Analytical Data
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Gene name
TNFRSF11A
- Application
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Alternative Names
TNFRSF11A；RANK；Tumor necrosis factor receptor superfamily member 11A
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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
Q9Y6Q6
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Expression Region
30-212aa
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AA Sequence
IAPPCTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVCLPCGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRCACTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVCKPCLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVCSSSLPARKPPNEPHVYLP
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Molecular Weight
50.0 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
TNFRSF11A, also known as Receptor Activator of Nuclear Factor-κB (RANK), is a critical member of the tumor necrosis factor receptor superfamily that plays a pivotal role in bone metabolism, immune system regulation, and cell survival. It primarily mediates osteoclastogenesis and is essential for maintaining bone homeostasis. Dysregulation of RANK signaling has been implicated in various pathological conditions, including osteoporosis, rheumatoid arthritis, and certain cancers. Consequently, the therapeutic modulation of RANK signaling has garnered considerable attention in the field of drug development. Research involving recombinant TNFRSF11A proteins aims to elucidate the mechanisms of RANK signaling and its interactions with ligands such as RANKL (RANK Ligand) and OPG (Osteoprotegerin). These studies are crucial for understanding how RANK functions at the molecular level and for developing targeted therapies that could inhibit or enhance RANK activity in disease contexts. Furthermore, recombinant RANK proteins serve as valuable tools for examining the receptor’s structure-function relationships and for screening potential inhibitors or agonists, fostering advancements in treatment strategies for bone-related diseases and malignancies.
