Anti-CRYBA2 monoclonal antibody (DCABH-11138) Made to order

Rabbit anti-Human CRYBA2 monoclonal antibody for WB, ELISA

View other CRYBA2 antibodies

Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Species Reactivity
Human
Immunogen
A synthetic peptide of human CRYBA2 is used for rabbit immunization.
Conjugate
Unconjugated

Target


Alternative Names
CRYBA2; crystallin, beta A2; beta-crystallin A2; eye lens structural protein
Entrez Gene ID
UniProt ID

Product Background


Gene summary
CRYBA2 (Crystallin Beta A2) is a Protein Coding gene. Diseases associated with CRYBA2 include cataract 42 and early-onset anterior polar cataract. GO annotations related to this gene include protein homodimerization activity and structural constituent of eye lens. An important paralog of this gene is CRYGC. Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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 but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported.
Antigen Description
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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 but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported. Cataract 42 (CTRCT42) [MIM:115900]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. Note=The disease is caused by mutations affecting the gene represented in this entry. The function about CRYBA2 antigen include molecular_function; protein homodimerization activity; structural constituent of eye lens.

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References


Graw, J; Klopp, N; et al. Ethylnitrosourea-induced mutation in mice leads to the expression of a novel protein in the eye and to dominant cataracts. GENETICS 157:1313-1320(2001).
Graw, J; Neuhauser-Klaus, A; et al. Ethylnitrosourea-induced base pair substitution affects splicing of the mouse gamma E-crystallin encoding gene leading to the expression of a hybrid protein and to a cataract. GENETICS 161:1633-1640(2002).

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