Invitrogen

Human CRYBA2 (aa 160-197) Control Fragment Recombinant Protein

Name: Human CRYBA2 (aa 160-197) Control Fragment Recombinant Protein
Brand: Invitrogen
SKU: RP-108468

Datasheet

Tech Support

Datasheet

Tech Support

Product Details

RP-108468

Applications

Tested Dilution

Publications

Control (Ctrl)

Assay-dependent

Blocking Assay (BLOCK)

Assay-dependent

Product Specifications

Species

Human

Expression System

E. coli

Amino acid sequence

GYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIRRVQH

Tag

His-ABP-tag

Class

Recombinant

Type

Protein

Purity

>80% by SDS-PAGE and Coomassie blue staining

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

≥5.0 mg/mL

Purification

purified

Storage buffer

PBS/1M urea, pH 7.4

Contains

no preservative

Storage conditions

-20°C, Avoid Freeze/Thaw Cycles

Product Specific Information

Highest antigen sequence indentity to the following orthologs: Mouse (89%), Rat (89%).

This recombinant protein control fragment may be used for blocking experiments with the corresponding antibody, PA5-84545. In IHC/ICC and WB experiments, we recommend a 100x molar excess of the protein fragment control based on the concentration and the molecular weight. Pre-incubate the antibody-protein control fragment mixture for 30 min at room temperature.

Target Information

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.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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Bioinformatics

Protein Aliases: Beta-A2 crystallin; Beta-crystallin A2; crystallin, beta A2; eye lens structural protein