Kassinin is a peptide derived from the skin of the African frog Kassina senegalensis. It belongs to tachykinin family of neuropeptides. It is secreted as a defense response, and is involved in neuropeptide signalling.
CAT No:10-101-66
CAS No:63968-82-1
Synonyms/Alias:CID45749; Kassinin; L-alpha-aspartyl-L-valyl-L-prolyl-L-lysyl-L-seryl-L-alpha-aspartyl-L-glutaminyl-L-phenylalanyl-L-valyl-glycyl-L-leucyl-L-methioninamide
Chemical Name:(3S)-3-amino-4-[[(2S)-1-[(2S)-2-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-amino-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-1-oxohexan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]amino]-4-oxobutanoic acid
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M.F/Formula | C59H95N15O18S |
M.W/Mr. | 1334.54 |
Sequence | One Letter Code: DVPKSDQFVGLM Three Letter Code: H-Asp-Val-Pro-Lys-Ser-Asp-Gln-Phe-Val-Gly-Leu-Met-NH2 |
Labeling Target | Neurokinin Receptor |
Application | Kassinin, belonging to the tachykinin family which excites neurons and provoke behaviorial responses, are potent vasodilators and secretagogues. |
Appearance | Solid powder |
Purity | >98% (or refer to the Certificate of Analysis) |
Biological Activity | Kassinin is a peptide derived from the Kassina frog. It belongs to tachykinin family of neuropeptides. It is secreted as a defense response, and is involved in neuropeptide signalling. |
Areas of Interest | Cardiovascular System & Diseases Pituitary & Hypothalamic Hormones |
Target | Neurokinin Receptor |
Source# | Synthetic |
Length | 12 |
Long-term Storage Conditions | Soluble in DMSO |
Shipping Condition | Shipped under ambient temperature as non-hazardous chemical. This product is stable enough for a few weeks during ordinary shipping and time spent in Customs. |
Short-term Storage Conditions | Dry, dark and at 0 - 4 °C |
Solubility | -20 °C |
InChI | InChI=1S/C59H95N15O18S/c1-30(2)24-38(53(86)66-35(49(63)82)20-23-93-7)65-44(77)28-64-58(91)47(31(3)4)72-55(88)39(25-33-14-9-8-10-15-33)69-52(85)37(18-19-43(62)76)67-54(87)40(27-46(80)81)70-56(89)41(29-75)71-51(84)36(16-11-12-21-60)68-57(90)42-17-13-22-74(42)59(92)48(32(5)6)73-50(83)34(61)26-45(78)79/h8-10,14-15,30-32,34-42,47-48,75H,11-13,16-29,60-61H2,1-7H3,(H2,62,76)(H2,63,82)(H,64,91)(H,65,77)(H,66,86)(H,67,87)(H,68,90)(H,69,85)(H,70,89)(H,71,84)(H,72,88)(H,73,83)(H,78,79)(H,80,81)/t34-,35-,36-,37-,38-,39-,40-,41-,42-,47-,48-/m0/s1 |
InChI Key | NXTPETCPVNEEOP-FJCMUPJRSA-N |
Canonical SMILES | CC(C)CC(C(=O)NC(CCSC)C(=O)N)NC(=O)CNC(=O)C(C(C)C)NC(=O)C(CC1=CC=CC=C1)NC(=O)C(CCC(=O)N)NC(=O)C(CC(=O)O)NC(=O)C(CO)NC(=O)C(CCCCN)NC(=O)C2CCCN2C(=O)C(C(C)C)NC(=O)C(CC(=O)O)N |
Isomeric SMILES | CC(C)C[C@@H](C(=O)N[C@@H](CCSC)C(=O)N)NC(=O)CNC(=O)[C@H](C(C)C)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@@H]2CCCN2C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(=O)O)N |
BoilingPoint | 1714.5±65.0 °C at 760 mmHg |
ShelfLife | >2 years if stored properly |
References | Tachykinins are among the most widely-studied families of regulatory peptides characterized by a highly-conserved C-terminal -Phe-X-Gly-Leu-Met.amide motif, which also constitutes the essential bioactive core. The amphibian skin has proved to be a rich source of these peptides with physalaemin from the skin of Physalaemus fuscomaculatus representing the archetypal aromatic tachykinin (X=Tyr or Phe) and kassinin from the skin of Kassina senegalensis representing the archetypal aliphatic tachykinin in which X=Val or Ile. Despite the primary structures of both mature peptides having been known for at least 30 years, neither the structures nor organizations of their biosynthetic precursors have been reported. Here we report the structure and organization of the biosynthetic precursor of kassinin deduced from cDNA cloned from a skin secretion library. In addition, a second precursor cDNA encoding the novel kassinin analog (Thr(2), Ile(9))-kassinin was identified as was the predicted mature peptide in skin secretion. Both transcripts exhibited a high degree of nucleotide sequence similarity and of open-reading frame translated amino acid sequences of putative precursor proteins. The translated preprotachykinins each consisted of 80 amino acid residues encoding single copies of either kassinin or its site-substituted analog. Synthetic replicates of each kassinin were found to be active on rat urinary bladder smooth muscle at nanomolar concentrations. The structural organization of both preprotachykinins differs from that previously reported for those of Odorrana grahami skin indicating a spectrum of diversity akin to that established for amphibian skin preprobradykinins. Wang, L., Zhou, M., Lynch, L., Chen, T., Walker, B., & Shaw, C. (2009). Kassina senegalensis skin tachykinins: Molecular cloning of kassinin and (Thr 2, Ile 9)-kassinin biosynthetic precursor cDNAs and comparative bioactivity of mature tachykinins on the smooth muscle of rat urinary bladder. Biochimie, 91(5), 613-619. |
Melting Point | N/A |
2. Implications of ligand-receptor binding kinetics on GLP-1R signalling
4. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
5. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
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