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Alpha B Crystallin ELISA Kit
Colorimetric detection of alpha B Crystallin
Artikelnummer
STRSKT-123-96
Verpackungseinheit
96 well
Hersteller
Stressmarq Biosciences
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Target: alpha B Crystallin
Product Type: ELISA Kits
Trademark: StressXpress®
Detection Method: Colorimetric Assay
Assay Type: Sandwich ELISA (Enzyme-linked Immunosorbent Assay)
Utility: ELISA kit used to quantitate alpha B crystallin concentration in samples.
Sample Type(s): Cell Lysates,Tissue,Serum
Number of Samples: 40 samples in duplicate
Incubation Time: 30 minutes
Sensitivity: 0.009 ng/ml
Assay Range: 0.352 - 22.5 ng/ml
Scientific Background: 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, 4, 5, 6, and 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).
References: 1. Merck K.B. et al. (1993) J Biol Chem. 268: 1046-1052.2. Horwitz J. (1992) Proc Natl Acad Sci USA 89(21): 10449-10453.3. Cobb B.A. and Petrash J.M. (2002) Biochemistry. 41: 483-4904. Horwitz J. (2003) Exp Eye Res. 76: 145-153.5. Bullard B. et al. (2004) J Biol Chem. 279: 7917-7924.6. Gangalum R.K., Schibler M.J. and Bhat S.P. (2004) J Biol Chem. 279: 43374.43377.7. Maddala R. and Rao V.P. (2005) Exp Cell Res. 306: 203-215.8. Yaung J., et al. (2007) Molecular Vision 13: 566-577.9. Head M.W. et al. (2000) Neuropathol Appl Neurobiol. 26: 304-312.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
Product Type: ELISA Kits
Trademark: StressXpress®
Detection Method: Colorimetric Assay
Assay Type: Sandwich ELISA (Enzyme-linked Immunosorbent Assay)
Utility: ELISA kit used to quantitate alpha B crystallin concentration in samples.
Sample Type(s): Cell Lysates,Tissue,Serum
Number of Samples: 40 samples in duplicate
Incubation Time: 30 minutes
Sensitivity: 0.009 ng/ml
Assay Range: 0.352 - 22.5 ng/ml
Scientific Background: 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, 4, 5, 6, and 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).
References: 1. Merck K.B. et al. (1993) J Biol Chem. 268: 1046-1052.2. Horwitz J. (1992) Proc Natl Acad Sci USA 89(21): 10449-10453.3. Cobb B.A. and Petrash J.M. (2002) Biochemistry. 41: 483-4904. Horwitz J. (2003) Exp Eye Res. 76: 145-153.5. Bullard B. et al. (2004) J Biol Chem. 279: 7917-7924.6. Gangalum R.K., Schibler M.J. and Bhat S.P. (2004) J Biol Chem. 279: 43374.43377.7. Maddala R. and Rao V.P. (2005) Exp Cell Res. 306: 203-215.8. Yaung J., et al. (2007) Molecular Vision 13: 566-577.9. Head M.W. et al. (2000) Neuropathol Appl Neurobiol. 26: 304-312.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
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