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Phospho-CaMKK2 (Ser495) Antibody #16737

Item# Description List Price Web Price Qty
16737S Phospho-CaMKK2 (Ser495) Antibody - 100 µl $433.00
*On-line ordering is for Canadian customers only. Web pricing is applicable only to orders placed online at
Application Dilution Species-Reactivity Sensitivity MW (kDa) Source
W Human, Mouse Endogenous 68, 70 Rabbit

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting


Species predicted to react based on 100% sequence homology: Rat.


Specificity / Sensitivity

Phospho-CaMKK2 (Ser495) Antibody recognizes endogenous levels of CaMKK2 protein only when phosphorylated at Ser495. Bands of unknown origin are observed at 42 kDa and 25 kDa.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser495 of human CaMKK2 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from LNCaP and SNB-19 cells, and mouse brain, untreated (-) or treated with λ phosphatase (+), using Phospho-CaMKK2 (Ser495) Antibody (upper), CaMKK2 (D8D4D) Rabbit mAb #16810 (middle), and β-Actin (D6A8) Rabbit mAb #8457 (lower).


Calcium/Calmodulin-dependent Protein Kinase Kinase 2 (CaMKK2) is a member of the CaMK family that contains a central Ser/Thr kinase domain followed by a regulatory domain consisting of overlapping autoinhibitory and CaM-binding regions (1). CaMKK2 can be distinguished from other CaMK family members by the presence of a unique Pro/Arg/Gly-rich insert following the ATP-binding domain (2). CaMKK2 phosphorylates CaMKI at Thr177 and CaMKIV at Thr200 (3). CaMKK2 also phosphorylates AMPKα in response to calcium (4). CaMKK2 has been implicated in long-term memory formation (5) and adipocyte development (6). CaMKK2 is phosphorylated at Ser511 by death-associated protein kinase (DAPK) in a signaling cascade thought to be involved in neuronal death (7).

Multiple CaMKK2 phosphorylation sites have been identified, including Ser495, and C-terminal phosphorylation of the CaMKK2 autoinhibitory region may regulate its function and localization (8).

  1. Tokumitsu, H. et al. (1997) Biochemistry 36, 12823-7.
  2. Tokumitsu, H. et al. (1995) J Biol Chem 270, 19320-4.
  3. Anderson, K.A. et al. (1998) J Biol Chem 273, 31880-9.
  4. Hawley, S.A. et al. (2005) Cell Metab 2, 9-19.
  5. Peters, M. et al. (2003) J Neurosci 23, 9752-60.
  6. Lin, F. et al. (2011) Endocrinology 152, 3668-79.
  7. Schumacher, A.M. et al. (2004) Biochemistry 43, 8116-24.
  8. Nakanishi, A. et al. (2017) J Biol Chem 292, 19804-13.

Application References

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