Cat # changed from RSKT-123R to SKT-123-96
Type
Sandwich ELISA, Biotin-labelled antibody
Applications
Serum, Tissue extract, Cell lysate
Storage/Expiration
2–8°C
Calibration Curve
Calibration Range
0.352–22.5 ng/mL
Limit of Detection
0.009 ng/mL
Features
- ELISA kit used to quantitate alpha B crystallin concentration in samples
- The total assay time is less than 4 hours
Research topic
Others
Summary
The alpha-crystallins are major water-soluble lens structural proteins of the vertebrate eye that are related to the small heat shock protein family. The alpha-crystallins possess
structural and functional similarities with Hsp25 and Hsp27 (1). Mammalian lens
cystallins are divided into alpha, beta and gamma families. Alpha and beta families are
further divided into acidic and basic groups (Alpha-A and Alpha-B respectively). In the
lens, alpha-crystallin primarily functions to maintain proper refractive index, however it
can also function as a molecular chaperone that binds to the denatured proteins, keeping
them in solution and thereby maintaining the translucency of the lens. When cellular stress
occurs, alpha-crystallin enters its’ phosphorylated state and may serve a structural control
function and play a role in protein maintenance (2). In addition to their interaction with
proteins, alpha-crystallins also interact with native molecules such as membrane proteins,
Golgi matrix protein, structural proteins, nuclear proteins and DNA (3-7). Two other
functions are an autokinase activity and participation in the intracellular architecture, and it
has also been proven that both alpha-A and B prevent apoptosis by inhibiting caspases (8).
Specifically, alpha-B cystallin is found in many cells and organs outside the lens, and alpha
B is overexpressed in several neurological disorders and in cell lines under stress conditions
(9)
Instructions for Use (RUO)
Instructions for Use (RUO)
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