Analytical Data
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Gene name
TTC4
- Application
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Alternative Names
TTC4; My044; Tetratricopeptide repeat Protein 4; TPR repeat Protein 4
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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
O95801
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Expression Region
1-387 aa
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AA Sequence
MEQPGQDPTS DDVMDSFLEK FQSQPYRGGF HEDQWEKEFE KVPLFMSRAP SEIDPRENPD LACLQSIIFD EERSPEEQAK TYKDEGNDYF KEKDYKKAVI SYTEGLKKKC ADPDLNAVLY TNRAAAQYYL GNFRSALNDV TAARKLKPCH LKAIIRGALC HLELKHFAEA VNWCDEGLQI DAKEKKLLEM RAKADKLKRI EQRDVRKANL KEKKERNQNE ALLQAIKARN IRLSEAACED EDSASEGLGE LFLDGLSTEN PHGARLSLDG QGRLSWPVLF LYPEYAQSDF ISAFHEDSRF IDHLMVMFGE TPSWDLEQKY CPDNLEVYFE DEDRAELYRV PAKSTLLQVL QHQRYFVKAL TPAFLVCVGS SPFCKNFLRG RKVYQIR
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Molecular Weight
44.6 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 TTC4 protein, part of the tetratricopeptide repeat (TPR) protein family, plays a crucial role in a variety of cellular processes, including protein folding, protein-protein interactions, and the regulation of signal transduction pathways. Understanding the function and mechanisms of TTC4 is particularly important due to its involvement in important biological processes and potential implications in diseases. Studies have shown that mutations and dysregulation of TTC4 can be associated with various pathological conditions, including neurodegenerative diseases and cancers, making it a significant target for therapeutic research. The interest in TTC4 has led to numerous studies focused on its structure, function, and interactions with other cellular components. Researchers employ various techniques such as X-ray crystallography, NMR spectroscopy, and cryo-electron microscopy to elucidate the three-dimensional structures of TTC4 and its complexes. These insights into its molecular architecture provide a foundation for understanding how TTC4 mediates its functions at a cellular level. Moreover, the development of TTC4 recombinant proteins allows for detailed biochemical assays and functional studies, paving the way for potential applications in drug discovery and the development of novel therapeutic strategies. Thus, the investigation of TTC4 and its role in cellular mechanisms remains a vital area of research with broad implications for understanding and treating human diseases.
