CaM Kinase II [p Thr286] Antibody [Unconjugated]

Western Blot of rat brain tissue lysate showing specific immunolabeling of the ~50 kDa alpha -CaMKII subunit phosphorylated at T286 and the ~60 kDa beta -CaMKII subunit phosphorylated at T287 (Control). The phosphospecificity of this labeling is demonstrated by treatment with 1200 U of lambda Phosphatase ( lambda -PPase) for 30 minutes before being exposed to the anti-phospho-CaMKII (T286). The immunolabeling is completely eliminated by treatment with lambda -PPase.

• Reactivity: Hu, Mu, Rt, Xp
• Applications: WB
• Clonality: Polyclonal
• Host: Rabbit
• Conjugate: Unconjugated

CaM Kinase II [p Thr286] Antibody [Unconjugated] Summary

• Immunogen: Phosphopeptide corresponding to amino acid residues surrounding phospho-T286 of CaM Kinase II
• Modification: p Thr286
• Specificity: Human, mouse, rat, bovine, chicken, Xenopus alpha -CaM Kinase II phosphorylated at T286 in Western blots.
• Source: N/A
• Isotype: IgG
• Clonality: Polyclonal
• Host: Rabbit
• Purity Statement: Antigen Affinity-purified

Applications/Dilutions

• Dilutions:
  • Western Blot 1:1000 dilution

Packaging, Storage & Formulations

• Storage: For long-term storage, ≤ -20° C is recommended. Product is stable at ≤ -20° C for at least 1 year.
• Buffer: 100 μL in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 μg/mL BSA and 50% glycerol.
• Preservative: No Preservative

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for CaM Kinase II [p Thr286] Antibody [Unconjugated]

• Calcium/calmodulin-dependent protein kinase;Calcium/calmodulin-dependent protein kinase type II subunit beta;CAM2;CAMK2;CAMK2B;CAMKB;CaMKIIbeta;MRD54
• CaM Kinase II
• CAMK2
• CAMK2B

Background

Calmodulin Kinase II (CaMKII) is a 500 kDa, 8-12 subunit multimer that belongs to the Ser/Thr protein kinase family. It is ubiquitously expressed and interacts with a very diverse group of substrates. In rat, there are four possible subunits/isozymes ( alpha , beta , gamma , δ) that vary from 480-540 amino acids in length. The alpha - and beta -isozymes predominate in the brain. Each subunit contains a catalytic, autoregulatory, and subunit-association domain. The enzyme complex is inactive, due to the association of an internal pseudosubstrate motif with each subunit’s catalytic domain. CaMKII is regulated by calmodulin (CaM), an intracellular receptor for calcium. Following an influx of calcium, two Ca⁺⁺-CaM complexes interact with inactive CaMKII at the autoregulatory site of two adjacent CaMKII subunits. This dissociates the catalytic site from the pseudosubstrate motif, allowing for the auto(cross)-phosphorylation of T286 on one alpha -subunit (T287 on a beta -subunit) by the catalytic site on an adjacent subunit. The T286 phosphorylation event blocks a reassociation of the catalytic domain with the internal pseudosubstrate motif, resulting in prolonged activation. Once activated, an autoinhibitory program ensues. The dissociation of Ca⁺⁺-CaM from CaMKII exposes a Thr at position 305. CaMKII autophosphorylation of Thr at this site downregulates existing CaMKII activity.

1. Griffith, L.C. (2004) J. Neurosci. 24:8391.
2. Hudmon, A. and H. Schulman (2002) Annu. Rev. Biochem. 71:473.
3. Lin, C.R. et al. (1987) Proc. Natl. Acad. Sci. USA 84:5962.
4. Thiel, G. et al. (1988) Proc. Natl. Acad. Sci. USA 85:6337.
5. Elgersma, Y. et al. (2002) Neuron 36:493.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for CaM Kinase II Antibody (PPS002)(3)

Publications using PPS002

• Ochiai, N;Etani, Y;Noguchi, T;Miura, T;Kurihara, T;Fukuda, Y;Hamada, H;Uemura, K;Takashima, K;Tamaki, M;Ishibashi, T;Ito, S;Yamakawa, S;Kanamoto, T;Okada, S;Nakata, K;Ebina, K; The pivotal role of the Hes1/Piezo1 pathway in the pathophysiology of glucocorticoid-induced osteoporosis JCI insight 2024-12-06 [PMID: 39641269] (Western Blot, Mouse)
• ME Schmidt, NS Caron, AE Aly, FL Lemarié, L Dal Cengio, Y Ko, N Lazic, L Anderson, B Nguyen, LA Raymond, MR Hayden DAPK1 Promotes Extrasynaptic GluN2B Phosphorylation and Striatal Spine Instability in the YAC128 Mouse Model of Huntington Disease Front Cell Neurosci, 2020-11-05;14(0):590569. 2020-11-05 [PMID: 33250715] (Immunoprecipitation, Mouse)
• Kummer M, Hammerschmidt T, Martinez A, Terwel D, Eichele G, Witten A, Figura S, Stoll M, Schwartz S, Pape H, Schultze J, Weinshenker D, Heneka M, Urban I Ear2 deletion causes early memory and learning deficits in APP/PS1 mice. J Neurosci, 2014-06-25;34(26):8845-54. 2014-06-25 [PMID: 24966384] (Western Blot, Mouse)