beta-Crystallin a3 (CRBA1) (C-Term) Peptide
CRBA1
Reactivity: Human
Host: Synthetic
BP, WB
Catalog No. ABIN5510817
$160.46
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100 μg
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Quick Overview for beta-Crystallin a3 (CRBA1) (C-Term) Peptide (ABIN5510817)
Target
CRBA1
(beta-Crystallin a3 (CRBA1))
Origin
Human
Source
Synthetic
Application
Blocking Peptide (BP), Western Blotting (WB)
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Protein Region
- C-Term
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Sequence
- SGAWVCYQYP GYRGYQYILE CDHHGGDYKH WREWGSHAQT SQIQSIRRIQ
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Characteristics
- This is a synthetic peptide designed for use in combination with anti-CRBA1 Antibody. It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications.
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Application Notes
- Optimal working dilution should be determined by the investigator.
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Restrictions
- For Research Use only
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Format
- Lyophilized
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Reconstitution
- Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
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Storage
- -20 °C
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Storage Comment
- For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
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- CRBA1 (beta-Crystallin a3 (CRBA1))
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Background
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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 acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'.
Alias Symbols: CRYBA1,CRYB1,
Protein Size: 215 -
Gene ID
- 1411
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NCBI Accession
- NP_005199
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UniProt
- P05813
Target
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