Name :
CRYBB1 (Human) Recombinant Protein (P01)
Biological Activity :
Human CRYBB1 full-length ORF ( AAH36790.1, 1 a.a. – 252 a.a.) recombinant protein with GST-tag at N-terminal.Full-Length Protein,Full-Length Proteins,Full-Length,Full Length,FullLength
Tag :
Best use within three months from the date of receipt of this protein.
Protein Accession No. :
AAH36790.1
Protein Accession No.URL :
https://www.ncbi.nlm.nih.gov/gene?cmd=Retrieve&dopt=Graphics&list_uids=1414
Amino Acid Sequence :
MSQAAKASASATVAVNPGPDTKGKGAPPAGTSPSPGTTLAPTTVPITSAKAAELPPGNYRLVVFELENFQGRRAEFSGECSNLADRGFDRVRSIIVSAGPWVAFEQSNFRGEMFILEKGEYPRWNTWSSSYRSDRLMSFRPIKMDAQEHKISLFEGANFKGNTIEIQGDDAPSLWVYGFSDRVGSVKVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQSLRRLRDKQWHLEGSFPVLATEPPK
Molecular Weight :
53.46
Storage and Stability :
Store at -80°C. Aliquot to avoid repeated freezing and thawing.
Host :
Wheat Germ (in vitro)
Interspecies Antigen Sequence :
Mouse (80); Rat (81)
Preparation Method :
in vitro wheat germ expression system
Purification :
Glutathione Sepharose 4 Fast Flow
Quality Control Testing :
12.5% SDS-PAGE Stained with Coomassie Blue.
Storage Buffer :
50 mM Tris-HCI, 10 mM reduced Glutathione, pH=8.0 in the elution buffer.
Applications :
Enzyme-linked Immunoabsorbent Assay， Western Blot (Recombinant protein)， Antibody Production， Protein Array，
Gene Name :
CRYBB1
Gene Alias :
CATCN3
Gene Description :
crystallin, beta B1
Gene 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
Other Designations :
OTTHUMP00000028719|eye lens structural protein
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