Analytical Data
-
Gene name
FAPa
- Application
-
Alternative Names
APCE; SIMP; DPPIV; Seprase; 170 kDa melanoma membrane-bound gelatinase; Post-proline cleaving enzyme; Serine integral membrane protease; Surface-expressed protease
-
Species
Rat
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
-
-
Expression Region
Gly542~Asp761
-
Molecular Weight
28kDa
-
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
FAPa, or fibroblast activation protein-alpha, is a serine protease that plays a crucial role in various physiological and pathological processes, particularly in cancer biology. It is predominantly expressed in activated fibroblasts within the tumor microenvironment, making it a significant marker for tumor-associated stromal cells. The overexpression of FAPa has been linked to tumor progression, metastasis, and poor patient prognosis in several cancer types, including pancreatic, colorectal, and breast cancers. Research has increasingly focused on FAPa as a therapeutic target due to its limited expression in normal tissues, which raises its potential as a selective target for cancer therapy. Additionally, FAPa has been explored in the development of diagnostic tools and imaging agents, enhancing the precision of cancer detection. The engineering of FAPa-targeting recombinant proteins has gained traction, allowing for the creation of antibody-drug conjugates and other biotherapeutics. These advancements aim to improve clinical outcomes and provide a foundation for novel treatments that leverage the unique properties of FAPa in the context of tumor biology. Given the increasing prevalence of cancer worldwide, understanding and manipulating FAPa activity through recombinant protein technology presents a promising avenue in the fight against malignant diseases, potentially leading to innovative strategies for treatment and management.
