Analytical Data
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Gene name
PTPRM
- Application
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Alternative Names
PTPR-M; PTPRL1; R-PTP-MU; RPTPM; RPTPU; HR-PTPu; R-PTP-mu; Receptor-Type Tyrosine-Protein Phosphatase Mu
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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 90% as determined by SDS-PAGE.
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Uniprot
P28827
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Expression Region
Thr1197~Ser1403
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Molecular Weight
27kDa
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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
PTPRM (Protein Tyrosine Phosphatase Receptor Type M) is a member of the receptor-type protein tyrosine phosphatase family, which plays crucial roles in various cellular processes, including cell signaling, adhesion, and differentiation. Its involvement in regulating tyrosine phosphorylation makes it a key player in cancer biology and other diseases. Dysregulation of PTPRM has been associated with several types of cancer, suggesting that it may serve as a potential tumor suppressor. Researchers have focused on the structural and functional aspects of PTPRM to better understand its role in cellular signaling pathways. Recombining this protein allows for detailed studies of its enzymatic activity, interaction with substrates, and impact on tumor progression. Advances in recombinant protein technology have facilitated the production of active PTPRM variants, enabling scientists to explore its therapeutic potential. Understanding the mechanisms governed by PTPRM could lead to novel strategies for cancer treatment and provide insights into the intricate networks of signaling involved in cell behavior. Thus, the study of recombinant PTPRM is not only vital for elucidating its biological functions but also holds promise for developing targeted therapies that leverage its regulatory capabilities in disease contexts.
