Recombinant Human Beta-crystallin A3 (CRYBA1)

Cat.No	ACP22223	Target Name	CRYBA1
Form	Lyophilized powder	Expression System	Custom Production. Please inquire and provide the desire expression system.
Expression Range	1-215	Protein Length	Full length protein
Purity	>85% (SDS-PAGE)	Storage Buffer	5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Cat.No

ACP22223

Target Name

CRYBA1

Form

Lyophilized powder

Expression System

Custom Production. Please inquire and provide the desire expression system.

Expression Range

1-215

Protein Length

Full length protein

Purity

>85% (SDS-PAGE)

Storage Buffer

5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Target Species	Human	Uniprot ID	P05813

Background Information

Uniprot Id

P05813
Target Species

Human
Target Name

CRYBA1
Target Full Name

Beta-crystallin A3
Target Function

Crystallins are the dominant structural components of the vertebrate eye lens.
Target Involvement

Cataract 10, multiple types (CTRCT10)
Target Protein Families

Beta/gamma-crystallin family
Target Synonyms

Beta crystallin A3 isoform A1 Delta4 form; Beta crystallin A3; Beta crystallin A3 isoform A1 Delta7 form; Beta crystallin A3 isoform A1 Delta8 form; Beta-crystallin A3; CRBA1_HUMAN; CRYB1; CRYBA1; Crystallin beta A1; Crystallin beta A3; Delta8 form; Eye lens structural protein; isoform A1
Target 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'.

Recombinant Human Beta-crystallin A3 (CRYBA1)

Specifications

Immunogen Information

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