Analytical Data
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Gene name
TTLL3
- Application
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Alternative Names
Tubulin monoglycylase TTLL3. EC:6.3.2.-. HOTTL. Tubulin--tyrosine ligase-like Protein 3
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y4R7
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Expression Region
1-101 aa
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AA Sequence
TEGDRNIWIVKPGAKSRGRGIMCMDHLEEMLKLVNGNPVVMKDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFSLKNLDK
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Molecular Weight
36.85 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
TTLL3 (tubulin tyrosine ligase-like 3) is an enzyme implicated in the post-translational modification of tubulin, a key component of the cytoskeleton in eukaryotic cells. Specifically, TTLL3 functions by adding a tyrosyl residue to the C-terminus of tubulin, a modification that is crucial for the stability and functionality of microtubules. The dynamics of microtubules are essential for various cellular processes, including mitosis, intracellular transport, and cell signaling. Research has indicated that aberrations in TTLL3 expression may be associated with several diseases, including cancer, where altered microtubule dynamics can lead to uncontrolled cell proliferation. Understanding the biochemical properties and regulatory mechanisms of TTLL3 is vital for elucidating its role in cellular homeostasis and disease pathology. Additionally, the potential of TTLL3 as a therapeutic target highlights the importance of studying its structure and function in detail. Recent advances in protein engineering and structural biology have enabled researchers to produce recombinant forms of TTLL3, facilitating in vitro studies on its enzymatic activity and interactions with tubulin and other cellular components. Investigating the TTLL3 recombinant protein will pave the way for further studies to develop strategies that modulate its activity, with implications for novel therapeutic approaches in diseases where microtubule dynamics are disrupted.
