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AB101625

Anti-NSUN4 antibody

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(2 Publications)

Rabbit Polyclonal NSUN4 antibody. Suitable for WB and reacts with Mouse, Human, Rat samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human NSUN4 aa 1-250.

View Alternative Names

5-cytosine rRNA methyltransferase NSUN4, 5-cytosine tRNA methyltransferase NSUN4, NOL1/NOP2/Sun domain family member 4, mRNA cytosine C(5)-methyltransferase NSUN4, NSUN4

4 Images
Western blot - Anti-NSUN4 antibody (AB101625)
  • WB

Unknown

Western blot - Anti-NSUN4 antibody (AB101625)

10% SDS PAGE

All lanes:

Western blot - Anti-NSUN4 antibody (ab101625) at 1/1000 dilution

All lanes:

HepG2 whole cell lysate at 30 µg

Predicted band size: 43 kDa

false

Western blot - Anti-NSUN4 antibody (AB101625)
  • WB

Supplier Data

Western blot - Anti-NSUN4 antibody (AB101625)

Samples were separated by 10% SDS PAGE. The signal was developed with Trident ECL plus-Enhanced.

All lanes:

Western blot - Anti-NSUN4 antibody (ab101625) at 1/1000 dilution

Lane 1:

Mouse muscle tissue extracts at 50 µg

Lane 2:

Mouse eye tissue extracts at 50 µg

Secondary

All lanes:

HRP-conjugated anti-rabbit IgG antibody

Predicted band size: 43 kDa

true

Western blot - Anti-NSUN4 antibody (AB101625)
  • WB

Supplier Data

Western blot - Anti-NSUN4 antibody (AB101625)

Samples were separated by 10% SDS PAGE.

All lanes:

Western blot - Anti-NSUN4 antibody (ab101625) at 1/500 dilution

All lanes:

Mouse liver tissue extract at 50 µg

Predicted band size: 43 kDa

false

Western blot - Anti-NSUN4 antibody (AB101625)
  • WB

CiteAb

Western blot - Anti-NSUN4 antibody (AB101625)

NSUN4 western blot using anti-NSUN4 antibody ab101625. Publication image and figure legend from Gkatza, N. A., Castro, C., et al., 2019, PLoS Biol, PubMed 31199786.

ab101625 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab101625 please see the product overview.

Levels of m5C changes site-specifically and dynamically in response to oxidative stress.(A) Time course of sodium arsenite treatment. (B) Log2 FC of Nsun2 RNA expression in NSUN2+/+ and NSUN2+/- cells relative to GAPDH and normalised to the untreated control ('Ctr'). Shown are 3 replicates. (C) Western blot analysis of the indicated proteins using whole cell lysates from NSUN2+/+ and NSUN2-/- cells. Hsp90 served as a loading control. (D,E) Detection of m5C in sodium arsenite–treated and untreated ('ctr') NSUN2+/+ and -/- cells using mass spectrometry. (n = 3 samples per time point). (F) Quantification of tRNA methylation percentage using RNA bisulfite sequencing of NSUN2+/+ and NSUN2-/- cells (n = 4 samples per time point). (G) Heatmap of methylation status of individual tRNA molecules shown in (F). (H,I) Quantification (H) and heatmap (I) of methylation changes in the tRNAs LeuCAA and AspGTC in NSUN2+/+ and NSUN2-/- cells. (J) Quantification of methylation in non-tRNA targets. Data represent median in F, H, and J. Error bars are ±SD. p-Values : Student's t test, *p < 0.05 and **p < 0.01. ***p < 0.001. The underlying data for this figure can be found in S8 and S9 Data and S1 File. FC, fold-change; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; HSP90, heat shock protein 90; m5C, 5-methylcytosine; NPMI, nucleophosmin; tRNA, transfer RNA; VL, variable loop.

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human, Mouse, Rat

Applications

WB

applications

Immunogen

Recombinant Fragment Protein within Human NSUN4 aa 1-250. The exact immunogen used to generate this antibody is proprietary information.

Q96CB9

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: 20% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

NSUN4 also known as NOP2/Sun domain family member 4 is a methyltransferase enzyme that modifies RNA molecules by adding a methyl group to cytosine residues. It has a mass of approximately 55 kDa. NSUN4 is found in the mitochondria where it is expressed in various tissues especially in those with high energy demands such as muscle and nerve tissues. Its function is essential for mitochondrial ribosomal activity contributing to the proper synthesis of proteins within the mitochondrion.
Biological function summary

NSUN4 plays a role in mitochondrial translation by forming a complex with MTERF4. This complex is important for the methylation of mitochondrial rRNA which ensures the correct assembly and functionality of the mitochondrial ribosome. Through this modification NSUN4 influences the expression of the mitochondrial genome supporting efficient protein synthesis necessary for cellular energetics and function.

Pathways

NSUN4 integrates into mitochondrial biogenesis and gene expression pathways. It is significantly involved in the regulation of mitochondrial translation a subprocess of the broader mitochondrial translation pathway. NSUN4's activity closely interacts with proteins such as MTERF4 which assists in maintaining mitochondrial DNA transcription and replication illustrating its critical place in sustaining mitochondrial integrity and energy homeostasis.

NSUN4 has implications in mitochondrial-related disorders particularly those affecting energy-dependent tissues. Dysfunction in NSUN4 can lead to challenges in mitochondrial bioenergetics contributing to conditions like mitochondrial myopathy and neurodegenerative diseases which can result from impaired mitochondrial translation. Additionally its interplay with MTERF4 suggests that disruptions in this protein complex might exacerbate conditions related to mitochondrial gene expression defects.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Mitochondrial RNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in various RNAs, such as rRNAs, mRNAs and some long non-coding RNAs (lncRNAs) (PubMed : 21531335, PubMed : 23022348, PubMed : 39019044). Involved in mitochondrial ribosome small subunit (SSU) maturation by catalyzing methylation of mitochondrial 12S rRNA; the function is independent of MTERFD2/MTERF4 and assembled mitochondrial ribosome large subunit (LSU) (PubMed : 21531335, PubMed : 23022348). Targeted to LSU by MTERFD2/MTERF4 and probably is involved in a final step in ribosome biogenesis to ensure that SSU and LSU are assembled (PubMed : 21531335, PubMed : 23022348). In vitro can methylate 16S rRNA of the LSU; the methylation is enhanced by MTERFD/MTERF4 (PubMed : 23022348). Also acts as a regulator of innate immunity by marking double-stranded mitochondrial RNAs(mt-dsRNAs) generated in response to stress : catalyzes m5C modification on mitochondrial RNAs, such as a mRNAs and lncRNAs, with a preference for the termini of light-strand lncRNAs, promoting their degradation and cytosolic release (PubMed : 39019044). Modified light-strand lncRNAs are then recognized by C1QBP reader and recruited to the mitochondrial degradosome complex, which promotes their degradation (PubMed : 39019044).
See full target information NSUN4

Publications (2)

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Molecular cell 84:2935-2948.e7 PubMed39019044

2024

RNA 5-methylcytosine marks mitochondrial double-stranded RNAs for degradation and cytosolic release.

Applications

Unspecified application

Species

Unspecified reactive species

Sujin Kim,Stephanie Tan,Jayoung Ku,Tria Asri Widowati,Doyeong Ku,Keonyong Lee,Kwontae You,Yoosik Kim

PLoS biology 17:e3000297 PubMed31199786

2019

Cytosine-5 RNA methylation links protein synthesis to cell metabolism.

Applications

Unspecified application

Species

Unspecified reactive species

Nikoletta A Gkatza,Cecilia Castro,Robert F Harvey,Matthias Heiß,Martyna C Popis,Sandra Blanco,Susanne Bornelöv,Abdulrahim A Sajini,Joseph G Gleeson,Julian L Griffin,James A West,Stefanie Kellner,Anne E Willis,Sabine Dietmann,Michaela Frye
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