Analytical Data
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Gene name
NID
- Application
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Alternative Names
NID；NID；Nidogen-1
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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
P14543
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Expression Region
927-1247aa
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AA Sequence
IHQGPAVPTAVIPLPPGTHLLFAQTGKIERLPLEGNTMRKTEAKAFLHVPAKVIIGLAFDCVDKMVYWTDITEPSIGRASLHGGEPTTIIRQDLGSPEGIAVDHLGRNIFWTDSNLDRIEVAKLDGTQRRVLFETDLVNPRGIVTDSVRGNLYWTDWNADNPKIETSYMDGTNRRILVQDDLGLPNGLTFDAFSSQLCWVDAGTNRAECLNPSQPSRRKALEGLQAPFAVTSYGKNLYFTDAKMNSVVALDLAISKETDAFQPHKQTALAGITTALSQCPQGHNYCSVNNGGCTHLCLATPGSRTCRCPDNTLGVDCIEQK
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Molecular Weight
42.0 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
NID recombinant proteins have gained significant attention in recent years due to their potential applications in various fields, including vaccine development, therapeutic interventions, and biomarker discovery. NID, or Neurodegenerative Disease, recombinant proteins are engineered to mimic specific protein structures found in neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's disease. The study of these proteins aims to elucidate the underlying mechanisms of neurodegeneration and the pathological roles of misfolded proteins, which are often implicated in disease progression. By using recombinant DNA technology, researchers can produce large quantities of NID proteins, facilitating detailed studies on their structure, function, and interactions with other cellular components. Furthermore, the development of NID recombinant proteins allows for the design of targeted therapies and diagnostics that could potentially halt or reverse neurodegeneration. Overall, the research on NID recombinant proteins represents a promising frontier in understanding complex neurodegenerative diseases and developing innovative solutions to combat these conditions.
