Analytical Data
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Gene name
PRMT1
- Application
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Alternative Names
CHTOP;C1orf77;FOP;Chromatin target of PRMT1 Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99873-3
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Expression Region
1-343aa
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AA Sequence
MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK DEVRTLTYRN SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE CSSISDYAVK IVKANKLDHV VTIIKGKVEE VELPVEKVDI IISEWMGYCL FYESMLNTVL YARDKWLAPD GLIFPDRATL YVTAIEDRQY KDYKIHWWEN VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY TVKVEDLTFT SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY RMR
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Molecular Weight
68 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
PRMT1 (protein arginine methyltransferase 1) is a key enzyme involved in the post-translational modification of proteins through the methylation of arginine residues. This modification plays a crucial role in various cellular processes, including gene regulation, signal transduction, and RNA metabolism. Dysregulation of PRMT1 is implicated in several diseases, including cancer, cardiovascular disorders, and neurodegenerative conditions, highlighting its potential as a therapeutic target. The study of PRMT1 and its recombinant protein production has gained significant attention as it allows for detailed functional analyses of the enzyme and its substrates. Recombinant PRMT1 provides an opportunity to explore its enzymatic activity, substrate specificity, and interaction with other molecular partners in vitro. Furthermore, understanding the structure-function relationship of PRMT1 through crystallography and mutagenesis studies can unveil mechanisms underlying its regulation and biological significance. Given the potential implications of PRMT1 in health and disease, the investigation of its recombinant protein also paves the way for the development of small-molecule inhibitors or modulators that could serve as novel therapeutic agents. As research progresses, insights gained from PRMT1 studies are expected to enhance our understanding of arginine methylation and its impact on cellular homeostasis, potentially leading to innovative approaches in treating diseases associated with aberrant PRMT1 activity.
