Analytical Data
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Gene name
PTP4A1
- Application
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Alternative Names
PRL1; HH72; PRL-1; PTP(CAAX1); PTPCAAX1; Protein-tyrosine phosphatase of regenerating liver 1; Protein-tyrosine phosphatase 4a1
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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
Q93096
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Expression Region
Met1~Gln173
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Molecular Weight
24kDa
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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
PTP4A1, also known as phosphatase of regenerating liver 1 (PRL-1), is a member of the protein tyrosine phosphatase family and plays a crucial role in cell signaling, particularly in processes related to cell growth, proliferation, and migration. Its overexpression has been implicated in various cancers, suggesting that PTP4A1 may function as an oncogene. Researchers have identified its involvement in multiple signaling pathways, including those regulated by Ras and Rho GTPases, making it a potential target for therapeutic interventions. The study of recombinant PTP4A1 protein is pivotal to understanding its biochemical properties and the mechanisms underlying its oncogenic activity. By producing and characterizing this protein, scientists aim to elucidate its structure-function relationships and investigate how it interacts with cellular partners. This knowledge could provide insights into developing targeted therapies for cancers associated with PTP4A1 dysregulation. Moreover, exploring its role in cellular processes—such as epithelial to mesenchymal transition and metastasis—can enhance our understanding of tumor biology and lead to innovative strategies for cancer treatment. The ongoing research into PTP4A1 not only sheds light on fundamental cellular mechanisms but also holds promise for advancing cancer diagnostics and therapeutics.
