Analytical Data
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Gene name
IHH
- Application
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Alternative Names
BDA1; HHG2
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Species
Mouse
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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
P97812
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Expression Region
Val45~Ser195
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Molecular Weight
21kDa
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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
IHH, or Indian Hedgehog, is a signaling molecule that plays a critical role in various developmental processes including limb formation, cartilage development, and cell differentiation. The IHH protein is part of the Hedgehog signaling pathway, which is essential for regulating cell growth, tissue patterning, and organogenesis during embryonic development. Dysregulation of IHH signaling has been implicated in several congenital disorders and malignancies, making it a significant focus of biomedical research. Recent studies have aimed at understanding the structural and functional characteristics of recombinant IHH protein to elucidate its mechanism of action and interactions with other proteins. By utilizing techniques such as protein engineering, molecular cloning, and expression systems, researchers have successfully synthesized and purified IHH protein in vitro. This has allowed for detailed investigations into its biochemical properties and potential therapeutic applications, particularly in regenerative medicine and cancer treatment. The ongoing research into recombinant IHH not only provides insights into fundamental biological processes but also opens avenues for developing novel strategies to manipulate Hedgehog signaling for therapeutic benefit.
