Leptin Human Recombinant - 1mg

growth factor
Catalog #: CYT-228Description: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.Synonyms:OB Protein, Obesity Protein, OBS, Obes ...Read more
Catalog # CYT-228 $225.00 each


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  • Description
  • Specifications

Catalog #: CYT-228

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.

Synonyms:
OB Protein, Obesity Protein, OBS, Obesity factor.

Source:
Escherichia Coli.

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.

Purity:
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Solubility:
The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.

Formulation:
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Stability:
Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0 °C. Reconstituted Leptin is best stored refrigerated at 4 °C.

Activity:
Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Physical Appearance:
Sterile Filtered White lyophilized (freeze-dried) powder.

Protein Content:
Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.878 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
2. Analysis by RP-HPLC, using a calibrated solution of Leptin as a Reference Standard.

Usage:
Denovo Biotechnology's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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 January 2011 vol. 34 no. 1 132-138 .
Link:http://care.diabetesjournals.org/content/34/1/132.full
2.Title:The Mammalian Target of Rapamycin as Novel Central Regulator of Puberty Onset via Modulation of Hypothalamic Kiss1 System.
Publication: Published online before print September 4, 2009, doi: 10.1210/en.2009-0096 Endocrinology November 1, 2009 vol. 150 no. 11 5016-5026
Link:http://endo.endojournals.org/content/150/11/5016.full

3.Title:p38 Mitogen-Activated Protein Kinase and Liver X Receptor-? Mediate the Leptin Effect on Sterol Regulatory Element Binding Protein-1c Expression in Hepatic Stellate Cells.
Publication:Mol Med. 2012; 18(1): 10–18.



Published online 2011 October 3. doi: 10.2119/molmed.2011.00243
Link:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3269638/

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