system fluoromax Search Results


raman emission horiba-mtb xplora spectrometer  (HORIBA Ltd)
90
HORIBA Ltd raman emission horiba-mtb xplora spectrometer
Raman Emission Horiba Mtb Xplora Spectrometer, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/raman emission horiba-mtb xplora spectrometer/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
raman emission horiba-mtb xplora spectrometer - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
spectrofluorometer horiba fluoromax-4  (HORIBA Ltd)
90
HORIBA Ltd spectrofluorometer horiba fluoromax-4
Spectrofluorometer Horiba Fluoromax 4, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/spectrofluorometer horiba fluoromax-4/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
spectrofluorometer horiba fluoromax-4 - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
aminco bowman series 2 spectrometer  (Polytec Inc)
90
Polytec Inc aminco bowman series 2 spectrometer
Aminco Bowman Series 2 Spectrometer, supplied by Polytec Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/aminco bowman series 2 spectrometer/product/Polytec Inc
Average 90 stars, based on 1 article reviews
aminco bowman series 2 spectrometer - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
fluoromax-3 fluorometer  (Hitachi Ltd)
90
Hitachi Ltd fluoromax-3 fluorometer
Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi <t>FluoroMax-3</t> fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.
Fluoromax 3 Fluorometer, supplied by Hitachi Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/fluoromax-3 fluorometer/product/Hitachi Ltd
Average 90 stars, based on 1 article reviews
fluoromax-3 fluorometer - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
fluoromax-3 monochromator  (HORIBA Ltd)
90
HORIBA Ltd fluoromax-3 monochromator
Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi <t>FluoroMax-3</t> fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.
Fluoromax 3 Monochromator, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/fluoromax-3 monochromator/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
fluoromax-3 monochromator - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
fluoromax plus  (HORIBA Ltd)
90
HORIBA Ltd fluoromax plus
Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi <t>FluoroMax-3</t> fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.
Fluoromax Plus, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/fluoromax plus/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
fluoromax plus - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
fluoromax-4 fluorescence spectrometer equipped with nano-led light sources  (HORIBA Ltd)
90
HORIBA Ltd fluoromax-4 fluorescence spectrometer equipped with nano-led light sources
Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi <t>FluoroMax-3</t> fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.
Fluoromax 4 Fluorescence Spectrometer Equipped With Nano Led Light Sources, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/fluoromax-4 fluorescence spectrometer equipped with nano-led light sources/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
fluoromax-4 fluorescence spectrometer equipped with nano-led light sources - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
spectrofluorometer fluoromax-4  (HORIBA Ltd)
90
HORIBA Ltd spectrofluorometer fluoromax-4
Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi <t>FluoroMax-3</t> fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.
Spectrofluorometer Fluoromax 4, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/spectrofluorometer fluoromax-4/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
spectrofluorometer fluoromax-4 - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
fluorescence plate reader fluoromax spectrofluorimeter  (HORIBA Ltd)
90
HORIBA Ltd fluorescence plate reader fluoromax spectrofluorimeter
Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi <t>FluoroMax-3</t> fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.
Fluorescence Plate Reader Fluoromax Spectrofluorimeter, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/fluorescence plate reader fluoromax spectrofluorimeter/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
fluorescence plate reader fluoromax spectrofluorimeter - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
time-correlated single-photon counting spectrometer horiba fluoromax-4  (HORIBA Ltd)
90
HORIBA Ltd time-correlated single-photon counting spectrometer horiba fluoromax-4
Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi <t>FluoroMax-3</t> fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.
Time Correlated Single Photon Counting Spectrometer Horiba Fluoromax 4, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/time-correlated single-photon counting spectrometer horiba fluoromax-4/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
time-correlated single-photon counting spectrometer horiba fluoromax-4 - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
confocal laser raman microscope horiba fluoromax  (HORIBA Ltd)
90
HORIBA Ltd confocal laser raman microscope horiba fluoromax
Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi <t>FluoroMax-3</t> fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.
Confocal Laser Raman Microscope Horiba Fluoromax, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/confocal laser raman microscope horiba fluoromax/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
confocal laser raman microscope horiba fluoromax - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
fluorescence intensity measuring apparatus horiba fluoromax-3  (HORIBA Ltd)
90
HORIBA Ltd fluorescence intensity measuring apparatus horiba fluoromax-3
Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi <t>FluoroMax-3</t> fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.
Fluorescence Intensity Measuring Apparatus Horiba Fluoromax 3, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/fluorescence intensity measuring apparatus horiba fluoromax-3/product/HORIBA Ltd
Average 90 stars, based on 1 article reviews
fluorescence intensity measuring apparatus horiba fluoromax-3 - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier

Image Search Results


Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi FluoroMax-3 fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.

Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

Article Title: Cyclic AMP-mediated endocytosis of intestinal epithelial NHE3 requires binding to synaptotagmin 1

doi: 10.1152/ajpgi.00379.2009

Figure Lengend Snippet: Syt 1 and NHE3 direct binding enables fluorescent resonance energy transfer. His-tagged full-length Syt 1 was labeled with (5-(((2-iodoacetyl)amino)ethyl)amino naphthalene-1-sulfonic acid) (IAEDANS), and His-tagged rat NHE3 COOH-terminal cytoplasmic tail (amino acids 436–831) was labeled with (4-(4-(dimethylamino) phenyl) azo)benzoic acid, succinimidyl ester (Dabcyl). IAEDANS-Syt 1 was excited at 295 nm, and emission was measured over the range 350–595 nm. NHE3 was phosphorylated in vitro by cAMP-dependent protein kinase with (left) or without ATP (right). Addition of all NHE3 constructs from reactions without ATP did not change the Syt 1 emission spectrum. However, addition of the wild-type (WT) NHE3 that had been phosphorylated by cAMP-dependent protein kinase caused a concentration-related shift in the emission spectral profile and decrease in emission intensity (top, left). Similar results were obtained with the NHE3 S505A mutation. When the PKA-phosphorylated S605A mutation was used, no changes were observed upon addition of the His-Dabcyl-tagged S605A NHE3. Addition of the NHE3 S552A mutation caused a concentration-dependent shift in the emission spectrum that differed from the wild-type or S505A mutation and slightly increased the emission maximum. Spectra shown were obtained on a Hitachi FluoroMax-3 fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.

Article Snippet: Spectra shown were obtained on a Hitachi FluoroMax-3 fluorometer and are representative of those of 3 separate experiments with different reagents (IAEDANS-Syt 1 and Dabcyl-NHE3) in each experiment.

Techniques: Binding Assay, Förster Resonance Energy Transfer, Labeling, In Vitro, Construct, Concentration Assay, Mutagenesis