Analytical Data
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Gene name
Shh
- Application
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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
Q15465
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Expression Region
24-197aa
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AA Sequence
CGPGRGFGKRRHPKKLTPLAYKQFIPNVAEKTLGASGRYEGKISRNSERF KELTPNYNPDIIFKDEENTGADRLMTQRCKDKLNALAISVMNQWPGVKLR VTEGWDEDGHHSEESLHYEGRAVDITTSDRDRSKYGMLARLAVEAGFDWV YYESKAHIHCSVKAENSVAAKSGG
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Molecular Weight
51 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
The study of Sonic Hedgehog (Shh) recombinant protein has gained significant attention in developmental biology and regenerative medicine due to its critical role in various signaling pathways that govern embryonic development, cell differentiation, and tissue patterning. Shh is a member of the Hedgehog signaling pathway, which is essential for proper organogenesis and is implicated in the regulation of cell proliferation and fate determination during embryonic development. Abnormal Shh signaling has been linked to a variety of congenital disorders and cancers, making it a crucial target for therapeutic interventions. Research focuses on producing Shh recombinant proteins to better understand their structure-function relationships and to explore their potential applications in tissue engineering and regenerative therapies. For instance, Shh has shown promise in promoting neural stem cell proliferation and differentiation, indicating its potential for treating neurodegenerative diseases or spinal cord injuries. Moreover, studying Shh in a controlled recombinant form allows researchers to investigate its interactions with other signaling molecules and its downstream effects on gene expression. Overall, the exploration of Shh recombinant protein holds significant promise for advancing our understanding of developmental processes and for developing innovative therapeutic strategies in various medical fields.
