Analytical Data
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Gene name
TTC32
- Application
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Alternative Names
TTC32；Tetratricopeptide repeat Protein 32
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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
Q5I0X7
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Expression Region
1-151aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMEGQRQESHATLTLAQAHFNNGEYAEA EALYSAYIRRCACAASSDESPGSKCSPEDLATAYNNRGQIKYFRVDFYEA MDDYTSAIEVQPNFEVPYYNRGLILYRLGYFDDALEDFKKVLDLNPGFQD ATLSLKQTILDKEEKQRRNVAKNY
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Molecular Weight
20 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
The TTC32 protein, also known as tetratricopeptide repeat protein 32, has garnered attention in the field of molecular biology and genetics due to its potential implications in various cellular processes. Research indicates that TTC32 is involved in regulating protein interactions and stability, playing a crucial role in cellular signaling pathways and maintaining cellular homeostasis. Its expression has been linked to several diseases, including cancer and neurodegenerative disorders, making it a target of interest for therapeutic interventions. Moreover, the unique tetratricopeptide repeat motif of TTC32 suggests that it may facilitate critical interactions among proteins, influencing their function and localization within the cell. Understanding the molecular mechanisms underlying TTC32's role could unveil new insights into disease mechanisms and identify novel biomarkers for early detection. Recent studies have begun to explore its interactions with other proteins, highlighting its importance in the context of cellular stress responses. As research continues to evolve, the characterization of TTC32's structure and function may pave the way for new strategies in drug development and precision medicine, ultimately contributing to improved treatment options for diseases associated with dysregulated protein interactions.
