-derived cells produce and respond to interleukin 6.. Proceedings of the National Academy of Sciences of the United States of America, 87(11), 4068-4072.

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Cytocompatibility of SiTiOC20 Electrodes under Pacing

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Cytocompatibility of the SiTiOC20 electrodes under pacing conditions was assessed with NHDFs encapsulated in collagen hydrogels. For cell encapsulation, NHDFs (PromoCell, cat. C12302, Lot 410Z037.5) were harvested and a cell suspension with 6'000'000 cells per mL cell culture medium was prepared. Collagen hydrogels at a ratio of collagen (10mg/mL, FibriCOl, Advanced BioMatrix) : 10X DMEM (Sigma) : 0.5M NaOH (Sigma) + cell-media suspension (8:1:1) were prepared to reach a final concentration of 100'000 cells per 250 L of hydrogel. The collagen-cell suspension was mixed gently and the pH of the hydrogel precursor was measured and adjusted to physiological pH (~7) with 0.5M NaOH. After UV-irradiation of the platform (for 1h), 250 µL of the hydrogel precursor were placed into each channel between the electrodes (SiTiOC20 working electrode, Pt counter electrode) of the PDMS pacing device (Fig. S1d). Gelation was allowed for

Vallachira Warriam Sasikumar P., Müller E., Clement P., Jang J., Kakkava E., Panusa G., Psaltis D., Maniura-Weber K., Rottmar M., Brugger J, & Blugan G. (2020). In Vitro Cytocompatibility Assessment of Ti-Modified, Silicon-oxycarbide-Based, Polymer-Derived, Ceramic-Implantable Electrodes under Pacing Conditions. ACS applied materials & interfaces, 12(15).

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3D Culture of Breast Epithelial Cells

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Three-dimensional collagen I matrix was prepared from 8 parts FibriCol (approx. 10 mg/ml; Advanced Biomatrix), 1 part 10 × PBS, 0.5 parts 0.1 M NaOH and 0.5 parts sterile water. The ready-to-use collagen I mixture was carefully mixed with Matrigel (Corning) in indicated ratios (75:25, 50:50, 25:75) to obtain different gel stiffness. Fifty-five µl of the mixed Matrigel-collagen I matrix, Matrigel or collagen I alone were gently spread per well of an eight-well chamber slide (Corning) following gelation at 37 °C for 1 h. For coating, 150 µl of a 1:10 diluted collagen IV solution (0.3 mg/mL, BioReagent) were added per well. After 90 min at 37 °C the solution was removed and the 3D gels rinsed with sterile Hanks ‘ Balanced Salt Solution (HBSS).
The matrix was then overlaid with 5000 MCF10A cells per well or primary organoids in 400 µl 3D culture medium. Synthetic polyacrylamide gels (12-well format, Matrigen SoftSlip) were covered with 2% Matrigel in PBS for 30 min at 37 ℃ before being overlaid with 100,000 MCF10A cells per well. For 3D morphogenesis assays MCF10A were cultured for max. 14 days with change of medium every second day. Primary organoids were cultured for a maximum of 6 days.

Melcher M.L., Block I., Kropf K., Singh A.K, & Posern G. (2022). Interplay of the transcription factor MRTF-A and matrix stiffness controls mammary acinar structure and protrusion formation. Cell Communication and Signaling : CCS, 20, 158.

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Preparation of Tissue-Derived Hydrogels

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For SIS and UBM the lyophilised powders were first digested using 1 mg/mL pepsin (Sigma, USA) in 0.01 N HCl for 48 hrs at room temperature whilst continuously stirring. Digested SIS and UBM were neutralised using 0.1 N NaOH and PBS to concentrations of 8 mg/mL (SIS) and 15 mg/mL (UBM). Collagen hydrogels (FibriCol, Advanced Biomatrix, USA) were formed according to manufacturer's instructions to a concentration of 8 mg/mL. 1 mM hSAF hydrogels were produced using previously described methods. [43]

Mehrban N., Pineda Molina C., Quijano L.M., Bowen J., Johnson S.A., Bartolacci J., Chang J.T., Scott D.A., Woolfson D.N., Birchall M.A, & Badylak S.F. (2020). Host macrophage response to injectable hydrogels derived from ECM and α-helical peptides. Acta biomaterialia, 111.

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