Analytical Data
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Gene name
DHH
- Application
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Alternative Names
DHH;Desert hedgehog Protein
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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
O43323
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Expression Region
23-198aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMIIGPGRGPVGRRRYARKQLVPLLYKQ FVPGVPERTLGASGPAEGRVARGSERFRDLVPNYNPDIIFKDEENSGADR LMTERCKERVNALAIAVMNMWPGVRLRVTEGWDEDGHHAQDSLHYEGRAL DITTSDRDRNKYGLLARLAVEAGFDWVYYESRNHVHVSVKADNSLAVRAG G
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Molecular Weight
22 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
DHH (Desert Hedgehog) is a member of the Hedgehog signaling pathway, which plays a crucial role in embryonic development, cell differentiation, and tissue patterning. Its involvement in various biological processes has garnered significant interest in the scientific community, particularly regarding its implications in developmental disorders and cancer. Researchers have focused on the study of DHH recombinant proteins to investigate the intricate mechanisms of Hedgehog signaling and its functional roles in various cellular contexts. By using recombinant technology, scientists can produce DHH in a controlled environment, allowing for detailed analyses of its structure, function, and interaction with signaling receptors. Furthermore, understanding how DHH operates at the molecular level can lead to insights into therapeutic strategies for diseases associated with its dysregulation. The production and characterization of DHH recombinant proteins serve as a valuable tool for dissecting the pathways influenced by Hedgehog proteins, ultimately contributing to advancements in regenerative medicine and cancer treatment. This research holds promise for uncovering novel interventions that target DHH's role in pathologies, potentially leading to more effective treatments and better patient outcomes.
