Analytical Data
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Gene name
DYNLL2
- Application
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Alternative Names
DNCL1B; Dlc2; RSPH22; 8 kDa dynein light chain b; Dynein light chain 2, cytoplasmic
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Species
Human
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Source
E. coli
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Tag
N-6His
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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
20~89aa
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Molecular Weight
11kDa
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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
Identification
Protein Description
DYNLL2, a member of the dynamin superfamily of proteins, plays a critical role in cellular processes such as vesicle trafficking, organelle dynamics, and cytoskeletal organization. Recent studies have highlighted its involvement in various diseases, including cancer and neurodegenerative disorders, making it a target of increasing interest in biomedical research. Functional studies suggest that DYNLL2 interacts with a range of binding partners, influencing cellular signaling pathways and cellular morphology. The recombinant expression of DYNLL2 allows researchers to investigate its biochemical properties, functional mechanisms, and interactions with other proteins in a controlled environment. By studying the recombinant protein, insights can be gained into its structural characteristics and the effects of mutations that may contribute to pathological conditions. Moreover, DYNLL2-recombinant protein can serve as a valuable tool for screening potential drug candidates and elucidating the molecular mechanisms underlying its role in health and disease. This research ultimately aims to unearth therapeutic strategies that can mitigate the effects of diseases associated with DYNLL2 dysregulation, contributing to advancements in precision medicine and targeted therapies.
