Analytical Data
-
Gene name
TEM8/ANTXR1
- Application
-
Alternative Names
rHuAnthrax toxin receptor 1, His; ANTXR1; ATR; Anthrax toxin receptor 1
-
Species
Human
-
Source
HEK293
-
Tag
C-Avi;C-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9H6X2-4
-
Expression Region
E33-K321
-
Molecular Weight
38-45 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 TEM8 (Tumor Endothelial Marker 8), also known as ANTXR1 (Anthrax Toxin Receptor 1), has gained significant attention in the fields of cancer biology and immunology due to its unique role in tumor angiogenesis and its potential as a therapeutic target. TEM8 is predominantly expressed in endothelial cells of tumor vessels, facilitating the interaction between tumors and their blood supply. Its involvement in promoting angiogenesis makes it a crucial player in tumor progression. Furthermore, TEM8 serves as a receptor for anthrax toxin, which has spurred investigations into its role in cellular signaling pathways and potential implications for targeted drug delivery systems. Understanding the structure and function of TEM8/ANTXR1, particularly through the development of recombinant proteins, can provide insights into its biological mechanisms and enhance the design of novel therapeutic strategies. This research not only aims to dissect the molecular interactions mediated by TEM8 but also explores its utility in immunotherapy, where its over-expression in tumors could be harnessed for targeted treatment modalities. Overall, studies on TEM8/ANTXR1 recombinant proteins are positioned at the intersection of cancer research and biopharmaceutical development, holding promise for innovations in cancer treatment and diagnostics.











