Analytical Data
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Gene name
TPPP
- Application
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Alternative Names
TPPP；TPPP1；Tubulin polymerization-promoting Protein
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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
O94811
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Expression Region
1-219aa
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AA Sequence
MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK
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Molecular Weight
50.7kDa
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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
TPPP (tubulin polymerization promoting protein) is a significant protein that plays a critical role in the regulation of microtubule dynamics and the stabilization of microtubules, which are essential components of the cytoskeleton in eukaryotic cells. Research into TPPP has gained momentum due to its implications in various cellular processes and potential links to neurological disorders, including multiple sclerosis and other demyelinating diseases. The protein enhances the polymerization of tubulin, which is critical for maintaining the structural integrity of neurons and facilitating intracellular transport. Studies have shown that TPPP can influence cell morphology and motility by modulating microtubule organization. Additionally, aberrant expression of TPPP has been associated with tumorigenesis, indicating its potential role in cancer biology. Understanding the molecular mechanisms underlying TPPP's function could lead to new therapeutic strategies targeting microtubule dynamics in various diseases. Researchers are focusing on the structural biology of TPPP, utilizing techniques such as X-ray crystallography and cryo-electron microscopy, to elucidate its functional domains and interaction partners. This concerted effort to unravel the complexities of TPPP is essential for developing novel interventions in diseases where microtubule stability and dynamics are disrupted.
