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Mouse Anti-MIB1 (AA 909-1006) Recombinant Antibody (CBFYM-2199) (CBMAB-M2382-FY)

This product is mouse antibody that recognizes MIB1. The antibody CBFYM-2199 can be used for immunoassay techniques such as: ELISA.
See all MIB1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-2199
Antibody Isotype
IgG2a, k
Application
ELISA

Basic Information

Immunogen
Recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.Immunogen sequence: PFIMCCGGKS SEDATDDISS GNIPVLQKDK DNTNVNADVQ KLQQQLQDIK EQTMCPVCLD RLKNMIFLCG HGTCQLCGDR MSECPICRKA IERRILLY
Specificity
Human
Antibody Isotype
IgG2a, k
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
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 909-1006

Target

Full Name
mindbomb homolog 1 (Drosophila)
Introduction
This gene encodes a protein containing multiple ankyrin repeats and RING finger domains that functions as an E3 ubiquitin ligase. The encoded protein positively regulates Notch signaling by ubiquitinating the Notch receptors, thereby facilitating their endocytosis. This protein may also promote the ubiquitination and degradation of death-associated protein kinase 1.
Entrez Gene ID
57534
UniProt ID
Q86YT6
Alternative Names
Mindbomb E3 Ubiquitin Protein Ligase 1; Zinc Finger ZZ Type With Ankyrin Repeat Domain Protein 2; RING-Type E3 Ubiquitin Transferase MIB1; DAPK-Interacting Protein 1; ZZANK2; DIP-1; DIP1; E3 Ubiquitin-Protein Ligase MIB1; Mindbomb Homolog 1 (Drosophila)
Function
E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis (By similarity).

Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation.
Biological Process
Blood vessel development Source: Ensembl
Endocytosis Source: GO_Central
Heart looping Source: Ensembl
In utero embryonic development Source: Ensembl
Negative regulation of neuron differentiation Source: Ensembl
Neural tube formation Source: Ensembl
Notch signaling pathway Source: GO_Central
Positive regulation of endocytosis Source: Ensembl
Protein ubiquitination Source: GO_Central
Somitogenesis Source: Ensembl
Ubiquitin-dependent protein catabolic process Source: CACAO
Cellular Location
Cytoskeleton
centriolar satellite
Plasma membrane
Cell membrane
Cytoplasm
Note: Localizes to the plasma membrane (By similarity). According to PubMed:15048887, it is mitochondrial, however such localization remains unclear. Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock.
Involvement in disease
Left ventricular non-compaction 7 (LVNC7):
A form of left ventricular non-compaction, a cardiomyopathy due to myocardial morphogenesis arrest and characterized by a hypertrophic left ventricle, a severely thickened 2-layered myocardium, numerous prominent trabeculations, deep intertrabecular recesses, and poor systolic function. Clinical manifestations are variable. Some affected individuals experience no symptoms at all, others develop heart failure. In some cases, left ventricular non-compaction is associated with other congenital heart anomalies. LVNC7 is an autosomal dominant condition.
PTM
Ubiquitinated; possibly via autoubiquitination (By similarity). Ubiquitinated; this modification is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock.

Saha, S., Huang, S. Y. N., Yang, X., Saha, L. K., Sun, Y., Khandagale, P., ... & Pommier, Y. (2023). The TDRD3-USP9X complex and MIB1 regulate TOP3B homeostasis and prevent deleterious TOP3B cleavage complexes. Nature Communications, 14(1), 7524.

Wang, H., Huang, Q., Xia, J., Cheng, S., Pei, D., Zhang, X., & Shu, X. (2022). The E3 ligase MIB1 promotes proteasomal degradation of NRF2 and sensitizes lung cancer cells to ferroptosis. Molecular Cancer Research, 20(2), 253-264.

Saraswathy, V. M., Kurup, A. J., Sharma, P., Polès, S., Poulain, M., & Fürthauer, M. (2022). The E3 ubiquitin ligase mindbomb1 controls planar cell polarity-dependent convergent extension movements during zebrafish gastrulation. Elife, 11, e71928.

Sarbanes, S. L., Blomen, V. A., Lam, E., Heissel, S., Luna, J. M., Brummelkamp, T. R., ... & Rice, C. M. (2021). E3 ubiquitin ligase Mindbomb 1 facilitates nuclear delivery of adenovirus genomes. Proceedings of the National Academy of Sciences, 118(1), e2015794118.

Zhang, B., Cheng, X., Zhan, S., Jin, X., & Liu, T. (2021). MIB1 upregulates IQGAP1 and promotes pancreatic cancer progression by inducing ST7 degradation. Molecular Oncology, 15(11), 3062-3075.

Saraswathy, V. M., Sharma, P., Kurup, A. J., Polès, S., Poulain, M., & Fürthauer, M. (2021). The E3 Ubiquitin Ligase Mindbomb1 controls zebrafish Planar Cell Polarity. bioRxiv, 2021-07.

Douanne, T., André-Grégoire, G., Thys, A., Trillet, K., Gavard, J., & Bidère, N. (2019). CYLD regulates centriolar satellites proteostasis by counteracting the E3 ligase MIB1. Cell reports, 27(6), 1657-1665.

Bauer, M., Flatt, J. W., Seiler, D., Cardel, B., Emmenlauer, M., Boucke, K., ... & Greber, U. F. (2019). The E3 ubiquitin ligase mind bomb 1 controls adenovirus genome release at the nuclear pore complex. Cell reports, 29(12), 3785-3795.

Dho, S. E., Silva-Gagliardi, N., Morgese, F., Coyaud, E., Lamoureux, E., Berry, D. M., ... & McGlade, C. J. (2019). Proximity interactions of the ubiquitin ligase Mind bomb 1 reveal a role in regulation of epithelial polarity complex proteins. Scientific Reports, 9(1), 12471.

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

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