Analytical Data
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Gene name
OGN
- Application
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Alternative Names
OGN；OIF；SLRR3A；Mimecan
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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
P20774
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Expression Region
21-298aa
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AA Sequence
PPTQQDSRIIYDYGTDNFEESIFSQDYEDKYLDGKNIKEKETVIIPNEKSLQLQKDEAITPLPPKKENDEMPTCLLCVCLSGSVYCEEVDIDAVPPLPKESAYLYARFNKIKKLTAKDFADIPNLRRLDFTGNLIEDIEDGTFSKLSLLEELSLAENQLLKLPVLPPKLTLFNAKYNKIKSRGIKANAFKKLNNLTFLYLDHNALESVPLNLPESLRVIHLQFNNIASITDDTFCKANDTSYIRDRIEEIRLEGNPIVLGKHPNSFICLKRLPIGSYF
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Molecular Weight
33.7kDa
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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
The research on OGN (Osteoglycin) recombinant protein is driven by its significant role in the extracellular matrix and its implications in various physiological and pathological processes. OGN, a small leucine-rich proteoglycan, is predominantly expressed in connective tissues, where it regulates collagen fibril formation and influences extracellular matrix organization. Initial studies have suggested that OGN may play a critical role in bone development, cartilage integrity, and wound healing. Furthermore, aberrations in OGN expression have been linked to various diseases, including osteoarthritis, fibrosis, and certain cancers. As a result, understanding OGN's structure and function at the molecular level is crucial for elucidating its biological roles. The advent of recombinant DNA technology has enabled the production of OGN as a fully functional protein, facilitating more in-depth studies on its biochemical properties and interactions. Researchers are now focusing on characterizing the recombinant OGN protein, evaluating its effects on cell behavior and matrix dynamics, and exploring its potential therapeutic applications. This knowledge could pave the way for innovative treatment strategies targeting conditions associated with altered OGN function, highlighting the importance of OGN in connective tissue biology and its potential as a biomarker or therapeutic target in disease management. Overall, the study of OGN recombinant protein holds promise for advancing our understanding of connective tissue disorders and developing novel interventions for enhancing tissue repair and regeneration.
