Q: Tween 20 vs. Triton X-100
daniela Rödl
via methods%40net.bio.net
(by daniela.roedl from lrz.tu-muenchen.de)
Wed Sep 12 00:15:52 EST 2007
Hi,
I found a bulletin in which some features of Tween20 and TritonX-100
were described. Maybe it helps you.
I by myself use TritonX-100 for permeabilization of cells before
intracellular staining with antibodies and for homogenization of cells
before an activity assay.
good wishes
dany rödl
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3D"960067_Bulletin_eps.gif
CAPTION: Detergentin Polystyrene in ELISA
Detergent is used = in ELISA for washing off loosely or
unspecifically bound reactants. It may = also be used for blocking
possible excess solid surface (e.g. polystyrene) = after coating
with one reactant to avoid unspecific immobilization of subsequent reactants.
Often a detergent is used according to = tradition and routine
procedures, or it is arbitrarily adopted from one = application to
another.
However, detergent may be a = double-edged sword and should be
selected with care depending on the particular assay = reactants and
immobilizing surface material.
In = this work five different detergents have been examined in a
two-layer = antibody sequence using polystyrene Nunc-Immuno™
MicroWells™ = MaxiSorp™ and PolySorp™.
3D"8-1.gif
- I've got such a poor crop this time...
- You would = always get a high yield on Nunclon Delta!
CAPTION:
Introduction
Detergents are molecules consisting = of a distinct hydrophobic and
hydrophilic part (Table = 1).
Their washing effect is based on the ability to disperse
hydrophobic = molecules in aqueous medium, i.e. to dissolve
unstable hydrophobic bonds = between surface and coating reactant,
and unspecific hydrophobic bonds = mutually between reactants on
the surface.
Their blocking = effect is based on the ability to compete with
other molecules for both = hydrophobic and hydrophilic binding
sites.
However, an immobilized = detergent may in itself affect further
specific and unspecific = immobilization characteristics of the
solid phase, e.g. by applying hydrophilic = groups to a hydrophobic
surface, or by interfering with the active sites of = reactant
molecules.
The reversibility of possible detergent = mediated solid phase
alterations depends on the detergent binding strength, = implying
detergent size, charge and structure in relation to the = other
assay ingredients. Therefore, the use of detergent should be optimized for each separate = application.
CAPTION:
3D"2.gif
Table 1
Schematic = illustration of the five detergents used in the
experiments. Tween 20 = = ikosaoxyethylene sorbitan monolaurate
(Merck 822184); Triton X-100 = octylphenoxy = octaethoxy ethanol
(Merck 8603); SDS = sodium dodecyl sulfate = (Serva 20760); DTAB
= dodecyltrimethylammonium bromide (Sigma D-8638); = CHAPS =
3-[(cholamidopropyl) dimethylammonio]-1-propanesulfonate (Sigma C-3023). According to other sources, the hydrophilic
polyoxyethylene part = of Tweens is divided into three separate
arms linked to the sorbitan part, = and the hydrophobic octyl part
og Triton X-100 is branched.
CAPTION:
Step Reagent Time
% = Detegent added
1st layer
1st wash
2nd = layer
2nd wash Sar, 5µg/ml PBS
or
None
PBS + 0.2 M extra NaCl
R:HRP, 1.3 = µg/ml in PBS
or
S:HRP, 1.3 µg/ml in PBS
PBS + 0.2 M extra NaCl overnight
3x
2 hr
3x (0)
0
0
0 (0)
.05
0
0 (0)
.05
.05
0 (0)
.05
0
.05 (0)
.05
.05
.05
Detergent code used in Figs. 1-3
– – – + = – – + = + – + = – + + = + +
Table 2
Procedure with MaxiSorp or PolySorp MicroWells using = each of the
five detergents in the five code alternatives (bottom row), = all in
one experiment. The procedure was followed by HRP reaction using
H[2]O[2]/OPD substrate. SaR = swine = anti-rabbit antibody (Dako
Z 196) = catching antibody; R:HRP = peroxidase = conjugated
rabbit antibody (Dako P 128) = target conjugate;S:HRP =
peroxidase = conjugated swine antibody (Dako P 217) =
indifferent conjugate.
CAPTION:
Method and Results
To elucidate some of the detergent = conditions mentioned above,
five detergents of various sizes and charges = (schematized in
Table 1) were tested in a catching antibody assay according to the procedure listed in Table 2. Nunc-Immuno Modules F8 with physically adsorbing surfaces, i.e. partly hydrophilic MaxiSorp
(Cat. No. = 468667) and hydrophobic PolySorp (Cat. No. 469078) were
= used.
The results are presented in Fig.1.
Discussion
From = the results with the present test system several detergent
effects relevant to = ELISA can be observed (cf. Fig. 1):
1. In = general, the detergents exert a blocking effect against
unspecific adsorption = only if they are present together with the
conjugates (+ + – = and + + +); only in these cases there are no
significant unspecific signals.
2. Tween 20 = makes an exception to statement 1. Its presence in
the 1st wash seems to be = sufficient for blocking unspecific
adsorption in subsequent layers = on both surfaces. This may be a
consequence of its relatively large size, = which presumably
implies that it remains firmly bound to the surface, = unlike the
other detergents. However, its larger size is due merely to a larger hydrophilic part, wherefore it is difficult to explain its
stable = blocking effect on the hydrophobic PolySorp surface.
3. The = positively charged DTAB implies large unspecific signals
in all cases. Probably it = binds to the conjugates, thereby
facilitating their unspecific adsorption.
4. Tween 20 = and DTAB seem to enhance the signals when used in the
2nd wash = (+ – + and + + +). This may be due to the presence of
detergent = remnants in the substrate solutions in those cases. In
a control experiment = with or without detergent added to the
substrate solution after direct = coating of the surfaces with HRP
conjugate it was indeed observed, especially = with MaxiSorp, that
Tween 20 and DTAB enhanced the substrate reaction; = SDS and CHAPS
somewhat reduced the reaction, whereas Triton X-100 was indifferent. There is no immediate explanation to these
interferences with the substrate reaction.
5. Tween 20, = Triton X-100, and in particular SDS imply small
specific PolySorp signals = (compared with CHAPS), whereas only SDS
implies relatively small = signals with MaxiSorp. This may be
explained by differences in washing = effects between the
detergents, SDS being the most harsh, combined with = the fact that
PolySorp binds less native antibody in a stable way than does MaxiSorp [1]. However, a consequence of this would be: the lower the specific signal, the higher the signal if the surface has only
= been cleared for loosely bound antibody by 1st wash detergent
(+ – –). This does not seem to be the case in = general, so an
additional inhibitory interference with the antibody specificities, especially by SDS, may be postulated in accordance
with findings = by others [2].
6. Without = detergent (– – –) there seems to be no
difference between = the signals with specific and unspecific
conjugate, nor between MaxiSorp and = PolySorp. In a control
experiment using 125I-labelled 1st layer antibody it was found that
equal amounts of antibody remained on = MaxiSorp and PolySorp when
no detergent was subsequently used. This can = explain the equality
of specific signals on MaxiSorp and PolySorp by absence = of
detergent, but not the equally large unspecific signals. The = latter
may be explained by occurrence of a second-positioned, unspecific adsorption of conjugate in competition with specific binding.
A figurative explanation of the = general detergent conditions is
attempted in Fig. 2, which has given rise = to the stoichiometric
modelling in Fig. = 3.
CAPTION:
CAPTION: MaxiSorp
Tween 20
3D"8-4a1.gif
Triton X-100
3D"8-4a2.gif
SDS
3D"8-4a2.gif
DTAB
3D"8-4a2.gif
CHAPS
3D"8-4a2.gif
CAPTION: PolySorp
Tween 20
3D"8-4a1.gif
Triton X-100
3D"8-4a2.gif
SDS
3D"8-4a2.gif
DTAB
3D"8-4a2.gif
CHAPS
3D"8-4a2.gif
Fig. 1
Mean = results with MaxiSorp (upper diagram block) and PolySorp
(lower diagram block) = from three independent experiments, each
one with mutually comparable = signals obtained according to the
procedure in Table 1. Left diagrams (in = MaxiSorp and PolySorp
block respectively) show results for target = conjugate; right
diagrams show results for indifferent conjugate; 3D"5-firk.gif =
with 1st layer; € = without 1st layer.
CAPTION:
3D"8-2x.gif
Fig. = 2
Schematized explanatory approach to the results in Fig. 1 for
MaxiSorp (above) = and PolySorp (below) with special reference to
the Triton X-100 = results. Left and right diagrams illustrate the
situations with target and = indifferent conjugates, respectively;
Y-shapes represent antibodies; Y-E represents enzyme conjugated
antibody = whose non-involved specific sites are indicated by the
small = »closing« lines above the arms.The overall idea is that
unless detergent is = subsequently used (= =) some
coatingantibody will be loosely bound (++) in = a secondary
position between the firmly bound antibody, resulting in mutual sterical hindrance ( # ) of antibody specificities.
Consequently,for = spatial reasons, the implied secondary,
unspecific binding sites are = assumed to compete with the specific
sites for target conjugate binding by = absence of detergent. For
simplicity, only the right arm antibody = specificities are
considered.
CAPTION: Detail from Fig. 1
Triton X-100
3D"8-61a.gif
A B
Triton X-100
3D"8-61b.gif
C D
CAPTION:
A B
3D"8-62a.gif
C D
3D"8-62b.gif
<= /TABLE>
Fig. = 3
Stoichiometric model, based on counts of immobilized enzymein Fig.
2, of the = results for coated surfaces, i.e. with 1st layer,
resembling most closely the = results with Triton X-100 (filled
columns in above detail) A & B: = MaxiSorp; C & D: PolySorp; A & C:
with target conjugate; B & D: = with indifferent conjugate; BLACK
= specific part of signals; GRAY = unspecific part of
signals.
CAPTION:
Conclusion
From this investigation some = general guidelines concerning the
use of detergent in ELISA can be = extracted:
1. Detergent = is necessary for washing off loosely adsorbed
reactant to abolish sterical = hindrances caused by reactant
crowding on the surface.
2. If no = other blocking agent is used, detergent must be present
during incubation with post-coating reactants to avoid unspecific
adsorption. Tween 20 is = an exception, as it performs a stable
blocking once applied, like = typical blocking agents such as BSA
or casein.
3. Detergents = with net charges like SDS and DTAB must be avoided
because of their = disadvantageous interferences with the assay
reactants.
4. Among the = investigated detergents, Triton X-100 or Tween 20
seem to be optimal for = application with the MaxiSorp surface,
whereas the apparently more gentle = CHAPS may be the best choice
with PolySorp.
This investigation does not give a = complete picture of the
detergent conditions with ELISA. Important aspects, = such as
detergent effect dependence on concentration and pH, or detergent
performance in concert with typical blocking agents, must wait to be addressed at a later time.
Peter = Esser
Nunc Laboratories
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CAPTION:
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Akiyama Y., Fukui K. & Kawata T. = (1989).
A comparison of competitive enzyme immunoassay and precipitin inhibition tests in the analysis of polysaccharide antigenic
determinants of = oral streptococci.
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Quantitation of a cationic antimicrobial granule = protein of human
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A rapid assay for circulating = anti-glomerular basement membrane
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Takata Y., Moriyama T., Fukumori = Y., Yoden A., Shima M. & Inai S.
(1989).
A biotin-avidin sandwich ELISA = for quantification of intact
complement component C9.
J. Immunol. = Methods 117, 107-113.
Nunc-Immuno Plate F96
Takeyama M., Kino T., Guo L.L., = Otaka A., Fujii N. & Yajima H.
(1989).
Immuno-affinity purification of = specific antibodies against human
gastrin releasing peptide (h-GRP) by the = h-GRP (1-8)-linked
polydimethylacrylamide resin.
Int. J. Protein Res. = 33, 457-462.
Nunc-Immuno Plate
Takeyma M., Kondo K., Hayashi Y. = & Yajima H.(1989).
Enzyme immunoassay of gastrin releasing peptide = (GRP)-like
immunoreactivity in milk.
Int. J. Protein Res. 34, 70-74.
Nunc-Immuno Module MaxiSorp = F8
Tranicard F., Chevrier D., Mazia = J.C. & Guesdon J.L. (1989).
Monoclonal anti-nucleoside antibodies.Characterization and
application in an enzyme = immunoassay of single-stranded DNA.
J. Immunol. Methods 123, 83-91.
Nunc-Immuno Plate F96
Tuson J.R.D., Jacob D.A., Pascoe = E.W. & Saxby S.J.Y. (1989).
Immunodetection of human tumor-associated cell-bound antigens by
human monoclonal antibodies.
J. Immunol. = Methods 121, 47-52.
Nunc-Immuno Plate F96
Usagawa T., Nishimura M., Uda T. = & Nakahara Y. (1989).
Preparation of monoclonal antibodies against methamphetamine.
J. Immunol. Methods 119, 111-115.
Nunc-Immuno Plate U96
Von GrEingen R. & Schneider = C.H. (1989).
Epitope analyses: biotinylated short peptides as = inhibitors of
anti-peptide antibody.
J. Immunol. Methods 125, 143-146.
Nunc-Immuno Plate MaxiSorp
Walsh B.J. & Howden M.E.H. = (1989).
A method for the detection of IgE binding sequences of allergens based on a modification of epitope mapping.
J. Immunol. Methods 121, 275-280.
Nunc-Immuno Plate
Yamada K., Akiyoshi K., Murakami = H., Sugahara T., Ikeda I.,
Toyoda K. & Omura H. (1989).
Partial = purification and characterization of immunoglobulin
production stimulating factor = derived from namalwa cells.
In Vitro 3, 243-247.
Nunc-Immuno = Plate
Zilow G., Naser W., Rutz R. & = Bruger R. (1989).
Quantitation of the anaphylatoxin C3a in the presence = of C3 by a
novel sandwich ELISA using monoclonal antibody to a C3a neoepitope.
J. Immunol. Methods 121, = 261-268.
Nunc-Immuno Plate F96
Zwirner J., Felber E., Reiter C., = RiethmEler G. & Feucht H.E.
(1989).
Deposition of complement = activation products on plastic-adsorbed
immunoglobulins.
J. Immunol. = Methods 124, 121-129.
Nunc-Immuno Plate F96
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