Overview

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      CLQIQRNDYVHALVTYFNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLED YLTVRRGEEIYGTISMKPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR
    • Amino acids
      235 to 334
    • Tags
      proprietary tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab153421 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    ELISA

    Western blot

  • Form
    Liquid
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • ANM8_HUMAN
    • Heterogeneous nuclear ribonucleoprotein methyltransferase like protein 4
    • Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4
    • HMT1 hnRNP methyltransferase like 3
    • HMT1 hnRNP methyltransferase like 4
    • HRMT1 L3
    • HRMT1 L4
    • HRMT1L 3
    • HRMT1L 4
    • HRMT1L3
    • HRMT1L4
    • prmt8
    • Protein arginine N methyltransferase 4
    • Protein arginine N methyltransferase 8
    • Protein arginine N-methyltransferase 8
    see all
  • Function
    Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS.
  • Tissue specificity
    Brain-specific.
  • Sequence similarities
    Belongs to the protein arginine N-methyltransferase family. PRMT8 subfamily.
  • Domain
    The SH3-binding motifs mediate the interaction with SH3 domain-containing proteins such as PRMT2 and FYN, possibly leading to displace the N-terminal domain and activate the protein.
    The N-terminal region (1-60) inhibits the enzymatic activity.
  • Cellular localization
    Cell membrane.
  • Information by UniProt

Images

  • ab153421 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab153421 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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