Analytical Data
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Gene name
PTMS
- Application
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Alternative Names
PTMS;Parathymosin
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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
P20962
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Expression Region
1-102aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEKSVE AAAELSAKDL KEKKEKVEEK ASRKERKKEV VEEEENGAEE EEEETAEDGE EEDEGEEEDE EEEEEDDEGP ALKRAAEEED EADPKRQKTE NGASA
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Molecular Weight
14 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
Related Products
Protein Description
PTMS (Post-Translational Modifications) refers to the various biochemical modifications that proteins undergo after their synthesis, significantly influencing their function, stability, localization, and interaction with other molecules. Research into PTMS-proteins has gained considerable traction, driven by the critical role these modifications play in cellular processes and disease mechanisms, including cancer, neurodegenerative disorders, and metabolic diseases. For instance, phosphorylation, ubiquitination, glycosylation, and acetylation are key examples of PTMS, each affecting protein activity and interactions in distinct ways. Over the past few decades, advancements in techniques such as mass spectrometry, cryo-electron microscopy, and label-free proteomics have facilitated the detailed analysis of PTM patterns at the proteome level. These methodologies have unveiled the dynamic nature of PTMS, highlighting their potential as biomarkers for disease diagnosis and therapeutic targets. Consequently, researchers are focusing on developing recombinant proteins that mimic these modifications to study their functional implications and to create novel therapeutic strategies. By elucidating the precise mechanisms through which PTMS affect protein behavior, scientists aim to contribute to a deeper understanding of biological systems and to harness this knowledge for innovative clinical applications. Thus, the investigation of PTMS in recombinant proteins stands at the frontier of molecular biology and biomedical research, offering promising avenues for future discovery and treatment development.











