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Mouse Anti-NAA50 Recombinant Antibody (2C6) (CBMAB-N1014-WJ)

This product is a Mouse antibody that recognizes NAA50. The antibody 2C6 can be used for immunoassay techniques such as: ELISA, WB.
See all NAA50 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
2C6
Antibody Isotype
IgG1, κ
Application
ELISA, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1, κ
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!]

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
N(Alpha)-Acetyltransferase 50, NatE Catalytic Subunit
Introduction
N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:19744929, PubMed:22311970, PubMed:21900231, PubMed:27484799). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (PubMed:27484799). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (PubMed:19744929). Autoacetylates in vivo (PubMed:19744929). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (PubMed:19744929). Component of a N-alpha-acetyltransferase complex containing NAA10 and NAA15, but NAA50 does not influence the acetyltransferase activity of NAA10: this multiprotein complex probably constitutes the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (PubMed:16507339, PubMed:27484799). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (PubMed:17502424, PubMed:27422821).
Entrez Gene ID
UniProt ID
Alternative Names
N(Alpha)-Acetyltransferase 50, NatE Catalytic Subunit; N-Acetyltransferase 13 (GCN5-Related); N-Acetyltransferase San Homolog; N-Epsilon-Acetyltransferase 50; N-Acetyltransferase 13; NatE Catalytic Subunit; N-Acetyltransferase 5; HNaa50p; NAT13; NAT5; MAK3;
Function
N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:19744929, PubMed:22311970, PubMed:21900231, PubMed:27484799).

Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (PubMed:27484799).

Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (PubMed:19744929).

Autoacetylates in vivo (PubMed:19744929).

The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (PubMed:19744929).

Component of N-alpha-acetyltransferase complexes containing NAA10 and NAA15, which has N-alpha-acetyltransferase activity (PubMed:16507339, PubMed:29754825, PubMed:27484799, PubMed:32042062).

Does not influence the acetyltransferase activity of NAA10 (PubMed:16507339, PubMed:27484799).

However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex) (PubMed:32042062).

The multiprotein complexes probably constitute the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (PubMed:16507339, PubMed:27484799).

Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (PubMed:17502424, PubMed:27422821).
Biological Process
Establishment of mitotic sister chromatid cohesion Source: UniProtKB
Histone acetylation Source: GO_Central
Mitotic sister chromatid cohesion Source: GO_Central
Mitotic sister chromatid cohesion, centromeric Source: UniProtKB
N-terminal protein amino acid acetylation Source: UniProtKB
Cellular Location
Cytoplasm
Nucleus
Note: Localizes to the cytoplasm in interphase cells (PubMed:17502424).

Lee, K., & Back, K. (2023). Human Naa50 Shows Serotonin N-Acetyltransferase Activity, and Its Overexpression Enhances Melatonin Biosynthesis, Resulting in Osmotic Stress Tolerance in Rice. Antioxidants, 12(2), 319.

Feng, J., Qin, M., Yao, L., Li, Y., Han, R., & Ma, L. (2022). The N-terminal acetyltransferase Naa50 regulates tapetum degradation and pollen development in Arabidopsis. Plant Science, 316, 111180.

Fang, T., Wang, D., Li, R., Yu, W., & Tian, H. (2022). Pan-cancer analysis reveals NAA50 as a cancer prognosis and immune infiltration-related biomarker. Frontiers in Genetics, 13, 1035337.

Weidenhausen, J., Kopp, J., Ruger-Herreros, C., Stein, F., Haberkant, P., Lapouge, K., & Sinning, I. (2022). Extended N-terminal acetyltransferase NAA50 in filamentous fungi adds to NAA50 diversity. International Journal of Molecular Sciences, 23(18), 10805.

Weidenhausen, J., Kopp, J., Armbruster, L., Wirtz, M., Lapouge, K., & Sinning, I. (2021). Structural and functional characterization of the N-terminal acetyltransferase Naa50. Structure, 29(5), 413-425.

Feng, J., Hu, J., Li, Y., Li, R., Yu, H., & Ma, L. (2020). The N-terminal acetyltransferase Naa50 regulates Arabidopsis growth and osmotic stress response. Plant and Cell Physiology, 61(9), 1565-1575.

Armbruster, L., Linster, E., Boyer, J. B., Brünje, A., Eirich, J., Stephan, I., ... & Wirtz, M. (2020). NAA50 is an enzymatically active N α-acetyltransferase that is crucial for development and regulation of stress responses. Plant Physiology, 183(4), 1502-1516.

Kung, P. P., Bingham, P., Burke, B. J., Chen, Q., Cheng, X., Deng, Y. L., ... & Stewart, A. E. (2020). Characterization of specific N-α-acetyltransferase 50 (Naa50) inhibitors identified using a DNA encoded library. ACS Medicinal Chemistry Letters, 11(6), 1175-1184.

Neubauer, M., & Innes, R. W. (2020). Loss of the acetyltransferase NAA50 induces endoplasmic reticulum stress and immune responses and suppresses growth. Plant Physiology, 183(4), 1838-1854.

Deng, S., Magin, R. S., Wei, X., Pan, B., Petersson, E. J., & Marmorstein, R. (2019). Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex. Structure, 27(7), 1057-1070.

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

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