Analytical Data
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Gene name
PTPN2
- Application
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Alternative Names
PTPN2;KIAA0387;Receptor-type tyrosine-Protein phosphatase N2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17706
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Expression Region
1-415aa
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AA Sequence
MPTTIEREFE ELDTQRRWQP LYLEIRNESH DYPHRVAKFP ENRNRNRYRD VSPYDHSRVK LQNAENDYIN ASLVDIEEAQ RSYILTQGPL PNTCCHFWLM VWQQKTKAVV MLNRIVEKES VKCAQYWPTD DQEMLFKETG FSVKLLSEDV KSYYTVHLLQ LENINSGETR TISHFHYTTW PDFGVPESPA SFLNFLFKVR ESGSLNPDHG PAVIHCSAGI GRSGTFSLVD TCLVLMEKGD DINIKQVLLN MRKYRMGLIQ TPDQLRFSYM AIIEGAKCIK GDSSIQKRWK ELSKEDLSPA FDHSPNKIMT EKYNGNRIGL EEEKLTGDRC TGLSSKMQDT MEENSESALR KRIREDRKAT TAQKVQQMKQ RLNENERKRK RWLYWQPILT KMGFMSVILV GAFVGWTLFF QQNAL
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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
PTPN2, or Protein Tyrosine Phosphatase Non-Receptor Type 2, is a critical enzyme that plays a significant role in various cellular processes, including cell signaling, proliferation, and differentiation. Research has shown that PTPN2 is linked to autoimmune diseases, such as type 1 diabetes and rheumatoid arthritis, as well as certain cancers. Its function is primarily to dephosphorylate tyrosine residues on target proteins, thereby regulating signaling pathways that are pivotal for immune response and cellular homeostasis. Given its involvement in these pathological conditions, PTPN2 has emerged as a potential therapeutic target. Recent advancements in recombinant protein technologies have enabled the production of purified PTPN2, facilitating detailed studies of its structure and function. Understanding PTPN2's role at the molecular level can provide insights into its regulatory mechanisms and the pathological processes involved in diseases, paving the way for novel treatment strategies. Further research into the functional dynamics of PTPN2, including its interactions with various signaling partners, could lead to the development of targeted therapies aimed at modulating its activity in disease contexts. The growing interest in PTPN2 as a biomarker and therapeutic target underscores the importance of delineating its biological functions and regulatory networks in both health and disease.











