TIMP-3 Antibody (MM0036-7D3) - Azide and BSA Free

The tissue inhibitors of metalloproteinases (TIMPs) are naturally occurring proteins that specifically inhibit matrix metalloproteinases and regulate extracellular matrix turnover and tissue remodeling by forming tightly bound inhibitory complexes with the MMPs. Thus, TIMPs maintain the balance between matrix destruction and formation. An imbalance between MMPs and the associated TIMPs may play a significant role in the invasive phenotype of malignant tumors. TIMP proteins share several structural features including six loops held in place by six disulfide bonds arranged in three knot like structures. The N terminal region is necessary for inhibitory activity. The N terminus of each TIMP contains a consensus sequence (VIRAK) and each TIMP is translated with a 29 amino acid leader sequence that is cleaved to produce the mature protein. The C terminal regions are divergent and enhance the inhibition selectivity and binding efficiency. Although the TIMP proteins share high homology, following secretion they are localized extracellularly either in soluble form (TIMP1, TIMP2, and TIMP4) or bound to extracellular matrix components (TIMP3). The MMPs and TIMPs can be divided into two groups with respect to gene expression: the majority exhibit inducible expression and a small number are produced constitutively or are expressed at very low levels and are not inducible. Among agents that induce MMP and TIMP production are the inflammatory cytokines TNF alpha and IL beta. A marked cell type specificity is a hallmark of both MMP and TIMP gene expression (i.e. a limited number of cell types can be induced to make these proteins). Tissue Inhibitor of Metalloproteinase 3 (TIMP3) was first purified from chicken embryo fibroblasts and identified as ChIMP3. The human homologue of TIMP3, was originally detected as an inducible serum protein in WI-38 fibroblasts. The TIMP3 localization differs from that of the other three TIMPs, and is thought to be primarily deposited into the extracellular matrix (ECM). TIMP3 is insoluble, binds to the ECM associated with a variety of cell types, and is widely distributed throughout the body. TIMP3 shows 30% amino acid homology with TIMP1 and 38% homology with TIMP2. TIMP3 has been shown to promote the detachment of transformed cells from ECM and to accelerate morphological changes associated with cell transformation. Furthermore, up regulation of TIMP 3 has been associated with a block in the G1 phase of the cell cycle during differentiation of HL60 leukemia cells. The human TIMP3 gene has the chromosomal location of 22q12-22q13. TIMP3 mRNA is highly expressed in placenta but is also found in the heart, kidney, lung, pancreas, uterus and skeletal muscle with low levels in the brain. In endometrium, TIMP3 is reported to be expressed in luminal epithelium, glands, stroma, endothelial cells and vascular smooth muscle cells. TIMP3 is also reported to be expressed by fibroblast like cells in ulcerated intestinal wall.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 1 confirmed species: Human.

Showing Publication 1 - 1 of 1.

Publication using NB110-61002	Applications	Species
Jeronimo A, Rodrigues G, Vilas-Boas F et al. Hydrogen peroxide regulates angiogenesis-related factors in tumor cells Biochem. Cell Biol. 2017-08-17 [PMID: 28817784] (Human)		Human

Array NB110-61002

• TIMP-3 Antibodies
• TIMP-3 ELISA Kit
• TIMP-3 Lysate
• TIMP-3 Proteins and Enzyme
• TIMP-3 ELISA