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|Antigen||Leptin Receptor (LEPR) Antibodies|
|Epitope||Extracellular Domain Alternatives|
|Conjugate||This Leptin Receptor antibody is un-conjugated Alternatives|
Enzyme Immunoassay (EIA), Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB)
|1 reference available|
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Product Details anti-Leptin Receptor AntibodyTarget Details Leptin Receptor Application Details Handling References for anti-Leptin Receptor antibody (ABIN114692) Images
|Purification||Affinity chromatography on Protein G|
|Immunogen||The Human Leptin Receptor is a recombinant protein produced in mouse myeloma cell line. DNA sequence including the extracellular domain of Leptin Receptor (amino acid residues 1 839) fused to the Fc region of human IgG (with IIEGR added at the amino terminus and 6 histidine residues added at the carboxy terminus).|
Target Details Leptin ReceptorProduct Details anti-Leptin Receptor Antibody Application Details Handling References for anti-Leptin Receptor antibody (ABIN114692) Images back to top
|Alternative Name||CD295 / Leptin Receptor (LEPR Antibody Abstract)|
|Background||Leptin receptor (OB R) was identified as a leptin binding protein (Leptin, the product of the ob gene, is a single chain 16 kDa protein consisting of 146 amino acid residues.) OB R was found to be a member of the class I cytokine receptor family with a large extracellular domain comprising 816 amino acid residues. Leptin receptor exists in multiple forms with a common extracellular domain and a variable length cytoplasmatic portion. Alternate splicing from a single gene derives the six isoforms of the Leptin receptor. The soluble form of the Leptin receptor, OB R contains no intracellular motifs or transmembrane residues, thus it consists entirely of the extracellular ligand binding domain of the receptor. Long forms of OB-R transcripts were reported to be expressed predominantly in regions of the hypothalamus which provides evidence that Leptin receptor is important in body weight regulation. Expression of short forms of OB-R transcripts have been found in multiple tissues, including the choroid plexus, lung, kidney, and primitive hematopoietic cell populations. Leptin receptor may act as a negative regulator of Leptin activity and it may maintain a pool of available bioactive Leptin by binding and delaying its clearance from circulation. Soluble Leptin receptor levels are indirectly proportional to adiposity and are increased in females versus males. Leptin receptor levels are highest in infants, decrease into adolescence, and remain relatively stable throughout adulthood. Soluble Leptin receptor is also found upregulated in patients with chronic heart failure, end-stage renal disease and anorexia.Synonyms: DB, HuB219, LEP-R, LEPR, OB receptor, OB-R, OBR|
|Pathways||JAK-STAT Signaling, AMPK Signaling, Feeding Behaviour|
Application DetailsProduct Details anti-Leptin Receptor Antibody Target Details Leptin Receptor Handling References for anti-Leptin Receptor antibody (ABIN114692) Images back to top
ELISA. Immunohistochemistry. Western Blot.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
|Restrictions||For Research Use only|
HandlingProduct Details anti-Leptin Receptor Antibody Target Details Leptin Receptor Application Details References for anti-Leptin Receptor antibody (ABIN114692) Images back to top
|Reconstitution||Restore with 0.1 mL of deionized water.|
|Buffer||0.05 M phosphate buffer, 0.1 M NaCl, pH 7.2. AZIDE FREE|
|Handling Advice||Avoid repeated freezing and thawing.|
|Storage Comment||Prior to reconstitution store at -70 °C. Following reconstitution store the antibody (in aliquots) at -20 °C for 6 month.|
|Expiry Date||6 months|
References for anti-Leptin Receptor antibody (ABIN114692)Product Details anti-Leptin Receptor Antibody Target Details Leptin Receptor Application Details Handling Images back to top
Verhaeghe, van Bree, Van Herck: "Maternal body size and birth weight: can insulin or adipokines do better?" in: Metabolism: clinical and experimental, Vol. 55, Issue 3, pp. 339-44, 2006