CRYBB1 Protein (Myc-DYKDDDDK Tag)
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- Target See all CRYBB1 Proteins
- CRYBB1 (Crystallin, beta B1 (CRYBB1))
- Protein Type
- Recombinant
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Origin
- Human
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Source
- HEK-293 Cells
- Purification tag / Conjugate
- This CRYBB1 protein is labelled with Myc-DYKDDDDK Tag.
- Application
- Antibody Production (AbP), Standard (STD)
- Characteristics
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- Recombinant human Beta-crystallin B1 protein expressed in HEK293 cells.
- Produced with end-sequenced ORF clone
- Purity
- > 80 % as determined by SDS-PAGE and Coomassie blue staining
- Top Product
- Discover our top product CRYBB1 Protein
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- Application Notes
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Recombinant human proteins can be used for:
Native antigens for optimized antibody production
Positive controls in ELISA and other antibody assays - Comment
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The tag is located at the C-terminal.
- Restrictions
- For Research Use only
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- Concentration
- 50 μg/mL
- Buffer
- 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10 % glycerol.
- Storage
- -80 °C
- Storage Comment
- Store at -80°C. Thaw on ice, aliquot to individual single-use tubes, and then re-freeze immediately. Only 2-3 freeze thaw cycles are recommended.
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- Target
- CRYBB1 (Crystallin, beta B1 (CRYBB1))
- Alternative Name
- beta-Crystallin b1 (CRYBB1 Products)
- Synonyms
- zgc:92706 Protein, CRYBB1 Protein, catcn3 Protein, Crybb1 Protein, CATCN3 Protein, CTRCT17 Protein, 3110006K12Rik Protein, BB1CRY Protein, CRYB1 Protein, CRYB11 Protein, crystallin, beta B1 Protein, crystallin beta B1 S homeolog Protein, crystallin beta B1 Protein, crybb1 Protein, crybb1.S Protein, CRYBB1 Protein, Crybb1 Protein
- Background
- 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.
- Molecular Weight
- 27.8 kDa
- NCBI Accession
- NP_001878
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