Analytical Data
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Gene name
GLI1
- Application
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Alternative Names
GLI1;GLI;Zinc finger Protein GLI1
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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
P08151
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Expression Region
401-500aa
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AA Sequence
GPLPRAPSISTVEPKREREGGPIREESRLTVPEGAMKPQPSPGAQSSCSS DHSPAGSAANTDSGVEMTGNAGGSTEDLSSLDEGPCIAGTGLSTLRRLEN
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Molecular Weight
37 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
GLI1, a key transcription factor in the Hedgehog signaling pathway, plays a critical role in embryonic development and tissue homeostasis. Abnormal regulation of GLI1 is implicated in various human diseases, particularly cancer, where it is often overexpressed, leading to unchecked cellular proliferation and survival. Understanding GLI1's function has significant therapeutic implications, especially in targeting Hedgehog pathway-related malignancies. Researchers have been increasingly focused on characterizing GLI1’s structure and function through recombinant protein studies. By utilizing techniques such as cloning, expression, and purification of GLI1, scientists aim to elucidate its mechanisms of action, interactions with other proteins, and the impact of post-translational modifications. These studies contribute to a deeper understanding of the molecular underpinnings of diseases associated with GLI1 dysregulation and pave the way for developing potential interventions, including small molecule inhibitors or gene therapies. Furthermore, recombinant GLI1 proteins serve as valuable tools in drug discovery, allowing for the screening of compounds that can modulate its activity. Overall, the research on recombinant GLI1 is essential for advancing our knowledge of cellular signaling pathways and their implications in health and disease.











