beta B1 Crystallin (CRYBB1) (NM_001887) Human Mass Spec Standard

CAT#: PH307718

CRYBB1 MS Standard C13 and N15-labeled recombinant protein (NP_001878)


  View other "beta B1 Crystallin" proteins (3)

USD 3,255.00

3 Weeks*

Size
    • 10 ug

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Specifications

Product Data
Tag C-Myc/DDK
Species Human
Expression Host HEK293
Expression cDNA Clone or AA Sequence RC207718
Predicted MW 28 kDa
Protein Sequence
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
Storage Store at -80°C. Avoid repeated freeze-thaw cycles.
Stability Stable for 3 months from receipt of products under proper storage and handling conditions.
Reference Data
RefSeq NP_001878
RefSeq Size 921
RefSeq ORF 756
Synonyms CATCN3; CTRCT17
Locus ID 1414
UniProt ID P53674
Cytogenetics 22q12.1
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, 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. [provided by RefSeq, Jul 2008]

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