Analytical Data
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Gene name
PTP4A2
- Application
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Alternative Names
HH13; HH7-2; HU-PP-1; OV-1; PRL-2; PRL2; PTP4A; PTPCAAX2; ptp-IV1a; ptp-IV1b; Protein-tyrosine phosphatase of regenerating liver 2; Protein-tyrosine phosphatase 4a2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q12974
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Expression Region
Met1~Gln167
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Molecular Weight
23kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
PTP4A2, also known as protein tyrosine phosphatase 4A2, is a member of the protein tyrosine phosphatase family, which plays a critical role in various cellular processes, including signal transduction, cell growth, and differentiation. Its dysregulation has been implicated in several diseases, particularly cancer, making it a significant target for therapeutic intervention. The interest in PTP4A2 has grown due to its association with increased cell motility and metastasis, highlighting its potential role in promoting aggressive tumor phenotypes. Research efforts have focused on the structural and functional characterization of PTP4A2, aiming to elucidate its enzymatic mechanisms and regulatory pathways. Additionally, the development of recombinant PTP4A2 proteins has enabled scientists to explore its biological functions in vitro and in vivo. These studies could ultimately lead to the identification of small-molecule inhibitors that selectively target PTP4A2, offering promising avenues for cancer treatment and other related disorders. Furthermore, the investigation of PTP4A2's interactions with various substrates and signaling molecules is critical for understanding its role in cellular physiology and pathology, providing insights that may enhance therapeutic strategies against malignancies where PTP4A2 is overexpressed or misregulated. Overall, the ongoing research on PTP4A2 not only sheds light on its biological significance but also holds potential for advancing cancer therapeutics.











