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The antibody against CRYBA1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-215 of human CRYBA1 (NP_005199.2) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
The antibody against CRYBA1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-215 of human CRYBA1 (NP_005199.2) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
| Cat.No | ADA-05174A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | CRYBA1 |
| Target Synonyms | CRYB1; CTRCT10; CRYBA1 | Form | Liquid |
| Species Reactivity | Mouse, Rat | Isotype | IgG |
| Storage Buffer | 50% Glycerol, PBS with 0.01% thimerosal, pH7.3. | Purification Method | Affinity purification |
| Positive Samples | Mouse eye, Rat eye | Application | ELISA, WB |
| Immunogen Description | Recombinant fusion protein containing a sequence corresponding to amino acids 1-215 of human CRYBA1 (NP_005199.2). | Target Species | Human |
|---|---|---|---|
| Uniprot ID | P05813 | Immunogen Sequence |
Uniprot Id
P05813
Target Species
Human
Target Name
CRYBA1
Target Full Name
Beta-crystallin A3
Target Function
Crystallins are the dominant structural components of the vertebrate eye lens.
Target Involvement
Cataract 10, multiple types (CTRCT10)
Target Protein Families
Beta/gamma-crystallin family
Target Synonyms
Beta crystallin A3 isoform A1 Delta4 form; Beta crystallin A3; Beta crystallin A3 isoform A1 Delta7 form; Beta crystallin A3 isoform A1 Delta8 form; Beta-crystallin A3; CRBA1_HUMAN; CRYB1; CRYBA1; Crystallin beta A1; Crystallin beta A3; Delta8 form; Eye lens structural protein; isoform A1
Target 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'.
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