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Mouse Anti-CAMKK2 Recombinant Antibody (239CT7.5.3) (CBMAB-C1269-CN)

This product is a Mouse antibody that recognizes CAMKK2. The antibody 239CT7.5.3 can be used for immunoassay techniques such as: ELISA, WB.
See all CAMKK2 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
239CT7.5.3
Antibody Isotype
IgM, κ
Application
ELISA, WB

Basic Information

Immunogen
CAMKK2 Mab is generated from mouse immunized with CAMKK2 recombinant protein
Specificity
Human, Mouse
Antibody Isotype
IgM, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Buffer
PBS, pH 7.2
Preservative
0.09% Sodium azide

Target

Full Name
Calcium/Calmodulin Dependent Protein Kinase Kinase 2
Introduction
This gene encodes a class I protein methyltransferase that acts in the formation of trimethyllysine in calmodulin. The protein contains a AdoMet-binding motif and may play a role in calcium-dependent signaling. [provided by RefSeq, Sep 2012]
Entrez Gene ID
Human10645
Mouse207565
UniProt ID
HumanQ96RR4
MouseQ8C078
Alternative Names
Calcium/Calmodulin Dependent Protein Kinase Kinase 2; Calcium/Calmodulin-Dependent Protein Kinase Kinase 2, Beta; Calcium/Calmodulin-Dependent Protein Kinase Kinase Beta; CaM-Kinase Kinase Beta; CaM-Kinase Kinase 2; CaM-KK Beta; CaM-KK 2; CAMKKB; Calcium/Calmodulin-Dependent Protein Kinase Kinase 2;
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.

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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