Analytical Data
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Gene name
OSX
- Application
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Alternative Names
Sp7 Transcription Factor; Specificity Protein 7; Zinc finger protein osterix
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TDD2
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Expression Region
Met19~Leu288
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Molecular Weight
33kDa
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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 study of OSX (Osterix) recombined proteins has emerged as a significant area of research in the field of developmental biology and bone physiology. OSX is a zinc-finger transcription factor that plays a crucial role in osteoblast differentiation and bone mineralization. It has been identified as a key regulator in the osteogenic lineage, primarily influencing the maturation of osteoblasts, the cells responsible for bone formation. The discovery of OSX's function dates back to its characterization in murine models, where its gene knockout led to severe defects in bone formation, highlighting its essential role in skeletal development. Subsequent studies have revealed the intricate molecular pathways through which OSX interacts with other transcription factors and signaling molecules, contributing to the complex network that governs bone homeostasis. The potential of OSX recombined proteins extends beyond basic research, as they may serve as useful tools in understanding bone diseases and developing therapeutic strategies for osteoporosis and other disorders related to bone density. By generating recombinant forms of OSX, researchers aim to dissect its functional domains and determine their specific contributions to osteogenesis. This endeavor not only enhances our understanding of bone biology but also opens avenues for biotechnological applications, including the engineering of bone grafts and the design of innovative treatments for skeletal disorders. As research progresses, the detailed exploration of OSX recombined proteins is expected to provide valuable insights into the mechanisms of bone formation and the potential for regenerative medicine.
