Leptin Recombinant Protein | LEP recombinant protein

Recombinant Human Leptin

Cat. Num. AAA958280

• Gene Names: LEP; OB; OBS; LEPD
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Leptin; Recombinant Human Leptin; Obese protein; Obesity factor; LEP recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 29-164aa; Partial
• Sequence: DDTKTLIKTIVTRINDISHTQSVSSKQKVTGLDFIPGLHPILTLSKMDQTLAVYQQILTSMPSRNVIQISNDLENLRDLLHVLAFSKSCHLPWASGLETLDSLGGVLEASGYSTEVVALSRLQGSLQDMLWQLDLS
• Sequence Length: 167

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for LEP recombinant protein

May function as part of a signaling pathway that acts to regulate the size of the body fat depot. An increase in the level of LEP may act directly or indirectly on the CNS to inhibit food intake and/or regulate energy expenditure as part of a homeostatic mechanism to maintain constancy of the adipose mass.

Product Categories/Family for LEP recombinant protein

Signal Transduction

References

Positional cloning of the mouse obese gene and its human homologue.Zhang Y., Proenca P., Maffei M., Barone M., Leopold L., Friedman J.M.Nature 372:425-432(1994) ErratumZhang Y., Proenca P., Maffei M., Barone M., Leopold L., Friedman J.M.Nature 374:479-479(1995) Human obese gene expression. Adipocyte-specific expression and regional differences in the adipose tissue.Masuzaki H., Ogawa Y., Isse N., Satoh N., Okazaki T., Shigemoto M., Mori K., Tamura N., Hosoda K., Yoshimasa Y., Jingami H., Kawada T., Nakao K.Diabetes 44:855-858(1995) Genomic structure and promoter analysis of the human obese gene.Gong D.W., Bi S., Pratley R.E., Weintraub B.D.J. Biol. Chem. 271:3971-3974(1996) Chehab F.F., Lim M.E.Structural organization and chromosomal assignment of the human obese gene.Isse N., Ogawa Y., Tamura N., Masuzaki H., Mori K., Okazaki T., Satoh N., Shigemoto M., Yoshimasa Y., Nishi S., Hosada K., Inazawa J., Nakao K.J. Biol. Chem. 270:27728-27733(1995) Human obese gene molecular screening in Japanese and Asian Indian NIDDM patients associated with obesity.Niki T., Mori H., Tamori Y., Kishimoto-Hashiramoto M., Ueno H., Araki S., Masugi J., Sawant N., Majithia H.R., Rais N., Hashiramoto M., Taniguchi H., Kasuga M.Diabetes 45:675-678(1996) Lu L., Fu Z., Xu M., Fu Y., Hu Z.SeattleSNPs variation discovery resource OB-BP1/Siglec-6. A leptin- and sialic acid-binding protein of the immunoglobulin superfamily.Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C., Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F., Varki A., Kastelein R.A.J. Biol. Chem. 274:22729-22738(1999) ErratumPatel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C., Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F., Varki A., Kastelein R.A.J. Biol. Chem. 274:28058-28058(1999) Leptin is a four-helix bundle secondary structure by NMR.Kline A.D., Becker G.W., Churgay L.M., Landen B.E., Martin D.K., Muth W.L., Rathnachalam R., Richardson J.M., Schoner B., Ulmer M., Hale J.E.FEBS Lett. 407:239-242(1997) Crystal structure of the obese protein leptin-E100.Zhang F., Basinski M.B., Beals J.M., Briggs S.L., Churgay L.M., Clawson D.K., Dimarchi R.D., Furman T.C., Hale J.E., Hsiung H.M., Schoner B.E., Smith D.P., Zhang X.Y., Wery J.P., Schevitz R.W.Nature 387:206-209(1997) A novel polymorphism in the leptin gene.Bartholomew D.W., McClellan J.M.Hum. Mutat. 12:220-220(1998) A leptin missense mutation associated with hypogonadism and morbid obesity.Strobel A., Issad T., Camoin L., Ozata M., Strosberg A.D.Nat. Genet. 18:213-215(1998)

NCBI and Uniprot Product Information

• NCBI GI #: 4557715
• NCBI GeneID: 3952
• NCBI Accession #: NP_000221.1
• NCBI GenBank Nucleotide #: NM_000230.2
• UniProt Accession #: P41159; O15158; Q56A88
• Molecular Weight: 19 kDa
• NCBI Official Full Name: leptin
• NCBI Official Synonym Full Names: leptin
• NCBI Official Symbol: LEP
• NCBI Official Synonym Symbols: OB; OBS; LEPD
• NCBI Protein Information: leptin
• UniProt Protein Name: Leptin
• Protein Family: Leptin
• UniProt Gene Name: LEP
• UniProt Entry Name: LEP_HUMAN

NCBI Description

This gene encodes a protein that is secreted by white adipocytes, and which plays a major role in the regulation of body weight. This protein, which acts through the leptin receptor, functions as part of a signaling pathway that can inhibit food intake and/or regulate energy expenditure to maintain constancy of the adipose mass. This protein also has several endocrine functions, and is involved in the regulation of immune and inflammatory responses, hematopoiesis, angiogenesis and wound healing. Mutations in this gene and/or its regulatory regions cause severe obesity, and morbid obesity with hypogonadism. This gene has also been linked to type 2 diabetes mellitus development. [provided by RefSeq, Jul 2008]

Uniprot Description

leptin: May function as part of a signaling pathway that acts to regulate the size of the body fat depot. An increase in the level of LEP may act directly or indirectly on the CNS to inhibit food intake and/or regulate energy expenditure as part of a homeostatic mechanism to maintain constancy of the adipose mass. Defects in LEP may be a cause of obesity (OBESITY). It is a condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat. Belongs to the leptin family.

Protein type: Hormone; Cell development/differentiation; Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 7q31.3

Cellular Component: cytoplasm; extracellular region; extracellular space

Molecular Function: growth factor activity; hormone activity; peptide hormone receptor binding

Biological Process: adult feeding behavior; bile acid metabolic process; central nervous system neuron development; cholesterol metabolic process; circadian rhythm; eating behavior; energy reserve metabolic process; fatty acid beta-oxidation; female pregnancy; glucose homeostasis; glucose metabolic process; glycerol biosynthetic process; hormone metabolic process; insulin secretion; intestinal absorption; leptin-mediated signaling pathway; leukocyte tethering or rolling; negative regulation of apoptosis; negative regulation of appetite; negative regulation of autophagy; negative regulation of glucose import; negative regulation of transcription from RNA polymerase II promoter; negative regulation of vasoconstriction; ovulation from ovarian follicle; placenta development; positive regulation of cytokine production; positive regulation of developmental growth; positive regulation of follicle-stimulating hormone secretion; positive regulation of insulin receptor signaling pathway; positive regulation of ion transport; positive regulation of JAK-STAT cascade; positive regulation of luteinizing hormone secretion; positive regulation of MAPKKK cascade; positive regulation of myeloid cell differentiation; positive regulation of phosphoinositide 3-kinase cascade; positive regulation of protein kinase B signaling cascade; positive regulation of T cell proliferation; positive regulation of TOR signaling pathway; positive regulation of tyrosine phosphorylation of Stat3 protein; prostaglandin secretion; regulation of angiogenesis; regulation of blood pressure; regulation of bone remodeling; regulation of cell cycle; regulation of cholesterol absorption; regulation of endothelial cell proliferation; regulation of gluconeogenesis; regulation of insulin secretion; regulation of natural killer cell activation; regulation of natural killer cell mediated cytotoxicity; regulation of natural killer cell proliferation; regulation of nitric-oxide synthase activity; regulation of steroid biosynthetic process; response to activity; response to dietary excess; response to estradiol stimulus; response to ethanol; response to hypoxia; response to insulin stimulus; response to vitamin E; sexual reproduction; T cell differentiation; tyrosine phosphorylation of STAT protein

Disease: Leptin Deficiency