Analytical Data
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Gene name
Stathmin
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简介
Stathmin Protein, a widely distributed cytosolic phosphoprotein, integrates regulatory signals and destabilizes microtubules, crucial for their assembly and disassembly. It exhibits broad expression in various tissues, highlighting its versatile role in cellular processes. Stathmin Protein, Human (His) is the recombinant human-derived Stathmin protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
"Stathmin; Leukemia-Associated Phosphoprotein p18; Metablastin; Oncoprotein 18; Op18; Phosphoprotein p19; pp19; Prosolin; Protein Pr22; pp17; STMN1; C1orf215; LAP18; OP18 "
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16949-1
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Expression Region
A1-D149
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Protein Length
Full Length of Isoform-1
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Molecular Weight
19 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 crucial regulatory protein involved in microtubule dynamics, influencing cell division, signaling pathways, and cytoskeletal organization. Discovered in the early 1990s, it has garnered significant interest due to its role in cancer progression and metastasis, as it is often overexpressed in various malignancies. Stathmin functions primarily by sequestering tubulin dimers, thereby preventing their assembly into microtubules, which is essential for maintaining cellular architecture and proper mitotic function. The dysregulation of stathmin activity can lead to aberrant cell proliferation and resistance to apoptosis, making it a potential therapeutic target. Recent studies have focused on the structure-function relationship of stathmin and the development of stathmin-targeting compounds. Recombining stathmin offers a means to study its functional properties in detail, facilitating a better understanding of its involvement in cellular processes and disease mechanisms. Moreover, elucidating the molecular mechanisms governing stathmin’s activity can inform the design of novel cancer therapies aimed at disrupting its pro-tumorigenic effects. This research not only enhances our fundamental knowledge of cell biology but also opens avenues for targeted interventions in cancer treatment.
