| Cat. No. |
Size |
Price |
Figures |
|---|
RP10422-1 mg
| 1 mg | $ 47.50 | HPLC: 20060721145615 (PDF)
MS: 20060721145555 (PDF)
MSDS: 20080630212940 (PDF)
STRUCTURE:
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References:
- Murphy FJ, et al. Disparate intracellular processing of human IL-12 preprotein subunits: atypical processing of the P35 signal peptide. J. Immunol. Jan 2000;164(2): 839-847.
- Gwang-Ho Jeohn, et al. Purification and characterization of a detergent-requiring membrane-bound metalloendopeptidase from porcine brain. Eur. J. Biochem. Mar 1999; 260(2): 318-324.
- Jeohn GH, et al. Isolation and characterization of gastric trypsin from the microsomal fraction of porcine gastric antral mucosa. J. Biol. Chem. Jun 1995; 270(24): 14748-14755.
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| Full Name | |
| Alias |
Bovine adrenal medulla dodecapeptide, BAM12P |
Sequence
(one-letter code) |
YGGFMRRVGRPE |
Sequence
(three-letter code) | {TYR}{GLY}{GLY}{PHE}{MET}{ARG}{ARG}{VAL}{GLY}{ARG}
{PRO}{GLU} |
|---|
| Description | Theoretical conformational analysis was used to study the spatial structure and conformational properties of the bovine adrenal medulla dodecapeptide BAM-12P (Tyr1-Gly2-Gly3-Phe4-Met5-Arg6-Arg7-Val8-Gly9-Arg10-Pro11-Glu12). Twenty-three low-energy conformations of the BAM-12P backbone were shown to represent the spatial structure of the peptide. The inverse structural problem was solved, and synthetic analogues of BAM-12P were proposed, the spatial structures of which correspond to a set of low-energy potentially physiologically active conformations of the natural dodecapeptide. |
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| Solubility | Soluble in water. The contents of this vial have been accurately determined. Both the stopper and the vial have been siliconized. Do not attempt to weight out a smaller portion of the contents. |
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| Formula | C62H97N21O16S1 |
|---|
| M.W. | 1424.63 |
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| Cas | 75513-71-2 |
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| Purity | > 95% |
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| Storage | Store at -20°C. Keep container tightly closed. |
| Notes | Potent opiate activity. |
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