beta Crystallin A3 (CRYBA1) (Center) Rabbit Polyclonal Antibody

Specifications

Product Data
Applications	IHC, WB
Recommend Dilution	ELISA: 1/1000 Western blot: 1/100-1/500. Immunohistochemistry on Paraffin Sections: 1/10-1/50.
Reactivity	Human, Mouse
Host	Rabbit
Clonality	Polyclonal
Immunogen	KLH conjugated synthetic peptide between 111-141 amino acids from the Central region of Human CRYBA1.
Specificity	This antibody recognizes Human and Mouse Beta-crystallin A3.
Formulation	PBS State: Aff - Purified State: Liquid purified Ig fraction Preservative: 0.09% Sodium Azide
Concentration	lot specific
Purification	Affinity Chromatography on Protein A
Conjugation	Unconjugated
Storage Condition	Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing.
Gene Name	crystallin beta A1
Database Link	Entrez Gene 12957 MouseEntrez Gene 1411 Human UniProt ID P05813
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 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'
Synonyms	CRYBA1, CRYB1
Note	Molecular Weight: 25150 Da
Reference Data

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