Analytical Data
-
Gene name
PTPA
- Application
-
Alternative Names
PTPA；PPP2R4；Serine/threonine-Protein phosphatase 2A activator
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q15257
-
Expression Region
2-358aa
-
AA Sequence
AEGERQPPPDSSEEAPPATQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVSEMWNEVHEEKEQAAKQSVSCDECIPLPRAGHCAPSEAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVATVVPTHLAAAVPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAIVFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVTSG
-
Molecular Weight
60.5 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
PTPA (Phosphotyrosine-Dependent Protein Phosphatase Activator) is a key regulator of protein phosphatase 2A (PP2A), an essential serine/threonine phosphatase involved in various cellular processes, including cell division, differentiation, and survival. The regulation of PP2A by PTPA is critical for maintaining cellular homeostasis and signaling pathways, as dysregulation of PP2A activities has been associated with various pathologies such as cancer, neurodegenerative diseases, and cardiovascular disorders. Research into PTPA and its role in activating PP2A has gained significant attention in recent years, as understanding this mechanism could lead to novel therapeutic strategies. Scientists aim to elucidate the structural and functional characteristics of PTPA and its interactions with PP2A, providing insights into the phosphatase's regulatory mechanisms. Advances in structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, have facilitated a deeper understanding of PTPA's interactions and conformational changes upon binding to PP2A. Additionally, the potential for targeting PTPA in drug design offers promising avenues for treating diseases related to PP2A dysregulation. Thus, the study of PTPA-recombinant proteins presents a vital area of research, as it not only enhances our understanding of phosphatase regulation but also contributes to the development of innovative therapeutic approaches in treating various diseases.
