Human MMP-8 enzyme-linked immunoassay kit

CAT: EH0103 Datasheet
Specification 96 Test
Sensitivity 1.59 pg/ml (50 μl);9.04 pg/ml (10 μl)
Standard Curve Range 13.72~10000 pg/ml
Standard Curve Gradient 7 Points/3 Folds
Number of Incubations 2
Sample Volume 50 μl/10 μl
Type Fully Ready-to-Use
Operation Duration 120min
pg/ml O.D. Average Corrected
0.00 0.0162 0.0172 0.0167
13.72 0.0324 0.0377 0.0351 0.0184
41.15 0.0650 0.0718 0.0684 0.0517
123.46 0.1828 0.1977 0.1903 0.1736
370.37 0.4943 0.5266 0.5105 0.4938
1111.11 1.1880 1.2360 1.2120 1.1953
3333.33 2.5860 2.9120 2.7490 2.7323
10000.00 4.2764 4.3073 4.2919 4.2752

Precision

Intra-assay Precision Inter-assay Precision
Sample Number S1 S2 S3 S1 S2 S3
22 22 22 6 6 6
Average(pg/ml) 195.0 1021.4 3035.2 184.8 986.8 2963.6
Standard Deviation 11 41.3 92.6 7.4 18.4 97.6
Coefficient of Variation(%) 5.7 4.0 3.0 4.0 1.9 3.3

Intra-assay Precision (Precision within an assay) Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.

Inter-assay Precision (Precision between assays) Three samples of known concentration were tested six times on one plate to assess intra-assay precision.

Spike Recovery

The spike recovery was evaluated by spiking 3 levels of human MMP-8 into health human serum sample. The un-spiked serum was used as blank in this experiment.
The recovery ranged from 84% to 100% with an overall mean recovery of 91%.

Sample Values

Sample Matrix Sample Evaluated Range (ng/ml) Detectable (%) Mean of Detectable (ng/ml)
Serum 30 4.84-76.92 100 23.05

Serum/Plasma – Thirty samples from apparently healthy volunteers were evaluated for the presence of VE Cadherin in this assay. No medical histories were available for the donors.

Background: MMP-8

The matrix metalloproteinases (MMPs) consist of 24 known human zinc proteases with essential roles in breaking down components of the extracellular matrix (ECM). Additional MMP substrates include cytokines, chemokines, growth factors and binding proteins, cell/cell adhesion molecules, and other proteinases. With a few exceptions, 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. MMP activities are modulated on several levels including transcription, pro-enzyme activation, or by their endogenous inhibitors, tissue inhibitors of metalloproteinases (TIMPs). A subset of MMPs are associated with membranes and designated as membrane-type metalloproteinases (MT-MMP).

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