CRYBB2 antibody

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935106861
info@markelab.com
name
CRYBB2 antibody
category
Primary Antibodies
provider
FineTest
reference
FNab02003
tested applications
ELISA, WB

Description

Crystallins are the dominant structural components of the vertebrate eye lens.

Documents del producto

Instrucciones
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Data sheet
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Product specifications

Category
Primary Antibodies
Immunogen Target
crystallin, beta B2 (CRYBB2)
Host
Rabbit
Reactivity
Human, Mouse, Rat
Recommended Dilution
WB: 1:500-1:2000
Clonality
polyclonal
Conjugation
Unconjugated
Isotype
IgG
Observed MW
24 kDa
Purity
≥95% as determined by SDS-PAGE
Purification
Immunogen affinity purified
Size 1
100µg
Form
liquid
Tested Applications
ELISA, WB
Storage
PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.)
UniProt ID
P43320
Gene ID
1415
Alias
Beta-crystallin B2,Beta-B2 crystallin,Beta-crystallin Bp,CRYBB2,CRYB2,CRYB2A
Background
Antibody anti-CRYBB2
Status
RUO
Note
Mol. Weight 24 kDa

Descripción

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Crystallins are the dominant structural components of the vertebrate eye lens.

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Crystallin Beta B2 (CRYBB2) Antibody

CRYBB2 Antibody is a Rabbit Polyclonal antibody against CRYBB2. 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, is part of a gene cluster with beta-A4, beta-B1, and beta-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts.

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