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Article

Immunohistochemical localization of matrix metalloproteinase 2 and its specific inhibitor TIMP-2 in neoplastic tissues with monoclonal antibodies.

International journal of cancer - 15 Feb 1994

Höyhtyä M, Fridman R, Komarek D, Porter-Jordan K, Stetler-Stevenson W G, Liotta L A, Liang C M

Abstract excerpt

Matrix metalloproteinase-2 (MMP-2), synthesized as a 631 amino-acid proenzyme, is activated by cleavage of the first 80 amino acids and naturally inhibited by tissue inhibitor of metalloproteinase-2 (TIMP-2). We report here the production of MAbs against MMP-2 and TIMP-2 and their use in localizing the respective antigens on tumor tissues. The anti-MMP-2 MAb recognized the latent and activated MMP-2 mutant...

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Identifiers

PMID: 8112886
DOI: 10.1002/ijc.2910560408

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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