Phospho-CaMKK2 (Ser495) (E7W9S) Rabbit mAb #35392
- WB
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 68, 70 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Phospho-CaMKK2 (Ser495) (E7W9S) Rabbit mAb recognizes endogenous levels of CaMKK2 protein only when phosphorylated at Ser495. Bands of unknown origin are observed at 42 kDa and 25 kDa.
Species Reactivity:
Human, Mouse
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser495 of human CaMKK2 protein.
Background
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).
- Tokumitsu, H. et al. (1997) Biochemistry 36, 12823-7.
- Tokumitsu, H. et al. (1995) J Biol Chem 270, 19320-4.
- Anderson, K.A. et al. (1998) J Biol Chem 273, 31880-9.
- Hawley, S.A. et al. (2005) Cell Metab 2, 9-19.
- Peters, M. et al. (2003) J Neurosci 23, 9752-60.
- Lin, F. et al. (2011) Endocrinology 152, 3668-79.
- Schumacher, A.M. et al. (2004) Biochemistry 43, 8116-24.
- Knittle, A.M. et al. (2017) J Biol Chem 292, 19890-19904.
Limited Uses
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