Analytical Data
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Gene name
SNTN
- Application
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Alternative Names
SNTN;S100A1L;Sentan
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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
A6NMZ2
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Expression Region
1-147aa
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AA Sequence
GSSHHHHHHSSGLVPRGSHMGGCMHSTQDKSLHLEGDPNPSAAPTSTCAP RKMPKRISISKQLASVKALRKCSDLEKAIATTALIFRNSSDSDGKLEKAI AKDLLQTQFRNFAEGQETKPKYREILSELDEHTENKLDFEDFMILLLSIT VMSDLLQNIRNVKIMK
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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
SNTN, or Stathmin1, is a well-characterized protein that plays a crucial role in cellular processes such as microtubule dynamics, cell signaling, and differentiation. Its dysregulation has been implicated in various pathological conditions, including cancer and neurodegenerative diseases. SNTN affects microtubule stability by binding to tubulin, thereby influencing cell shape, motility, and proliferation. As researchers continue to explore the intricate mechanisms by which SNTN contributes to disease progression, the production of recombinant SNTN proteins has become increasingly important for studying its function and interactions in vitro. These recombinant proteins facilitate detailed investigations into the biochemical and biophysical properties of SNTN, allowing for high-throughput screening of potential therapeutic agents that could modulate its activity. Furthermore, expressing and purifying SNTN in a controlled laboratory setting enables researchers to unravel its role in cytoskeletal dynamics and its interaction with other signaling molecules, providing insights that could lead to novel therapeutic strategies aimed at restoring normal cellular function in diseases associated with SNTN dysregulation.
