Type I and Type II Collagen, FITC Conjugated,
Exalpha's Collagen Type I FITC and Collagen Type II FITC are highly purified telo-peptide free. Type I is extracted from bovine skin tissue and Type II is extracted from bovine articular cartilage. To minimize background levels in collagenase assays, FITC-labeled collagens are enzymatically pre-treated and further purified by ion-exchange chromatography. They are suitable for use as substrates for mammalian collagenases in a fluorimetric assay procedures (1,2,3,4).
for Collagenase Assays
For collagenase assays in cell culture, the degradation products may be detected directly in the culture medium by fluorescence spectroscopy using an excitation wavelength of 490 nm and an emission wavelength of 520 nm.
About Collagens and Collagenases:
Type I collagen is the major collagen of tendon and bone, but it is widely distributed in other tissues, such as skin, cornea, tooth dentin, heart valve, lung, liver, fascia, and scar tissue. Type II collagen is a major component of cartilage, while type III collagen is a major component of large blood vessels. These three collagen types form fibrils that are stabilized by the crosslinking of adjacent collagen molecules both within and between fibrils. Collagen fibrils strengthen the tissue in which they are located.
Collagenases and gelatinases are members of a group of secreted zinc metalloproteases (MMP) that, in mammals, degrade the collagens of the extracellular matrix. Collagenase-1 (MMP1, interstitial collagenase) is the principal enzyme involved in initiating the breakdown of fibrillar collagens, types I and III while both collagenase 1, and collagenase 3 (MMP13) appear to be involved in the breakdown of type II collagen. Gelatinases degrade denatured collagens and the nonfibrillar type IV (basement membrane) collagen. Since collagens are the most abundant proteins in the body, collagenases play a key role in the remodeling that occurs in normal and disease processes. Additional function of MMPs, they are capable of degrading all kinds of extracellular matrix proteins, and also can process a number of bioactive molecules. They are involved in the cleavage of cell surface receptors, the release of apoptotic ligands (such as the FAS ligand), and chemokine/cytokine in/activation. MMPs also play a major role on cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
MMPs are zinc-dependent endopeptidases; other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily. They were first described in vertebrates (1962), including humans, but have since been found in invertebrates and plants. They are distinguished from other endopeptidases by their dependence on metal ions as cofactors, their ability to degrade extracellular matrix.
|Cat. No.||Name||Product Type||Size|
|X1098||Bovine Type I Collagen||FITC Conjugate||100 Tests (10 mg)|
|X1099||Bovine Type II Collagen||FITC Conjugate||100 Tests (10 mg)|
Collagen and Collagenase related products
|Cat. No.||Name||Product Type||Size|
|X2053M||Matrix Metalloproteinase 1 (MMP1)||Monoclonal Antibody||200 µg|
|X2054M||Matrix Metalloproteinase 2 (MMP2)||Monoclonal Antibody||200 µg|
|X2056M||Matrix Metalloproteinase 9 (MMP9)||Monoclonal Antibody||200 µg|
|X2057M||Matrix Metalloproteinase 9 (MMP9)||Monoclonal Antibody||200 µg|
|X2219P||Matrix Metalloproteinase 9 (MMP9)||Antigen Affinity Purified Polyclonal||50 µg|
|X2220P||Matrix Metalloproteinase 9 (MMP9)||Antigen Affinity Purified Polyclonal||200 µg|