CRYbB2 Protein (Myc-DYKDDDDK Tag)

Catalog No. ABIN2715239

Recombinant CRYbB2 protein expressed in HEK-293 Cells.

Quick Overview for CRYbB2 Protein (Myc-DYKDDDDK Tag) (ABIN2715239)

Target: CRYbB2 (Crystallin, beta B2 (CRYbB2))

Protein Type: Recombinant

Origin: Human

Source: HEK-293 Cells

Application: Antibody Production (AbP), Standard (STD)

Purity: > 80 % as determined by SDS-PAGE and Coomassie blue staining

Product Details

Purification tag / Conjugate: This CRYbB2 protein is labelled with Myc-DYKDDDDK Tag.

Characteristics:

• Recombinant human Beta-crystallin B2 protein expressed in HEK293 cells.
• Produced with end-sequenced ORF clone

Application Details

Application Notes: Recombinant human proteins can be used for:
Native antigens for optimized antibody production
Positive controls in ELISA and other antibody assays

Comment:

The tag is located at the C-terminal.

Restrictions: For Research Use only

Handling

Concentration: 50 μg/mL

Buffer: 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10 % glycerol.

Storage: -80 °C

Storage Comment: Store at -80°C. Thaw on ice, aliquot to individual single-use tubes, and then re-freeze immediately. Only 2-3 freeze thaw cycles are recommended.

Target Details

Target: CRYbB2 (Crystallin, beta B2 (CRYbB2))

Alternative Name: beta-Crystallin b2

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 basic group member, is part of a gene cluster with beta-A4, beta-B1, and beta-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts.

Molecular Weight: 23.2 kDa

NCBI Accession: NP_000487