Analytical Data
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Gene name
OSTN
- Application
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Alternative Names
OSTN;Osteocrin
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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
P61366
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Expression Region
83-132aa
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AA Sequence
SFSGFGSP LDRLSAGSVD HKGKQRKVVD HPKRRFGIPM DRIGRNRLSN SR
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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
OSTN (Osteocrin) is a secreted protein that belongs to the family of small leucine-rich proteoglycans. It has garnered interest in biomedical research due to its unique structural properties and potential roles in various physiological processes, particularly in musculoskeletal development and regulation. Initially identified in bone tissue, OSTN is involved in the modulation of cellular activities and extracellular matrix composition, influencing bone formation and remodeling. Recent studies have suggested that OSTN can affect muscle function and may play a critical role in obesity and metabolic diseases, as its expression is closely linked to adipose tissue and energy metabolism. Understanding the molecular mechanisms through which OSTN exerts its effects could lead to novel therapeutic approaches for metabolic disorders, bone diseases, and muscle-related conditions. The exploration of OSTN’s potential as a reprogramming factor in stem cell biology has further expanded the scope of its research. Investigating the structural characteristics and functional implications of OSTN in various biological contexts holds promise for uncovering new insights into cell signaling pathways and tissue regeneration. Thus, the characterization of OSTN as a recombinant protein is a crucial step in elucidating its biological functions and therapeutic applications, paving the way for innovations in regenerative medicine and the treatment of metabolic syndromes.
