The Cultrex® Collagen I Cell Invasion Assay is a 96-well microplate-based assay designed to accelerate the screening process for compounds that influence chemotaxis. Invasive migration is a fundamental function underlying cellular processes such as angiogenesis, embryonic development, immune response, metastasis, and invasion of cancer cells. The Cultrex Collagen I Cell Invasion Assay offers a flexible, standardized, high-throughput format for quantitating the degree to which invasive cells penetrate a barrier consisting of extracellular matrix protein Collagen I in response to chemoattractants and/or inhibiting compounds. This assay kit contains all the reagents needed for monitoring cell movement through Collagen I, including a simplified 96-well Boyden chamber with an 8 μm pore polyethylene terephthalate (PET) membrane, which is coated with the extracellular matrix by the end-user prior to use.
Cell Invasion Chamber
Collagen I Coating Solution
Cell Wash Buffer
Cell Dissociation Solution
Quantification of Cell Invasion through Different Extracellular Matrix Components
FBS Stimulates Migration of NIH-3T3 and HT1080 Cells. The NIH-3T3 mouse embryonic fibroblast cell line and the HT1080 human fibrosarcoma cell line were treated with 10% fetal bovine serum (FBS). The migration of untreated (yellow bars) and treated (green bars) NIH-3T3 and HT1080 cells against different extracellular matrix components, including BME, Laminin I, Collagen I, Collagen IV, were quantified using the Cultrex Cell Invasion Assay Kits (Catalog # 3455-096-K, 3456-096-K, 3457-096-K, 3458-096-K, respectively). Data from four experiments was quantified for both non-invasive (NIH-3T3) and invasive (HT1080) cell types.
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The product requires storage at -20 to -70 °C, 2 - 8 °C, and room temperature. Consult the product insert for specific storage temperatures. Do not use past expiration date.
Background: Collagen I
Collagens comprise a large family of insoluble extracellular glycoproteins that are essential components of connective tissues such as tendons, ligaments, cartilage, bone and skin. The mature polypeptides are secreted as coiled, left-handed helices that subsequently assemble into rope-like collagen fibers. Collagen I is a fibril-forming collagen that requires N- and C- terminal processing. Collagen IV is a network forming collagen whose C-terminus forms dimers and N-terminus forms tetramers.
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