Analytical Data
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Gene name
NOG
- Application
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Alternative Names
；
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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
Q13253
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Expression Region
28-232aa
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AA Sequence
QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC
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Molecular Weight
23 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
NOG, or noggin, is a secreted protein that plays a critical role in the regulation of bone and cartilage development by antagonizing bone morphogenetic proteins (BMPs). Its study has gained prominence due to its vital functions in embryonic development and cellular differentiation. Research has shown that NOG is essential for proper skeletal patterning, and its dysregulation is linked to various skeletal disorders, including joint deformities and bone malformations. Additionally, NOG is involved in the maintenance of progenitor cell pools and has implications in regenerative medicine and tissue engineering. The recombinant production of NOG has become a focus of investigation to better understand its biological functions and potential therapeutic applications. By using recombinant DNA technology, researchers can generate large quantities of functional NOG protein, allowing for in-depth studies of its mechanisms of action in development and disease. Furthermore, investigations into NOG's interactions with other signaling pathways could pave the way for novel strategies in treating bone-related diseases and enhance the efficacy of stem cell therapies. Overall, the exploration of NOG and its recombinant forms represents a promising frontier in developmental biology and regenerative medicine, with significant implications for health and disease outcomes.
