Analytical Data
-
Gene name
SAG
- Application
-
Alternative Names
SAG；OPN2；Rhodopsin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P10523
-
Expression Region
1-405aa
-
AA Sequence
MAASGKTSKSEPNHVIFKKISRDKSVTIYLGNRDYIDHVSQVQPVDGVVLVDPDLVKGKKVYVTLTCAFRYGQEDIDVIGLTFRRDLYFSRVQVYPPVGAASTPTKLQESLLKKLGSNTYPFLLTFPDYLPCSVMLQPAPQDSGKSCGVDFEVKAFATDSTDAEEDKIPKKSSVRLLIRKVQHAPLEMGPQPRAEAAWQFFMSDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVVLYSSDYYVKPVAMEEAQEKVPPNSTLTKTLTLLPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVLGILVSYQIKVKLTVSGFLGELTSSEVATEVPFRLMHPQPEDPAKESYQDANLVFEEFARHNLKDAGEAEEGKRDKNDVDE
-
Molecular Weight
47.1 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
SAG (S-adenosyl-L-methionine-dependent methyltransferase) is a vital protein that plays a significant role in various biological processes, including methylation reactions that affect gene expression and protein function. The research on SAG has gained momentum due to its involvement in critical cellular pathways, including those related to development, metabolism, and disease. Understanding the structure and function of SAG is crucial for deciphering its mechanisms of action and potential therapeutic applications, especially in cancer and other pathologies where methylation patterns are altered. Advances in protein engineering and recombinant DNA technology have enabled scientists to produce SAG in a controlled laboratory setting, facilitating detailed studies of its biochemical properties and interactions. High-throughput screening methods and structural biology techniques, such as X-ray crystallography and NMR spectroscopy, have further enhanced our understanding of SAG's functional domains and regulatory mechanisms. Additionally, exploring SAG's role in epigenetics and its interaction with small molecules paves the way for developing novel drugs and therapeutic strategies. As the field continues to evolve, ongoing research into SAG's multifaceted roles promises to uncover new insights into its contributions to health and disease, making it a focal point of biomedical research.
