Analytical Data
-
Gene name
OX
- Application
-
Alternative Names
OX；MOX1；MOX2；；OX-2 membrane glycoProtein
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P41217
-
Expression Region
1-278aa
-
AA Sequence
MERLVIRMPFSHLSTYSLVWVMAAVVLCTAQVQVVTQDEREQLYTPASLKCSLQNAQEALIVTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNSTITFWNITLEDEGCYMCLFNTFGFGKISGTACLTVYVQPIVSLHYKFSEDHLNITCSATARPAPMVFWKVPRSGIENSTVTLSHPNGTTSVTSILHIKDPKNQVGKEVICQVLHLGTVTDFKQTVNKGYWFSVPLLLSIVSLVILLVLISILLYWKRHRNQDRGELSQGVQKMT
-
Molecular Weight
31.2 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
OX recombinant proteins are an area of increasing interest in biotechnology and biomedical research, primarily due to their potential applications in therapeutic development and diagnostics. The OX protein family, known for their roles in cell signaling, immune response, and metabolic regulation, has garnered attention for their involvement in various diseases, including cancer and autoimmune disorders. The ability to produce OX proteins through recombinant DNA technology allows for large-scale production and better characterization, facilitating the understanding of their biological functions and mechanisms. In recent years, advancements in cloning, expression systems, and purification techniques have enhanced the feasibility of studying these proteins in vitro and in vivo. Furthermore, the recombinant OX proteins are being explored as candidates for vaccine development and as therapeutic agents due to their specificity and potential for targeted delivery. Research in this field aims to elucidate the structural properties and functional dynamics of OX proteins, profile their interactions with other biomolecules, and assess their efficacy in clinical applications. With ongoing developments in protein engineering and synthetic biology, the study of OX recombinant proteins holds promise for significant contributions to modern medicine and therapeutic innovations.
