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Mouse Anti-HMCES Recombinant Antibody (CBFYH-1491) (CBMAB-H2448-FY)

This product is mouse antibody that recognizes HMCES. The antibody CBFYH-1491 can be used for immunoassay techniques such as: WB, IP, IF, ELISA.
See all HMCES antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-1491
Application
WB, IP, IF, ELISA

Basic Information

Specificity
Human
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.

Target

Full Name
5-Hydroxymethylcytosine Binding, ES Cell Specific
Introduction
HMCES (5-Hydroxymethylcytosine Binding, ES Cell Specific) is a Protein Coding gene. Gene Ontology (GO) annotations related to this gene include peptidase activity.
Entrez Gene ID
56941
UniProt ID
Q96FZ2
Alternative Names
5-Hydroxymethylcytosine Binding, ES Cell Specific; Embryonic Stem Cell-Specific 5-Hydroxymethylcytosine-Binding Protein; 5-Hydroxymethylcytosine (HmC) Binding, ES Cell-Specific; ES Cell-Specific 5hmC-Binding Protein; SRAP Domain-Containing Protein 1; Putative Peptidase SRAPD1; C3orf37
Function
Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites (PubMed:30554877, PubMed:31235915, PubMed:31235913).

Acts as an enzyme that recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue (PubMed:30554877, PubMed:31235913).

The HMCES DNA-protein cross-link is then degraded by the proteasome (PubMed:30554877).

Promotes error-free repair of abasic sites by acting as a 'suicide' enzyme that is degraded, thereby protecting abasic sites from translesion synthesis (TLS) polymerases and endonucleases that are error-prone and would generate mutations and double-strand breaks (PubMed:30554877).

Has preference for ssDNA, but can also accommodate double-stranded DNA with 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction (PubMed:31235915, PubMed:31806351).

Also involved in class switch recombination (CSR) in B-cells independently of the formation of a DNA-protein cross-link: acts by binding and protecting ssDNA overhangs to promote DNA double-strand break repair through the microhomology-mediated alternative-end-joining (Alt-EJ) pathway (By similarity).

Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity).
Biological Process
Cellular response to DNA damage stimulus Source: UniProtKB
Double-strand break repair via alternative nonhomologous end joining Source: Ensembl
Positive regulation of isotype switching Source: UniProtKB
Protein-DNA covalent cross-linking Source: UniProtKB
Cellular Location
Chromosome. Recruited to chromatin following DNA damage (PubMed:30554877). Localizes to replication forks (PubMed:30554877).
PTM
Ubiquitinated; the covalent HMCES DNA-protein cross-link is ubiquitinated, leading to its degradation by the proteasome.

Sugimoto, Y., Masuda, Y., Iwai, S., Miyake, Y., Kanao, R., & Masutani, C. (2023). Novel mechanisms for the removal of strong replication-blocking HMCES-and thiazolidine-DNA adducts in humans. Nucleic Acids Research, 51(10), 4959-4981.

Semlow, D. R., MacKrell, V. A., & Walter, J. C. (2022). The HMCES DNA-protein cross-link functions as an intermediate in DNA interstrand cross-link repair. Nature structural & molecular biology, 29(5), 451-462.

Wu, L., Shukla, V., Yadavalli, A. D., Dinesh, R. K., Xu, D., Rao, A., & Schatz, D. G. (2022). HMCES protects immunoglobulin genes specifically from deletions during somatic hypermutation. Genes & Development, 36(7-8), 433-450.

Pan, Y., Zuo, H., Wen, F., Huang, F., Zhu, Y., Cao, L., ... & Shen, L. (2022). HMCES safeguards genome integrity and long-term self-renewal of hematopoietic stem cells during stress responses. Leukemia, 36(4), 1123-1131.

Biayna, J., Garcia-Cao, I., Álvarez, M. M., Salvadores, M., Espinosa-Carrasco, J., McCullough, M., ... & Stracker, T. H. (2021). Loss of the abasic site sensor HMCES is synthetic lethal with the activity of the APOBEC3A cytosine deaminase in cancer cells. PLoS Biology, 19(3), e3001176.

Srivastava, M., Su, D., Zhang, H., Chen, Z., Tang, M., Nie, L., & Chen, J. (2020). HMCES safeguards replication from oxidative stress and ensures error‐free repair. EMBO reports, 21(6), e49123.

Mehta, K. P., Lovejoy, C. A., Zhao, R., Heintzman, D. R., & Cortez, D. (2020). HMCES maintains replication fork progression and prevents double-strand breaks in response to APOBEC deamination and abasic site formation. Cell reports, 31(9).

Shukla, V., Halabelian, L., Balagere, S., Samaniego-Castruita, D., Feldman, D. E., Arrowsmith, C. H., ... & Aravind, L. (2020). HMCES functions in the alternative end-joining pathway of the DNA DSB repair during class switch recombination in B cells. Molecular cell, 77(2), 384-394.

Mohni, K. N., Wessel, S. R., Zhao, R., Wojciechowski, A. C., Luzwick, J. W., Layden, H., ... & Cortez, D. (2019). HMCES maintains genome integrity by shielding abasic sites in single-strand DNA. Cell, 176(1), 144-153.

Halabelian, L., Ravichandran, M., Li, Y., Zeng, H., Rao, A., Aravind, L., & Arrowsmith, C. H. (2019). Structural basis of HMCES interactions with abasic DNA and multivalent substrate recognition. Nature structural & molecular biology, 26(7), 607-612.

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

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