Analytical Data
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Gene name
TUB
- Application
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Alternative Names
F10B5.4; rd5; TUB 1; TUB; TUB_HUMAN; Tubby homologue; Tubby Protein homolog 1; Tubby Protein homolog
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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
P50607
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Expression Region
1-506 aa
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AA Sequence
MTSKPHSDWIPYSVLDDEGRNLRQQKLDRQRALLEQKQKKKRQEPLMVQANADGRPRSRR ARQSEEQAPLVESYLSSSGSTSYQVQEADSLASVQLGATRPTAPASAKRTKAAATAGGQG GAARKEKKGKHKGTSGPAALAEDKSEAQGPVQILTVGQSDHAQDAGETAAGGGERPSGQD LRATMQRKGISSSMSFDEDEEDEEENSSSSSQLNSNTRPSSATSRKSVREAASAPSPTAP EQPVDVEVQDLEEFALRPAPQGITIKCRITRDKKGMDRGMYPTYFLHLDREDGKKVFLLA GRKRKKSKTSNYLISVDPTDLSRGGDSYIGKLRSNLMGTKFTVYDNGVNPQKASSSTLES GTLRQELAAVCYETNVLGFKGPRKMSVIVPGMNMVHERVSIRPRNEHETLLARWQNKNTE SIIELQNKTPVWNDDTQSYVLNFHGRVTQASVKNFQIIHGNDPDYIVMQFGRVAEDVFTM DYNYPLCALQAFAIALSSFDSKLACE
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Molecular Weight
55.6 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
TUB recombinant proteins are an area of significant interest in molecular biology and biotechnology due to their potential applications in various research and therapeutic contexts. Tubulin, a key protein in the cytoskeleton of eukaryotic cells, plays a crucial role in maintaining cell shape, enabling intracellular transport, and facilitating cell division. The study of TUB recombinant proteins is primarily driven by the need to understand tubulin's dynamic behavior and interactions in cellular processes. Researchers have successfully engineered TUB proteins to explore their structural properties, functions, and the mechanisms underlying polymerization and depolymerization of microtubules. Additionally, advancements in recombinant protein production techniques have enabled the generation of large quantities of TUB proteins, which are critical for structural studies, drug discovery, and the development of novel therapeutic strategies targeting microtubule dynamics. Such studies have implications for cancer treatment, neurodegenerative diseases, and understanding the fundamental processes of cell biology. The ongoing research in this field aims to manipulate tubulin behavior for biotechnological applications and therapeutic interventions, thus underscoring the significance of TUB recombinant proteins in contemporary biological research.
