Beta crystallin S (CRYGS) Rabbit Polyclonal Antibody

Specifications

Product Data
Applications	WB
Recommend Dilution	WB: 500-2000 WB positive control: Mouse eye tissue lysate
Reactivity	Human, Mouse, Rat
Host	Rabbit
Clonality	Polyclonal
Immunogen	Full length fusion protein
Formulation	pH7.4 PBS, 0.05% NaN3, 40% Glycerol
Concentration	lot specific
Purification	Antigen affinity purification
Conjugation	Unconjugated
Storage Condition	Store at -20°C.
Predicted Protein Size	21 kDa
Gene Name	crystallin gamma S
Database Link	Entrez Gene 1427 Human UniProt ID P22914
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.
Synonyms	CRYG8; Gamma-S-crystallin; GRYG8; OTTHUMP00000210173
Reference Data

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