Analytical Data
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Gene name
DYNLL2
- Application
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Alternative Names
DYNLL2；DLC2;Dynein light chain 2. 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
Q96FJ2
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Expression Region
1-89aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSDRKAVIKNADMSEDMQQDAVDCATQAME KYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQ 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
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Protein Description
DYNLL2, or dynein light chain 2, is a crucial protein that plays a significant role in cellular processes, particularly in the context of intracellular transport and cytoskeletal dynamics. As a member of the dynein complex, it is involved in the retrograde transport of cellular cargo along microtubules, impacting various cellular functions such as organelle positioning, vesicle trafficking, and cell division. Research on DYNLL2 has gained traction due to its implications in various diseases, including neurodegenerative disorders and certain types of cancer, where disruptions in dynein-mediated transport can affect cellular homeostasis. The functional versatility of DYNLL2 extends beyond scaffolding in the dynein complex; it is also known to interact with other proteins, influencing signaling pathways and cellular stress responses. Recombinant DYNLL2 protein is therefore of great interest in biochemical and biophysics research, enabling scientists to study its structural properties, binding characteristics, and functional roles in vitro. Understanding the molecular mechanisms of DYNLL2 not only enhances our knowledge of dynein function but also paves the way for potential therapeutic strategies targeting transport-related diseases. Consequently, the exploration of DYNLL2 as a recombinant protein serves as a vital step in elucidating the complex interplay of protein interactions within the cell and may contribute to innovative approaches in drug development or disease treatment.
