| Identification | Back Directory | [Name]
H-SER-CYS-SER-LEU-PRO-GLN-THR-SER-GLY-LEU-GLN-LYS-PRO-GLU-SER-NH2 | [CAS]
258276-95-8 | [Synonyms]
SCSLPQTSGLQKPES
LEP (116-130) (mouse)
LEPTIN (116-130) MOUSE
Mouse leptin(116-130) amide
LEPTIN (116-130) AMIDE (MOUSE)
obese gene peptide 116-130 amide
LEPTIN FRAGMENT 116-130 AMIDE, MOUSE
OBESE GENE PEPTIDE (116-130) AMIDE (MOUSE)
Leptin fragment 116-130 amide mouse, >95%(HPLC)
SER-CYS-SER-LEU-PRO-GLN-THR-SER-GLY-LEU-GLN-LYS-PRO-GLU-SER
SER-CYS-SER-LEU-PRO-GLN-THR-SER-GLY-LEU-GLN-LYS-PRO-GLU-SER-NH2
H-Ser-Cys-Ser-Leu-Pro-Gln-Thr-Ser-Gly-Leu-Gln-Lys-Pro-Glu-Ser-OH
H-SER-CYS-SER-LEU-PRO-GLN-THR-SER-GLY-LEU-GLN-LYS-PRO-GLU-SER-NH2
Leptin (116-130) aMide (Mouse)
Obese Gene Peptide (116-130) aMide (Mouse)
SER-CYS-SER-LEU-PRO-GLN-THR-SER-GLY-LEU-GLN-LYS-PRO-GLU-SER: SCSLPQTSGLQKPES
SER-CYS-SER-LEU-PRO-GLN-THR-SER-GLY-LEU-GLN-LYS-PRO-GLU-SER-NH2: SCSLPQTSGLQKPES-NH2
L-Serinamide,L-seryl-L-cysteinyl-L-seryl-L-leucyl-L-prolyl-L-glutaminyl-L-threonyl-L-serylglycyl-L-leucyl-L-glutaminyl-L-lysyl-L-prolyl-L-a-glutamyl-
L-Serinamide, L-seryl-L-cysteinyl-L-seryl-L-leucyl-L-prolyl-L-glutaminyl-L-threonyl-L-serylglycyl-L-leucyl-L-glutaminyl-L-lysyl-L-prolyl-L-α-glutamyl-
L-Seryl-L-cysteinyl-L-seryl-L-leucyl-L-prolyl-L-glutaminyl-L-threonyl-L-serylglycyl-L-leucyl-L-glutaminyl-L-lysyl-L-prolyl-L-alpha-glutamyl-L-serinamide | [Molecular Formula]
C64H109N19O24S | [MDL Number]
MFCD01318804 | [MOL File]
258276-95-8.mol | [Molecular Weight]
1560.73 |
| Chemical Properties | Back Directory | [Boiling point ]
2035.4±65.0 °C(Predicted) | [density ]
1.372±0.06 g/cm3(Predicted) | [storage temp. ]
−20°C
| [solubility ]
insoluble in EtOH; ≥156 mg/mL in DMSO; ≥24.15 mg/mL in H2O | [form ]
white powder
| [pka]
4.44±0.10(Predicted) | [color ]
White to off-white | [Sequence]
H-Ser-Cys-Ser-Leu-Pro-Gln-Thr-Ser-Gly-Leu-Gln-Lys-Pro-Glu-Ser-OH |
| Hazard Information | Back Directory | [Uses]
LEP(116-130)(mouse) is a synthetic leptin peptide fragment. | [Biological Activity]
leptin (116-130), amide, mouse(c64h109n19o24s),a peptide with the sequence ser-cys-ser-leu-pro-gln-thr-ser-gly-leu-gln-lys-pro-glu-ser-nh2. leptin is an adipocyte-derived hormone that acts as a major regulator for food intake and energy homeostasis. leptin deficiency or resistance can result in profound obesity, diabetes, and infertility in humans. since the discovery of leptin, the breadth of biological actions has dramatically expanded and served to broaden the initial perspective, where this protein was viewed solely as an antiobesity hormone. important biological activities have been discovered in peripheral tissues that demonstrate the pleiotropic effects of this molecule in such areas as hematopoiesis, angiogenesis, blood pressure, bone mass, lymphoid organ homeostasis, and t lymphocyte function. recent data indicate that leptin(116-130), an active fragment of the native molecule, exerts effects similar to those of the native peptide on body weight and food intake.figure1 formula of leptin (116-130)figure2 signal transduction pathways of leptin | [in vivo]
LEP-(116-130) (1 mg, i.p.) results in a reduced rate of body weight gain in the presence of increased food intake compared with vehicle-injcted control mice. LEP-(116-130) significantly reduces blood glucose levels by appr 100 mg/dL. Administration of LEP-(116-130) to wild-type (+/+) C57BLKS/J-m mice for 4 or 7 days has no effect on their ability to thermoregulate[1]. | [References]
1. Zhang F, Basinski MB, Beals JM, Briggs SL, Churgay LM, Clawson DK, DiMarchi RD, Furman TC, Hale JE, Hsiung HM, Schoner BE, Smith DP, Zhang XY, Wery JP, Schevitz RW (May 1997). "Crystalstructure of the obese protein leptin-E100". Nature 387 (6629): 206–9.2. Brennan AM, Mantzoros CS (June 2006). "Drug Insight: the role of leptin in human physiology and pathophysiology--emerging clinical applications". Nat Clin Pract Endocrinol Metab 2 (6): 318–327. 3. GreGreen ED, Maffei M, Braden VV, Proenca R, DeSilva U, Zhang Y, Chua SC Jr, Leibel RL, Weissenbach J, Friedman JM (August 1995). "The human obese (OB) gene: RNA expression pattern and mapping on the physical, cytogenetic, and genetic maps of chromosome 7". Genome Res. 5 (1): 5–12.4. Margetic S, Gazzola C, Pegg GG, Hill RA (2002). "Leptin: a review of its peripheral actions and interactions". Int. J. Obes. Relat. Metab. Disord. 26 (11): 1407–1433. |
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