Analytical Data
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Gene name
PTP4A3
- Application
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Alternative Names
PRL3; PRL-3; PRL-R; Protein-tyrosine phosphatase of regenerating liver 3; Protein-tyrosine phosphatase 4a3
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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
O75365
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Expression Region
Met1~Cys170
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Molecular Weight
25kDa
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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
Related Products
Protein Description
PTP4A3, also known as protein tyrosine phosphatase type IVA member 3, is a member of the PTP family that has garnered significant attention due to its involvement in various cellular processes, including cell proliferation, migration, and differentiation. Emerging evidence suggests that PTP4A3 plays a crucial role in cancer biology, particularly in the progression and metastasis of several tumor types, making it a potential biomarker and therapeutic target. Its aberrant expression has been linked to poor prognosis in cancers such as breast, prostate, and colorectal cancer. The enzyme is believed to modulate key signaling pathways, including those governed by growth factors, which further underscores its relevance in oncogenic processes. Research on the recombinant forms of PTP4A3 has focused on elucidating its biochemical properties, interaction with substrates, and role in cellular signaling networks. These investigations aim to provide deeper insights into its mechanistic functions and implications in disease. The study of PTP4A3 also holds promise for the development of novel therapeutic strategies, as inhibiting its activity could potentially lead to reduced tumor growth and metastasis. Consequently, ongoing research endeavors are directed towards characterizing this protein at structural and functional levels, with the goal of translating these findings into clinical applications for cancer treatment and diagnosis.
