Analytical Data
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Gene name
GLI2
- Application
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Alternative Names
GLI2；THP；Zinc finger Protein GLI2
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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
P10070
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Expression Region
412-641aa
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AA Sequence
EQLADLKEDLDRDDCKQEAEVVIYETNCHWEDCTKEYDTQEQLVHHINNE HIHGEKKEFVCRWQACTREQKPFKAQYMLVVHMRRHTGEKPHKCTFEGCS KAYSRLENLKTHLRSHTGEKPYVCEHEGCNKAFSNASDRAKHQNRTHSNE KPYICKIPGCTKRYTDPSSLRKHVKTVHGPDAHVTKKQRNDVHLRTPLLK ENGDSEAGTEPGGPESTEASSTSQAVEDCL
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Molecular Weight
31 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
GLI2 is a crucial transcription factor that plays a significant role in the Hedgehog signaling pathway, which is essential for embryonic development and tissue homeostasis. Aberrant activation or mutations of GLI2 have been implicated in various cancers and developmental disorders, making it a critical target for therapeutic intervention. The study of GLI2 recombinant proteins provides valuable insights into its biological functions and regulatory mechanisms. By producing and characterizing GLI2 in a recombinant form, researchers aim to elucidate its binding interactions with other proteins, DNA, and the molecular processes leading to its activation or repression. Additionally, understanding the structure and dynamics of GLI2 can reveal potential drug-binding sites, paving the way for the development of small molecules that can modulate its activity. Recent advancements in protein expression systems have enabled the efficient production of GLI2 recombinant proteins, facilitating in vitro studies and high-throughput screening assays. Overall, research on GLI2 recombinant proteins is critical for advancing our understanding of its role in health and disease, and it holds promise for the development of novel therapeutics targeting GLI2-related pathways.
