Human Leptin ( Leptin Human )

Catalog # PT_41403

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$201.00
DescriptionLeptin Human produced syntheticaly contains 35 amino acids (22-56 a.a.) having a molecular mass of 3950.6 Dalton.Physical AppearanceSterile Filtered White lyophilized (freeze-dried) powder.FormulationThe protein was lyophilized from a
Product Size: 200ug
Quantity

Data sheet

Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Solubility
The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.
Purity
Greater than 95.0% as determined by:(a) Analysis by SEC-HPLC.(b) Analysis by SDS-PAGE.
Description
Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Protein Background
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Expression host
Escherichia Coli.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Reagent Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.
Amino acid sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
Biological Activity
Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.
References
1.Title:Leptin and Amylin Act in an Additive Manner to Activate Overlapping Signaling Pathways in Peripheral Tissues In vitro and ex vivo studies in humans.Publication:Published online before print September 24, 2010, doi: 10.2337/dc10-0518 Diabetes Care
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