beta B1 Crystallin (CRYBB1) (NM_001887) Human Recombinant Protein

Specifications

Product Data
Species	Human
Expression Host	HEK293T
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) >RC207718 protein sequence Red=Cloning site Green=Tags(s) MSQAAKASASATVAVNPGPDTKGKGAPPAGTSPSPGTTLAPTTVPITSAKAAELPPGNYRLVVFELENFQ GRRAEFSGECSNLADRGFDRVRSIIVSAGPWVAFEQSNFRGEMFILEKGEYPRWNTWSSSYRSDRLMSFR PIKMDAQEHKISLFEGANFKGNTIEIQGDDAPSLWVYGFSDRVGSVKVSSGTWVGYQYPGYRGYQYLLEP GDFRHWNEWGAFQPQMQSLRRLRDKQWHLEGSFPVLATEPPK TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag	C-Myc/DDK
Predicted MW	27.8 kDa
Concentration	>0.05 µg/µL as determined by microplate BCA method
Purity	> 80% as determined by SDS-PAGE and Coomassie blue staining
Buffer	25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
Preparation	Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
Note	For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
Storage	Store at -80°C.
Stability	Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Reference Data
RefSeq	NP_001878
Locus ID	1414
UniProt ID	P53674
Refseq Size	921
Cytogenetics	22q12.1
Refseq ORF	756
Synonyms	CATCN3; CTRCT17
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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