Analytical Data
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Gene name
TBCB
- Application
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Alternative Names
TBCB；CG22；Tubulin-folding cofactor B
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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
Q99426
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Expression Region
1-244aa
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AA Sequence
MEVTGVSAPT VTVFISSSLN TFRSEKRYSR SLTIAEFKCK LELLVGSPAS CMELELYGVD DKFYSKLDQE DALLGSYPVD DGCRIHVIDH SGARLGEYED VSRVEKYTIS QEAYDQRQDT VRSFLKRSKL GRYNEEERAQ QEAEAAQRLA EEKAQASSIP VGSRCEVRAA GQSPRRGTVM YVGLTDFKPG YWIGVRYDEP LGKNDGSVNG KRYFECQAKY GAFVKPAVVT VGDFPEEDYG LDEI
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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
The study of TBCB (T-complex protein 1, subunit beta) recombinant proteins is rooted in the broader context of protein folding and cellular chaperone mechanisms. TBCB is part of the T-complex chaperone system, which plays a critical role in facilitating the proper folding of nascent polypeptides and ensuring protein stability within the cell. Research has shown that misfolded proteins can lead to various diseases, including neurodegenerative disorders. Thus, understanding the function of TBCB and its interactions with other chaperones provides insights into the molecular mechanisms governing protein homeostasis. The ability to produce TBCB as a recombinant protein in vitro allows for detailed structural and functional analyses, enabling researchers to dissect its role in the protein folding process. Furthermore, exploring the therapeutic potential of TBCB in ameliorating protein misfolding diseases has emerged as a promising avenue for drug development. This research is significant not only for basic science but also for potential clinical applications in improving targeted treatments for diseases arising from protein misfolding.
