Analytical Data
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Gene name
TUBd
- Application
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Alternative Names
TUBd；TUBD；Tubulin delta chain
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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
Q9UJT1
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Expression Region
1-453aa
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AA Sequence
MSIVTVQLGQ CGNQIGFEVF DALLSDSHSS QGLCSMRENE AYQASCKERF FSEEENGVPI ARAVLVDMEP KVINQMLSKA AQSGQWKYGQ HACFCQKQGS GNNWAYGYSV HGPRHEESIM NIIRKEVEKC DSFSGFFIIM SMAGGTGSGL GAFVTQNLED QYSNSLKMNQ IIWPYGTGEV IVQNYNSILT LSHLYRSSDA LLLHENDAIH KICAKLMNIK QISFSDINQV LAHQLGSVFQ PTYSAESSFH YRRNPLGDLM EHLVPHPEFK MLSVRNIPHM SENSLAYTTF TWAGLLKHLR QMLISNAKME EGIDRHVWPP LSGLPPLSKM SLNKDLHFNT SIANLVILRG KDVQSADVEG FKDPALYTSW LKPVNAFNVW KTQRAFSKYE KSAVLVSNSQ FLVKPLDMIV GKAWNMFASK AYIHQYTKFG IEEEDFLDSF TSLEQVVASY CNL
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Molecular Weight
51 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
TUBd, or Tubulin-binding domain proteins, have garnered significant interest in the field of molecular biology and biochemistry due to their essential role in microtubule dynamics and cellular processes. The study of TUBd proteins is crucial for understanding the intricacies of the cytoskeleton, which not only provides structural support to cells but also facilitates intracellular transport, cell division, and motility. Research has shown that TUBd proteins interact with tubulin, a fundamental component of microtubules, influencing their assembly and disassembly, thereby impacting various cellular functions. Increased understanding of TUBd and its interactions may reveal insights into various diseases, including cancer, where microtubule dynamics play a pivotal role in tumorigenesis and metastasis. Furthermore, TUBd has potential therapeutic applications, as targeting tubulin dynamics could lead to the development of new anti-cancer drugs. The exploration of TUBd proteins, their structure, function, and regulatory mechanisms represents a promising area of research that could lead to advancements in both basic science and clinical applications. Thus, the investigation of TUBd proteins is integral to unraveling the complexities of cellular architecture and identifying novel approaches to combat diseases linked to microtubule dysfunction.
