SouthernBiotech offers purified ECM proteins including collagens, fibronectin, and laminin.

Collagen is the main structural protein in the extracellular space and is the most abundant protein in the ECM. They are divided into two classes - fibril (types I, II, III, V) and non-fibril (types IV, VI).

Our highly purified human, bovine, mouse, and rat collagens are quality tested by SDS-PAGE and/or ELISA to ensure purity. They are typically used as standards in applications such as ELISA and in cell culture to facilitate cell attachment, growth, differentiation, migration, and tissue morphogenesis.

Fibronectin is a high molecular weight ECM glycoprotein composed of two nearly identical monomers (220-250 kDa) linked by disulfide bonds. It is present in two forms - the soluble form (the major component of blood plasma which is mainly produced by hepatocytes) and insoluble form (a major component of the ECM which is secreted by various cells prior to being assembled into an insoluble matrix). By binding to other ECM components such as collagen, integrins, and heparin, fibronectin plays an important role in cell adhesion, migration, growth, and differentiation.

Our highly purified fibronectin is quality tested by SDS-PAGE to ensure purity.

Laminins are high-molecular weight ECM proteins that are a major component of the basal lamina of the basement membrane. They consist of an α-chain, a β-chain, and a γ-chain which form a cross-like structure that bind to cell membranes and other ECM proteins. Laminins contribute to cell attachment, differentiation, and motility.

Our highly purified laminin is quality tested by SDS-PAGE and ELISA to ensure purity. It has been used in adhesion and migration assays.

SouthernBiotech offers polyclonal and monoclonal antibodies to ECM proteins including collagens, fibronectin, and matrix metalloproteinases. They are frequently used in ELISA, immunohistochemistry / immunocytochemistry, electron microscopy, western blotting, and immunoprecipitation.