Analytical Data
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Gene name
Igfl
- Application
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Alternative Names
Igfl；Insulin growth factor-like family member 1
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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
P05019
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Expression Region
49-118aa
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AA Sequence
GP ETLCGAELVD ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPAKSA
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Molecular Weight
8 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
Igfl (Insulin-like growth factor-like protein) is an essential protein that has garnered significant attention in the fields of endocrinology and developmental biology due to its roles in growth and metabolism. The research surrounding Igfl primarily focuses on its structural characteristics, functional mechanisms, and potential applications in therapeutic contexts. This protein is implicated in various biological processes including cell growth, differentiation, and proliferation, largely interacting with insulin-like growth factor receptors. Studies have shown that aberrations in Igfl signaling pathways can lead to developmental disorders and metabolic diseases. Moreover, its involvement in postoperative recovery and muscle regeneration positions Igfl as a crucial factor within regenerative medicine. Recombination techniques for producing Igfl proteins are a focal point in ongoing research, aimed at elucidating its biological activity and therapeutic potential. By creating recombinant Igfl proteins, scientists aim to better understand their roles in disease and health, as well as explore their potential in therapeutic interventions, including tissue engineering and regenerative therapies. This ongoing research not only provides insight into fundamental biological processes but also opens up new avenues for innovative treatment strategies, positioning Igfl as a promising candidate for future investigations in both basic and applied biomedical research.
