|Application ||WB, E|
|Other Accession||P10067, NP_008822.2|
|Calculated MW||20738 Da|
|Antigen Region||73-101 aa|
|Other Names||Gamma-crystallin D, Gamma-D-crystallin, Gamma-crystallin 4, CRYGD, CRYG4|
|Target/Specificity||This CRYGD antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 73-101 amino acids from the Central region of human CRYGD.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CRYGD Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Crystallins are the dominant structural components of the vertebrate eye lens.|
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Provided below are standard protocols that you may find useful for product applications.
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. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
Acosta-Sampson, L., et al. J. Mol. Biol. 401(1):134-152(2010)
Wang, Y., et al. Proc. Natl. Acad. Sci. U.S.A. 107(30):13282-13287(2010)
Pande, A., et al. Biochemistry 49(29):6122-6129(2010)
Das, P., et al. Protein Sci. 19(1):131-140(2010)
Roshan, M., et al. Mol. Vis. 16, 887-896 (2010) :
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