• PN: B115635

COMPONENTS

45x Ab-conjugated beads (S5P5 - Human MMP-9 Ab-bead). PN: B115635A. One vial containing 100 µL of anti-human MMP-9 conjugated to AimPlex Bead S5P5.

25x Biotin-detection Ab (Human MMP-9 Biotin-dAb). PN: B115635B. One vial containing 100 µL of biotinylated anti- Human MMP-9.

Lyophilized Standard Mix - Human MMP-9. PN: B115635S. One vial containing lyophilized MMP-9.

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.

APPLICATION: Optimal antibody pair and antigen standard for assaying human MMP-9/GELB (Total). 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.

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): < 100 pg/mL

Quantitation range:

LLOQ: <200 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:

Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is a matrixin, a class of enzymes that belong to the zinc-metalloproteinases family involved in the degradation of the extracellular matrix. MMP-9, along with elastase, appears to be a regulatory factor in neutrophil migration across the basement membrane.MMP-9 plays several important functions within neutrophil action, such as degrading extracellular matrix, activation of IL-1β, and cleavage of several chemokines. In a mouse model, MMP-9 deficiency resulted in resistance to endotoxin shock, suggesting that MMP-9 is important in sepsis. MMP-9 is greatly upregulated during human respiratory epithelial healing. Using a MMP-9 deficient mouse model, it was seen that MMP-9 coordinated epithelial wound repair and deficient mice were unable to remove the fibrinogen matrix during wound healing. MMP-9 has been found to be associated with numerous pathological processes, including cancer, immunologic and cardiovascular diseases. Diseases also associated with MMP-9 include metaphyseal anadysplasia 2 and metaphyseal anadysplasia.

References:

1.       Nagase H, Woessner JF (1999). "Matrix metalloproteinases". The Journal of Biological Chemistry 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.

2.       Wang J, Tsirka SE (2005). "Neuroprotection by inhibition of matrix metalloproteinases in a mouse model of intracerebral haemorrhage.". Brain 128 (7): 1622–33. doi:10.1093/brain/awh489. PMID 15800021.

3.       Van; Vandooren, J; den Steen, PE; Opdenakker, G. (2013). "Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9) The next decade". Crit Rev Biochem Mol Biol. 48 (3): 222–72. doi:10.3109/10409238.2013.770819. PMID 23547785.

4.       Van; den Steen, PE; Dubois, B; Nelissen, I; Rudd, PM; Dwek, RA; Opdenakker, G (2002). "Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9)".". Crit Rev Biochem Mol Biol 37 (6): 375–536. doi:10.1080/10409230290771546. PMID 12540195.