Analytical Data
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Gene name
TTC9B
- Application
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Alternative Names
TTC9B; Tetratricopeptide repeat Protein 9B; TPR repeat Protein 9B
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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
Q8N6N2
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Expression Region
1-239 aa
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AA Sequence
MQRGALSPVL MLSAAPEPPP RPPPALSPPG SGPGSGSRHG SARPGPTPEP SGSLGAALDS SLRAAVAFKA EGQRCYREKK FREAIGKYHR ALLQLKAAQG ARPSGLPAPA PGPTSSPGPA RLSEEQRRLV ESTEVECYDS LTACLLQSEL VNYERVREYC LKVLEKQQGN FKATYRAGIA FYHLGDYARA LRYLQEARSR EPTDTNVLRY IQLTQLKMNR CSLQREDSGA GSQTRDVIG
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Molecular Weight
25.9 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
TTC9B (Tetratricopeptide Repeat Domain 9B) is a protein that has garnered attention due to its potential involvement in various biological processes and diseases. Emerging evidence suggests that TTC9B plays a critical role in cellular mechanisms, including protein-protein interactions and intracellular signaling pathways. Research has indicated that TTC9B may be implicated in neurodegenerative disorders and certain types of cancers, highlighting its significance in health and disease. The study of TTC9B, particularly in its recombinant form, allows for a more detailed examination of its functional properties and interactions. Recombinant protein technologies provide a means to produce TTC9B in controlled laboratory settings, allowing researchers to explore its structure and biochemical activities. Understanding the functional dynamics of TTC9B could lead to insights into its role in pathophysiological conditions and potentially uncover new therapeutic targets. Moreover, the engineering of TTC9B for experimental applications could enhance our capability to manipulate cellular pathways and investigate its role in disease mechanisms, making it a promising candidate for future biotechnological applications. Overall, the exploration of TTC9B as a recombinant protein represents a vital area of research with implications for understanding fundamental biological processes and developing novel strategies for disease intervention.
