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CRYAB antibody

This anti-CRYAB antibody is a Rabbit Polyclonal antibody detecting CRYAB in WB. Suitable for Human.
Catalog No. ABIN2854419

Quick Overview for CRYAB antibody (ABIN2854419)

Target

See all CRYAB Antibodies
CRYAB (Crystallin, alpha B (CRYAB))

Reactivity

  • 139
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Human

Host

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Rabbit

Clonality

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Polyclonal

Conjugate

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  • 1
  • 1
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  • 1
This CRYAB antibody is un-conjugated

Application

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Western Blotting (WB)
  • Cross-Reactivity

    Mouse, Rat

    Characteristics

    Rabbit polyclonal antibody to crystallin alpha B (crystallin, alpha B)
    crystallin alpha B antibody [N1C3]

    Purification

    Purified by antigen-affinity chromatography.

    Immunogen

    Recombinant protein encompassing a sequence within the center region of human alpha B Crystallin. The exact sequence is proprietary.

    Isotype

    IgG
  • Application Notes

    WB: 1:5000-1:50000. Optimal dilutions/concentrations should be determined by the researcher. Not tested in other applications.

    Comment

    Positive Control: mouse eye

    Restrictions

    For Research Use only
  • Format

    Liquid

    Concentration

    0.98 mg/mL

    Buffer

    0.1M Tris-Glycine ( pH 7), 20 % Glycerol, 0.01 % Thimerosal

    Preservative

    Thimerosal (Merthiolate)

    Precaution of Use

    This product contains Thimerosal (Merthiolate): a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

    Storage

    4 °C,-20 °C

    Storage Comment

    Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4°C. For long-term storage, aliquot and store at -20°C or below. Avoid multiple freeze-thaw cycles.
  • Target

    CRYAB (Crystallin, alpha B (CRYAB))

    Alternative Name

    crystallin alpha B

    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. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone, instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits, the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed, alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases, a missense mutation cosegregated in a family with a desmin-related myopathy.

    Molecular Weight

    20 kDa

    Gene ID

    1410

    UniProt

    P02511
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