Analytical Data
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Gene name
DYNLL1
- Application
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Alternative Names
DYNLL1;DLC1;DNCL1;DNCLC1;Dynein light chain 1. cytoplasmic
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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
P63167
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Expression Region
1-89aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMCDRKAVIKNADMSEEMQQDSVECATQALE KYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQ VAILLFKSG
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Molecular Weight
13 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
Related Products
Protein Description
DYNLL1, or Dynein Light Chain 1, is a crucial protein involved in intracellular transport, primarily functioning as a co-factor in dynein-based retrograde transport along microtubules. Its role in cellular processes like organelle positioning, vesicle trafficking, and mitosis highlights its importance in maintaining cellular homeostasis. Dysfunctions in DYNLL1 have been implicated in various diseases, including neurodegenerative disorders and certain cancers, underscoring the need for deeper understanding of its molecular mechanisms. Recombinant DYNLL1 protein has been utilized in research to elucidate its interactions with other proteins and its involvement in cellular pathways. By producing and studying this protein, researchers aim to reveal insights into its regulatory functions and potential as a therapeutic target. Understanding the dynamics of DYNLL1 at a molecular level not only contributes to our knowledge of cellular transport mechanisms but also opens avenues for developing interventions in diseases where its function is compromised. This makes the study of DYNLL1 and its recombinant forms an area of significant interest in cell biology and therapeutic research.











