Analytical Data
-
Gene name
PPP2R3B
- Application
-
Alternative Names
PP2A subunit B isoform PR48Protein phosphatase 2A 48KDA regulatory subunit
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y5P8
-
Expression Region
1-176aa
-
Molecular Weight
36.1 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
PPP2R3B, a regulatory subunit of protein phosphatase 2A (PP2A), plays a crucial role in various cellular processes by modulating the phosphorylation state of key proteins involved in signaling pathways. PP2A is known for its involvement in the regulation of cell growth, division, and apoptosis, making it a significant player in tumorigenesis and other diseases. Research into PPP2R3B has gained momentum as scientists seek to elucidate its specific functions and regulatory mechanisms within the PP2A complex. Aberrations in PP2A activity, often due to mutations and altered expression of its subunits, have been associated with cancer and other pathological conditions, highlighting the importance of understanding PPP2R3B’s role. Recent advances in recombinant protein technology have made it feasible to produce and characterize PPP2R3B protein, allowing for detailed studies on its biochemical properties, interactions with other proteins, and potential as a therapeutic target. By investigating the structure-function relationship of PPP2R3B, researchers aim to uncover its contribution to cellular signaling networks and therapeutic implications in diseases where PP2A activity is dysregulated. This research not only enhances our understanding of PPP2R3B’s functions but also potentially paves the way for novel strategies in cancer treatment and other disorders linked to phosphatase activity.
