Collagen Type I and III, Mouse, 5 mg
Purified native collagen type I and III from tail tendons of the mouse, 5 mg. Type I collagen is the most abundant collagen and is found in connective tissues including tendon,...
Purified native collagen type I and III from tail tendons of the mouse, 5 mg.
Type I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.
Type III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such as skin, lungs, intestinal walls and walls of blood vessels. It is a homotrimer comprised of three alpha-1 chains and resembles other fibrillar collagens in structure and function. It is synthesized as procollagen, similary to collagen I, but the N-terminal propeptide remains attached in the mature fibrillar type III form.
- Collagen type III, alpha 1
- osteogenesis imperfecta
Civitarese, R. A., Talior-Volodarsky, I., Desjardins, J. F., Kabir, G., Switzer, J., Mitchell, M., ... & Connelly, K. A. (2016). The α11 integrin mediates fibroblast–extracellular matrix–cardiomyocyte interactions in health and disease. American Journal of Physiology-Heart and Circulatory Physiology, 311(1), H96-H106.
Product Insert (PDF) - Informational use only. Please refer to insert included with product)
Murine collagen type I - 45%
Murine collagen type III - 45%
Murine collagen type IV - 10%
Murine collagen type V - below 1%
Non-collagen proteins - below 0.5%
Form: 5 mg lyophilized, salt-free
Purification: Partial pepsin digestion in acidic conditions and differential salt precipitation.
Source: Mouse tail tendons
Reconstitution: Use 0.05 M acetic acid, pH 2.5 at 4°C. Dissolved collagen retains immunologic properties of native collagen. Structure of native collagen confirmed by ability to form microfibrils.
Storage: Collagen dissolved in acetic acid is stable at 4 °C for 1 month. Lyophilized collagen long term storage (2 years) at -20°C or lower.