Analytical Data
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Gene name
PTPMT1
- Application
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Alternative Names
PTPMT1;MOSP;PLIP;Phosphatidylglycerophosphatase and Protein-tyrosine phosphatase 1
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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
Q8WUK0
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Expression Region
28-201aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMKVPGRAHRDWYHRIDPTVLLGALPL RSLTRQLVQDENVRGVITMNEEYETRFLCNSSQEWKRLGVEQLRLSTVDM TGIPTLDNLQKGVQFALKYQSLGQCVYVHCKAGRSRSATMVAAYLIQVHK WSPEEAVRAIAKIRSYIHIRPGQLDVLKEFHKQITARATKDGTFVISKT
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Molecular Weight
23 kDa
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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
PTPMT1, or Protein Tyrosine Phosphatase Membrane Type 1, is a pivotal enzyme involved in various cellular processes, including growth, differentiation, and signaling pathways. The dysregulation of PTPMT1 has been linked to several pathological conditions, including cancer and metabolic disorders, making it a significant target for therapeutic interventions. In recent years, research has increasingly focused on understanding the structure and function of PTPMT1, particularly its role in modulating signal transduction pathways through dephosphorylation of tyrosine residues. The recombinant expression of PTPMT1 provides a valuable tool for studying its biochemical properties and interactions with other cellular proteins. Advances in recombinant DNA technology have enabled researchers to produce high-yield, active forms of PTPMT1, facilitating extensive biochemical characterization and validation of its functional roles. Furthermore, investigating the modulation of PTPMT1 activity presents promising avenues for drug development, as small molecules or biologics targeting this enzyme could potentially restore normal signaling pathways disrupted in diseases. Overall, the study of PTPMT1 not only enhances our understanding of fundamental cellular processes but also holds promise for innovative therapeutic strategies.
