Analytical Data
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Gene name
NEFL
- Application
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Alternative Names
NEFL；Zinc finger Protein 180
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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
P07196
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Expression Region
2-543aa
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AA Sequence
SSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSL SVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRF ASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAE DATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADE AALARAELEKRIDSLMDEISFLKKVHEEEIAELQAQIQYAQISVEMDVTK PDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAA KDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTI NKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLS FTSVGSITSGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQ IEVEETIEAAKAEEAKDEPPSEGEAEEEEKDKEEAEEEEAAEEEEAAKEE SEEAKEEEEGGEGEEGEETKEAEEEEKKVEGAGEEQAAKKKD
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Molecular Weight
81 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
The study of NEFL (neurofilament light chain) recombinant proteins has gained significant interest in the field of neurobiology due to their crucial roles in neuronal structure and function. Neurofilaments are integral components of the neuronal cytoskeleton, providing mechanical support and stability to axons. Alterations in neurofilament proteins, particularly NEFL, have been implicated in various neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), Alzheimer's disease, and other forms of tauopathies. Understanding the molecular mechanisms behind NEFL's function and its involvement in neurodegenerative processes is essential for developing potential therapeutic strategies. Furthermore, NEFL can serve as a biomarker for axonal damage, making it a valuable target for diagnostic tools in clinical settings. The ability to produce recombinant NEFL proteins allows researchers to study their biochemical properties, interactions, and pathological implications in a controlled environment. This research may lead to insights into how disruptions in neurofilament dynamics contribute to neuronal cell death and disease progression. As such, NEFL recombinant protein studies are pivotal for elucidating the complexities of neurodegeneration and for paving the way towards innovative treatments for neurological disorders.
