Analytical Data
-
Gene name
aa9
- Application
-
Alternative Names
aa9；AA9 family lytic polysaccharide monooxygenase AA9-X282
-
Species
Collariella
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
A0A223GEC9
-
Expression Region
23-274aa
-
AA Sequence
HTRMFSVWVNGVDQGDGQNVYIRTPPNTDPIKDLASPALACNVKGGEPVPQFVSASAGDKLTFEWYRVKRGDDIIDPSHSGPITTWIAAFTSPTMDGTGPVWSKIHEEGYDASTKSWAVDKLIANKGMWDFTLPSQLKPGKYMLRQEIVAHHESDATFDKNPKRGAQFYPSCVQVDVKGVGGDAVPDQAFDFNKGYKYSDPGIAFDMYTDFDSYPIPGPPVWDAQDEGCCFIDGVDTTSVKEVVKQIICVLK
-
Molecular Weight
29.2 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
The research on aa9 recombinant proteins has emerged as a significant area of study in the field of biotechnology and protein engineering. These proteins, derived from specific genetic sequences, have garnered attention due to their potential applications in various domains, including medicine, agriculture, and industrial processes. The aa9 family is characterized by its unique structural properties, which play crucial roles in catalytic activities and interactions with other biomolecules. Understanding the structure-function relationship of these proteins is critical for optimizing their performance in therapeutic applications, such as enzyme replacement therapies or as novel drug targets. Additionally, the ability to engineer these proteins for enhanced stability and activity can lead to breakthroughs in biofuel production and bioremediation efforts. Current advancements in genetic engineering techniques, such as CRISPR and synthetic biology, have further propelled research in this area, allowing for more efficient and precise modifications of aa9 proteins. As researchers continue to explore the diverse functionalities and potential uses of aa9 recombinant proteins, the findings could contribute to new solutions for pressing global challenges, including health care, environmental sustainability, and resource management. The ongoing investigations into the expression, purification, and characterization of these proteins promise to unveil novel insights that could transform both fundamental science and practical applications.
