Crystallin, gamma S (CRYGS) (C-Term), (AA 136-166) antibody

Details for Product No. ABIN950652
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Antigen
Synonyms CRYG8, CTRCT20, AI327013, Opj, rncat
Epitope
C-Term, AA 136-166
(11), (7), (3), (1), (1), (1)
Reactivity
Human, Mouse (Murine)
(38), (30), (26), (24), (24), (24)
Host
Rabbit
(38), (2)
Clonality
Polyclonal
Conjugate
Un-conjugated
(3), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1)
Application
ELISA, Western Blotting (WB)
(22), (20), (8), (6), (2), (2), (1)
Pubmed 5 references available
Quantity 0.4 mL
Shipping to United States (Change)
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Catalog No. ABIN950652
357.50 $
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Immunogen KLH conjugated synthetic peptide between 136-166 amino acids from the C-terminal region of human CRYGS
Specificity This antibody reacts to human and mouse CRYGS.
Purification Affinity chromatography on Protein A
Alternative Name Beta-crystallin S
Background Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families, beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C- terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
Alternate names: CRYGS, GRYG8, Gamma-S-crystallin, Gamma-crystallin S
Gene ID 1427
NCBI Accession NP_060011
Restrictions For Research Use only
Format Liquid
Concentration 0.25 mg/mL
Buffer PBS 0.09% (w/v) sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer.
Expiry Date 12 months
Background publications Mills, Flaugh, Kosinski-Collins et al.: "Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin." in: Protein science : a publication of the Protein Society, Vol. 16, Issue 11, pp. 2427-44, 2007 (PubMed).

Vanita, Singh, Singh et al.: "Novel mutation in the gamma-S crystallin gene causing autosomal dominant cataract." in: Molecular vision, Vol. 15, pp. 476-81, 2009 (PubMed).

Chen, Callis, King: "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." in: Biochemistry, Vol. 48, Issue 17, pp. 3708-16, 2009 (PubMed).

Ma, Piszczek, Wingfield et al.: "The G18V CRYGS mutation associated with human cataracts increases gammaS-crystallin sensitivity to thermal and chemical stress." in: Biochemistry, Vol. 48, Issue 30, pp. 7334-41, 2009 (PubMed).

Acosta-Sampson, King: "Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone." in: Journal of molecular biology, Vol. 401, Issue 1, pp. 134-52, 2010 (PubMed).

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