Analytical Data
-
Gene name
Leptin
- Application
-
Alternative Names
OB; OBS; Obesity Homolog; Obesity Factor; Obese Protein
-
Species
Human
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P41159
-
Expression Region
Val22~Cys167
-
Protein Length
Partial
-
Molecular Weight
46kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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.
Related Products
Protein Description
Leptin is a critical adipocyte-derived hormone that plays a pivotal role in regulating energy balance, appetite, and metabolism. Discovered in the mid-1990s, leptin is primarily involved in signaling the brain to inhibit hunger and promote energy expenditure, thereby contributing to body weight homeostasis. Dysregulation of leptin signaling can lead to obesity, metabolic syndrome, and related health issues. As a result, leptin has become a significant focus in biomedical research aimed at understanding these conditions. Recombinant leptin protein, produced through genetic engineering techniques, enables detailed studies into leptin's physiological effects and mechanisms of action. Such research has implications not only for basic science but also for developing therapeutic strategies for obesity and its complications. Understanding the structure-function relationship of leptin and its receptor interactions through recombinant forms may pave the way for novel treatment options, including leptin-based therapies. Moreover, these recombinant proteins can serve as valuable tools for studying leptin's role in various biological systems, validating its potential as a biomarker for obesity-related disorders.
