Analytical Data
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Gene name
PRMT6
- Application
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Alternative Names
PRMT6；HRMT1L6；Protein arginine N-methyltransferase 6
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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
Q96LA8
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Expression Region
2-375aa
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AA Sequence
SQPKKRKLESGGGGEGGEGTEEEDGAEREAALERPRRTKRERDQLYYECY SDVSVHEEMIADRVRTDAYRLGILRNWAALRGKTVLDVGAGTGILSIFCA QAGARRVYAVEASAIWQQAREVVRFNGLEDRVHVLPGPVETVELPEQVDA IVSEWMGYGLLHESMLSSVLHARTKWLKEGGLLLPASAELFIAPISDQML EWRLGFWSQVKQHYGVDMSCLEGFATRCLMGHSEIVVQGLSGEDVLARPQ RFAQLELSRAGLEQELEAGVGGRFRCSCYGSAPMHGFAIWFQVTFPGGES EKPLVLSTSPFHPATHWKQALLYLNEPVQVEQDTDVSGEITLLPSRDNPR RLRVLLRYKVGDQEEKTKDFAMED
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Molecular Weight
43 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
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Protein Description
PRMT6 (Protein Arginine Methyltransferase 6) is a member of the protein arginine methyltransferase family, which plays a crucial role in the post-translational modification of proteins through methylation of arginine residues. This enzyme has garnered significant attention in recent years due to its involvement in various biological processes, including gene regulation, signaling pathways, and the modulation of chromatin structure. Dysregulation of PRMT6 has been linked to various human diseases, including cancer and neurological disorders, making it a potential target for therapeutic interventions. Research into PRMT6 has focused on its enzymatic mechanisms, substrate specificity, and regulatory roles within the cell. Additionally, the production of recombinant PRMT6 protein facilitates in-depth studies of its biochemical properties and interactions with other proteins, aiding in the understanding of its functional significance in cellular contexts. By elucidating the structure-function relationships of PRMT6 through recombinant protein studies, researchers aim to uncover its contributions to health and disease, ultimately paving the way for novel diagnostic and therapeutic strategies.
