Recombinant Human LKB1 + CAB39 + LYK5 protein (ab95249)

Overview

  • Product nameRecombinant Human LKB1 + CAB39 + LYK5 protein
  • Protein lengthFull length protein

Description

  • NatureRecombinant
  • SourceBaculovirus
  • Amino Acid Sequence
    • SpeciesHuman

Specifications

Our Abpromise guarantee covers the use of ab95249 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 10% Glycerol, 0.05% Tween 20, 3mM DTT, 25mM Tris HCl, 100mM Sodium chloride, pH 8.0

General Info

  • Alternative names
    • 2610019A05Rik
    • 6030402H20Rik
    • AA408040
    • AI480680
    • Calcium binding protein 39
    • CGI 66
    • E130112C09Rik
    • FLJ22682
    • FLJ90524
    • Lkb1
    • LKB1 short isoform
    • LYK5
    • MGC93856
    • MO25
    • NY BR 96
    • OTTMUSP00000003173
    • OTTMUSP00000020599
    • OTTMUSP00000020600
    • OTTMUSP00000043767
    • PJS
    • PMSE
    • Polarization related protein LKB1
    • Protein kinase LYK5
    • R75140
    • Renal carcinoma antigen NY REN 19
    • RP23-81G14.9
    • Serine/threonine kinase 11
    • Serine/threonine protein kinase 11
    • Serine/threonine protein kinase LKB1
    • Serologically defined breast cancer antigen NY BR 96
    • STE20 related adapter protein
    • STE20 related kinase adapter protein alpha
    • STE20 related kinase adaptor alpha
    • STK11
    • Stlk
    • STRAD
    • STRAD alpha
    • STRADA
    see all
  • RelevanceLKB1 regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms. Members of the STE-20 like kinase family are known to stimulate MAPK pathways by directly activating MAPKKK. LYK5 is a novel pseudokinase member of this family consisting of a STE-20 like kinase domain but lacks several residues that are required for its catalytic activity. It specifically binds LKB1 and plays a key role in regulating the tumor suppressor activities of LKB1. It functions as an upstream activator of LKB1 and also directs the sub-cellular localization of LKB1 by anchoring it in the cytoplasm. LYK5-LKB1 interaction results in phosphorylation of LYK5 and enhanced autophosphorylation of LKB1.
  • Cellular localizationCytoplasmic and Nuclear

Recombinant Human LKB1 + CAB39 + LYK5 protein images

  • SDS-PAGE showing ab95249 at approximately 49, 66 and 74 kDa (10µg). Smaller band represents LKB1, larger band represents CAB39 and LYK5. Lane 2 represent the MW marker ladder.

References for Recombinant Human LKB1 + CAB39 + LYK5 protein (ab95249)

ab95249 has not yet been referenced specifically in any publications.

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