B-Crystallin ELISA Kit

Storage

Store all components at 4°C. See page 3 for storage of reconstituted material.

Performance Characteristics

Typical Data
The results shown below are for illustration only and should not be used to interpret results from another assay.


Sensitivity
The sensitivity, or limit of detection, of this assay is 0.59 ng/mL. It was determined by interpolation at 2 standard deviations above the mean signal at background, using data from 5 standard curves.

Specificity
This assay detects human, mouse, rat, and bovine αB-Crystallin. Cross reactivity with γ-Crystallin and αA-Crystallin is 0.06% and 0.4%, respectively. There is no cross reactivity observed with ?βL-Crystallin, Hsp10, Hsp25 and Hsp27.

Dilutional Linearity
To determine possible interference from the sample matrix, the indicated sample types were serially diluted into assay buffer. The concentrations of αB-Crystallin were measured in the assay, and the results were analyzed to determine the range over which a linear response was obtained. These data may be used as a guideline to determine minimal recommended dilution (MRD) for similar samples.

CL: Cell Lysate

Parallelism
Dose-response curves from cell lysates diluted into assay buffer (using the MRD) were compared to the recombinant αB-Crystallin standard curve. Parallelism indicates that the antibody-binding characteristics of the native and standard proteins are similar, allowing accurate determination of the analyte.

General Description

α-crystallins composed of ~20 kDa αA and αB subunits function asmajor water-soluble proteins accounting for almost 50% of total protein in the mammalian transparent eye lens, also existing in a variety of other tissues. The α-crystallin proteins are members of the small heat shock protein (sHsp) family, as their expression can be induced by heat and other stress insults in a variety of organisms. The α-crystallins possess structural and functional similarities and share sequence homology with Hsp25/27. The conserved α-crystallin domain participates in oligomer assembly, which is critical to their function in the prevention of irreversible protein aggregation.