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Mouse Anti-CAMKK2 Recombinant Antibody (3H6) (CBMAB-0184-YC)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
3H6
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
E. coli-derived recombinant protein, aa 1-446 of human CaMKK II.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:2,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS
Preservative
0.09% sodium azide
Concentration
1 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Calcium/Calmodulin Dependent Protein Kinase Kinase 2
Introduction
CAMKK2 (calcium/calmodulin dependent protein kinase kinase 2) belongs to the Serine/Threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. The major isoform of this gene plays a role in the calcium/calmodulin-dependent (CaM) kinase cascade by phosphorylating the downstream kinases CaMK1 and CaMK4. CAMKK2 regulates production of the appetite stimulating hormone neuropeptide Y and functions as an AMPK kinase in the hypothalamus. It also has an important role in the development of hyperalgesia and tolerance to opioid analgesic drugs, through reduction in downstream signalling pathways and mu opioid receptor downregulation. Inhibition of CAMKK2 in mice reduces appetite and promotes weight loss.
Entrez Gene ID
10645
UniProt ID
Q96RR4
Alternative Names
Calcium/Calmodulin-Dependent Protein Kinase Kinase 2, Beta; CaM-Kinase Kinase Beta; CaM-Kinase Kinase 2; CaM-KK Beta; CaM-KK 2; CAMKKB; Calcium/Calmodulin-Dependent Protein Kinase Kinase Beta; Calcium/Calmodulin-Dependent Protein Kinase Beta; CAMKK Beta Protein; EC 2.7.11.17; CaMKK Beta; EC 2.7.11; KIAA0787; CaMKK 2; CAMKK
Function
Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca2+ signals (By similarity).
Seems to be involved in hippocampal activation of CREB1 (By similarity).
May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.
Biological Process
Calcium-mediated signaling Source: UniProtKB
CAMKK-AMPK signaling cascade Source: ParkinsonsUK-UCL
Cellular response to reactive oxygen species Source: ParkinsonsUK-UCL
Chemical synaptic transmission Source: Reactome
MAPK cascade Source: UniProtKB
Positive regulation of autophagy of mitochondrion Source: ParkinsonsUK-UCL
Positive regulation of protein phosphorylation Source: ParkinsonsUK-UCL
Positive regulation of transcription, DNA-templated Source: UniProtKB
Protein autophosphorylation Source: UniProtKB
Protein phosphorylation Source: UniProtKB
Regulation of protein kinase activity Source: UniProtKB
Cellular Location
Nucleus; Cytoplasm; Neuron projection. Predominantly nuclear in unstimulated cells, relocalizes into cytoplasm and neurites after forskolin induction.
PTM
Autophosphorylated and phosphorylated by PKA. Each isoform may show a different pattern of phosphorylation.
More Infomation

Wang, S., Yi, X., Wu, Z., Guo, S., Dai, W., Wang, H., ... & Li, C. (2021). CAMKK2 Defines Ferroptosis Sensitivity of Melanoma Cells by Regulating AMPK‒NRF2 Pathway. Journal of Investigative Dermatology.

Zhang, Y., Recouvreux, M. V., Jung, M., Galenkamp, K. M., Li, Y., Zagnitko, O., ... & Commisso, C. (2021). Macropinocytosis in Cancer-Associated Fibroblasts is Dependent on CaMKK2/ARHGEF2 Signaling and Functions to Support Tumor and Stromal Cell Fitness. Cancer Discovery.

Langendorf, C. G., O'Brien, M. T., Ngoei, K. R., McAloon, L. M., Dhagat, U., Hoque, A., ... & Scott, J. W. (2020). CaMKK2 is inactivated by cAMP-PKA signaling and 14-3-3 adaptor proteins. Journal of Biological Chemistry, 295(48), 16239-16250.

Spengler, K., Zibrova, D., Woods, A., Langendorf, C. G., Scott, J. W., Carling, D., & Heller, R. (2020). Protein kinase A negatively regulates VEGF-induced AMPK activation by phosphorylating CaMKK2 at serine 495. Biochemical Journal, 477(17), 3453-3469.

Lentini Santo, D., Petrvalska, O., Obsilova, V., Ottmann, C., & Obsil, T. (2020). Stabilization of Protein–Protein Interactions between CaMKK2 and 14–3–3 by Fusicoccins. ACS chemical biology, 15(11), 3060-3071.

O’Byrne, S. N., Scott, J. W., Pilotte, J. R., Santiago, A. D. S., Langendorf, C. G., Oakhill, J. S., ... & Drewry, D. H. (2020). In depth analysis of kinase cross screening data to identify CAMKK2 inhibitory scaffolds. Molecules, 25(2), 325.

Racioppi, L., Nelson, E. R., Huang, W., Mukherjee, D., Lawrence, S. A., Lento, W., ... & McDonnell, D. P. (2019). CaMKK2 in myeloid cells is a key regulator of the immune-suppressive microenvironment in breast cancer. Nature communications, 10(1), 1-16.

Tojkander, S., Ciuba, K., & Lappalainen, P. (2018). CaMKK2 regulates mechanosensitive assembly of contractile actin stress fibers. Cell reports, 24(1), 11-19.

Penfold, L., Woods, A., Muckett, P., Nikitin, A. Y., Kent, T. R., Zhang, S., ... & Carling, D. (2018). CAMKK2 promotes prostate cancer independently of AMPK via increased lipogenesis. Cancer research, 78(24), 6747-6761.

Jin, L., Chun, J., Pan, C., Kumar, A., Zhang, G., Ha, Y., ... & Kang, S. (2018). The PLAG1-GDH1 axis promotes anoikis resistance and tumor metastasis through CamKK2-AMPK signaling in LKB1-deficient lung cancer. Molecular cell, 69(1), 87-99.

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For research use only. Not intended for any clinical use.

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