Key features and details
- Expression system: Baculovirus infected Sf9 cells
- Purity: >= 92% SDS-PAGE
- Active: Yes
- Tags: His-DDDDK tag N-Terminus
- Suitable for: SDS-PAGE, Functional Studies
Product nameRecombinant human PRMT8 protein
See all PRMT8 proteins and peptides
Specific activity: 2.22 pmol/min/µg.
Purity>= 92 % SDS-PAGE.
Expression systemBaculovirus infected Sf9 cells
Protein lengthProtein fragment
SequenceMSKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHVF KDKVVLDVGSGTGILSMFAAKAGAKKVFGIECSSISDYSEKIIKANHLDN IITIFKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKP GGLMFPDRAALYVVAIEDRQYKDFKIHWWENVYGFDMTCIRDVAMKEPLV DIVDPKQVVTNACLIKEVDIYTVKTEELSFTSAFCLQIQRNDYVHALVTY FNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLEDYLTVRRGEEIYGTISM KPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR
Predicted molecular weight41 kDa including tags
Amino acids61 to 394
TagsHis-DDDDK tag N-Terminus
Our Abpromise guarantee covers the use of ab196394 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.63% Tris HCl, 0.64% Sodium chloride, 0.02% Potassium chloride, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 20% Glycerol (glycerin, glycerine)
80 µg/mL FLAG peptide
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Heterogeneous nuclear ribonucleoprotein methyltransferase like protein 4
- Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4
FunctionMembrane-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.
Sequence similaritiesBelongs to the protein arginine N-methyltransferase family. PRMT8 subfamily.
DomainThe 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 localizationCell membrane.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab196394 has not yet been referenced specifically in any publications.