CRYBB1 (Human) Recombinant Protein (Q01)
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More Files
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Specification
Product Description
Human CRYBB1 partial ORF ( NP_001878, 37 a.a. - 137 a.a.) recombinant protein with GST-tag at N-terminal.
Sequence
TTLAPTTVPITSAKAAELPPGNYRLVVFELENFQGRRAEFSGECSNLADRGFDRVRSIIVSAGPWVAFEQSNFRGEMFILEKGEYPRWNTWSSSYRSDRLM
Host
Wheat Germ (in vitro)
Theoretical MW (kDa)
36.85
Interspecies Antigen Sequence
Mouse (79); Rat (79)
Preparation Method
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.
Storage Instruction
Store at -80°C. Aliquot to avoid repeated freezing and thawing.
Note
Best use within three months from the date of receipt of this protein.
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Applications
Enzyme-linked Immunoabsorbent Assay
Western Blot (Recombinant protein)
Antibody Production
Protein Array
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Gene Info — CRYBB1
Entrez GeneID
1414GeneBank Accession#
NM_001887Protein Accession#
NP_001878Gene Name
CRYBB1
Gene Alias
CATCN3
Gene Description
crystallin, beta B1
Omim ID
600929Gene Ontology
HyperlinkGene 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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