Product Name	Anti-CRYBA4/PE-Cy3
Chinese Name	PE-Cy3标记的β晶体体蛋白A4/βA4-crystallin抗体
Alias	Beta A4 crystallin; Beta crystallin A4; Beta-A4 crystallin; Beta-crystallin A4; CRBA4_HUMAN; CRYBA4; Crystallin beta A4; Crystallin, beta polypeptide A4; Eye lens structural protein; MCOPCT4; Beta-A4 crystallin.
Research Area	Cell biology  Neurobiology
Immunogen Species	Rabbit
Clonality	Polyclonal
React Species	(predicted: Human, Mouse, Rat, Dog, Pig, Cow, Horse, Sheep, )
Applications	ICC=1:50-200 IF=1:50-200  not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user.
Molecular weight	22kDa
Form	Lyophilized or Liquid
Concentration	1mg/ml
immunogen	KLH conjugated synthetic peptide derived from human CRYBA4
Lsotype	IgG
Purification	affinity purified by Protein A
Storage Buffer	0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
Storage	Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
Product Detail	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. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, is part of a gene cluster with beta-B1, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008] Function: Crystallins are the dominant structural components of the vertebrate eye lens. DISEASE: Defects in CRYBA4 are the cause of cataract zonular type 2 (CZ2) [MIM:610425]; also known as lamellar cataract 2. A form of zonular cataract. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes. Defects in CRYBA4 are a cause of microphthalmia isolated with cataract type 4 (MCOPCT4) [MIM:610426]. Microphthalmia is a clinically heterogeneous disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, cataractand other abnormalities like cataract may also be present. Similarity: Belongs to the beta/gamma-crystallin family. Contains 4 beta/gamma crystallin 'Greek key' domains. Database links: Entrez Gene: 1413 Human Entrez Gene: 12959 Mouse Omim: 123631 Human SwissProt: P53673 Human SwissProt: Q9JJV0 Mouse Unigene: 57690 Human Unigene: 40324 Mouse Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.

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