Analytical Data
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Gene name
Stathmin
- Application
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Alternative Names
Stathmin；Stathmin-4
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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
P16949
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Expression Region
2-149aa
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AA Sequence
ASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQ KKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKL THKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD
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Molecular Weight
18 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
Stathmin, also known as oncoprotein 18, is a key regulator of microtubule dynamics, playing a crucial role in cell signaling, proliferation, and migration. Its dysregulation has been implicated in various cancers, making it an important target for therapeutic intervention. The protein interacts with tubulin, promoting microtubule depolymerization, thus influencing the cytoskeletal structure and cellular architecture. Given its significant role in cell cycle regulation and apoptosis, understanding the structural and functional properties of Stathmin is essential for elucidating its involvement in tumorigenesis. Researchers have focused on the recombinant production of Stathmin to study its biophysical characteristics and interactions with microtubules in detail. This approach allows for controlled experimental conditions and the ability to modify the protein for functional assays and potential drug development. The elucidation of Stathmin's structure through techniques like X-ray crystallography and nuclear magnetic resonance (NMR) has provided insights into its mechanism of action and identified potential inhibitors that could disrupt its function, presenting new avenues for cancer therapy. Moreover, the study of Stathmin's role in cellular processes may also inform on its function in normal physiological conditions, thereby deepening the understanding of cellular motility and division. As research progresses, Stathmin continues to be a focal point in the quest for novel cancer treatments, highlighting the intersection of basic science and therapeutic innovation.
