All cells within tissues are surrounded by an extracellular matrix (ECM) giving the tissues shape and structure. The ECM is constantly being remodeled and constant communication is maintained between cells through this matrix. Secreted proteins, termed matrix metalloproteinases (MMPs), are involved in the modulation of cell matrix interactions. MMPs are Zn2+ binding endopeptidases that degrade various components of the ECM. MMPs are enzymes implicated in normal and pathologic tissue remodeling processes, wound healing, angiogenesis, and tumor invasion. These enzymes are very potent when active, and are associated with extracellular space inhibitors called TIMPs (tissue inhibitors of matrix metalloproteinases). MMP1, also known as interstitial collagenase, is the only enzyme able to initiate the breakdown of the interstitial collagens, types I, II, and III.

Additional sequence homology is noted with mouse (81%) and rat (75%).

The antibody recognizes an internal domain of human MMP-1 containing the hinge region. It does not cross react with MMP-2, MMP-9, or MMP-13.

KLH-conjugated synthetic peptide corresponding to the hinge region of human MMP-1.

Anti-MMP-1 Antibody, hinge region is an antibody against MMP-1 for use in WB.

Evaluated on a representative lot by Western blot on A431 cell lysate.

Western Blot Analysis: 0.5 µg/ml of this antibody detected MMP-1 on 10 µg of A431 cell lysate.

54 kDa In Western Blot, bands around 53 kDa and 51 kDa (proenzyme) are observed in reduced proteins.

Replaces: 04-1122

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.