Hsp22 Recombinant Rabbit monoclonal Antibody IgG

SKU: BA111907-100µl
$279.00Price

Fig1: Western blot analysis of Hsp22 on different lysates using anti-Hsp22 antibody at 1/1,000 dilution.

Positive control:   

Lane 1: HepG2       

Lane 2: Mouse skeletal muscle

Fig2: ICC staining Hsp22 in Hela cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Fig3: ICC staining Hsp22 in A431 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Bon Opus Cat. #BA111907
Size
  • Host Species; Species Reactivity

    Rabbit; Human, Mouse, Rat
  • Immunogen

    Recombinant protein
  • Application Summary

    WB, ICC/IF, IHC
  • Purification; Formulation

    ProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
  • ALTnames

    Heat shock protein beta-8, Alpha-crystallin C chain, E2-induced gene 1 protein, Protein kinase H11, Small stress protein-like protein HSP22
  • Background

    Crystallins are the major proteins expressed in the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b and g families; b and g-crystallins compose a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. a-crystallins consist of three gene products, aA, aB and aC-crystallin, which are members of the small heat shock protein family (HSP20). They are induced by heat shock, and act as molecular chaperones by holding denatured proteins in large soluble aggregates. However, unlike other molecular chaperones, a-crystallins do not renature these proteins. Research indicates that binding occurs between membranes and aC-crystallin. The binding site appears to be at the polar-apolar interface in membrane protein (MIP26) and aC-crystallin; the lipid bilayer becomes less mobile with aC-crystallin binding.(ET1701-11)

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