CRYBA1 DNAxPab
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Specification
Product Description
Rabbit polyclonal antibody raised against a full-length human CRYBA1 DNA using DNAx™ Immune technology.
Technology
Immunogen
Full-length human DNA
Sequence
METQAEQQELETLPTTKMAQTNPTPGSLGPWKITIYDQENFQGKRMEFTSSCPNVSERSFDNVRSLKVESGAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPICSANHKESKMTIFEKENFIGRQWEISDDYPSLQAMGWFNNEVGSMKIQSGAWVCYQYPGYRGYQYILECDHHGGDYKHWREWGSHAQTSQIQSIRRIQQ
Host
Rabbit
Reactivity
Human
Purification
Protein A
Quality Control Testing
Antibody reactive against mammalian transfected lysate.
Storage Buffer
In 1x PBS, pH 7.4
Storage Instruction
Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing.
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Applications
Western Blot (Transfected lysate)
Immunofluorescence (Transfected cell)
Flow Cytometry (Transfected cell)
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Gene Info — CRYBA1
Entrez GeneID
1411GeneBank Accession#
NM_005208.3Protein Accession#
NP_005199.2Gene Name
CRYBA1
Gene Alias
CRYB1
Gene Description
crystallin, beta A1
Gene Ontology
HyperlinkGene Summary
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, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'. [provided by RefSeq
Other Designations
crystallin, beta A3|eye lens structural protein
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