Analytical Data
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Gene name
PTPN12
- Application
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Alternative Names
PTP-PEST; PTPG1; Protein-tyrosine phosphatase G1
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35831
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Expression Region
Met1~Leu293
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Molecular Weight
65kDa
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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
PTPN12, also known as protein-tyrosine phosphatase non-receptor type 12, is a key member of the protein tyrosine phosphatase (PTP) family, which plays a crucial role in signaling pathways that regulate various cellular processes, including growth, differentiation, and immune responses. Dysregulation of PTPN12 has been implicated in various diseases, especially cancer, where altered signaling pathways can lead to uncontrolled cell proliferation and survival. Research has shown that PTPN12 acts as a tumor suppressor by dephosphorylating critical signaling molecules, thus inhibiting oncogenic pathways. In recent years, the production of recombinant PTPN12 protein has garnered attention, allowing for detailed studies on its structure, function, and interaction with other cellular proteins. By employing techniques such as recombinant DNA technology and protein expression systems, researchers can generate large quantities of active PTPN12 for biochemical assays and structural analysis. This research is vital for understanding the mechanisms by which PTPN12 regulates cellular functions and its potential as a therapeutic target. Moreover, exploring the molecular interactions of PTPN12 can provide insights into the design of innovative strategies for cancer treatment, aiming to restore its normal phosphatase activity in tumorigenic contexts. Overall, the study of recombinant PTPN12 not only enhances our knowledge of cellular signaling networks but also holds promise for advancing targeted therapies in oncology.
