96 Tests PN:B115623
Components:
45x Ab-conjugated beads (S5P6- Human MMP-2 ab-bead). PN: B115623A. One vial containing 100 µL of anti-human MMP-2 conjugated to AimPlex Bead S5P6.
25x Biotin-detection Ab (Human MMP-2 Biotin-dAb). PN B115623B. One vial containing 100 µL of biotinylated anti- Human MMP-2.
Lyophilized Standard Mix - Human MMP-2. PN: B115623S. One vial containing lyophilized MMP-2.
Applications: Optimal antibody pair and antigen standard for assaying human Human MMP-2/Gelatinase A. To be used in conjunction with the AimPlex NR Basic Kit (PN: P100001) and a diluent kit. Refer to the AimPlex Multiplex Immunoassay User Manual and kit inserts for the assay procedure.
Storage: 2-8 C in the dark.
Important: Sodium azide forms explosive compounds with heavy metals. These products contain <0.05% (w/w) azide which with repeated contact with lead and copper commonly found in plumbing drains may result in the buildup of shock sensitive compounds. Dispose in accordance with regulations from your institute.
For Research Use Only. Not for use in diagnostic procedures.
Assay Specifications:
Sample types: Cell culture supernatant, serum, plasma, bodily fluid and tissue/cell lysate
Sensitivity (LOD): < 200 pg/mL
Quantitation range:
LLOQ: < 400 pg/mL
ULOQ: > 50,000 pg/mL
Standard dose recovery: 70-130%
Intra-assay CV: < 10%
Inter-assay CV: < 20%
Sample volume: 15 µL/test
Description:
MMP-2/Gelatinase A (Accession P08253) is a member of the matrix metalloprotease family. It is a zinc-dependent endopeptidase created in cells throughout the body and becomes part of the extracellular matrix. Unlike other members of the matrix metalloprotease family, MMP-2 can be activated on the cell membrane as well as intracellularly by its S-glutathiolation without removing its pro-domain. MMP-2 functions to cleave protein type IV collagen. MMP-2 is involved in multiple pathways, including the nervous system. It also plays a role in repairing damaged tissues and bone remodeling, as well as breakdown of the endometrium during menstruation, cardiac remodeling, and inflammation. In conjunction with MMP-9, MMP-2 expression is correlated with various cancers such as urogenital, brain, intraocular, lung, and colorectal.
References:
Corbel, M, Boichot, E, Lagente, V. Role of gelatinases MMP-2 and MMP-9 in tissue remodeling following acute lung injury. Braz J Med Biol Res. 2000; 33(7) 749-754. doi: 10.1590/S0100-879X2000000700004.
Klein T, Bischoff R. Physiology and pathophysiology of matrix metalloproteases. Amino Acids. 2011;41(2):271–290. doi:10.1007/s00726-010-0689-x.
Nagase, H, Visse, R, Murphy, G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovascular Research. 2006; 69(3). doi: 10.1016/j.cardiores.2005.12.002.
Webb AH, Gao BT, Goldsmith ZK, Irvine AS, Saleh N, Lee RP, Lendermon JB, Bheemreddy R, Zhang Q, Brennan RC, Johnson D, Steinle JJ, Wilson MW, Morales-Tirado VM. Inhibition of MMP-2 and MMP-9 decreases cellular migration, and angiogenesis in in vitro models of retinoblastoma. BMC Cancer. 2017; 17 (4). doi: 10.1186/s12885-017-3418-y.