Analytical Data
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Gene name
PIN/DYNLL1
- Application
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Alternative Names
8KDA dynein light chain ;DLC8Dynein light chain LC8-type 1;Protein inhibitor of neuronal nitric oxide synthase ;PIN
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Species
Human
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Source
E. coli
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Tag
N- GST
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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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Molecular Weight
37.4 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
The study of PIN/DYNLL1 recombinant protein is rooted in its significant role in cellular processes, particularly in intracellular transport and signal transduction. PIN, also known as DYNLL1 (dynein light chain 1), is a highly conserved protein that serves as a crucial adaptor in the dynein motor complex, facilitating the transport of cellular cargo along microtubules. This protein has been implicated in various physiological processes, including cell division, neuronal function, and organelle positioning. Disruptions in its function have been associated with various pathologies, including neurological disorders and cancer. Recent advancements in recombinant protein technology have enabled the production of PIN/DYNLL1 in significant quantities, allowing researchers to investigate its structural properties, binding interactions, and functional mechanisms in greater detail. Understanding the biochemistry of PIN/DYNLL1 not only contributes to the fundamental knowledge of cellular dynamics but also holds potential for therapeutic applications in diseases linked to dynein dysfunction. As research continues to unveil the complexities of its interactions and regulatory mechanisms, PIN/DYNLL1 stands as a promising target for innovative drug development aimed at restoring normal cellular function in disease contexts.
