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AB163025

Recombinant Human NAT10 protein (GST tag N-Terminus)

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Recombinant Human NAT10 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 1025 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

ALP, KIAA1709, NAT10, RNA cytidine acetyltransferase, 18S rRNA cytosine acetyltransferase, N-acetyltransferase 10, N-acetyltransferase-like protein, hALP

1 Images
SDS-PAGE - Recombinant Human NAT10 protein (AB163025)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human NAT10 protein (AB163025)

ab163025 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

Q9H0A0

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

This product was previously labelled as ALP.
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Sequence info

[{"sequence":"MHRKKVDNRIRILIENGVAERQRSLFVVVGDRGKDQVVILHHMLSKATVKARPSVLWCYKKELGFSSHRKKRMRQLQKKIKNGTLNIKQDDPFELFIAATNIRYCYYNETHKILGNTFGMCVLQDFEALTPNLLARTVETVEGGGLVVILLRTMNSLKQLYTVTMDVHSRYRTEAHQDVVGRFNERFILSLASCKKCLVIDDQLNILPISSHVATMEALPPQTPDESLGPSDLELRELKESLQDTQPVGVLVDCCKTLDQAKAVLKFIEGISEKTLRSTVALTAARGRGKSAALGLAIAGAVAFGYSNIFVTSPSPDNLHTLFEFVFKGFDALQYQEHLDYEIIQSLNPEFNKAVIRVNVFREHRQTIQYIHPADAVKLGQAELVVIDEAAAIPLPLVKSLLGPYLVFMASTINGYEGTGRSLSLKLIQQLRQQSAQSQVSTTAENKTTTTARLASARTLHEVSLQESIRYAPGDAVEKWLNDLLCLDCLNITRIVSGCPLPEACELYYVNRDTLFCYHKASEVFLQRLMALYVASHYKNSPNDLQMLSDAPAHHLFCLLPPVPPTQNALPEVLAVIQVCLEGEISRQSILNSLSRGKKASGDLIPWTVSEQFQDPDFGGLSGGRVVRIAVHPDYQGMGYGSRALQLLQMYYEGRFPCLEEKVLETPQEIHTVSSEAVSLLEEVITPRKDLPPLLLKLNERPAERLDYLGVSYGLTPRLLKFWKRAGFVPVYLRQTPNDLTGEHSCIMLKTLTDEDEADQGGWLAAFWKDFRRRFLALLSYQFSTFSPSLALNIIQNRNMGKPAQPALSREELEALFLPYDLKRLEMYSRNMVDYHLIMDMIPAISRIYFLNQLGDLALSAAQSALLLGIGLQHKSVDQLEKEIELPSGQLMGLFNRIIRKVVKLFNEVQEKAIEEQMVAAKDVVMEPTMKTLSDDLDEAAKEFQEKHKKEVGKLKSMDLSEYIIRGDDEEWNEVLNKAGPNASIISLKSDKKRKLEAKQEPKQSKKLKNRETKNKKDMKLKRKK","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":1025,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q9H0A0","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

N-acetyltransferase 10 (NAT10) also called hALP is an enzyme with a molecular mass of about 116 kDa. The NAT10 protein is expressed ubiquitously across tissues and primarily found in the nucleolus of cells. It exhibits acetyltransferase activity facilitating the transfer of acetyl groups to specific substrates. This enzyme also has known RNA binding capacity and shows involvement in various cellular processes including cell cycle regulation and rRNA synthesis.
Biological function summary

This enzyme plays a significant role in cellular activities by modulating chromatin dynamics and influencing cell cycle progression through acetylation of histones and non-histone proteins. NAT10 participates in rRNA transcription enhancing ribosomal biogenesis and therefore supporting protein synthesis within the cell. It functions as part of larger chromatin-associated complexes indicating its involvement in broader cellular systems beyond individual enzymatic activity.

Pathways

The NAT10 protein operates within important molecular pathways such as the p53 signaling and DNA damage response pathways. It contributes toward cellular response mechanisms to damage and stress acting alongside other proteins like p53 and CREB-binding protein connecting regulation of cell cycle arrest and apoptosis with its enzymatic activity. NAT10 also modulates the acetylation dynamics in these pathways affecting cellular outcomes under stress conditions.

Researchers have linked NAT10 to cancer and Hutchinson-Gilford progeria syndrome (HGPS). In cancer the relationship of NAT10 with p53 establishes its role in tumorigenesis where altered acetylation patterns may affect tumor suppression functions. In HGPS NAT10's impact on chromatin architecture connects it to lamin A dysfunction a hallmark of the disease. Its acetylation activity emerges as a critical factor influencing disease pathology making it a target for therapeutic exploration in these conditions.
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Specifications

Form

Liquid

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General info

Function

RNA cytidine acetyltransferase that catalyzes the formation of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed : 25411247, PubMed : 25653167, PubMed : 30449621, PubMed : 35679869). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed : 30449621, PubMed : 35679869). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed : 30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed : 25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed : 25411247, PubMed : 25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed : 25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed : 14592445, PubMed : 17631499, PubMed : 19303003, PubMed : 26882543, PubMed : 27993683, PubMed : 30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed : 30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed : 14592445, PubMed : 18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed : 31722219). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed : 34516797).

Sequence similarities

Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily.

Post-translational modifications

Acetylation at Lys-426 is required to activation of rRNA transcription (PubMed:27993683). May be autoacetylated; however ability to autoacetylate in vivo requires additional evidences (PubMed:27993683).

Subcellular localisation

Nucleus

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Product protocols

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Target data

RNA cytidine acetyltransferase that catalyzes the formation of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed : 25411247, PubMed : 25653167, PubMed : 30449621, PubMed : 35679869). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed : 30449621, PubMed : 35679869). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed : 30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed : 25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed : 25411247, PubMed : 25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed : 25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed : 14592445, PubMed : 17631499, PubMed : 19303003, PubMed : 26882543, PubMed : 27993683, PubMed : 30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed : 30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed : 14592445, PubMed : 18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed : 31722219). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed : 34516797).
See full target information NAT10
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