| Catalog_no | AB1039 |
| Product_name | CRYBA1 Antibody (Center) |
| Category | 抗原抗体 |
| Applications | WB, IHC-P |
| Reactivity | H, M |
| Size | 100μL/50μL |
| Price | 2000.00/1100.00 |
| immunogen | HUMAN:104-133 |
| Specificity | This CRYBA1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 104-133 amino acids from the Central region of human CRYBA1. |
| Dilution | WB,1:1000;WB,1:1000;IHC-P,1:10~50; |
| Purification | 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. |
| othername | Beta-crystallin A3, Beta-crystallin A3, isoform A1, Delta4 form, Beta-crystallin A3, isoform A1, Delta7 form, Beta-crystallin A3, isoform A1, Delta8 form, CRYBA1, CRYB1 |
| Isotype | Rabbit Ig |
| 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, 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'. |
| Instructions | 
查看与下载 |
| Share |
|
