Human alpha-N-terminal Methyltransferase 1A/METTL11A Antibody Summary
Accession # Q9BV86
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Human alpha -N-terminal Methyltransferase 1A/
METTL11A by Western Blot.
Western blot shows lysates of U937 human histiocytic lymphoma cell line. PVDF membrane was probed with 2 µg/mL of Sheep Anti-Human alpha ‑N‑terminal Methyltransferase 1A/METTL11A Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7159) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for alpha ‑N‑terminal Methyltransferase 1A/
METTL11A at approximately 25 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: alpha-N-terminal Methyltransferase 1A/METTL11A
METTL11A, also named N‑terminal RCC1 methyltransferase (NRMT), is an alpha‑N‑methyltransferase that methylates the N‑terminal amino group of target proteins containing the N‑terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved (1). It is responsible for N‑terminal methylation of RCC1, KLHL31, MYL2, MYL3, RB1, RPL23A and SET. NRMT lacks a SET domain but possesses a Rossman‑like a/b fold. The residues Asn169, Asp178, Asp181, and Ser183 of NRMT are important for substrate binding (2). RCC1 (Ran guanine nucleotide‑exchange factor) is the first protein for which any biological function of alpha‑N‑methylation by NRMT has been identified (3, 4). The multi‑spindle phenotype associated with either NRMT knockdown or methylation‑defective RCC1 mutants demonstrated the importance of alpha‑N‑methylation of RCC1 for normal bipolar spindle formation and chromosome aggregation (2). NRMT is robustly overexpressed in gastrointestinal cancers.
- Webb, K. J. et al. (2010) Biochemistry 49:5225.
- Christine, S. E. et al. (2010) Nature 466:1125.
- Chen, T. et al. (2007) Nature Cell Biol. 9:596.
- Hao, Y. et al. (2008) J. Cell. Biol. 182:827.
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