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- Product number
- ABIN950652 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Crystallin, gamma S (CRYGS) (AA 136-166), (C-Term) antibody
- Antibody type
- Polyclonal
- Description
- Affinity chromatography on Protein A
- Reactivity
- Human, Mouse
- Host
- Rabbit
- Epitope
- C-Term, AA 136-166
- Vial size
- 0.4 mL
- Storage
- Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer.
- Handling
- Avoid repeated freezing and thawing.
Submitted references Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone.
Novel mutation in the gamma-S crystallin gene causing autosomal dominant cataract.
Mechanism of the very efficient quenching of tryptophan fluorescence in human gamma D- and gamma S-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage.
The G18V CRYGS mutation associated with human cataracts increases gammaS-crystallin sensitivity to thermal and chemical stress.
Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.
Acosta-Sampson L, King J
Journal of molecular biology 2010 Aug 6;401(1):134-52
Journal of molecular biology 2010 Aug 6;401(1):134-52
Novel mutation in the gamma-S crystallin gene causing autosomal dominant cataract.
Vanita V, Singh JR, Singh D, Varon R, Sperling K
Molecular vision 2009;15:476-81
Molecular vision 2009;15:476-81
Mechanism of the very efficient quenching of tryptophan fluorescence in human gamma D- and gamma S-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage.
Chen J, Callis PR, King J
Biochemistry 2009 May 5;48(17):3708-16
Biochemistry 2009 May 5;48(17):3708-16
The G18V CRYGS mutation associated with human cataracts increases gammaS-crystallin sensitivity to thermal and chemical stress.
Ma Z, Piszczek G, Wingfield PT, Sergeev YV, Hejtmancik JF
Biochemistry 2009 Aug 4;48(30):7334-41
Biochemistry 2009 Aug 4;48(30):7334-41
Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.
Mills IA, Flaugh SL, Kosinski-Collins MS, King JA
Protein science : a publication of the Protein Society 2007 Nov;16(11):2427-44
Protein science : a publication of the Protein Society 2007 Nov;16(11):2427-44
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