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Vial of Frag 176-191

Fragment 176-191

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$26.99$39.99

Concentration
2 mg per vial
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This product is prepared for LABORATORY RESEARCH USE ONLY and may not be used for other purposes.

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Properties

Molecular Formula C78H123N23O22S2
Molecular Weight 1799.1
Monoisotopic Mass 1797.86544499
Polar Area 784
Complexity 3670
XLogP -3.4
Heavy Atom Count 125
Hydrogen Bond Donor Count 26
Hydrogen Bond Acceptor Count 29
Rotatable Bond Count 63
Physical Appearance Fine White Lyophilized Powder
Stability Lyophilized protein is to be stored at -20°C. It is recommended to aliquot the reconstituted (dissolved) protein into several discrete vials in order to avoid repeated freezing and thawing. Reconstituted protein can be stored at 4°C
PubChem LCSS Fragment 176-191 Laboratory Chemical Safety Summary

Identifiers

CID 16131230
CAS 66004-57-7
InChI InChI=1S/C78H123N23O22S2/c1-9-42(8)62(101-69(114)49(23-17-29-88-78(85)86)92-70(115)51(30-39(2)3)95-64(109)46(80)31-43-18-12-10-13-19-43)74(119)100-61(41(6)7)76(121)122-58(106)27-25-50(66(111)90-34-59(107)123-75(120)52(32-44-20-14-11-15-21-44)91-57(105)33-89-67(112)54(37-124)97-65(110)47(81)35-102)94-73(118)60(40(4)5)99-71(116)53(36-103)96-68(113)48(22-16-28-87-77(83)84)93-72(117)55(38-125)98-63(108)45(79)24-26-56(82)104/h10-15, 18-21, 38-42, 45-55, 60-62, 102-103, 124H, 9, 16-17, 22-37, 79-81H2, 1-8H3, (H2, 82, 104)(H, 89, 112)(H, 90, 111)(H, 91, 105)(H, 92, 115)(H, 93, 117)(H, 94, 118)(H, 95, 109)(H, 96, 113)(H, 97, 110)(H, 98, 108)(H, 99, 116)(H, 100, 119)(H, 101, 114)(H4, 83, 84, 87)(H4, 85, 86, 88)/t42-, 45-, 46-, 47-, 48-, 49-, 50-, 51-, 52-, 53-, 54-, 55-, 60-, 61-, 62-/m0/s1
InChIKey LSTCHEVTSMJOCE-YWWHUHEESA-N
Isomeric SMILES CC[C@H](C)[C@@H](C(=O)N[C@@H](C(C)C)C(=O)OC(=O)CC[C@@H](C(=O)NCC(=O)OC(=O)[C@H](CC1=CC=CC=C1)NC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CO)N)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](C=S)NC(=O)[C@H](CCC(=O)N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC2=CC=CC=C2)N
Canonical SMILES CCC(C)C(C(=O)NC(C(C)C)C(=O)OC(=O)CCC(C(=O)NCC(=O)OC(=O)C(CC1=CC=CC=C1)NC(=O)CNC(=O)C(CS)NC(=O)C(CO)N)NC(=O)C(C(C)C)NC(=O)C(CO)NC(=O)C(CCCNC(=N)N)NC(=O)C(C=S)NC(=O)C(CCC(=O)N)N)NC(=O)C(CCCNC(=N)N)NC(=O)C(CC(C)C)NC(=O)C(CC2=CC=CC=C2)N
IUPAC Name [(2S)-2-[[(2S, 3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylpentanoyl]amino]-3-methylbutanoyl] (4S)-5-[[2-[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-amino-3-hydroxypropanoyl]amino]-3-sulfanylpropanoyl]amino]acetyl]amino]-3-phenylpropanoyl]oxy-2-oxoethyl]amino]-4-[[(2S)-2-[[(2S)-2-[[(2S)-5-carbamimidamido-2-[[(2R)-2-[[(2S)-2, 5-diamino-5-oxopentanoyl]amino]-3-sulfanylidenepropanoyl]amino]pentanoyl]amino]-3-hydroxypropanoyl]amino]-3-methylbutanoyl]amino]-5-oxopentanoate

2D Structure

Generated by Extreme Peptide with Open Babel, version 2.3.1, http://openbabel.org (accessed June 28, 2022)

Fragment 176-191 2D molecular structure vector generated with oBabel

Description

Fragment 176-191 is a 16 amino acid fragment of the much larger growth hormone (GH) peptide1. This particular GH fragment was isolated and biosynthesized in order to develop a lipolytic (fat cell destroying) and lipogenic (preventing the accumulation of body fat) agent2 without stimulating effects on growth and insulin resistance, which GH has been shown to do in animal test subjects3. Fragment 176-191 functions by emulating the way native GH manages fat metabolism Regular administration of Fragment 176-191 has been shown to reduce body fat levels in mice that were obese, mildly overweight, and of average body types4. While burning fat and preventing storage of additional fat stores, Fragment 176-191 showed no effect on the consumption habits of test animals5.

Product Comparison

Since Fragment 176-191 is a fragment of the larger GH peptide, its similarities in structure and in function are distinct. Fragment 176-191 was developed from the C-terminal end of GH, which was observed to be the end active in fat management. The remaining amino acids present in GH are those responsible for activity in growth, IGF production, and muscle mass development, which are functionalities also conserved in GH secretagogues like Hexarelin6 and Sermorelin7. Since Fragment 176-191 only retains the 16 amino acids present in the C-terminal end, it acts as a singular, very effect agent for the reduction of excess adipose tissue. Fragment 176-191 is very similar in character to AOD9604, or hGH Fragment 177-1918. They each have lipolytic and anti-lipogenic actions, but researchers have developed colloquial preferences in each direction. Some have reported a longer lasting fat-burning effect in AOD9604, while Fragment 176-191 demonstrates an excellent peak rate of lipolysis. Preference between the two agents must be determined by the research goal.

Synonyms:

hGH Fragment 176-191; HGH 176-191;

Peer-Reviewed Sources:

  1. Ng, F. M., Sun, J., Sharma, L., Libinaka, R., Jiang, W. J., & Gianello, R. (1999). Metabolic studies of a synthetic lipolytic domain of human growth hormone. Hormone research, 53(6), 274-278. ↩︎
  2. Heffernan, M., Summers, R. J., Thorburn, A., Ogru, E., Gianello, R., Jiang, W. J., & Ng, F. M. (2001). The Effects of Human GH and Its Lipolytic Fragment on Lipid Metabolism Following Chronic Treatment in Obese Mice andβ 3-AR Knock- Out Mice. Endocrinology, 142(12), 5182-5189. ↩︎
  3. Pöykkö, S. M., Kellokoski, E., Hörkkö, S., Kauma, H., Kesäniemi, Y. A., & Ukkola, O. (2003). Low plasma ghrelin is associated with insulin resistance, hypertension, and the prevalence of type 2 diabetes. Diabetes, 52(10), 2546- 2553. ↩︎
  4. Heffernan, M. A., Thorburn, A. W., Fam, B., Summers, R., Conway-Campbell, B., Waters, M. J., & Ng, F. M. (2001). Increase of fat oxidation and weight loss in obese mice caused by chronic treatment with human growth hormone or a modified C-terminal fragment. International journal of obesity and related metabolic disorders: journal of the International Association for the Study of Obesity, 25(10), 1442-1449. ↩︎
  5. Atkinson, T. J. (2008). Central and peripheral neuroendocrine peptides and signalling in appetite regulation: considerations for obesity pharmacotherapy. Obesity reviews, 9(2), 108-120. ↩︎
  6. Deghenghi, R., Cananzi, M. M., Torsello, A., Battisti, C., Muller, E. E., & Locatelli, V. (1994). GH-releasing activity of hexarelin, a new growth hormone releasing peptide, in infant and adult rats. Life sciences, 54(18), 1321-1328. ↩︎
  7. Prakash, Amitabh, and Karen L. Goa. “Sermorelin.” BioDrugs 12.2 (1999): 139-157. ↩︎
  8. Wu, Z. & Ng, FM. (1993) Antilipogenic action of synthetic C-terminal sequence 177-191 of human growth hormone. Biochemistry and molecular biology international journal. 5(2), 1281-1327. ↩︎

All literature, information, and data, provided on this website are for informational and educational purposes only.

Accurate research is our priority.

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