Analytical Data
-
Gene name
PTP alpha/PTPRA
- Application
-
Alternative Names
PTPR-A; LRP; PTPA; HEPTP; HLPR; HPTPA; HPTPalpha; PTPRL2; R-PTP-alpha; RPTPA; Receptor-type tyrosine-protein phosphatase alpha
-
Species
Rat
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
Q66HJ7
-
Expression Region
Trp618~Lys796
-
Molecular Weight
24kDa
-
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
PTP alpha (PTPRA) is a member of the protein tyrosine phosphatase (PTP) family, which plays a critical role in various cellular processes, including cell signaling, growth, and differentiation. Dysregulation of PTPs, including PTPRA, has been implicated in several diseases, particularly cancers and autoimmune disorders, making them significant targets for therapeutic intervention. The study of PTPRA, specifically its recombinant protein, allows for a deeper understanding of its functional mechanisms and interactions within signaling pathways. Recent advancements in recombinant protein technology enable the production of PTPRA with high purity and activity, facilitating detailed biochemical characterization and structural studies. Such investigations can reveal insights into substrate specificity, regulatory mechanisms, and the overall role of PTPRA in cellular physiology. Moreover, the reconstitution of PTPRA function in model systems could illuminate its contributions to disease processes. Consequently, research on recombinant PTPRA is crucial for identifying potential drug targets and developing novel therapeutic strategies aimed at diseases related to PTP dysregulation.











