Clone: 2A5.
Background: TIMP-1, TIMP-2, TIMP-3 and TIMP-4 (for tissue inhibitor of metalloproteinases-1, -2, -3 and -4) complex with metalloproteinases such as collagenases, gelatinases and stromelysins, resulting in irreversible inactivation of the metalloproteinase. TIMP-1 was found to be identical to EPA (erythroidpotentiation activity). Parathyroid hormone has been shown to be a regulator of TIMP-2 in osteoblastic cells. TIMP-3 may be involved in regulating trophoblastic invasion of the uterus as well as in regulating remodeling of the extracellular matrix during the folding of epithelia, and in the formation, branching and expansion of epithelial tubes. TIMP-4 is most highly expressed in heart and low levels of TIMP-4 are expressed in liver, brain, lung, thymus and spleen.
Positive Control: Colon and gastric tissues. Stronger expression observed in tumor versus normal protein.
Immunogen: Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the human TIMP-1 protein and mouse myeloma Ag8563 cells. Sequence common in monkey.
Purification Method: Protein A/G Chromatography.
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide.
References: 1. Hoikkala, S., et al. (2006). Tissue MMP-2 and MMP-9 [corrected] are better prognostic factors than serum MMP-2/TIMP-2--complex or TIMP-1 [corrected] in stage [corrected] I-III lung carcinoma. Cancer Lett. 236(1):125-132
2. Bodden, M.K., et al. (1994). Functional domains of human TIMP-1 (tissue inhibitor of metalloproteinases). J. Biol. Chem. 269(29):18943-18952.
UniProt: P01033 (Human)
Q95KL9 (Macaca).
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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