(800) 943-6396

150 Essex St, Millburn, NJ 07041, USA

©2019 by Bon Opus Biosciences, LLC.

MKLP1 Recombinant Rabbit monoclonal Antibody IgG

SKU: BA111485-100µl
$279.00Price

Fig1: Western blot analysis of MKLP1 on different lysates using anti-MKLP1 antibody at 1/1,000 dilution.

Positive control:   

Lane 1: A549                

Lane 2: Hela

Fig2: ICC staining MKLP1 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 MKLP1 in A549 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Bon Opus Cat. #BA111485
Size
  • Host Species; Species Reactivity

    Rabbit; Human, Mouse, Rat
  • Immunogen

    Recombinant protein
  • Application Summary

    WB, ICC/IF
  • Purification; Formulation

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

    Kinesin-like protein KIF23
  • Background

    The monoclonal antibody CHO1 detects a spindle antigen required for mitotic progression. Screening a HeLa cell cDNA expression library with this antibody has been shown to yield a cDNA predicted to encode a protein significantly related within its amino terminal half to the motor ends of members of the kinesin superfamily. Since this similarity does not extend further, it has been suggested that the CHO1 antigen, now designated MKLP-1 (mitotic kinesin-like protein-1), represents a novel kinesin. Sequence analysis has also been shown to predict that MKLP-1 possesses features typical of nuclear proteins. Immunocytological studies have demonstrated that MKLP-1 moves from the nucleus early in mitosis and then to the midbody after cytokinesis. MKLP-1 has been shown to bundle antiparallel microtubules in vitro and to move them at rates comparable to spindle elongation in vivo. A hamster homolog of MKLP-1, designated CHO1 antigen, has also been isolated. Although apparently functionally equivalent with respect to microtubule bundling activity, there are significant differences between the human and hamster proteins at their C-termini, possibly due to alternative splicing or the presence of more than one MKLP-1 locus.(ET1607-63)