N6-Methyladenosine/m6A Antibody (Rabbit mAb) [B12K9]

Application: Reactivity: All Species Expected

Usage Information

Dilution

Application
Dot Blot

Reactivity
All Species Expected

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Datasheet & SDS

Biological Description

Specificity
N6-Methyladenosine/m6A Antibody (Rabbit mAb) [B12K9] detects N6-methyladenosine (m6A) modifications on RNA.

Clone
B12K9

Synonym(s)
N6-methyladenosine \| m6A

Background
N6‑Methyladenosine (m6A) is a reversible methylation of adenosine at the N6 position that represents the most abundant internal RNA modification on eukaryotic mRNA and many non‑coding RNAs, where it acts as an epitranscriptomic mark that shapes RNA fate and gene expression without altering the underlying nucleotide sequence. The modification is installed by a multicomponent “writer” complex centred on METTL3 and METTL14, with auxiliary factors such as WTAP, VIRMA and RBM15/15B, and occurs preferentially at consensus DRACH motifs (D = A/G/U, R = A/G, H = A/C/U) enriched in exons, near stop codons and in 3′ UTRs; it is removed by Fe²⁺/α‑ketoglutarate–dependent dioxygenase “erasers” including FTO and ALKBH5, and interpreted by “reader” proteins such as YTHDF1/2/3, YTHDC1, IGF2BP1–3 and hnRNPs that bind m6A and modulate splicing, nuclear export, translation and decay. Transcriptome‑wide m6A mapping and functional studies show that m6A influences almost every step of RNA metabolism: methylation in pre‑mRNA can recruit splicing regulators and alter exon inclusion; m6A in mature mRNA affects nuclear export and cytoplasmic localization; reader‑mediated interactions in the cytoplasm can either promote translation initiation and elongation or accelerate mRNA deadenylation and decay, depending on reader identity, so that dynamic m6A deposition and removal fine‑tune the abundance and translation of key transcripts in development, stress responses and disease. In cancer biology, m6A has emerged as a central regulator of oncogenic processes: dysregulation of m6A writers, erasers or readers can reprogram differentiation, sustain cancer stem cell self‑renewal, promote proliferation, metastasis and therapy resistance, and alter the tumour immune microenvironment by modulating immune checkpoint expression, cytokine transcripts and innate immune sensing of double‑stranded RNA; recent reviews highlight that METTL3, METTL14, WTAP, FTO, ALKBH5 and YTH family proteins have context‑dependent tumour‑promoting or suppressive roles across leukaemias and solid tumours, and that small‑molecule inhibitors of METTL3 or FTO can disrupt m6A‑dependent oncogenic pathways and enhance anti‑tumour immunity in preclinical models. m6A also modifies non‑coding RNAs—long non‑coding RNAs, microRNAs and circular RNAs—and thereby affects their biogenesis, stability and function; for example, m6A marks in pri‑miRNAs recruit DGCR8 to promote miRNA processing, m6A in lncRNAs can control their nuclear scaffolding roles, and m6A on circRNAs influences their translation or ability to act as competing endogenous RNAs, linking m6A to post‑transcriptional regulation of inflammatory, metabolic and developmental pathways.

Background

N6‑Methyladenosine (m6A) is a reversible methylation of adenosine at the N6 position that represents the most abundant internal RNA modification on eukaryotic mRNA and many non‑coding RNAs, where it acts as an epitranscriptomic mark that shapes RNA fate and gene expression without altering the underlying nucleotide sequence. The modification is installed by a multicomponent “writer” complex centred on METTL3 and METTL14, with auxiliary factors such as WTAP, VIRMA and RBM15/15B, and occurs preferentially at consensus DRACH motifs (D = A/G/U, R = A/G, H = A/C/U) enriched in exons, near stop codons and in 3′ UTRs; it is removed by Fe²⁺/α‑ketoglutarate–dependent dioxygenase “erasers” including FTO and ALKBH5, and interpreted by “reader” proteins such as YTHDF1/2/3, YTHDC1, IGF2BP1–3 and hnRNPs that bind m6A and modulate splicing, nuclear export, translation and decay. Transcriptome‑wide m6A mapping and functional studies show that m6A influences almost every step of RNA metabolism: methylation in pre‑mRNA can recruit splicing regulators and alter exon inclusion; m6A in mature mRNA affects nuclear export and cytoplasmic localization; reader‑mediated interactions in the cytoplasm can either promote translation initiation and elongation or accelerate mRNA deadenylation and decay, depending on reader identity, so that dynamic m6A deposition and removal fine‑tune the abundance and translation of key transcripts in development, stress responses and disease. In cancer biology, m6A has emerged as a central regulator of oncogenic processes: dysregulation of m6A writers, erasers or readers can reprogram differentiation, sustain cancer stem cell self‑renewal, promote proliferation, metastasis and therapy resistance, and alter the tumour immune microenvironment by modulating immune checkpoint expression, cytokine transcripts and innate immune sensing of double‑stranded RNA; recent reviews highlight that METTL3, METTL14, WTAP, FTO, ALKBH5 and YTH family proteins have context‑dependent tumour‑promoting or suppressive roles across leukaemias and solid tumours, and that small‑molecule inhibitors of METTL3 or FTO can disrupt m6A‑dependent oncogenic pathways and enhance anti‑tumour immunity in preclinical models. m6A also modifies non‑coding RNAs—long non‑coding RNAs, microRNAs and circular RNAs—and thereby affects their biogenesis, stability and function; for example, m6A marks in pri‑miRNAs recruit DGCR8 to promote miRNA processing, m6A in lncRNAs can control their nuclear scaffolding roles, and m6A on circRNAs influences their translation or ability to act as competing endogenous RNAs, linking m6A to post‑transcriptional regulation of inflammatory, metabolic and developmental pathways.

References
https://pubmed.ncbi.nlm.nih.gov/23453015/ https://pubmed.ncbi.nlm.nih.gov/31801551/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Handling Instructions

Tel: +1-832-582-8158 Ext:3

If you have any other enquiries, please leave a message.

Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%