CRYBA2 purified MaxPab mouse polyclonal antibody (B01P)
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More Files
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Specification
Product Description
Mouse polyclonal antibody raised against a full-length human CRYBA2 protein.
Immunogen
CRYBA2 (AAH06285, 1 a.a. ~ 197 a.a) full-length human protein.
Sequence
MSSAPAPGPAPASLTLWDEEDFQGRRCRLLSDCANVCERGGLPRVRSVKVENGVWVAFEYPDFQGQQFILEKGDYPRWSAWSGSSSHNSNQLLSFRPVLCANHNDSRVTLFEGDNFQGCKFDLVDDYPSLPSMGWASKDVGSLKVSSGAWVAYQYPGYRGYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIRRVQH
Host
Mouse
Reactivity
Human
Interspecies Antigen Sequence
Mouse (91); Rat (92)
Quality Control Testing
Antibody reactive against mammalian transfected lysate.
Storage Buffer
In 1x PBS, pH 7.4
Storage Instruction
Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing.
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Applications
Western Blot (Transfected lysate)
Western Blot analysis of CRYBA2 expression in transfected 293T cell line (H00001412-T01) by CRYBA2 MaxPab polyclonal antibody.
Lane 1: CRYBA2 transfected lysate(21.67 KDa).
Lane 2: Non-transfected lysate.
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Gene Info — CRYBA2
Entrez GeneID
1412GeneBank Accession#
BC006285Protein Accession#
AAH06285Gene Name
CRYBA2
Gene Alias
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Gene Description
crystallin, beta A2
Omim ID
600836Gene Ontology
HyperlinkGene Summary
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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 but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported. [provided by RefSeq
Other Designations
eye lens structural protein
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Interactome
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Disease
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