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Mouse Anti-CAMKK2 Recombinant Antibody (EG471) (CBMAB-EN534-LY)


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Published Data
CBMAB-EN534-LY-1
Mouse Anti-CAMKK2 Recombinant Antibody (EG471) (CBMAB-EN534-LY) in Immunoblot
Depletion of CDC25B does not change the AMPK -LKB1 interaction or AMPK-CaMKKβ interaction. HS578T cells were transfected with Negative siRNA or siCDC25B. 48 hours later, cell lysates were subjected to immunoprecipitation with control IgG or anti-AMPK antibody. The immunoprecipitates were blotted with the indicated antibodies. Data information: all data presented are a representation of N=3 independent experiments. ...View More
Cairns, J., Ly, R. C., Niu, N., Kalari, K. R., Carlson, E. E., & Wang, L. (2020). CDC25B partners with PP2A to induce AMPK activation and tumor suppression in triple negative breast cancer. NAR cancer, 2(4), zcaa039.

Summary

Host Animal
Mouse
Specificity
Human
Clone
EG471
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 1-95 mapping at the N-terminus of CaMKKβ of human origin.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
ELISA1:100-1:1,000
IF(ICC)1:50-1:500

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

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

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
Rat83506
UniProt ID
HumanQ96RR4
MouseQ8C078
RatO88831
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.
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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