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The antibody against CRYBA4 was raised in rabbit using the Recombinant Human Beta-crystallin A4 protein (2-196AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB, IHC.
The antibody against CRYBA4 was raised in rabbit using the Recombinant Human Beta-crystallin A4 protein (2-196AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB, IHC.
$299.00
| Cat.No | ADC-22151A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | CRYBA4 |
| Form | Liquid | Species Reactivity | Human, Mouse |
| Isotype | IgG | Storage Buffer | 0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4 |
| Purification Method | >95%, Protein G purified | Conjugate | Non-conjugated |
| Application | ELISA, IHC, WB | Storage | Upon receipt |
| Immunogen Description | Recombinant Human Beta-crystallin A4 protein (2-196AA) | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | P53673 |
Uniprot Id
P53673
Target Species
Human
Target Name
CRYBA4
Target Full Name
Beta-crystallin A4
Target Function
Crystallins are the dominant structural components of the vertebrate eye lens.
Target Involvement
Cataract 23, multiple types (CTRCT23)
Target Protein Families
Beta/gamma-crystallin family
Target Synonyms
Beta A4 crystallin; Beta crystallin A4; Beta-A4 crystallin; Beta-crystallin A4; CRBA4_HUMAN; CRYBA4; Crystallin beta A4; Crystallin; beta polypeptide A4; CTRCT23; Eye lens structural protein; MCOPCT4
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, is part of a gene cluster with beta-B1, beta-B2, and beta-B3.
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