• NatureRecombinant
  • SourceBaculovirus infected Sf9 cells
  • Amino Acid Sequence
    • AccessionO75385
    • SpeciesHuman
    • Molecular weight125 kDa including tags
    • Amino acids1 to 649

Associated products


Our Abpromise guarantee covers the use of ab125656 in the following tested applications.

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

  • Biological activityThe specific activity of ab125656 was determined to be 50 - 56 nmol/min/mg.
  • Applications

    Western blot

    Functional Studies


  • Purity> 70 % Densitometry.
    Purity was determined to be >70% by densitometry.
  • FormLiquid
  • Additional notes

    ab64311 (Myelin Basic Protein protein) can be utilized as a substrate for assessing kinase activity

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 7.50
    Constituents: 0.31% Glutathione, 0.002% PMSF, 0.004% DTT, 0.79% Tris HCl, 0.003% EDTA, 25% Glycerol, 0.88% Sodium chloride

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • ATG 1
    • ATG1
    • ATG1 autophagy related 1 homolog
    • ATG1A
    • Autophagy related protein 1 homolog
    • Autophagy-related protein 1 homolog
    • FLJ38455
    • FLJ46475
    • hATG1
    • KIAA0722
    • Serine/threonine protein kinase ULK1
    • Serine/threonine protein kinase Unc51.1
    • Serine/threonine-protein kinase ULK1
    • ULK 1
    • ULK1
    • ULK1_HUMAN
    • UNC 51
    • Unc 51 (C. elegans) like kinase 1
    • Unc 51 like kinase 1
    • Unc-51 like kinase 1 (C. elegans)
    • Unc-51-like kinase 1
    • UNC51
    • UNC51, C. elegans, homolog of
    • Unc51.1
    see all
  • FunctionSerine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation. May also phosphorylate SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165).
  • Tissue specificityUbiquitously expressed. Detected in the following adult tissues: skeletal muscle, heart, pancreas, brain, placenta, liver, kidney, and lung.
  • Sequence similaritiesBelongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily.
    Contains 1 protein kinase domain.
  • Post-translational
    Autophosphorylated. Phosphorylated under nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. Under nutrient sufficiency, phosphorylated by MTOR/mTOR, disrupting the interaction with AMPK and preventing activation of ULK1 (By similarity). In response to nutrient limitation, phosphorylated and activated by AMPK, leading to activate autophagy.
  • Cellular localizationCytoplasm, cytosol. Preautophagosomal structure. Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome.
  • Information by UniProt

Recombinant human ULK1 protein images

  • SDS-PAGE analysis of ab125656.
  • Sample Kinase Assay showing the specific activity of ab125656 as 50 nmol/min/mg.

References for Recombinant human ULK1 protein (ab125656)

ab125656 has not yet been referenced specifically in any publications.

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