Description
The LANCE® Ultra Human MMP-7 Detection Kit is designed for detection and quantitation of human MMP-7 in buffered solution and cell culture media using a homogeneous TR-FRET (no-wash steps, no separation steps) assay.
No-wash steps, no separation steps
TR-FRET technology
Sensitive detection
High reproducibility
Faster time-to-results
Easy automation
96-well, 384-well, and 1536-well formats
LANCE® and LANCE® (Lanthanide chelate excite) Ultra are our TR-FRET (time-resolved fluorescence resonance energy transfer), homogeneous (no wash) technologies. One antibody of interest is labeled with a donor fluorophore (a LANCE Europium chelate) and the second molecule is labeled with an acceptor fluorophore (ULight™ dye). Upon excitation at 320 or 340 nm, energy can be transferred from the donor Europium chelate to the acceptor fluorophore if sufficiently close for FRET (~10 nm). This results in the emission of light at 665 nm.
MMP-7 (Matrylisin) is a proteolytic enzyme belonging to Matrix Metalloproteinase (MMPs) family which consists of 24 known human zinc and calcium proteases with essential roles in breaking down components of the extracellular matrix (ECM). MMPs share common structural motifs including a pro-peptide domain, a catalytic domain, a hinge region, and a hemopexin-like domain. Synthesized as pro-enzymes, most MMPs are secreted before conversion to their active form. Structurally, MMP-7 is the smallest of the MMPs and consists of two domains: a pro-domain that is cleaved upon activation and a catalytic domain containing the zinc-binding site which can degrade a wide range of extracellular matrix including collagen IV and X, gelatin, casein, laminin, aggrecan, entactin and elastin and also activate several other MMPs. MMP-7 is expressed in epithelial cells of normal and diseased tissues and plays key roles in connective tissue remodeling and cancer metastasis.
