Analytical Data
-
Gene name
spi
- Application
-
Alternative Names
spi；Transcription factor Spi-B
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P17947
-
Expression Region
1-270aa
-
AA Sequence
MLQACKMEGFPLVPPPSEDLVPYDTDLYQRQTHEYYPYLSSDGESHSDHYWDFHPHHVHSEFESFAENNFTELQSVQPPQLQQLYRHMELEQMHVLDTPMVPPHPSLGHQVSYLPRMCLQYPSLSPAQPSSDEEEGERQSPPLEVSDGEADGLEPGPGLLPGETGSKKKIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKVKKKLTYQFSGEVLGRGGLAERRHPPH
-
Molecular Weight
35.1 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 study of SPI (serine protease inhibitor) recombinant proteins has gained significant attention in the fields of molecular biology and biotechnology due to their potential therapeutic applications and roles in regulating proteolytic activity in various biological processes. SPIs are key regulators of protease activity, which is crucial in numerous physiological functions, including blood coagulation, immune responses, and protein digestion. Their dysregulation is often linked to various diseases, such as cancer, cardiovascular disorders, and inflammatory conditions. With advances in genetic engineering and recombinant DNA technology, scientists can now produce high-yield, functionally active SPI proteins in host systems such as bacteria, yeasts, or mammalian cells. This allows for detailed characterization of their structure-function relationships, as well as exploration of their use in drug development, diagnostic tools, and therapeutic interventions. Additionally, understanding the interaction between SPIs and their target proteases provides insights into the intricate regulatory networks within proteolytic pathways. The ongoing research not only enhances our comprehension of biological processes but also opens pathways for innovative solutions to combat diseases associated with protease imbalances.
