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Mouse Anti-FBXO22 (AA 1-300) Recombinant Antibody (CBXF-0398) (CBMAB-F0282-CQ)

This product is a mouse antibody that recognizes FBXO22 (AA 1-300). The antibody CBXF-0398 can be used for immunoassay techniques such as: ELISA, WB.
See all FBXO22 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-0398
Antibody Isotype
IgG1
Application
ELISA, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
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
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 1-300

Target

Full Name
F-box protein 22
Introduction
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class and, as a transcriptional target of the tumor protein p53, is thought to be involved in degradation of specific proteins in response to p53 induction. Alternative splicing results in multiple transcript variants.
Entrez Gene ID
26263
UniProt ID
Q8NEZ5
Alternative Names
F-Box Protein 22; FIST Domain Containing 1; F-Box Protein FBX22p44; F-Box Only Protein 22; FBX22; FISTC1;
Research Area
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function.
Biological Process
Cellular protein modification process Source: ProtInc
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: GO_Central
Protein polyubiquitination Source: GO_Central
Regulation of skeletal muscle fiber development Source: GO_Central
Ubiquitin-dependent protein catabolic process Source: ProtInc
Cellular Location
Z line

Liu, P., Cong, X., Liao, S., Jia, X., Wang, X., Dai, W., ... & Tan, M. (2022). Global identification of phospho-dependent SCF substrates reveals a FBXO22 phosphodegron and an ERK-FBXO22-BAG3 axis in tumorigenesis. Cell Death & Differentiation, 29(1), 1-13.

Lin, M., Zhang, J., Bouamar, H., Wang, Z., Sun, L. Z., & Zhu, X. (2022). Fbxo22 promotes cervical cancer progression via targeting p57Kip2 for ubiquitination and degradation. Cell death & disease, 13(9), 1-14.

De, S., Holvey-Bates, E. G., Mahen, K., Willard, B., & Stark, G. R. (2021). The ubiquitin E3 ligase FBXO22 degrades PD-L1 and sensitizes cancer cells to DNA damage. Proceedings of the National Academy of Sciences, 118(47), e2112674118.

Ge, M. K., Zhang, N., Xia, L., Zhang, C., Dong, S. S., Li, Z. M., ... & Shen, S. M. (2020). FBXO22 degrades nuclear PTEN to promote tumorigenesis. Nature communications, 11(1), 1-14.

Cheng, J., Lin, M., Chu, M., Gong, L., Bi, Y., & Zhao, Y. (2020). Emerging role of FBXO22 in carcinogenesis. Cell death discovery, 6(1), 1-7.

Johmura, Y., Harris, A. S., Ohta, T., & Nakanishi, M. (2020). FBXO22, an epigenetic multiplayer coordinating senescence, hormone signaling, and metastasis. Cancer Science, 111(8), 2718-2725.

Hou, X. K., & Mao, J. S. (2020). Long noncoding RNA SNHG14 promotes osteosarcoma progression via miR-433-3p/FBXO22 axis. Biochemical and biophysical research communications, 523(3), 766-772.

Zhang, L., Chen, J., Ning, D., Liu, Q., Wang, C., Zhang, Z., ... & Chen, X. (2019). FBXO22 promotes the development of hepatocellular carcinoma by regulating the ubiquitination and degradation of p21. Journal of Experimental & Clinical Cancer Research, 38(1), 1-16.

Zhu, X. N., He, P., Zhang, L., Yang, S., Zhang, H. L., Zhu, D., ... & Yu, Y. (2019). FBXO22 mediates polyubiquitination and inactivation of LKB1 to promote lung cancer cell growth. Cell death & disease, 10(7), 1-11.

Sun, R., Xie, H. Y., Qian, J. X., Huang, Y. N., Yang, F., Zhang, F. L., ... & Li, D. Q. (2018). FBXO22 Possesses Both Protumorigenic and Antimetastatic Roles in Breast Cancer ProgressionDual Roles of FBXO22 in Mammary Tumorigenesis and Metastasis. Cancer research, 78(18), 5274-5286.

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

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