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Mouse Anti-FOXK2 (AA 561-660) Recombinant Antibody (CBXF-3158) (CBMAB-F3854-CQ)

This product is a mouse antibody that recognizes FOXK2 (AA 561-660). The antibody CBXF-3158 can be used for immunoassay techniques such as: ELISA, IF, WB.
See all FOXK2 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-3158
Antibody Isotype
IgG
Application
ELISA, IF, WB

Basic Information

Immunogen
FOXK2 (NP_004505.2, 561aa-660aa) partial recombinant protein with GST tag
Specificity
Human
Antibody Isotype
IgG
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 7.4
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 561-660

Target

Full Name
forkhead box K2
Introduction
The protein encoded by this gene contains a fork head DNA binding domain. This protein can bind to the purine-rich motifs of the HIV long terminal repeat (LTR), and to the similar purine-rich motif in the interleukin 2 (IL2) promoter. It may be involved in the regulation of viral and cellular promoter elements.
Entrez Gene ID
3607
UniProt ID
Q01167
Alternative Names
Forkhead Box K2; Interleukin Enhancer-Binding Factor 1; Cellular Transcription Factor ILF-1; FOXK1; ILF1; ILF; Interleukin Enhancer Binding Factor 1; Forkhead Box Protein K2; ILF-1;
Function
Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis and autophagy (By similarity).

Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context (PubMed:22083952, PubMed:25451922).

Together with FOXK1, acts as a key regulator of metabolic reprogramming towards aerobic glycolysis, a process in which glucose is converted to lactate in the presence of oxygen (By similarity).

Acts by promoting expression of enzymes for glycolysis (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate kinase (PKLR) and lactate dehydrogenase), while suppressing further oxidation of pyruvate in the mitochondria by up-regulating pyruvate dehydrogenase kinases PDK1 and PDK4 (By similarity).

Probably plays a role in gluconeogenesis during overnight fasting, when lactate from white adipose tissue and muscle is the main substrate (By similarity).

Together with FOXK1, acts as a negative regulator of autophagy in skeletal muscle: in response to starvation, enters the nucleus, binds the promoters of autophagy genes and represses their expression, preventing proteolysis of skeletal muscle proteins (By similarity).

In addition to the 5'-GTAAACA-3' DNA motif, also binds the 5'-TGANTCA-3' palindromic DNA motif, and co-associates with JUN/AP-1 to activate transcription (PubMed:22083952).

Also able to bind to a minimal DNA heteroduplex containing a G/T-mismatch with 5'-TRT[G/T]NB-3' sequence (PubMed:20097901).

Binds to NFAT-like motifs (purine-rich) in the IL2 promoter (PubMed:1339390).

Positively regulates WNT/beta-catenin signaling by translocating DVL proteins into the nucleus (PubMed:25805136).

Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements (PubMed:1909027).
Biological Process
Canonical glycolysis Source: UniProtKB
Cellular glucose homeostasis Source: UniProtKB
Negative regulation of autophagy Source: UniProtKB
Negative regulation of transcription, DNA-templated Source: UniProtKB
Positive regulation of transcription, DNA-templated Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: NTNU_SB
Regulation of glucose metabolic process Source: UniProtKB
Regulation of transcription, DNA-templated Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: GO_Central
Response to starvation Source: UniProtKB
Cellular Location
Cytoplasm; Nucleus
PTM
Hyperphosphorylated during mitosis by CDK1 and, to a lower extent, CDK2 (PubMed:20810654). Phosphorylation at Ser-373 and Ser-428 affects stability by promoting degradation (PubMed:20810654).

Li, Y., Chen, J., Wang, B., Xu, Z., Wu, C., Ma, J., ... & Yao, Y. (2023). FOXK2 affects cancer cell response to chemotherapy by promoting nucleotide de novo synthesis. Drug Resistance Updates, 100926.

Zhang, Y., Wang, Y., Zhao, G., Tanner, E. J., Adli, M., & Matei, D. (2022). FOXK2 promotes ovarian cancer stemness by regulating the unfolded protein response pathway. The Journal of Clinical Investigation, 132(10).

Wang, Z., Liu, X., Wang, Z., & Hu, Z. (2022). FOXK2 transcription factor and its roles in tumorigenesis. Oncology Letters, 24(6), 1-21.

Li, S., Wang, P., Ju, H., Zhu, T., Shi, J., & Huang, Y. (2022). FOXK2 promotes the proliferation of papillary thyroid cancer cell by down-regulating autophagy. Journal of Cancer, 13(3), 858.

Nestal de Moraes, G., Carneiro, L. D. T., Maia, R. C., Lam, E. W. F., & Sharrocks, A. D. (2019). FOXK2 transcription factor and its emerging roles in cancer. Cancers, 11(3), 393.

Sukonina, V., Ma, H., Zhang, W., Bartesaghi, S., Subhash, S., Heglind, M., ... & Enerbäck, S. (2019). FOXK1 and FOXK2 regulate aerobic glycolysis. Nature, 566(7743), 279-283.

Sakaguchi, M., Cai, W., Wang, C. H., Cederquist, C. T., Damasio, M., Homan, E. P., ... & Kahn, C. R. (2019). FoxK1 and FoxK2 in insulin regulation of cellular and mitochondrial metabolism. Nature Communications, 10(1), 1582.

Zhang, F., Ma, X., Li, H., Zhang, Y., Li, X., Chen, L., ... & Zhang, X. (2018). FOXK2 suppresses the malignant phenotype and induces apoptosis through inhibition of EGFR in clear‐cell renal cell carcinoma. International journal of cancer, 142(12), 2543-2557.

Liu, X., Wei, X., Niu, W., Wang, D., Wang, B., & Zhuang, H. (2018). Downregulation of FOXK2 is associated with poor prognosis in patients with gastric cancer. Molecular medicine reports, 18(5), 4356-4364.

Nestal de Moraes, G., Ji, Z., Fan, L. Y. N., Yao, S., Zona, S., Sharrocks, A. D., & Lam, E. W. F. (2018). SUMOylation modulates FOXK2-mediated paclitaxel sensitivity in breast cancer cells. Oncogenesis, 7(3), 29.

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

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