Analytical Data
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Gene name
LEP
- Application
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Alternative Names
LEP;OB;OBS;Leptin
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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
P41159
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Expression Region
22-167aa
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AA Sequence
VPIQKVQDDT KTLIKTIVTR INDISHTQSV SSKQKVTGLD FIPGLHPILT LSKMDQTLAV YQQILTSMPS RNVIQISNDL ENLRDLLHVL AFSKSCHLPW ASGLETLDSL GGVLEASGYS TEVVALSRLQ GSLQDMLWQL DLSPGC
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Molecular Weight
16.0 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
Protein Description
LEP (leptin) is a hormone predominantly produced by adipose tissue, playing a crucial role in energy balance, appetite regulation, and metabolism. Its significance has garnered considerable attention in obesity and metabolic disorder research. LEP functions by binding to its receptor, LEPR, located in the hypothalamus, modulating various physiological processes such as food intake and energy expenditure. The study of LEP and its recombinant proteins has emerged as a pivotal area in biomedical research, particularly for understanding the mechanisms of obesity and related diseases. Recombinant LEP proteins are utilized to explore their therapeutic potential, offering insights into weight regulation and potential interventions for obesity-related pathologies. Additionally, these studies aim to unravel the functional and structural properties of LEP, as mutations or dysregulation of this hormone can lead to severe metabolic syndrome and other health complications. The development of animal models and in vitro systems expressing recombinant LEP facilitates investigations into its signaling pathways, effectiveness in modulating food intake, and interactions with other hormones. As research progresses, the implications of LEP in clinical settings could pave the way for innovative treatments for obesity and improve overall metabolic health. Understanding LEP's intricate role in human physiology remains critical, as it opens avenues for designing targeted therapies that address the growing obesity epidemic globally.
