γS-crystallin Antibody (E-9): sc-515095
- γS-crystallin Antibody (E-9) is a mouse monoclonal IgG1 κ provided at 200 µg/ml
- raised against amino acids 66-115 mapping within an internal region of γS-crystallin of human origin
- recommended for detection of γS-crystallin of mouse, rat and human origin by WB, IP, IF and ELISA
- m-IgG Fc BP-HRP and m-IgG1 BP-HRP are the preferred secondary detection reagents for γS-crystallin Antibody (E-9) for WB applications. These reagents are now offered in bundles with γS-crystallin Antibody (E-9) (see ordering information below).
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γS-crystallin Antibody (E-9) is a mouse monoclonal IgG1 antibody that detects γS-crystallin in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). γS-crystallin, also known as Beta-crystallin S, is a 178 amino acid protein characterized by its monomeric form and unique two-domain beta structure, which is crucial for maintaining lens transparency and refractive index in the eye. Anti-γS-crystallin antibody (E-9) belongs to the beta/gamma-crystallin gene family and is mapped to human chromosome 3. γS-crystallin′s structural integrity is vital, as any alterations can lead to aggregation and subsequent lens opacity, a hallmark of congenital cataracts. γS-crystallin monoclonal antibody (E-9) is particularly valuable for researchers studying the molecular mechanisms underlying lens transparency and cataract formation, providing insights into potential therapeutic targets for eye disorders.
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γS-crystallin Antibody (E-9) References:
- Gamma crystallins of the human eye lens. | Vendra, VP., et al. 2016. Biochim Biophys Acta. 1860: 333-43. PMID: 26116913
- Deamidation of N76 in human γS-crystallin promotes dimer formation. | Ray, NJ., et al. 2016. Biochim Biophys Acta. 1860: 315-24. PMID: 26318015
- Divalent Cations and the Divergence of βγ-Crystallin Function. | Roskamp, KW., et al. 2019. Biochemistry. 58: 4505-4518. PMID: 31647219
- The cataract-related S39C variant increases γS-crystallin sensitivity to environmental stress by destroying the intermolecular disulfide cross-links. | Yang, X., et al. 2020. Biochem Biophys Res Commun. 526: 459-465. PMID: 32234236
- Human γS-Crystallin-Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage. | Roskamp, KW., et al. 2020. Biochemistry. 59: 2371-2385. PMID: 32510933
- Cataract-causing G18V eliminates the antagonization by ATP against the crowding-induced destabilization of human γS-crystallin. | He, Y., et al. 2020. Biochem Biophys Res Commun. 530: 554-560. PMID: 32753316
- Human γS-Crystallin Resists Unfolding Despite Extensive Chemical Modification from Exposure to Ionizing Radiation. | Norton-Baker, B., et al. 2022. J Phys Chem B. 126: 679-690. PMID: 35021623
- Acquired Disorder and Asymmetry in a Domain-Swapped Model for γ-Crystallin Aggregation. | Sagar, V. and Wistow, G. 2022. J Mol Biol. 434: 167559. PMID: 35341744
- Impact of hydrogen peroxide on structure, stability, and aggregational properties of human γS-crystallin. | Vendra, VPR. 2023. J Biosci. 48: PMID: 36856090
- The 18th amino acid glycine plays an essential role in maintaining the structural stabilities of γS-crystallin linking with congenital cataract. | Zhu, S., et al. 2023. Int J Biol Macromol. 251: 126339. PMID: 37586630
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
γS-crystallin Antibody (E-9) | sc-515095 | 200 µg/ml | $316.00 | |||
γS-crystallin Antibody (E-9): m-IgG Fc BP-HRP Bundle | sc-541027 | 200 µg Ab; 10 µg BP | $354.00 | |||
γS-crystallin Antibody (E-9): m-IgG1 BP-HRP Bundle | sc-542539 | 200 µg Ab; 20 µg BP | $354.00 |