Analytical Data
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Gene name
DYNLT1
- Application
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Alternative Names
DYNLT1；TCTEL1；TCTEX-1；TCTEX1;Dynein light chain Tctex-type 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
P63172
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Expression Region
1-113aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMEDYQAAEETAFVVDEVSNIVKEAIESAIG GNAYQHSKVNQWTTNVVEQTLSQLTKLGKPFKYIVTCVIMQKNGAGLHTA SSCFWDSSTDGSCTVRWENKTMYCIVSAFGLSI
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Molecular Weight
15 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
DYNLT1, or Dynein Light Chain T1, is a member of the dynein motor protein complex, which plays a crucial role in intracellular transport, cellular division, and organelle positioning. Recent studies have highlighted the significance of DYNLT1 in various cellular processes, including endocytosis, mitosis, and neurodegenerative diseases. Dysregulation of dynein activity, associated with mutations or altered expression of dynein subunits like DYNLT1, has been implicated in a range of pathological conditions, particularly in the central nervous system. Understanding the structure and function of DYNLT1 is essential for elucidating its role in these processes. The recombinant production of DYNLT1 allows researchers to study its biochemical properties, interactions with other protein partners, and effects on cellular transport mechanisms in detail. This has significant implications for developing therapeutic strategies targeting dynein-related disorders. As researchers continue to explore the potential of DYNLT1 as a biomarker or therapeutic target, the recombinant protein serves as a vital tool for advancing our understanding of dynein biology and its impact on health and disease.
