• Product name

    Anti-PYK2 (phospho Y402) antibody
    See all PYK2 primary antibodies
  • Description

    Rabbit polyclonal to PYK2 (phospho Y402)
  • Host species

  • Specificity

    ab131543 detects endogenous levels of PYK2 only when phosphorylated at Tyrosine 402.
  • Tested applications

    Suitable for: WB, IHC-P, ICC/IFmore details
  • Species reactivity

    Reacts with: Mouse, Rat, Human
  • Immunogen

    Synthetic peptide conjugated to KLH, corresponding to a region surrounding Tyrosine 402


    of Human PYK2 (NP_004094.3).

  • Positive control

    • HeLa cells; Jurkat whole cell lysate (ab7899) (PMA-treated); Human breast carcinoma tissue.



Our Abpromise guarantee covers the use of ab131543 in the following tested applications.

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

Application Abreviews Notes
WB 1/500 - 1/1000. Predicted molecular weight: 116 kDa.
IHC-P 1/50 - 1/100.
ICC/IF 1/100 - 1/200.


  • Function

    Involved in calcium induced regulation of ion channel and activation of the map kinase signaling pathway. May represent an important signaling intermediate between neuropeptide activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity. Interacts with the SH2 domain of Grb2. May phosphorylate the voltage-gated potassium channel protein Kv1.2. Its activation is highly correlated with the stimulation of c-Jun N-terminal kinase activity. Involved in osmotic stress-dependent SNCA 'Tyr-125' phosphorylation. In concert with SRC, plays an important role in osteoclastic bone resorption. Both the formation of a SRC-PTK2B complex, and SRC kinase activity are necessary for this function. The Tyr-402 phosphorylated form serves as a docking site for SRC and is important for the organization of the osteoclast actin cytoskeleton and attachment sites and for bone resorption.
  • Tissue specificity

    Most abundant in the brain, with highest levels in amygdala and hippocampus. Low levels in kidney. Also expressed in spleen and lymphocytes.
  • Sequence similarities

    Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.
    Contains 1 FERM domain.
    Contains 1 protein kinase domain.
  • Post-translational

    Phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration, as well as by PKC activation. Recruitment by nephrocystin to cell matrix adhesions initiates Tyr-402 phosphorylation. In monocytes, adherence to substrata is required for tyrosine phosphorylation and kinase activation. Angiotensin II, thapsigargin and L-alpha-lysophosphatidic acid (LPA) also induce autophosphorylation and increase kinase activity.
  • Cellular localization

    Cytoplasm. Cell membrane. Interaction with nephrocystin induces the membrane-association of the kinase.
  • Information by UniProt
  • Database links

  • Alternative names

    • CADTK antibody
    • CAK-beta antibody
    • CAKB antibody
    • CAKbeta antibody
    • Calcium regulated non receptor proline rich tyrosine kinase antibody
    • Calcium-dependent tyrosine kinase antibody
    • Cell adhesion kinase beta antibody
    • E430023O05Rik antibody
    • EC antibody
    • FADK 2 antibody
    • FADK2 antibody
    • FAK2 antibody
    • FAK2_HUMAN antibody
    • Focal adhesion kinase 2 antibody
    • MGC124628 antibody
    • PKB antibody
    • Proline-rich tyrosine kinase 2 antibody
    • Protein kinase B antibody
    • Protein Tyrosine Kinase 2 Beta antibody
    • Protein-tyrosine kinase 2-beta antibody
    • PTK antibody
    • PTK2B antibody
    • PTK2B protein tyrosine kinase 2 beta antibody
    • PYK2 antibody
    • RAFTK antibody
    • RAFTK2 antibody
    • Related adhesion focal tyrosine kinase antibody
    see all


  • All lanes : Anti-PYK2 (phospho Y402) antibody (ab131543) at 1/500 dilution

    Lane 1 : Jurkat cell lysate, untreated
    Lane 2 : Jurkat cell lysate, treated with PMA

    Predicted band size: 116 kDa

  • Immunoflourescent analysis of methanol-fixed HeLa cells labelling PYK2 (phospho-Y402) with ab131543 at 1/100 dilution.
  • Immunohistochemical analysis of Human breast carcinoma tissue labelling PYK2 (phospho Y402) with ab131543 at 1/50 dilution. The image on the right is treated with the synthesized peptide.


This product has been referenced in:

  • Salazar SV  et al. Alzheimer's Disease Risk Factor Pyk2 Mediates Amyloid-ß-Induced Synaptic Dysfunction and Loss. J Neurosci 39:758-772 (2019). Read more (PubMed: 30518596) »
  • Grenier K  et al. Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy. J Biol Chem 289:29519-30 (2014). Read more (PubMed: 25217637) »
See all 2 Publications for this product

Customer reviews and Q&As


Thank you for contacting us and your interest in our products. I am sorry for the delay in getting back to you.

As we discussed over the phone, I have looked into how the Anti-PYK2 (phospho Y402) antibodies ab4800 and ab131543 have been characterized for their potential cross-reactivity with other phospho-proteins.

No specific experiments have been carried out to ascertain the cross-reactivity of either of these antibodies. However, the western results are based on total cell lysates which contains thousands of other proteins many of which are phosphorylated. As the Western blot images for these antibodies show, only one band was detected in the molecular range from 37 kDa up to 250 kDa, there is no other visible band.

In addition, with ab4800 the target band was competed out with the phosphorylated immunogen peptide indicating the band we see is the targe Pyk2 pY402. This supports at least in the cells (primary CDF cells, and SDF-1a treated Reh cells) we studied we did not see any cross reactivity with other proteins (phosphorylated or not phosphorylated).

From blast search of the immunogens used, the area does not seem to share homology with any other protein (that have been added to this databank) suggesting there should not be any cross-reactivity observed.

Read More

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