Analytical Data
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Gene name
LCN1
- Application
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Alternative Names
LCN1；VEGP；Lipocalin-1
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Species
Human
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Source
HEK293
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Tag
C- 10*His tag
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P31025
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Expression Region
19-176aa
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AA Sequence
HHLLASDEEIQDVSGTWYLKAMTVDREFPEMNLESVTPMTLTTLEGGNLEAKVTMLISGRCQEVKAVLEKTDEPGKYTADGGKHVAYIIRSHVKDHYIFYCEGELHGKPVRGVKLVGRDPKNNLEALEDFEKAAGARGLSTESILIPRQSETCSPGSD
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Molecular Weight
20-22 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
Identification
Protein Description
LCN1 (Lipocalin 1), also known as LgfA or β-Lactoglobulin, is a member of the lipocalin family, which is characterized by its ability to bind small hydrophobic molecules. It has a significant role in various physiological processes, including cellular differentiation, inflammation, and metabolic regulation. Research on LCN1 has gained attention due to its involvement in several pathological conditions, such as cancer and obesity, and its potential as a biomarker for disease progression. The recombinant production of LCN1 protein presents an opportunity to explore its biological functions and interactions in a controlled environment. By utilizing techniques such as recombinant DNA technology and protein expression systems, researchers can produce LCN1 in sufficient quantities for structural and functional studies. Such investigations aim to elucidate the protein's mechanisms of action, binding affinities, and therapeutic potentials. Understanding LCN1 at the molecular level could lead to innovative strategies for diagnosis and treatment of diseases where LCN1 plays a critical role, further emphasizing the importance of continued research on this intriguing protein.
