Analytical Data
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Gene name
IGFL1
- Application
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Alternative Names
IGFL1；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
Q6UW32
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Expression Region
25-110aa
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AA Sequence
APVAPMTPYLMLCQPHKRCGDKFYDPLQHCCYDDAVVPLARTQTCGNCTFRVCFEQCCPWTFMVKLINQNCDSARTSDDRLCRSVS
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Molecular Weight
38.7 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
IGFL1 (Insulin-like Growth Factor-Like 1) is a member of the insulin-like growth factor family, which plays a crucial role in growth and development by mediating various cellular processes such as proliferation, differentiation, and apoptosis. This protein has garnered attention due to its potential implications in both physiological and pathological conditions, including muscle hypertrophy, cancer, and metabolic diseases. The study of recombinant IGFL1 has become increasingly important as it provides a means to understand its biological functions and therapeutic potential. By expressing IGFL1 in a recombinant system, researchers can obtain sufficient quantities for rigorous analysis, including binding studies and functional assays. Additionally, recombinant IGFL1 allows for the exploration of its interactions with other growth factors and receptors, shedding light on its role in signaling pathways. Understanding these mechanisms may lead to novel therapeutic strategies for conditions where IGFL1 is implicated. Furthermore, the investigation of IGFL1 can contribute to the development of biomarker diagnostics and targeted treatments for diseases such as cancer, where its altered expression may signify disease progression or therapeutic response. Overall, the research on recombinant IGFL1 not only enhances our understanding of fundamental biological processes but also opens new avenues for clinical applications in regenerative medicine and oncology.
