Analytical Data
-
Gene name
PPBP
- Application
-
Alternative Names
PPBP；CTAP3；CXCL7；SCYB7；Platelet basic Protein
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P02775
-
Expression Region
59-128aa
-
AA Sequence
AELRCMCIKT TSGIHPKNIQ SLEVIGKGTH CNQVEVIATL KDGRKICLDP DAPRIKKIVQ KKLAGDESAD
-
Molecular Weight
7.6 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
PPBP, or Platelet-Poor Plasma Binding Protein, plays a crucial role in various physiological and pathological processes, including inflammation, angiogenesis, and tumor progression. The study of PPBP recombinant proteins has garnered attention due to their potential therapeutic applications, particularly in targeting diseases associated with abnormal angiogenesis, such as cancer and diabetic retinopathy. Research has shown that PPBP interacts with different cell types, influencing cellular behaviors such as migration and proliferation. Consequently, recombinant PPBP proteins offer a unique opportunity to explore their mechanisms of action and therapeutic potentials. Advances in biotechnology allow for the expression and purification of these proteins for further investigation. Understanding the structure-function relationships of PPBP can lead to the development of novel strategies for disease intervention. Furthermore, utilizing recombinant forms of PPBP can pave the way for innovative drug delivery systems and biomaterials in regenerative medicine, enhancing the efficacy of treatments related to cardiovascular and inflammatory diseases. Overall, continued research in this area promises to uncover valuable insights into the functional roles of PPBP and its implications in health and disease.
