Analytical Data
-
Gene name
PI15
- Application
-
Alternative Names
P25TI; CRISP-8; 25 kDa trypsin inhibitor; Cysteine-rich secretory protein 8
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O43692
-
Expression Region
Ser20~Lys258
-
Molecular Weight
31kDa
-
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
PI15, or Proteinase Inhibitor 15, is a serine protease inhibitor predominantly expressed in various tissues, including the skin and the digestive system. It plays a critical role in regulating proteolytic activity, which is essential for maintaining homeostasis and modulating inflammatory responses. Research has shown that PI15 is involved in protecting cells against proteolysis, which can lead to tissue damage and chronic inflammation if left unchecked. Additionally, PI15 has garnered interest due to its potential implications in metabolic disorders and cancer, as it may influence tumor progression by modulating the extracellular matrix and impacting cell migration. Understanding the structure and function of PI15 at the molecular level is crucial for elucidating its role in physiological and pathological processes. Recent advancements in biotechnology have facilitated the recombinant production of PI15, providing a valuable tool for studying its mechanism of action and exploring its therapeutic potential. These studies aim to harness PI15 as a biomarker for disease diagnosis and as a target for novel therapeutic strategies, highlighting its significance in health and disease. The ongoing research into PI15 not only enhances our understanding of protease inhibition but also opens new avenues for the development of innovative treatments for various conditions associated with protease dysregulation.
