Analytical Data
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Gene name
Nid1
- Application
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Alternative Names
Nid1;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
1-1247aa
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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
Nid1, or Nidogen-1, is a key component of the extracellular matrix that plays a crucial role in the maintenance and organization of basement membranes. It functions as a bridge between various matrix components, such as laminins and collagen IV, thereby influencing tissue architecture and cell behavior. The study of Nid1 recombinant proteins has gained considerable attention due to its potential implications in understanding various diseases, including cancer, fibrosis, and neurodegenerative disorders. Research has demonstrated that alterations in Nid1 expression or function can disrupt normal cellular interactions and contribute to pathological conditions. By generating and studying recombinant Nid1 proteins, scientists aim to elucidate its structural and functional properties, investigate its interactions with other extracellular matrix proteins, and assess its impact on cell adhesion, migration, and signaling pathways. Furthermore, recombinant Nid1 proteins offer valuable tools for developing therapeutic strategies, as they can be used to create biomaterials for tissue engineering or as potential targets for drug design. Overall, the investigation of Nid1 recombinant proteins not only enhances our understanding of extracellular matrix dynamics but also paves the way for novel approaches in treating diseases associated with matrix dysfunction.











