CRYBB2 (NM_000496) Human Mass Spec Standard

CAT#: PH310125

CRYBB2 MS Standard C13 and N15-labeled recombinant protein (NP_000487)



  View other "CRYBB2" proteins (3)

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CNY 19,520.00


货期*
4周

规格
    • 10 ug

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经常一起买 (2)
Transient overexpression lysate of crystallin, beta B2 (CRYBB2)
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Specifications

Product Data
Description CRYBB2 MS Standard C13 and N15-labeled recombinant protein (NP_000487)
Species Human
Expression Host HEK293
Expression cDNA Clone or AA Sequence RC210125
Predicted MW 23.4 kDa
Protein Sequence
Tag C-Myc/DDK
Purity > 80% as determined by SDS-PAGE and Coomassie blue staining
Concentration >0.05 µg/µL as determined by microplate BCA method
Labeling Method Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
Buffer 25 mM Tris-HCl, 100 mM glycine, pH 7.3
Reference Data
RefSeq NP_000487
RefSeq Size 781
RefSeq ORF 615
Synonyms CCA2; CRYB2; CRYB2A; CTRCT3; D22S665
Locus ID 1415
Cytogenetics 22q11.23
Summary 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. [provided by RefSeq, Jul 2008]
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