Analytical Data
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Gene name
TGFa
- Application
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Alternative Names
TGFa；Protransforming growth factor alpha
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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
P01135
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Expression Region
24-98aa
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AA Sequence
ENSTSPLSADPPVAAAVVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVC HSGYVGARCEHADLLAVVAASQKKQ
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Molecular Weight
17 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
Transforming Growth Factor Alpha (TGFa) is a crucial cytokine involved in various physiological processes, including cell proliferation, differentiation, and survival. It exerts its effects primarily through the epidermal growth factor receptor (EGFR) pathway, playing a significant role in embryonic development and tissue regeneration. Dysregulation of TGFa has been implicated in several diseases, particularly cancer, where it can promote tumor growth and metastasis by enhancing cellular proliferation and influencing the tumor microenvironment. The recombinant production of TGFa has garnered significant interest due to its potential applications in therapeutic interventions and tissue engineering. By utilizing advanced biotechnological methods, researchers aim to produce functional TGFa proteins that can be utilized in both in vitro and in vivo studies. Understanding the structure-function relationship of TGFa and its interactions with cellular receptors is essential for elucidating its role in disease mechanisms and developing targeted therapies. Additionally, the ability to produce TGFa in a recombinant form allows for the standardization of doses and enhances the reproducibility of experiments, facilitating drug development. Overall, ongoing research into TGFa recombinant proteins promises to advance our understanding of its biological significance and improve treatment strategies for various diseases, particularly in oncology and regenerative medicine.
