Human Complement factor D enzyme-linked immunoassay kit(one step)

CAT: EHY0242 Datasheet
Specification 96 Test
Sensitivity 0.01 ng/ml (10 μl)
Standard Curve Range 0.41~300 ng/ml
Standard Curve Gradient 7 Points/3 Folds
Number of Incubations 2
Detectable sample serum, plasma
Sample Volume 10 μl
Type Fully Ready-to-Use
Operation Duration 60min
ng/ml O.D. Average Corrected
0.00 0.0089 0.0083 0.0086
0.41 0.0171 0.0172 0.0172 0.0086
1.23 0.0395 0.0399 0.0397 0.0311
3.70 0.1106 0.1147 0.1127 0.1041
11.11 0.3221 0.3323 0.3272 0.3186
33.33 0.9434 0.9330 0.9382 0.9296
100.00 2.4900 2.4320 2.4610 2.4524
300.00 4.3547 4.3549 4.3548 4.3462

Precision

Intra-assay Precision Inter-assay Precision
Sample Number S1 S2 S3 S1 S2 S3
22 22 22 6 6 6
Average(ng/ml) 4.9 24.7 90.1 5.1 25.9 94.7
Standard Deviation 0.1 0.7 3.8 0.2 1.1 4.2
Coefficient of Variation(%) 2.1 2.7 4.2 4.1 4.1 4.4

Intra-assay Precision (Precision within an assay) Three samples of known concentration were tested twenty-two 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 Complement factor D into health human serum sample. The un-spiked serum was used as blank in this experiment.
The recovery ranged from 92% to 105% with an overall mean recovery of 98%.

Sample Values

Sample Matrix Sample Evaluated Range (ng/ml) Detectable (%) Mean of Detectable (ng/ml)
Serum30433.18-943.01100713.99

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

Background: Complement factor D

Complement Factor D, also known as adipsin, is a serine protease that catalyzes the initial proteolytic step in the alternative pathway of complement. It is an exceptionally specific protease and the only known protein substrate is factor B in complex with C3.3 Factor D protease activity is regulated by reversible conformational changes, which differs from the majority of serine proteases whose regulation involves either activation by processing of the zymogens or inactivation by binding of the inhibitors.

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