CRYGS
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Official Full Name
crystallin, gamma S -
Overview
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. -
Synonyms
CRYGS;crystallin, gamma S;CRYG8;beta-crystallin S;crystallin;gamma 8;rncat;AI327013;CRBS_HUMAN;Crystallin, gamma 8;Crystallin, gamma polypeptide 8;Gamma crystallin S;Gamma S crystallin;Gamma-crystallin S;Gamma-S-crystallin;Opacity due to poor secondary fiber cell junction;recessive nuclear cataract;Opj;OTTHUMP00000210173;OTTHUMP00000210174
Recombinant Proteins
- Human
- Mouse
- Rat
- Chicken
- E.coli
- Mammalian Cell
- Wheat Germ
- Human
- HEK293
- In Vitro Cell Free System
- His
- His&T7
- GST
- Non
- His&Fc&Avi
- Myc&DDK
Involved Pathway
CRYGS involved in several pathways and played different roles in them. We selected most pathways CRYGS participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with CRYGS were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
Protein Function
CRYGS has several biochemical functions, for example, structural constituent of eye lens. Some of the functions are cooperated with other proteins, some of the functions could acted by CRYGS itself. We selected most functions CRYGS had, and list some proteins which have the same functions with CRYGS. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| structural constituent of eye lens | HSPB6,CRYAA,ATXN1,LIM2.2,CRYGF,CRYBB2,CRYGC,ASL1,CRYBB1,CRYBA1 |
Interacting Protein
CRYGS has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with CRYGS here. Most of them are supplied by our site. Hope this information will be useful for your research of CRYGS.
TINF2;POT1;TERF2IP
Resources
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References
- Moody, IS; Verde, SC; et al. In vitro evolution of an HIV integrase binding protein from a library of C-terminal domain gamma S-crystallin variants. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS 22:5584-5589(2012).
- Chidlow, G; Daymon, M; et al. Localization of a Wide-Ranging Panel of Antigens in the Rat Retina by Immunohistochemistry: Comparison of Davidson's Solution and Formalin as Fixatives. JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY 59:884-898(2011).
