Analytical Data
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Gene name
RUNX2
- Application
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Alternative Names
RUNX2；AML3；CBFA1；OSF2；Runt-related transcription factor 2
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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
Q13950
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Expression Region
311-450aa
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AA Sequence
TSPSIHSTTPLSSTRGTGLPAITDVPRRISDDDTATSDFCLWPSTLSKKS QAGASELGPFSDPRQFPSISSLTESRFSNPRMHYPATFTYTPPVTSGMSL GMSATTHYHTYLPPPYPGSSQSQSGPFQTSSTPYLYYGTS
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Molecular Weight
41 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
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Protein Description
RUNX2, a key transcription factor in bone development and mineralization, plays a crucial role in osteoblast differentiation and function. Mutations or dysregulation of RUNX2 are associated with various bone disorders, including cleidocranial dysostosis, characterized by abnormal bone growth and development. The study of RUNX2 is essential for understanding these conditions and for potential therapeutic interventions. Recombinant RUNX2 proteins are valuable tools in research, allowing scientists to investigate the molecular mechanisms of osteogenesis and the regulatory pathways influencing bone formation. By producing RUNX2 in a recombinant form, researchers can explore its interaction with other proteins and identify potential targets for drug development. Furthermore, studying the biochemical properties and functional outcomes of RUNX2 enables a deeper understanding of its role in skeletal biology. This knowledge holds promise for advancing regenerative medicine and developing strategies for treating osteoporosis and other skeletal diseases. The ongoing research into RUNX2 and its recombinant protein applications may lead to breakthroughs in therapies aimed at enhancing bone regeneration and understanding the genetic basis of skeletal abnormalities.
