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The antibody against CRYBB1 was raised in rabbit using the Recombinant Human Beta-crystallin B1 protein (1-252AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB.
The antibody against CRYBB1 was raised in rabbit using the Recombinant Human Beta-crystallin B1 protein (1-252AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB.
$299.00
| Cat.No | ADC-17612A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | CRYBB1 |
| Form | Liquid | Species Reactivity | Human, Mouse |
| Isotype | IgG | Storage Buffer | 50% Glycerol, PBS with 0.02% sodium azide, pH7.3. |
| Purification Method | Antigen affinity purified | Conjugate | Non-conjugated |
| Application | ELISA, WB | Storage | Upon receipt |
| Immunogen Description | Recombinant Human Beta-crystallin B1 protein (1-252AA) | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | P53674 |
Uniprot Id
P53674
Target Species
Human
Target Name
CRYBB1
Target Full Name
Beta-crystallin B1
Target Function
Crystallins are the dominant structural components of the vertebrate eye lens.
Target Involvement
Cataract 17, multiple types (CTRCT17)
Target Protein Families
Beta/gamma-crystallin family
Target Synonyms
Beta crystallin B1; Beta-B1 crystallin; Beta-crystallin B1; CATCN3; CRBB1_HUMAN; CRYBB 1; Crybb1; Crystallin beta B1; CTRCT17; Eye lens structural protein; OTTHUMP00000028719
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 basic group member, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3.
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