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Mouse Anti-MUTYH (AA 436-535) Recombinant Antibody (CBFYM-2837) (CBMAB-M3030-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-2837
Antibody Isotype
IgG1, k
Application
ELISA, IF, WB

Basic Information

Immunogen
Recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.Immunogen sequence: KLTYQVYGLA LEGQTPVTTV PPGARWLTQE EFHTAAVSTA MKKVFRVYQG QQPGTCMGSK RSQVSSPCSR KKPRMGQQVL DNFFRSHIST DAHSLNSAAQ
Specificity
Human
Antibody Isotype
IgG1, k
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 436-535

Target

Full Name
MutY DNA Glycosylase
Introduction
This gene encodes a DNA glycosylase involved in oxidative DNA damage repair. The enzyme excises adenine bases from the DNA backbone at sites where adenine is inappropriately paired with guanine, cytosine, or 8-oxo-7,8-dihydroguanine, a major oxidatively damaged DNA lesion. The protein is localized to the nucleus and mitochondria. This gene product is thought to play a role in signaling apoptosis by the introduction of single-strand breaks following oxidative damage. Mutations in this gene result in heritable predisposition to colorectal cancer, termed MUTYH-associated polyposis. Multiple transcript variants encoding different isoforms have been found for this gene.
Entrez Gene ID
4595
UniProt ID
Q9UIF7
Alternative Names
MutY DNA Glycosylase; MutY Homolog; MYH; A/G-Specific Adenine DNA Glycosylase; Adenine DNA Glycosylase; MutY Homolog (E. Coli)
Function
Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase activities.
Biological Process
Base-excision repair Source: GO_Central
Depurination Source: Reactome
DNA repair Source: ProtInc
Mismatch repair Source: GO_Central
Cellular Location
Mitochondrion
Nucleus
Involvement in disease
Familial adenomatous polyposis 2 (FAP2):
A condition characterized by the development of multiple colorectal adenomatous polyps, benign neoplasms derived from glandular epithelium. Some affected individuals may develop colorectal carcinoma.
Gastric cancer (GASC):
A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.
More Infomation

Robinson, P. S., Thomas, L. E., Abascal, F., Jung, H., Harvey, L. M., West, H. D., ... & Stratton, M. R. (2022). Inherited MUTYH mutations cause elevated somatic mutation rates and distinctive mutational signatures in normal human cells. Nature Communications, 13(1), 3949.

Magrin, L., Fanale, D., Brando, C., Corsini, L. R., Randazzo, U., Di Piazza, M., ... & Bazan, V. (2022). MUTYH-associated tumor syndrome: The other face of MAP. Oncogene, 41(18), 2531-2539.

Barreiro, R. A. S., Sabbaga, J., Rossi, B. M., Achatz, M. I. W., Bettoni, F., Camargo, A. A., ... & AF Galante, P. (2022). Monoallelic deleterious MUTYH germline variants as a driver for tumorigenesis. The Journal of Pathology, 256(2), 214-222.

Mizuno, Y., Abolhassani, N., Mazzei, G., Sakumi, K., Saito, T., Saido, T. C., ... & Nakabeppu, Y. (2021). MUTYH actively contributes to microglial activation and impaired neurogenesis in the pathogenesis of Alzheimer’s disease. Oxidative medicine and cellular longevity, 2021.

Nielsen, M., Infante, E., & Brand, R. (2021). MUTYH polyposis.

Hutchcraft, M. L., Gallion, H. H., & Kolesar, J. M. (2021). MUTYH as an emerging predictive biomarker in ovarian cancer. Diagnostics, 11(1), 84.

Jang, S., Schaich, M. A., Khuu, C., Schnable, B. L., Majumdar, C., Watkins, S. C., ... & Van Houten, B. (2021). Single molecule analysis indicates stimulation of MUTYH by UV-DDB through enzyme turnover. Nucleic Acids Research, 49(14), 8177-8188.

Nakamura, T., Okabe, K., Hirayama, S., Chirifu, M., Ikemizu, S., Morioka, H., ... & Yamagata, Y. (2021). Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer. Nucleic acids research, 49(12), 7154-7163.

Curia, M. C., Catalano, T., & Aceto, G. M. (2020). MUTYH: Not just polyposis. World Journal of Clinical Oncology, 11(7), 428.

Raetz, A. G., & David, S. S. (2019). When you’re strange: Unusual features of the MUTYH glycosylase and implications in cancer. DNA repair, 80, 16-25.

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

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