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

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

-------------- next part --------------


   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
     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™.

   - I've got such a poor crop this time...
   - You would = always get a  high yield on Nunclon Delta!



   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
     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 
     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.


   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.


   Step Reagent Time

   % = Detegent  added

   1st  layer

   1st wash

   2nd = layer

   2nd  wash Sar, 5µg/ml  PBS
   PBS + 0.2 M extra NaCl
   R:HRP, 1.3 = µg/ml in  PBS
   S:HRP, 1.3 µg/ml in PBS
   PBS + 0.2 M extra  NaCl overnight


   2  hr

   3x (0)



   0 (0)



   0 (0)



   0 (0)



   .05 (0)



   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.


   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.

   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: MaxiSorp

   Tween 20
   Triton X-100

   CAPTION: PolySorp

   Tween 20
   Triton X-100

   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.



   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 

   CAPTION: Detail from Fig.  1

   Triton X-100
   A B
   Triton X-100
   C D


   A B
   C D
   <= /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 



   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

   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

   1.  Esser P. (1988).
   Principles in adsorption to = polystyrene.
   Nunc  Bulletin No. 6, second edition 1997, 1-5.

   2. Crumpton M.J. & Parkhouse = R.M.E.  (1972).
   Comparison of the effects of various detergents on  antigen-antibody
   FEBS Letters 22,  210-212.


   Reference 1989 to Nunc = Products

   Cell and Tissue Culture

   Alston-Mills B., Li Q.C. & = Ottinger M.A.  (1989).
   Production of monoclonal antibodies against avian = LHRL-1.
   In  Vitro 10, 934-938.
   Nunclon D Dish 6 cm
   Nunclon = D = Multidish  24

   Andersson U., Adolf G., Dohlsten = M., Möller G.  & Sjögren H.O.
   Characterization of individual = tumor  necrosis factor a- and
   b-producing cells after polyclonal T cell = activation.
   J. Immunol.  Methods 123, 233-240.
   Nunclon D = Flask

   Barkley D., Feldmann M. & Maini = R.N.  (1989).
   The detection by immunofluorescence of distinct cell  populations
   producing interleukin-1a and = interleukin-1b in = activated human 
   peripheral blood.
   J. Immunol. Methods 120, = 277-283.
   Nunclon  D Multidish  24

   Bertrand L. & Chafouleas J.G.  (1989).
   High yield production of synchronized cells for cell = cycle 
   American Biotechnology Laboratory.
   Nunc = Cell  Factory

   Däumler R. & Simmermann U. = (1989).
   High  yields of stable transformants by hypo-osmolar plasmid 
   J. Immunol. Methods 122, = 203-210.
   Nunc  Petri Dish

   De Boer M., Ossendrop F.A., Van = Duijn G.,  Voorde G.H.J.T. & Tager
   J.M. (1989).
   Optimal conditions for = the  generation of monoclonal antibodies
   using primary immunisation of = mouse  splenocytes in vitro under
   serum-free conditions.
   J. = Immunol.  Methods 121, 253-260.
   Nunclon D Multidish = 6

   Fager G., Hansson G.K., Gown A.M., = Larson D.M.,  Skalli O. &
   Bondjers G. (1989).
   Human arterial smooth = muscle cells  in culture: Inverse
   relationship between proliferation and = expression of  contractile
   In Vitro 6, 511-520.
   Nunclon  D Dish 9  cm
   Nunclon D Flask 260 ml

   Faulmann E.L., Otten R.A., Barrett = D.J. &  Boyle M.D.P. (1989).
   Immunological applications of type III Fc = binding 
   proteins.Comparison of different sources of protein G.
   J. = Immunol.  Methods 123, 269-281.
   Nunclon D MicroWell  Plate

   Hakalahti L. & Vihko P.  (1989).
   Purification of monoclonal antibodies raised against 
   prostatespecific acid phosphatase for use in vivo in = radioimaging 
   of prostatic cancer.
   J. Immunol. Methods 117,  131-136.
   Nunclon D Flask
   Nunc Cell = Factory

   Hansen M.B., Nielsen S.E. & = Berg K.  (1989).
   Re-examination and further development of a precise and = rapid  dye
   method for measuring cell growth/cell kill.
   J. Immunol. = Methods  119, 203-210.
   Nunclon D = Flask

   Hewish D.R. & Werkmeister J.A.  (1989).
   The use of an electroporation apparatus for the = production of 
   murine hybridomas.
   J. Immunol. Methods 120, = 285-289.
   Nunclon  D MicroWell  Plate

   Hutchings P.R., Cambridge G., Tite = J.P., Meager  T. & Cooke A.
   The detection and enumeration of  cytokine-secreting cells in mice
   and man and the clinical = application of  these assays.
   J. Immunol. Methods 120, 1-8.
   Nunclon  D MicroWell  Plate
   Nunclon D Multidish 24

   Nowak J. & Klose J. = (1989).
   Radioactive  labelling of proteins in culturedpostimplantation mouse
   embryos = II. Dose  and time dependency.
   In Vitro 7, 634-642.
   Nunclon  D Dish 4  cm

   Park E.-H., Lee J.-S., Yi A.-K. = & Etoh H.  (1989).
   Fish cell line (ULF-23HU) derived from the fin of the = central 
   mudminnow (Umbra limi): Suitable characteristics for  clastogenicity
   In Vitro 11, 987-994.
   Nunclon  D Multidish  6

   Parkar B.A. & Reeves W.G. = (1989).
   In  vitro priming of human lymphocytes to heterologous = insulins.
   J.  Immunol. Methods 120, 159-165.
   Nunclon D = Dish

   Pedersen P.S. (1989).
   Human = sweat duct cells  in primary culture.Basic bioelectric
   properties of cultures = derived from  normal and patients with
   cystic fibrosis.
   In Vitro 4,  342-352.
   Nunclon D Multidish 6

   Petersen O.W. & van Deurs B.  (1989).
   Distinction between vascular smooth muscle cells and  myoepithelial
   cells in primary monolayer cultures of human breast  tissue.
   In Vitro 3, 259-266.
   Nunclon D  Flask

   Ricciardelli C., Horsfall D.J., = Skinner J.M.,  Henderson D.W.,
   Marshall V.R. & Tilley W.D. = (1989).
   Development and  characterization of primary cultures of smooth
   muscle cells from = the  fibromuscular stroma of the guinea pig
   In Vitro 11,  1016-1024.
   Nunclon D = Flask

   Riss T.L., Stewart B.H. & = Sirbasku D.A.  (1989).
   Rat pituitary tumor cells in serum-free culture. I. = Selection  of
   thyroid hormone-responsive and autonomous cells.
   In Vitro 2, = 127-135.
   Nunclon D Multidish 6

   Riss T.L. & Sirbasku D.A. = (1989).
   Rat  pituitary tumor cells in serum-free culture II.Serum factor and
   = thyroid  hormone requirements for estrogen-responsive growth.
   In Vitro = 2,  136-142.
   Nunclon D Multidish 6

   Sakakura Y., Fujiwara N. & Nawa = T.  (1989).
   A simple, disposable, and improved organ culture system = for 
   maintaining three-dimensional development of mouse embryonic = molars.
   In  Vitro 10, 959-964.
   Nunclon D Multidish = 24

   Schauer U., Krolikowski U. & = Rieger C.H.L.  (1989).
   Detection of activated lymphocyte subsets = byfluorescence and  MTT
   J. Immunol. Methods 116, = 221-227.
   Nunclon  D Dish 6  cm

   Sechler, J.M.G., Warren M.K. & = Gallin J.I.  (1989).
   Human non-transformed monocyte-derived macrophage cell  lines.
   J. Immunol. Methods 119, 277-285.
   Nunc Tube  (polypropylene)

   Sedgwick J.D., MacPhee I.A.M. & = Puklavec  M.(1989).
   Isolation of encephalitogenic CD4+4T cell clones in = the  rat.
   J. Immunol. Methods 121, 185-196.
   Nunclon = D Flask = 260  ml

   Suzuki T., Ohta M. & Hoshi H.  (1989).
   Serum-free, chemically defined medium to evaluate the = direct 
   effects of growth factors and inhibitors on proliferation and    function of  neonatal rat cardiac muscle cells in culture.
   In Vitro 7,  601-606.
   Nunclon D Multidish 24

   Theobald M., Hoffmann T. & Heit = W.  (1989).
   Assessment of human allospecific IL-2 secreting helper = T 
   lymphocytes in limiting dilution cultures using restimulation and    split  well analysis.
   J. Immunol. Methods 121, = 19-32.
   Nunclon  D MicroWell  Plate V96, F96

   Uchiyama H. & Akatsuka J.  (1989).
   ELISA-plaque assay for the detection of platelet  antibody-secreting
   cells.I. Studies on optimization of reagent  concentrations and
   culture conditions for enumeration of = spot-forming  cells.
   J. Immunol. Methods 117, 199-203.
   Nunclon  D Multidish  24

   Anicetti = V.R.,  Simonetti M.A., Blackwood L.L., Jones A.J.S. &
   Chen A.B.  (1989).
   Immunization procedures for E. coli  proteins.
   Applied Biochemistry and Biotechnology  22,151-168.
   Nunc-Immuno Plate F96

   Bator J.M. & Reading C.L.  (1989).
   Measurement of antibody affinity for cell surface = antigens  using
   an enzyme-linked immunosorbent assay.
   J. Immunol. Methods = 125,  167-176.
   Nunc-Immuno Plate F96

   Bloemena E., Roos M.T.L., Van = Heijst J.L.A.M.,  Vossen J.M.J.J. &
   Schellekens P.T.A. (1989).
   Whole-blood = lymphocyte  cultures.
   J. Immunol. Methods 122, = 161-167.
   Nunc-Immuno  Plate F96

   Bloom J.W., Wong M.F. & Mitra = G.  (1989).
   Detection and reduction of Protein A contamination in  immobilized
   Protein A purified monoclonal antibody = preparations.
   J.  Immunol. Methods 117, 83-89.
   Nunc-Immuno Plate  F96

   Bobrow M.N., Harris T.D., = Shaughnessy K.J.  & Litt G.J. (1989).
   Catalyzed reporter deposition, a novel = method  of signal
   amplification. Application to immunoassays.
   J. = Immunol.  Methods 125, 279-285.
   Nunc-Immuno = Module

   Buchs J.P. & Nydegger U.E.  (1989).
   Development of an ABO-ELISA for the quantitation of = human blood 
   group anti-A and anti-B IgM and IgG antibodies.
   J. Immunol. = Methods  118, 37-46.
   Nunc-Immuno Plate F96

   Cromie R.L., Standford J.L., Brown = M.J. &  Price D.J. (1989).
   The transport and culture conditions for = optimum  transformation
   responses of wildfowl lymphocytes to mycobacterial  antigens.
   J. Immunol. Methods 122, = 195-201.
   Nunc-Immuno  Plate F96

   Ellis H.J., Freedman A.R. & = Ciclitira P.J.  (1989).
   The production and characterisation of monoclonal = antibodies to 
   wheat gliadin peptides.
   J. Immunol. Methods 120, = 17-22.
   Nunc  MicroWell Plate

   Flynn J.N., Harkiss G.D. & = Hopkins J.  (1989).
   Generation of sheep × mouse heterohybridoma cell line    (1C6.3a6T.1D7) and evaluation of its use in the production of    ovine  monoclonal antibodies.
   J. Immunol. Methods 121,  237-246.
   Nunc-Immuno Plate F96

   Fujii K., Tsuji M., Murota K., = Terato K.,  Shimozuru Y. & Nagai Y.
   An improved enzyme-linked  immunosorbent assay of anti-collagen
   antibodies in human = serum.
   J.  Immunol. Methods 124, 67-70.
   Nunc-Immuno Plate  F96

   FElistaller P. = (1989).
   Comparison  of immunoglobulin binding capacities and ligand leakage
   using = eight  different protein A affinity chromography matrices.
   J. Immunol. = Methods  124, 171-177.
   Nunc-Immuno Plate F96

   Garred P., Mollnes T.E., Lea T. = & Lachmann  P.J. (1989).
   Enzyme immunoassay detection of circulating immune = complexes by
   monoclonal antibodies to C3 neoepitopes with special  reference to
   IgG concentration and to interfering = anti-immunoglobulin 
   J. Immunol. Methods 117, = 59-66.
   Nunc-Immuno  Plate MaxiSorp F96

   Hobbs R.N. (1989).
   Solid-phase = immunoassay  of serum antibodies to peptides. Covalent
   antigen binding to = adsorbed  phenylalanine-lysine copolymers.
   J. Immunol. Methods 117,  199-203.
   Nunc-Immuno Plate F96

   Hong T.-H., Chen S.-T., Tang T.-K., = Wang S.-C.  & Chang T.H.
   The production of polyclonal and = monoclonal  antibodies in mice
   using novel immunization methods.
   J. = Immunol.  Methods 120, 151-157.
   Nunc-Immuno Plate = F96

   Ishibashi K., Hanada S., Uozumi K., = Otsuka M.,  Sakurami T. &
   Hashimoto S. (1989).
   An enzyme-linked = immunosorbent  assay for immune complex of
   J. Immunol. Methods 119,  217-221.
   Nunc-Immuno Plate F96

   Jagannath C. & Sehgal S.  (1989).
   Enhancement of the antigen-binding capacity of = incomplete IgG 
   antibodies to Brucella melitensis through Fc region = interactions 
   with staphylococcal protein A.
   J. Immunol. Methods 124,  251-257.
   Nunc-Immuno Plate F96

   Jepras R.I., Clarke D.J. & = Coakley W.T.  (1989).
   Agglutination of Legionella pneumophila by = antiserum  is
   accelerated in an ultrasonic standing wave.
   J. Immunol. = Methods 120,  201-205.
   Nunc-Immuno Plate F96

   Kemeny D.M., Richards D., Durnin S. = &  Johannson A. (1989).
   Ultrasensitive enzyme-linked immunosorbent = assay  (ELISA) for the
   detection of picogram quantities of IgE.
   J. = Immunol.  Methods 120, 251-258.
   Nunc-Immuno Plate  MaxiSorp

   Kim W.B., Jo Y.W., Choi E.C. & = Kim B.K.  (1989).
   Inhibition ELISA for hepatitis B surface antigen = (HBsAg) using 
   monoclonal idiotype-anti-idiotype interaction.
   J. Immunol. = Methods 125,  273-278.
   Nunc-Immuno Plate F96

   Kitamura K., Matsuda K., Ide M., = Tokunaga T.  & Honda M. (1989).
   A fluorescence sandwich ELISA for = detecting  soluble and
   cell-associated human interleukin-2.
   J. Immunol. = Methods  121, 281-288.
   Nunc-Immuno Plate F96
   Nunc-Immuno  Wash

   Klein-Schneegans A.-S., Gavériaux = C., Fonteneau  P. & Loor F.
   Indirect double sandwich ELISA for the = specific and quantitative
   measurement of mouse IgM, IgA and IgG  subclasses.
   J. Immunol. Methods 119, = 117-125.
   Nunc-Immuno  Plate MaxiSorp

   Klein-Schneegans A.-S., Kuntz L., = Fonteneau P.  & Loor F. (1989).
   An indirect asymmetrical sandwich ELISA = using  anti-allotype
   antibodies for the specific and quantitative = measurement of  mouse
   IgG2a of Igh-1^b  allotype.
   J. Immunol. Methods 125, = 207-213.
   Nunc-Immuno  Plate MaxiSorp

   Kronborg G., Fomsgaard A., Shand = G.H. &  Høiby N. (1989).
   Determination of the components of immune = complexes  made in vitro
   with antigens derived from Pseudomonas  aeruginosa.
   J. Immunol. Methods 122, = 51-57.
   Nunc-Immuno  Plate F96

   Maneta-Peyret L., Freyburger G., = Bessoule J.-J.  & Cassagne C.
   Specific immunocytochemical = visualization of  phospatidylserine.
   J. Immunol. Methods 122,  155-158.
   Nunc-Immuno Plate F96

   Mihelic M., Kalbacher H., Hannappel = E. &  Voelter W. (1989).
   MicroELISA method for the determination of = thymosin  b[9] 
   discriminating between thymosin b[9] and  the structurally closely
   related thymosin b[4].
   J. Immunol. Methods 122, = 7-13.
   Nunc-Immuno Plate  F96

   Motojima H., Kobayashi T., Shimane = M., Kamachi  S.-I. & Fukushima
   M. (1989).
   Quantitative enzyme = immunoassay for  human granulocyte colony
   stimulating factor (G-CSF).
   J. = Immunol.  Methods 118, 187-192.
   Nunc-Immuno Tube  MaxiSorp

   Ota F., Hirota K., Nagamune H., = Senesi S.,  Satomi Y., Yasuoka M.,
   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.
   J. Immunol. Methods 124, = 259-266.
   Nunc-Immuno  Plate MaxiSorp

   Overall M.L., Marzuki S. & = Hertzog P.J.  (1989).
   Comparison of different ELISAs for the detection of = monoclonal 
   antibodies to human interferon-a.
   J. Immunol. Methods 119,  27-33.
   Nunc-Immuno Plate MaxiSorp

   Pereira H.A., Martin L.E. & = Spitznagel J.K.  (1989).
   Quantitation of a cationic antimicrobial granule = protein of  human
   polymorphonuclear leukocytes by ELISA.
   J. Immunol. = Methods 117,  115-120.
   Nunc-Immuno Plate MaxiSorp = F96

   Prowse C., George E., Micklem L.R., = Hornsey V.,  Brown J. & James
   K. (1989).
   Human atrial natriuretic factor = (ANF).Characterisation of a
   monoclonal antibody panel and its use = in  radioimmunoassay.
   J. Immunol. Methods 118,  91-100.
   Nunc-Immuno Plate F96

   Pullman W.E., Elsbury S., Kobayashi = M.,  Hargreaves J., Preston
   L., van Leeuwen B. & Hapel A.J.  (1989).
   Rapid assay and identification of human haemopoietic = growth 
   J. Immunol. Methods 117, = 153-161.
   Nunc-Immuno Plate  F96

   Rieben R. & Blaser K.  (1989).
   Quantification of IgG and IgG4 antibodies to bee venom 
   phospholipase A2 by competitive inhibition in ELISA.
   J. = Immunol.  Methods 119, 1-8.
   Nunc-Immuno Plate  MaxiSorp

   Saxena R., Isaksoon B., Bygren P. = &  Wieslander J. (1989).
   A rapid assay for circulating = anti-glomerular  basement membrane
   antibodies in Goodpasture syndrome.
   J. = Immunol.  Methods 118, 73-78.
   Nunc-Immuno = Plate

   Takata Y., Moriyama T., Fukumori = Y., Yoden A.,  Shima M. & Inai S.
   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.
   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 GrEingen 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., = RiethmEler  G. & Feucht H.E.
   Deposition of complement = activation  products on plastic-adsorbed
   J. Immunol. = Methods 124,  121-129.
   Nunc-Immuno Plate  F96

More information about the Methods mailing list