CRBB1 Rabbit polyclonal antibody, anti-human, mouse, rat

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.

Research Area: Neuroscience

Synonyms: CRBB1

Immunogen: The antiserum was produced against synthesized peptide derived from human AMPK alpha around the phosphorylation site of Thr172. AA range:140-189

Purification: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Formulation: Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Concentration: 1 mg/ml

Storage:
-20°C for 1 year