Monoclonal Anti-CRYBA2 antibody produced in mouse

NA.41

Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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 but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported. (provided by RefSeq)

CRYBA2 (NP_005200.1, 94 a.a. ~ 193 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
SFRPVLCANHNDSRVTLFEGDNFQGCKFDLVDDYPSLPSMGWASKDVGSLKVSSGAWVAYQYPGYRGYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIR

Solution in phosphate buffered saline, pH 7.4

100

mouse

unconjugated

purified immunoglobulin

primary antibodies

2G9, monoclonal

buffered aqueous solution

antigen ~37.11 kDa

human

capture ELISA: suitable
indirect ELISA: suitable

IgG2aκ

NM_005209

P53672

dry ice

−20℃

human ... CRYBA2(1412)

13 - Non Combustible Solids

WGK 1