ライフサイエンスコーパス: PAGE

1 PAGE analysis suggests that SlpB is produced at lower le

2 differential proteomic approach employing 1D PAGE revealed differences in accumulated proteins at the

3 edium rare prepared beef were assessed by 2D PAGE for the comparison of protein profiles.

4 2D-PAGE images showed that proteins in the biocake (S3) at

5 Two-dimensional electrophoresis (2D-PAGE) for protein fractionation, graphite furnace atomic

6 ional polyacrylamide gel electrophoresis (2D-PAGE) separation and matrix-assisted laser desorption/io

7 ional polyacrylamide gel electrophoresis (2D-PAGE), and the total mercury concentrations in protein s

8 tides in the samples was obtained through 2D-PAGE fractioning followed by mass spectrometry (ESI-MS/M

9 Using 2D-PAGE, we demonstrate that mutant alpha-tropomyosinslow w

10 ect of O2 when exposed to UV, resulting in a PAGE-in-PDMS device.

11 rther performed pathway enrichment analysis (PAGE algorithm).

12 Using microscopy and PAGE analysis, we show that Kdo-N3 is localized to the o

13 environments with limited diffusion, such as PAGE.

14 lsilane)-b-poly(allyl glycidyl ether) (PFS-b-PAGE) decorated with triethylene glycol (TEG), abbreviat

15 units showed loss of NDUFB8, confirmed by BN-PAGE analysis of CI assembly and IHC using an alternativ

16 ) in schizophrenia OFC were identified by BN-PAGE.

17 ative Polyacrylamide Gel Electrophoresis (BN-PAGE) and dot immunoblotting for quantifying various pho

18 ative polyacrylamide gel electrophoresis (BN-PAGE) from digitonin-solubilized thylakoids were similar

19 ative polyacrylamide gel electrophoresis (BN-PAGE) indicates that PP4 holoenzyme complexes, like thos

20 ative polyacrylamide gel electrophoresis (BN-PAGE) to demonstrate BbHtrA oligomeric structures that w

21 s during blue native gel electrophoresis (BN-PAGE).

22 ative polyacrylamide gel electrophoresis (BN-PAGE).

23 demonstrated by complexome profiling from BN-PAGE.

24 In BN-PAGE, the SNARE heterotrimer was identified as a 150-kDa

25 -polyacrylamide gel electrophoresis (MICS-BN-PAGE).

26 rus was detected in 39 specimens (11.17%) by PAGE and in 38 specimens (10.88%) by LAT.

27 triggered assembly behavior was examined by PAGE analysis, and the morphologies of the grown dendrim

28 ypass polymerases kappa and eta, followed by PAGE-based assays to determine the catalytic efficiency

29 Nfo), the analysis of cleavage fragments by PAGE and MALDI-TOF/MS show that the G*[C8-N3]T* lesions

30 expressed spots, which were collected in 2-D PAGE gels and identified via mass spectrometry (nESI-QTO

31 -SR-B1 cells were analyzed by non-denaturing PAGE, size-exclusion chromatography, and the distributio

32 16 proteins were detected with 2-dimensional PAGE in combination with liquid chromatography/tandem ma

33 tions and examined by means of 2-dimensional PAGE.

34 Two-dimensional PAGE and Phos-tag gel analysis of stress-stimulated STMN

35 other proteins as judged by two-dimensional PAGE of metabolically labeled/immunoprecipitated PMEL an

36 A proteomic (two-dimensional PAGE with mass spectrometric analysis) comparison betwee

37 l time quantitative RT-PCR and 2-dimensional-PAGE showed that gamma-tubulin-1 is the dominant isotype

38 ns as both a molecular sieving matrix during PAGE and a blotting scaffold during immunoprobing.

39 y native polyacrylamide gel electrophoresis (PAGE) and cryogenic electron microscopy (cryoEM) imaging

40 otifs by polyacrylamide gel electrophoresis (PAGE) and fluorescence spectroscopy and demonstrated the

41 Polyacrylamide Gel Electrophoresis (PAGE) and Latex Agglutination Test (LAT) were utilized t

42 te (SDS)-polyacrylamide gel electrophoresis (PAGE) in a PDMS/glass microfluidic chip.

43 te (SDS)-polyacrylamide gel electrophoresis (PAGE) method for measuring the amount of SWNTs in lysate

44 routine polyacrylamide gel electrophoresis (PAGE) methods lack the separation resolution necessary t

45 bsequent polyacrylamide gel electrophoresis (PAGE) of the single-cell lysate.

46 Using polyacrylamide gel electrophoresis (PAGE) to separate monomeric from dimeric (boron-bridged)

47 gates on polyacrylamide gel electrophoresis (PAGE), as compared with those of APTS.

48 ility of polyacrylamide gel electrophoresis (PAGE), we develop a technique for fabrication of PAGE mo

49 /MS) and polyacrylamide gel electrophoresis (PAGE).

50 rchitecture using Genomics and Epidemiology (PAGE) study conducted a GWAS of 26 clinical and behaviou

51 rchitecture using Genomics and Epidemiology (PAGE) study, we identify susceptibility loci and investi

52 rchitecture using Genomics and Epidemiology (PAGE) study.

53 By applying FDF-PAGE, we provide evidence that both strands of viral sma

54 To address this problem, we established FDF-PAGE (fully-denaturing formaldehyde polyacrylamide gel e

55 Comparing non-denaturing conditions to FDF-PAGE uncovered extensive sequestration of miRNAs in mode

56 toggles from an "enclosed" microchannel for PAGE and blotting to an "open" PA gel lane for immunopro

57 Proteomic analysis of aggregate bands from PAGE gels reveal an abundance of Gly/Ala/Ser/Thr repeats

58 ical lysis of cells in each microwell; (iii) PAGE of each single-cell lysate; (iv) exposure of the ge

59 and fluorescently labeled chelator heads in PAGE and blot membranes.

60 lator heads to detect His-tagged proteins in PAGE and blot membranes.

61 In studies of the covalent mechanism, PAGE fluorography showed labeling of GLP-1R in immunopre

62 parable reproducibility to glass microdevice PAGE.

63 ding the application and use of microfluidic PAGE without the need for a glass microfabrication infra

64 al models in the integrated assessment model PAGE-ICE to explore nonlinear transitions in the Arctic

65 Multimer-PAGE provides a simple inexpensive biochemical technique

66 resembled those observed following multimer-PAGE.

67 ed linearly with protein input into multimer-PAGE, suggesting to some extent, multimers were also for

68 Here we developed a method, termed "multimer-PAGE," that combines in-gel chemical cross-linking with

69 Once the multimer-PAGE technique was validated, relative stoichiometric co

70 dant soluble multimer detection via multimer-PAGE.

71 Native PAGE demonstrated that this ASADH tetramerization is app

72 We adapted a native PAGE method to assess the formation and thermostabilitie

73 ng, size exclusion chromatography and native PAGE show that Hs11S is assembled in different oligomeri

74 Blue native PAGE analyses verify the presence of a SecYEG-PpiD compl

75 Blue native PAGE analysis identified high molecular weight complexes

76 Blue native PAGE and FRET assays revealed 1% n-dodecyl beta-d-maltos

77 RE1alpha complexes in cells with blue native PAGE immunoblotting.

78 downs, pharmacologic inhibitors, blue native PAGE, mass spectrometry, and assessment of mitochondrial

79 Analyses by SEC, blue native PAGE, SDS-PAGE, and dynamic light scattering indicated t

80 We investigated these species by Blue Native PAGE, Suc density gradient centrifugation, 77K fluoresce

81 Blue-native PAGE analysis showed that the variant TatC proteins prod

82 ing on mammalian synapses we use blue-native PAGE and 'gene-tagging' of GluN1 to report the first bio

83 h unprocessed 12S globulin by 2D blue-native PAGE/SDS-PAGE indicated that the nhx5 nhx6 knockouts sho

84 thylakoid complexes was performed by native PAGE and sucrose density centrifugation.

85 lytical ultracentrifugation and clear native PAGE analysis show that NRC is a stable pigment-protein

86 aeruginosa cell lysates separated on native PAGE gels and stained for iron with Ferene S.

87 omatography and analyzed by SDS-PAGE, native PAGE, and Western immunoblot analysis.

88 Parallel native PAGE, immunoblotting and Complex I activity assays furth

89 se results highlight the power of the native PAGE assay for membrane protein biochemistry and provide

90 ar mass estimated, using SDS-PAGE and native-PAGE electrophoresis, to be 86kDa.

91 Under native condition, Blue Native-PAGE and Blue Native-PAGE/SDS-PAGE 2D analyses demonstra

92 bserved in separate complexes by blue native-PAGE, the two proteins coimmunoprecipitated both during

93 Although Blue Native-PAGE, total internal reflection fluorescence microscopy,

94 condition, Blue Native-PAGE and Blue Native-PAGE/SDS-PAGE 2D analyses demonstrated co-existence of t

95 oximate molecular weight estimated by NATIVE-PAGE and SDS-PAGE electrophoresis was approximately 60 k

96 capabilities of T-oligo using nondenaturing PAGE, nuclear magnetic resonance, and immunofluorescence

97 the diagonal line in the second dimension of PAGE.

98 n between the first and second dimensions of PAGE, holo-metalloproteins in the original sample were c

99 ), we develop a technique for fabrication of PAGE molecular sieving gels in PDMS microchannel network

100 abrication method compatible with performing PAGE protein separations in a composite PDMS-glass micro

101 en alpha1/alpha2 ratio was determined by SDS PAGE and by qRT-PCR in ex-vivo bone explants.

102 demonstrated by glycoprotein staining of SDS PAGE gels.

103 n content was not altered significantly, SDS PAGE profiling exhibited minor modifications in the prot

104 SDS-PAGE analyses indicated the formation of hydrolysates an

105 SDS-PAGE analysis of the dry-enriched protein fractions show

106 SDS-PAGE analysis showed high degree of protein polymerizati

107 SDS-PAGE analysis showed that salt addition contributes to h

108 SDS-PAGE analysis showed that the band intensity of tropomyo

109 SDS-PAGE and immunoassay analysis with rabbit polyclonal ser

110 SDS-PAGE and MS analysis revealed that the sheared archaella

111 SDS-PAGE and SEM analyses were also carried out to compare e

112 SDS-PAGE coupled to LC-MS analysis of sand fly saliva, befor

113 SDS-PAGE electrophoresis qualitatively detected three major

114 SDS-PAGE gels stained for catecholase activity showed multip

115 SDS-PAGE gels were used to determine abundance of the CO2 -f

116 SDS-PAGE in non-reducing and reducing conditions revealed th

117 SDS-PAGE patterns show distinctive bands for each kind of ho

118 SDS-PAGE profile of PPI revealed major bands ranging from 50

119 SDS-PAGE results revealed a reduction in the casein and alph

120 SDS-PAGE showed that annonacinone inhibited formation of PAI

121 SDS-PAGE showed that collagens extracted with different meth

122 SDS-PAGE showed that the molecular mass of purified enzyme w

123 SDS-PAGE showed that the protein bands corresponding to the

124 SDS-PAGE showed that the purified protein had molecular weig

125 SDS-PAGE shows the presence of a well separated protein band

126 SDS-PAGE under reducing and non-reducing conditions did not

127 SDS-PAGE was carried out for all collagens extracted under d

128 SDS-PAGE, DLS, and TEM were used to confirm and characterize

129 SDS-PAGE, surface hydrophobicity, circular dichroism, FTIR s

130 The 2D SDS-PAGE separation demonstrated the presence of a few prote

131 Large aggregates unable to enter a 4% SDS-PAGE gel were formed at pH 6.5 and 8.5, which became sol

132 single polypeptide band of 83.1kDa after SDS-PAGE.

133 Although SDS-PAGE did not show any differences for either the number

134 Spectroscopic and SDS-PAGE binding assays of Sin a 2 and Ara h 1 with differen

135 lly compared to references: Kjeldahl and SDS-PAGE densitometry for the determination of the proportio

136 Proteomic analysis and SDS-PAGE electrophoresis of the extracted proteome suggested

137 ular weight estimated by NATIVE-PAGE and SDS-PAGE electrophoresis was approximately 60 kDa.

138 current reference methods, Kjeldahl and SDS-PAGE electrophoresis.

139 X-ray crystallography and SDS-PAGE further show that trimer 4(F20Cha), a covalently st

140 ahigh pressure liquid chromatography and SDS-PAGE gels.

141 tests (SPTs), specific IgEs (sIgEs) and SDS-PAGE immunoblotting.

142 opy, secondary ion mass spectrometry and SDS-PAGE indicate that Cba. tepidum biogenic S(0) globules c

143 ted through the degree of hydrolysis and SDS-PAGE profiles.

144 Gel filtration chromatography and SDS-PAGE revealed that the enzyme is monomeric with a molecu

145 ormance liquid chromatography (HPLC) and SDS-PAGE subunit analysis reveal that the first step of ther

146 Fluorescence spectroscopy and SDS-PAGE techniques were employed to explore quantitative an

147 tease showed a single band on native and SDS-PAGE with a molecular weight of 24kDa on SDS-PAGE.

148 6 were determined by sandwich ELISA and SDS-PAGE, and the allergenicities of treated peanuts were co

149 ion, lectin affinity chromatography, and SDS-PAGE.

150 be observed by X-ray crystallography and SDS-PAGE.

151 ned by electrophoretic technique such as SDS-PAGE.

152 he sera of patients with diabetes before SDS-PAGE.

153 Biochemical (SDS-PAGE, Size exclusion chromatography and LC-MS/MS) and im

154 h); investigate SMALP protein purity by SDS-PAGE analysis and estimate protein concentration (4 h);

155 es with high specificity as confirmed by SDS-PAGE analysis with a phosphoprotein-specific stain and m

156 ion during in vitro GID was evaluated by SDS-PAGE and by measuring the nitrogen content of ultrafiltr

157 ed on this concept, we first measured by SDS-PAGE and confocal microscopy the level of inclusion bodi

158 he samples were dialyzed and analyzed by SDS-PAGE and for OA content.

159 r triple-helical structure, confirmed by SDS-PAGE and FTIR.

160 Peptides were detected by SDS-PAGE and GC-MS was used to determine carbohydrate conten

161 d the structure of recombinant CLEC3A by SDS-PAGE and immunoblot, glycan analysis, matrix-assisted la

162 th previous studies it was identified by SDS-PAGE and MALDI-TOF-MS that ZnPP formation takes place in

163 lecular weight <15 kDa) as determined by SDS-PAGE and MALDI-TOF/MS analyses.

164 ovalently cross-linked dimer isolated by SDS-PAGE and mass analysis showed that dityrosine dimer was

165 Chemical analysis was performed by SDS-PAGE and mass spectrometry.

166 alysed by mass spectrometry, followed by SDS-PAGE and subsequent immunoblotting with antibodies detec

167 Examination by SDS-PAGE followed by protein staining revealed protein profi

168 IgG molecular integrity was assessed by SDS-PAGE immunoblotting.

169 The protein fractions analysed by SDS-PAGE showed similar bands, indicating different solubili

170 nal major peptide bands were detected by SDS-PAGE treatments as compared to the solar or freeze dryin

171 time-of-flight mass spectrometry and by SDS-PAGE using biotinylated PGA1 (PGA1-B).

172 troducing kansui, which was confirmed by SDS-PAGE, FTIR, and HPLC results.

173 olecular mass of approximately 85 kDa by SDS-PAGE, it elutes in fractions corresponding to approximat

174 -exchange chromatography and analyzed by SDS-PAGE, native PAGE, and Western immunoblot analysis.

175 to 240 min and subsequently analysed by SDS-PAGE, quantitative LC-MS/MS, untargeted LC-MS/MS and ELI

176 of AS-48 digestion fragments in bulk by SDS-PAGE, RP-HPLC, and MALDI-TOF proves that the previous pe

177 64mgg(-1)) were analysed and compared by SDS-PAGE, showing differences in their electrophoretic prote

178 c plaques are diagnostic of CBD(7,8); by SDS-PAGE, so too are detergent-insoluble, 37 kDa fragments o

179 ation into receptor subunits resolved by SDS-PAGE, there was etomidate-inhibitable labeling by [(3)H]

180 By SDS-PAGE, two forms of NS5A with distinct apparent molecular

181 nzymatic treatments under sonication, by SDS-PAGE, western blot and ELISA, with serum IgE of allergic

182 and 2 h, the pellicles were analyzed by SDS-PAGE.

183 Peak homogeneity was confirmed by SDS-PAGE.

184 dins and glutenins profiling was done by SDS-PAGE.

185 ication of the small cleavage product by SDS-PAGE.

186 rs were reduced (-70.5%), as assessed by SDS-PAGE.

187 re noticeably different when analyzed by SDS-PAGE.

188 f OT upon these laccases were studied by SDS-PAGE.

189 , differential scanning fluorimetry, CD, SDS-PAGE, and immunoblotting with conformation-dependent and

190 f USP20 correlates with a characteristic SDS-PAGE mobility shift of the protein, blocks its deubiquit

191 tor followed by affinity chromatography, SDS-PAGE, and identification of protein bands evident only w

192 torial peptide ligand libraries (CPLLs), SDS-PAGE, nLC-ESI-MS/MS, and database search, permitted iden

193 by HPP, this processing modified the 1-D SDS-PAGE sarcoplasmic patterns in a direct-dependent manner

194 omplex was confirmed by second dimension SDS-PAGE, Western blotting, mass spectrometry, and the use o

195 ion of complexes that were stable during SDS-PAGE.

196 ate poly acrylamide gel electrophoreses (SDS-PAGE) indicated that the integrity of major myofibrillar

197 fate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the OM revealed a high molecular mass

198 hate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis revealed the localization of phosvitin in

199 fate polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption/ionization-ti

200 hate-polyacrylamide gel electrophoresis (SDS-PAGE) combined with principal component analysis (PCA).

201 oteins separated by gel electrophoresis (SDS-PAGE) to be detected as peptides by mass spectrometry in

202 ring polyacrylamide gel electrophoresis (SDS-PAGE) was used to separate proteins.

203 fate polyacrylamide gel electrophoresis (SDS-PAGE), which was eliminated by phosphatase treatment.

204 hate-polyacrylamide gel electrophoresis (SDS-PAGE).

205 ate-polyaccrylamide gel electrophoresis (SDS-PAGE).

206 fate-polyacrylamide gel electrophoresis (SDS-PAGE).

207 hate polyacrylamide gel electrophoresis (SDS-PAGE).

208 lfate-polyacrylamide gel electrophoresis SDS-PAGE-immunoblotting with patient sera and rabbit serum a

209 r proteins using OFFGEL electrophoresis, SDS-PAGE and protein identification by MALDI-TOF MS.

210 The simple approach employing SDS-PAGE and PCA reported in this paper may provide a useful

211 mass spectrometry MYDGF assay, employing SDS-PAGE-based protein fractionation to deplete high-abundan

212 s carried out included sugar estimation, SDS-PAGE, GPC, color, FT-IR, DSC, thermal stability, solubil

213 As expected, SDS-PAGE patterns were species-specific but differences, due

214 The results from SDS-PAGE illustrated that the most adsorbed quantity among p

215 pearance of small protein fragments from SDS-PAGE in dry-aged samples compared to the unaged.

216 Seventeen protein bands from SDS-PAGE were analysed and 26 proteins were identified.

217 Moreover, 19 protein bands from SDS-PAGE were analyzed and a total of 45 different proteins

218 l changes (surface hydrophobicity, FTIR, SDS-PAGE and thiol content) of gluten in relation to its ant

219 identified as type-I collagens by FTIR, SDS-PAGE, and molecular weight distribution analyses.

220 Furthermore, SDS-PAGE analysis showed high similarity among the protein f

221 (MALDI-TOF MS), gas chromatography (GC), SDS-PAGE, Toll-like receptor 4 (TLR4) stimulation, and immun

222 polyacrylamide gel electrophoresis (IEF/SDS-PAGE) and fluorescence measurements.

223 ately, with distinctive protein bands in SDS-PAGE at 140 kDa and 110 kDa for bovine and porcine sampl

224 form of Gdown1 with altered mobility in SDS-PAGE that appears during mitosis.

225 No fragmentation was observed in SDS-PAGE while transmission electron micrographs showed comp

226 70 generated products that comigrated in SDS-PAGE with the C1 and C2 forms, respectively, and mutatio

227 equence, a 76-kDa moiety was detected in SDS-PAGE without reducing agent and heat inactivation.

228 arance of a 160 kDa myosin-4 fragment in SDS-PAGE, further decreased water-holding of myofibrils and

229 rresponding to the tetramer (152 kDa) in SDS-PAGE, suggesting that the MGAT2 enzyme primarily functio

230 lecular-weight complexes and Blue Native/SDS-PAGE and isoelectric focusing demonstrated that differen

231 fter immunoprecipitation and blue native/SDS-PAGE.

232 ance energy transfer (FRET), nonreducing SDS-PAGE, and strategic mutation of the Ab hinge region was

233 The observed SDS-PAGE bands did not show any evidence of zein crosslinkin

234 Herein, we describe the use of SDS-PAGE and microprobe Raman spectroscopy to detect and dis

235 method has been used as a replacement of SDS-PAGE for purity analysis of adeno-associated virus (AAV)

236 Densitometry analysis of SDS-PAGE gels confirmed no size degradation (P>0.05) as a fu

237 teomics tools based on image analysis of SDS-PAGE protein gels and protein identification by tandem m

238 lecular mass of approximately 150 kDa on SDS-PAGE and did not contain Gbeta5 Mass spectrometry analys

239 ) present in cheese whey is difficult on SDS-PAGE due to their close proximity during electrophoresis

240 these fibroblasts was mildly delayed on SDS-PAGE gel, suggesting some overmodification of collagen d

241 ine with the migration shift detected on SDS-PAGE of cell culture collagen, extracts of bone collagen

242 The anomalous migration of SNORC on SDS-PAGE was due to its primary polypeptide features, sugges

243 ealed the same abnormal chain pattern on SDS-PAGE with an overabundance of a gamma112 cross-linked tr

244 The enzyme preparation when analysed on SDS-PAGE, displayed a single protein band with Mr 33 kDa; Su

245 PAGE with a molecular weight of 24kDa on SDS-PAGE.

246 itions than under reducing conditions on SDS-PAGE.

247 as a dimer while migrating at 66 kDa on SDS-PAGE.

248 in super-family members were revealed on SDS-PAGE.

249 is not sufficient for regular SDS CGE or SDS-PAGE assay.

250 in vitro by laying labeled bacteria over SDS-PAGE-separated salivary proteins.

251 Analyses by SEC, blue native PAGE, SDS-PAGE, and dynamic light scattering indicated that the re

252 n, Blue Native-PAGE and Blue Native-PAGE/SDS-PAGE 2D analyses demonstrated co-existence of the alpha1

253 ssed 12S globulin by 2D blue-native PAGE/SDS-PAGE indicated that the nhx5 nhx6 knockouts showed compr

254 ted and freeze-dried in order to perform SDS-PAGE and immunoblotting tests.

255 In this article, we present SDS-PAGE differential mobility studies combined with fluores

256 subjected to analysis of total protein, SDS-PAGE and size exclusion chromatography.

257 species were estimated by a quantitative SDS-PAGE.

258 Non-reducing SDS-PAGE confirms assembly of the predicted Cys(820)-linked

259 Non-reducing SDS-PAGE shows two bands of about 38kDa exhibiting strong ac

260 Analyses by non-reducing SDS-PAGE, size exclusion chromatography, and sedimentation v

261 d neutralization process by non-reducing SDS-PAGE.

262 alysed by static laser light scattering, SDS-PAGE and optical-fluorescence microscopy.

263 ystallization and they presented similar SDS-PAGE profiles, with bands close to 20 and 37 kDa.

264 n, as shown by a decrease in solubility, SDS-PAGE pattern, and Confocal Laser Scanning Microscopy.

265 tography coupled with mass spectrometry, SDS-PAGE and immunoassay.

266 109, as documented by mass spectrometry, SDS-PAGE, isoelectric focusing, size-exclusion chromatograph

267 o the high sensitivity of silver stained SDS-PAGE.

268 sitivity is comparable to silver-stained SDS-PAGE.

269 Phos-tag SDS-PAGE coupled with MS analysis disclosed that SnRK1 indee

270 rotein was also detected by the Phos-tag SDS-PAGE method.

271 The SDS-PAGE pattern of A. mellifera proteins honey showed three

272 egree of hydrolysis of HPIs by HT in the SDS-PAGE profiles.

273 Through SDS-PAGE analysis, an increased degree of hydrolysis with lo

274 etone treatment of cocoa powder prior to SDS-PAGE led to losses of nitrogenous compounds.

275 utral pH by high resolution Tris-Tricine SDS-PAGE and matrix-assisted laser desorption ionization tim

276 by staining acrylamide gel after tricine SDS-PAGE using cationic 'stains all' dye.

277 ated to be approximately 62,000Da, using SDS-PAGE and 57151Da, based on mass spectrometry results.

278 Proteins were studied by using SDS-PAGE and immunoblotting with sera from patients with pea

279 of equal molecular mass estimated, using SDS-PAGE and native-PAGE electrophoresis, to be 86kDa.

280 lycation endproducts were measured using SDS-PAGE gels and by ELISA whereas Amadori products were ass

281 before and after plasma treatment using SDS-PAGE, FTIR, UPLC-MS/MS and ELISA.

282 These aggregates can be observed using SDS-PAGE, size-exclusion chromatography, dynamic light scatt

283 Hydrolysis profiles were displayed using SDS-PAGE.

284 drolysis profiles were illustrated using SDS-PAGE.

285 ydrolysis profiles were visualised using SDS-PAGE.

286 -0.5 Pa/s and then further separated via SDS-PAGE in a 25 mm long channel.

287 influence of HD on BLG molecular weight SDS-PAGE was used.

288 dent NF-kappaB responses; however, while SDS-PAGE analysis showed similar LPS ladder patterns for B.

289 native (BN) electrophorese combined with SDS-PAGE yielded NOX4 to reside in macromolecular complexes.

290 SDS/PAGE, mass spectrometry, and Edman degradation identifie

291 Additionally, standard PAGE denatures proteins prior to analysis precluding det

292 We then characterize the PAGE separation performance.

293 the LAT was 82.61% sensitive compared to the PAGE, which was 84.78% sensitive.

294 We see this PAGE-in-PDMS fabrication technique as expanding the appl

295 facilitates the protocol by eliminating two PAGE purification steps.

296 phoretic approaches [native, urea, acid urea PAGEs and isoelectric focusing (IEF)] as the first-dimen

297 ctive towards kappa-casein, analysed by Urea-PAGE and LC-ESI-MS, whereas the degradation of alpha and

298 Using PAGE and HPLC analysis, we observed that the IP6K1/2-kno

299 nable synthesis of IP(6) We also found using PAGE mass assay that metabolic blockage by phosphate sta

300 s, we devise a simple approach, called UVHis-PAGE, that uses metal ion-loaded and fluorescently label