Analytical Data
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Gene name
TTLL1
- Application
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Alternative Names
TTLL1; C22orf7; Probable tubulin polyglutamylase TTLL1; EC 6.-.-.-; Tubulin polyglutamylase complex subunit 3; PGs3; Tubulin--tyrosine ligase-like Protein 1
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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
O95922
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Expression Region
1-423 aa
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AA Sequence
MAGKVKWVTD IEKSVLINNF EKRGWVQVTE NEDWNFYWMS VQTIRNVFSV EAGYRLSDDQ IVNHFPNHYE LTRKDLMVKN IKRYRKELEK EGSPLAEKDE NGKYLYLDFV PVTYMLPADY NLFVEEFRKS PSSTWIMKPC GKAQGKGIFL INKLSQIKKW SRDSKTSSFV SQSNKEAYVI SLYINNPLLI GGRKFDLRLY VLVSTYRPLR CYMYKLGFCR FCTVKYTPST SELDNMFVHL TNVAIQKHGE DYNHIHGGKW TVSNLRLYLE STRGKEVTSK LFDEIHWIIV QSLKAVAPVM NNDKHCFECY GYDIIIDDKL KPWLIEVNAS PSLTSSTAND RILKYNLIND TLNIAVPNGE IPDCKWNKSP PKEVLGNYEI LYDEELAQGD GADRELRSRQ GQSLGPRAGR SRDSGRAVLT TWK
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Molecular Weight
48.9 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
TTLL1, or Tubulin Tyrosine Ligase 1, is an enzyme that plays a crucial role in the post-translational modification of tubulin, a key component of the cytoskeleton in eukaryotic cells. This modification involves the addition of a tyrosine residue to the carboxy-terminal end of tubulin dimers, a process essential for proper microtubule dynamics and stability. Dysregulation of this modification has been linked to various diseases, including cancer and neurodegenerative disorders, highlighting the importance of TTLL1 research. The study of recombinant TTLL1 protein provides insights into its enzymatic function, mechanisms of action, and potential therapeutic targets. By producing TTLL1 in a recombinant system, researchers can dissect its activity, explore interactions with other cellular components, and identify substrates. Furthermore, understanding the structural and functional characteristics of TTLL1 can facilitate the development of inhibitors or modulators that may have significant clinical implications. As a result, TTLL1 has garnered attention in the fields of cell biology, biochemistry, and medicinal chemistry, paving the way for novel approaches to treat diseases associated with microtubule dysfunction.
