Analytical Data
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Gene name
STATH
- Application
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Alternative Names
STATH；Statherin
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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
P02808
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Expression Region
20-62aa
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AA Sequence
DSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTF
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Molecular Weight
23.7 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
STATH (Stathmin) is a key phosphoprotein that plays a crucial role in various cellular processes, particularly in microtubule dynamics and cell signaling. Its involvement in the regulation of microtubule stability has made it a significant focus of research, especially in understanding cell proliferation, differentiation, and motility. Alterations in STATH expression and function have been associated with several diseases, including cancer, where its dysregulation can promote tumor growth and metastasis. Researchers have been particularly interested in the reconstitution of STATH as a recombinant protein to study its biochemical properties and interactions in controlled experimental settings. This approach allows for the detailed examination of its structural features, post-translational modifications, and biological functions. By using techniques such as site-directed mutagenesis and affinity purification, scientists aim to elucidate the role of STATH in microtubule dynamics, which has implications not only for basic cell biology but also for the development of targeted therapies in oncology. Understanding STATH's mechanisms at a molecular level could provide insights into novel therapeutic strategies for diseases linked to microtubule dysfunction, highlighting the significance of this research in both basic and applied biomedical fields.
