Anti-TIMP1, clone rTIMP1/1710

1 mg/ml in 1X PBS, BSA free, sodium azide free. 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 is identical to EPA (erythroid-potentiation activity). PTH 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 tissues. Studies have demonstrated that TIMP1 is useful as a biomarker for early detection of colorectal cancer, outperforming CEA. Additionally, TIMP1 studies have demonstrated its role in CRC tumorigenesis, as well as observing its overexpression in metastatic lymph nodes. Protein function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro, but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. [The UniProt Consortium]