PIPES
Chemical structure of PIPES
Names
Preferred IUPAC name
2,2′-(Piperazine-1,4-diyl)di(ethane-1-sulfonic acid)
Other names
PIPES
Identifiers
3D model (JSmol)
ChemSpider
ECHA InfoCard 100.024.598
UNII
  • InChI=1S/C8H18N2O6S2/c11-17(12,13)7-5-9-1-2-10(4-3-9)6-8-18(14,15)16/h1-8H2,(H,11,12,13)(H,14,15,16) ☒N
    Key: IHPYMWDTONKSCO-UHFFFAOYSA-N ☒N
  • InChI=1/C8H18N2O6S2/c11-17(12,13)7-5-9-1-2-10(4-3-9)6-8-18(14,15)16/h1-8H2,(H,11,12,13)(H,14,15,16)
    Key: IHPYMWDTONKSCO-UHFFFAOYAG
  • C1CN(CCN1CCS(=O)(=O)O)CCS(=O)(=O)O
Properties
C8H18N2O6S2
Molar mass 302.37
Appearance White powder
Melting point Decomposes above 300 °C
Boiling point Decomposes
1 g/L (100 °C)
Hazards
Occupational safety and health (OHS/OSH):
Main hazards
 Irritant
NFPA 704 (fire diamond)
NFPA 704 four-colored diamond
1
0
0
Safety data sheet (SDS) External MSDS
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

PIPES (piperazine-N,N′-bis(2-ethanesulfonic acid)) is a frequently used buffering agent in biochemistry. It is an ethanesulfonic acid buffer developed by Good et al. in the 1960s.[1]

Applications

PIPES has two pKa values. One pKa (6.76 at 25 °C) is near the physiological pH which makes it useful in cell culture work. Its effective buffering range is 6.1-7.5 at 25 °C. The second pKa value is at 2.67 with a buffer range of from 1.5-3.5. PIPES has been documented minimizing lipid loss when buffering glutaraldehyde histology in plant and animal tissues.[2][3] Fungal zoospore fixation for fluorescence microscopy and electron microscopy were optimized with a combination of glutaraldehyde and formaldehyde in PIPES buffer.[4] It has a negligible capacity to bind divalent ions.[5]

See also

References

  1. ↑ Good, Norman E.; Winget, G. Douglas; Winter, Wilhelmina; Connolly, Thomas N.; Izawa, Seikichi; Singh, Raizada M. M. (1966). "Hydrogen Ion Buffers for Biological Research". Biochemistry. 5 (2): 467–77. doi:10.1021/bi00866a011. PMID 5942950.
  2. ↑ Salema, R. and Brando, I., J. Submicr. Cytol., 9, 79 (1973).
  3. ↑ Schiff, R.I. and Gennaro, J.F., Scaning Electron Microsc., 3, 449 (1979).
  4. ↑ Hardham, A.R. (1985). "Studies on the cell surface of zoospores and cysts of the fungus Phytophthora cinnamomi: The influence of fixation on patterns of lectin binding". Journal of Histochemistry. 33 (2): 110–8. doi:10.1177/33.2.3918095. PMID 3918095.
  5. ↑ "Hopax Fine Chemicals - Biological buffers and their interactions with metal ions".


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