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CRYAB anticorps

L’anticorps Lapin Polyclonal anti-CRYAB a été validé pour WB et ELISA. Il convient pour détecter CRYAB dans des échantillons de Humain, Rat et Souris.
N° du produit ABIN7235811

Aperçu rapide pour CRYAB anticorps (ABIN7235811)

Antigène

Voir toutes CRYAB Anticorps
CRYAB (Crystallin, alpha B (CRYAB))

Reactivité

  • 138
  • 81
  • 76
  • 15
  • 7
  • 6
  • 6
  • 5
  • 4
  • 4
  • 4
  • 3
  • 2
Humain, Rat, Souris

Hôte

  • 137
  • 48
  • 2
  • 1
Lapin

Clonalité

  • 131
  • 57
Polyclonal

Conjugué

  • 84
  • 9
  • 9
  • 7
  • 4
  • 4
  • 4
  • 4
  • 4
  • 4
  • 4
  • 4
  • 4
  • 4
  • 4
  • 4
  • 3
  • 3
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Cet anticorp CRYAB est non-conjugé

Application

  • 136
  • 73
  • 66
  • 52
  • 52
  • 36
  • 32
  • 23
  • 19
  • 12
  • 12
  • 10
  • 1
  • 1
  • 1
Western Blotting (WB), ELISA
  • Attributs du produit

    Polyclonal Antibody

    Purification

    Affinity purification

    Immunogène

    Recombinant protein of human CRYAB

    Isotype

    IgG
  • Indications d'application

    WB 1:500-1:2000

    Restrictions

    For Research Use only
  • Format

    Liquid

    Concentration

    0.2 mg/mL

    Buffer

    PBS with 0.05 % sodium azide and 50 % glycerol, PH7.4

    Agent conservateur

    Sodium azide

    Précaution d'utilisation

    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

    Stock

    -20 °C

    Stockage commentaire

    Store at -20°C. Avoid freeze / thaw cycles.
  • Antigène

    CRYAB (Crystallin, alpha B (CRYAB))

    Autre désignation

    Crystallin-alpha B

    Sujet

    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.

    Poids moléculaire

    20 kDa

    UniProt

    P02511
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