it is amazing how some "SCIENTISTS" treat others' COPYRIGHTS with contempt.
Your "Hope, content is useful for you", declared above in your reply [026] is a sentence which might insinuate yourself into others' confidence you might have not created your reply - which in veritas / as a matter of fact! is a "collection of sentences" - by yourself...
I always thought ResearchGate is not only a kind of "social media platform" like others where you might insert some 'imponderables', yet flib / blarney(s) or lies... as you like... I always thought the ResearchGate platform is a splendid service to researchers and scientific colleagues to present their thoughts and opinions, discuss and (not only) exchange and evaluate their findings and to forward their academic encouragement to others - even to those who -eventually - are in need of help.
You have managed to use at least 5-6 different (but certainly copyrighted!) sources from the / available in the www. to COPY and PASTE your reply at a rip-off level of at least 90%. This 'might' be called PLAGIARISM.
I DON'T point with this my reply here at you and say "Shame on you"... you NOT only arranged the sentences in a new fashion and for some parts of sentences you "shortened a bit" and used your own wording... This is not to blame you... it may be called your "compilation" therefore .
BUT: it is NOT an academically or scientifically desired behaviour to copy and paste WITHOUT mentioning the source and / or an Author, if applicable -and especially, if copyrights are declared !!
You should know that others - copyright owners! - could find out too and may blame you for plagiarism...
Your Reply [026] above has been copied into my files so you need not to delete your answer... you ONLY need to add the web-sources/publications/articles you used for your plagiarization >pieced together<.... (I know which sources these are / have been).
it is amazing how some "SCIENTISTS" treat others' COPYRIGHTS with contempt.
Your "Hope, content is useful for you", declared above in your reply [026] is a sentence which might insinuate yourself into others' confidence you might have not created your reply - which in veritas / as a matter of fact! is a "collection of sentences" - by yourself...
I always thought ResearchGate is not only a kind of "social media platform" like others where you might insert some 'imponderables', yet flib / blarney(s) or lies... as you like... I always thought the ResearchGate platform is a splendid service to researchers and scientific colleagues to present their thoughts and opinions, discuss and (not only) exchange and evaluate their findings and to forward their academic encouragement to others - even to those who -eventually - are in need of help.
You have managed to use at least 5-6 different (but certainly copyrighted!) sources from the / available in the www. to COPY and PASTE your reply at a rip-off level of at least 90%. This 'might' be called PLAGIARISM.
I DON'T point with this my reply here at you and say "Shame on you"... you NOT only arranged the sentences in a new fashion and for some parts of sentences you "shortened a bit" and used your own wording... This is not to blame you... it may be called your "compilation" therefore .
BUT: it is NOT an academically or scientifically desired behaviour to copy and paste WITHOUT mentioning the source and / or an Author, if applicable -and especially, if copyrights are declared !!
You should know that others - copyright owners! - could find out too and may blame you for plagiarism...
Your Reply [026] above has been copied into my files so you need not to delete your answer... you ONLY need to add the web-sources/publications/articles you used for your plagiarization >pieced together<.... (I know which sources these are / have been).
maybe you can use HPLC to help remove glutaraldehyde residues. Protein has adsorption effection with some special columns, but glutaraldehyde doesn't have this characteristic, and you can isolate them in this way.
maybe you can use HPLC to help remove glutaraldehyde residues. Protein has adsorption effection with some special columns, but glutaraldehyde doesn't have this characteristic, and you can isolate them in this way.
Free glutaraldehyde is toxic for cells not the crosslinked one. So u have to remove uncrosslinked glutaraldehyde. U can remove it by water wash. Wash the sponges with distilled water several times and test the filterate for Benedict's test or Fehling's test. If the test gives negative result then sponges doesnot contain uncrosslinked gluteraldehyde good luck
Free glutaraldehyde is toxic for cells not the crosslinked one. So u have to remove uncrosslinked glutaraldehyde. U can remove it by water wash. Wash the sponges with distilled water several times and test the filterate for Benedict's test or Fehling's test. If the test gives negative result then sponges doesnot contain uncrosslinked gluteraldehyde good luck
I have been successfully able to leach out glutaraldehyde and other toxic reagents by giving a 48 hrs wash to the hydrogels. I let the gels stand in PBS for 48 hrs. Alternatively, you can incubate your samples in PBS for 24 hrs and keep them on a mechanical rocker. Hope this helps you!
I have been successfully able to leach out glutaraldehyde and other toxic reagents by giving a 48 hrs wash to the hydrogels. I let the gels stand in PBS for 48 hrs. Alternatively, you can incubate your samples in PBS for 24 hrs and keep them on a mechanical rocker. Hope this helps you!
Just a comment to get reproducible results in long lasting experiments. Reaction with primary amines works good in blocking free aldehyde however the reaction gives rise also to Schiff bases that might exhibit some degree of instability with time thus regenerating the free aldehyde group and hence its cytotoxicity. Therefore the use of NaBH4 would be advisable for stable and reliable blocking of such substrates.
Just a comment to get reproducible results in long lasting experiments. Reaction with primary amines works good in blocking free aldehyde however the reaction gives rise also to Schiff bases that might exhibit some degree of instability with time thus regenerating the free aldehyde group and hence its cytotoxicity. Therefore the use of NaBH4 would be advisable for stable and reliable blocking of such substrates.
Glutaraldehyde is used as a biocide in medical, industrial, agricultural, oil and natural gas industry, and laboratory settings. Glutaraldehyde degrades rapidly under both aerobic and anaerobic conditions in water and under aerobic conditions in soil.
Glutaraldehyde is hydrophilic and can be removed from the atmosphere by wet deposition. Glutaraldehyde can be deactivated chemically by adding a suitable amount of alkalinating or reducing agents. Heat removal, carbon oxide treatment even water may be also one of major solution for the same. Two options are available, depending on the concentration of glutaraldehyde to be deactivated. With Sodium Bisulfite and With Sodium Hydroxide (Caustic Soda) could be used. An effective chemical method that can be used to deactivate concentrations of glutaraldehyde (up to 5%) is by addition of sodium bisulfite (SBS). In order to assure rapid, complete inactivation, it is recommended that 2-3 parts (by weight) of SBS be added per part of active glutaraldehyde. Addition of 2-3 parts SBS will rapidly reduce the concentration of glutaraldehyde in solution to less than 2 ppm active within five minutes at room temperature.
Adding a sufficient amount of sodium hydroxide solution to maintain a pH of 12 will reduce the concentration of glutaraldehyde to approximately 20 ppm or less within 8 hours at room temperature. Maintaining the pH at 12 or higher is critical, as a lower pH will result in a significantly slower deactivation of glutaraldehyde. CO2 treatment and heat based removal of glutaraldehyde can be done. CO2 can be used to extract residual glutaraldehyde from crosslinked collagen (Collagen is the most abundant protein in the human body) films. Since CO2 is a nontoxic, nonflammable substance that is relatively inert and can be used to process biomaterials at mild pressures and physiologic temperatures. Collagen scaffolds require crosslinking to improve mechanical strength, requiring agents like glutaraldehyde that have high residual cytotoxicity. First, reduce glutaraldehyde concentration in ppm level or percentage. CO2 treatment can have negligible alteration of thermal stability but can significantly increase film stiffness and tensile strength. However, these changes were minor compared to heat-based removal of glutaraldehyde.
Glutaraldehyde is used as a biocide in medical, industrial, agricultural, oil and natural gas industry, and laboratory settings. Glutaraldehyde degrades rapidly under both aerobic and anaerobic conditions in water and under aerobic conditions in soil.
Glutaraldehyde is hydrophilic and can be removed from the atmosphere by wet deposition. Glutaraldehyde can be deactivated chemically by adding a suitable amount of alkalinating or reducing agents. Heat removal, carbon oxide treatment even water may be also one of major solution for the same. Two options are available, depending on the concentration of glutaraldehyde to be deactivated. With Sodium Bisulfite and With Sodium Hydroxide (Caustic Soda) could be used. An effective chemical method that can be used to deactivate concentrations of glutaraldehyde (up to 5%) is by addition of sodium bisulfite (SBS). In order to assure rapid, complete inactivation, it is recommended that 2-3 parts (by weight) of SBS be added per part of active glutaraldehyde. Addition of 2-3 parts SBS will rapidly reduce the concentration of glutaraldehyde in solution to less than 2 ppm active within five minutes at room temperature.
Adding a sufficient amount of sodium hydroxide solution to maintain a pH of 12 will reduce the concentration of glutaraldehyde to approximately 20 ppm or less within 8 hours at room temperature. Maintaining the pH at 12 or higher is critical, as a lower pH will result in a significantly slower deactivation of glutaraldehyde. CO2 treatment and heat based removal of glutaraldehyde can be done. CO2 can be used to extract residual glutaraldehyde from crosslinked collagen (Collagen is the most abundant protein in the human body) films. Since CO2 is a nontoxic, nonflammable substance that is relatively inert and can be used to process biomaterials at mild pressures and physiologic temperatures. Collagen scaffolds require crosslinking to improve mechanical strength, requiring agents like glutaraldehyde that have high residual cytotoxicity. First, reduce glutaraldehyde concentration in ppm level or percentage. CO2 treatment can have negligible alteration of thermal stability but can significantly increase film stiffness and tensile strength. However, these changes were minor compared to heat-based removal of glutaraldehyde.
Ashish Thakur ,
it is amazing how some "SCIENTISTS" treat others' COPYRIGHTS with contempt.
Your "Hope, content is useful for you", declared above in your reply [026] is a sentence which might insinuate yourself into others' confidence you might have not created your reply - which in veritas / as a matter of fact! is a "collection of sentences" - by yourself...
I always thought ResearchGate is not only a kind of "social media platform" like others where you might insert some 'imponderables', yet flib / blarney(s) or lies... as you like...
I always thought the ResearchGate platform is a splendid service to researchers and scientific colleagues to present their thoughts and opinions, discuss and (not only) exchange and evaluate their findings and to forward their academic encouragement to others - even to those who -eventually - are in need of help.
You have managed to use at least 5-6 different (but certainly copyrighted!) sources from the / available in the www. to COPY and PASTE your reply at a rip-off level of at least 90%.
This 'might' be called PLAGIARISM.
I DON'T point with this my reply here at you and say "Shame on you"... you NOT only arranged the sentences in a new fashion and for some parts of sentences you "shortened a bit" and used your own wording...
This is not to blame you... it may be called your "compilation" therefore .
BUT: it is NOT an academically or scientifically desired behaviour to copy and paste WITHOUT mentioning the source and / or an Author, if applicable -and especially, if copyrights are declared !!
You should know that others - copyright owners! - could find out too and may blame you for plagiarism...
Your Reply [026] above has been copied into my files so you need not to delete your answer...
you ONLY need to add the web-sources/publications/articles you used for your plagiarization >pieced together<.... (I know which sources these are / have been).
Ashish Thakur ,
it is amazing how some "SCIENTISTS" treat others' COPYRIGHTS with contempt.
Your "Hope, content is useful for you", declared above in your reply [026] is a sentence which might insinuate yourself into others' confidence you might have not created your reply - which in veritas / as a matter of fact! is a "collection of sentences" - by yourself...
I always thought ResearchGate is not only a kind of "social media platform" like others where you might insert some 'imponderables', yet flib / blarney(s) or lies... as you like...
I always thought the ResearchGate platform is a splendid service to researchers and scientific colleagues to present their thoughts and opinions, discuss and (not only) exchange and evaluate their findings and to forward their academic encouragement to others - even to those who -eventually - are in need of help.
You have managed to use at least 5-6 different (but certainly copyrighted!) sources from the / available in the www. to COPY and PASTE your reply at a rip-off level of at least 90%.
This 'might' be called PLAGIARISM.
I DON'T point with this my reply here at you and say "Shame on you"... you NOT only arranged the sentences in a new fashion and for some parts of sentences you "shortened a bit" and used your own wording...
This is not to blame you... it may be called your "compilation" therefore .
BUT: it is NOT an academically or scientifically desired behaviour to copy and paste WITHOUT mentioning the source and / or an Author, if applicable -and especially, if copyrights are declared !!
You should know that others - copyright owners! - could find out too and may blame you for plagiarism...
Your Reply [026] above has been copied into my files so you need not to delete your answer...
you ONLY need to add the web-sources/publications/articles you used for your plagiarization >pieced together<.... (I know which sources these are / have been).
More
VOTE
maybe you can use HPLC to help remove glutaraldehyde residues. Protein has adsorption effection with some special columns, but glutaraldehyde doesn't have this characteristic, and you can isolate them in this way.
maybe you can use HPLC to help remove glutaraldehyde residues. Protein has adsorption effection with some special columns, but glutaraldehyde doesn't have this characteristic, and you can isolate them in this way.
More
VOTE
Free glutaraldehyde is toxic for cells not the crosslinked one. So u have to remove uncrosslinked glutaraldehyde. U can remove it by water wash. Wash the sponges with distilled water several times and test the filterate for Benedict's test or Fehling's test. If the test gives negative result then sponges doesnot contain uncrosslinked gluteraldehyde
good luck
Free glutaraldehyde is toxic for cells not the crosslinked one. So u have to remove uncrosslinked glutaraldehyde. U can remove it by water wash. Wash the sponges with distilled water several times and test the filterate for Benedict's test or Fehling's test. If the test gives negative result then sponges doesnot contain uncrosslinked gluteraldehyde
good luck
More
VOTE
I have been successfully able to leach out glutaraldehyde and other toxic reagents by giving a 48 hrs wash to the hydrogels. I let the gels stand in PBS for 48 hrs. Alternatively, you can incubate your samples in PBS for 24 hrs and keep them on a mechanical rocker.
Hope this helps you!
I have been successfully able to leach out glutaraldehyde and other toxic reagents by giving a 48 hrs wash to the hydrogels. I let the gels stand in PBS for 48 hrs. Alternatively, you can incubate your samples in PBS for 24 hrs and keep them on a mechanical rocker.
Hope this helps you!
More
VOTE
Just a comment to get reproducible results in long lasting experiments. Reaction with primary amines works good in blocking free aldehyde however the reaction gives rise also to Schiff bases that might exhibit some degree of instability with time thus regenerating the free aldehyde group and hence its cytotoxicity. Therefore the use of NaBH4 would be advisable for stable and reliable blocking of such substrates.
Just a comment to get reproducible results in long lasting experiments. Reaction with primary amines works good in blocking free aldehyde however the reaction gives rise also to Schiff bases that might exhibit some degree of instability with time thus regenerating the free aldehyde group and hence its cytotoxicity. Therefore the use of NaBH4 would be advisable for stable and reliable blocking of such substrates.
More
VOTE
Dear Maurice:
For your convenience:
All information retrieved „blindely“ from the „dark dark“ Google-data „base“ within 0.3 secs:
Only searchphrase: „| Glycine 0.1M | or also: | Glycine 0.1M quenching agent |
Check: HOFFMAN et al, 2015:
Formaldehyde Crosslinking: A Tool for the Study of Chromatin Complexes
First Published on September 9, 2015 doi: 10.1074/jbc.R115.651679 October 30, 2015 The Journal of Biological Chemistry 290, 26404-26411. FREE FULL TEXT:
http://www.jbc.org/content/290/44/26404.full
Further references:
https://www.researchgate.net/post/Does_anyone_know_what_is_the_purpose_of_glycine_to_blocking_solution_in_ELISA_assay
https://www.researchgate.net/post/Any_advice_for_quenching_formaldehyde_protein-protein_crosslinking_Glycine_or_Tris
http://www.angelfire.com/clone2/fouad/techniques/Confocal_Immunofluorescence_using_PFA_as_a_fixative.pdf
https://ki.mit.edu/files/ki/cfile/sbc/microscopy/immunofluorescence-protocol.pdf
https://www.thermofisher.com/at/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/chemistry-crosslinking.html
http://www.protocol-online.org/biology-forums-2/posts/15808.html
http://www.protocol-online.org/biology-forums/posts/34079.html
https://www.thermofisher.com/at/en/home/life-science/cell-analysis/cellular-imaging/ihc/zymed-buffer-recipes.html
https://www.abcam.com/kits/blocking-for-ihc
https://electron-microscopy.hms.harvard.edu/methods
http://cshprotocols.cshlp.org/content/2008/8/pdb.rec11433.full?text_only=true
https://www.qgelbio.com/wp-content/uploads/2017/08/N.3.1-Cell-Fixation-in-gel-Protocol_QGel-96wp-format_v1.2.pdf
https://en.wikipedia.org/wiki/Glycine
http://europepmc.org/abstract/MED/26314115
Hope, I have made your day, best,
WHM
Dear Maurice:
For your convenience:
All information retrieved „blindely“ from the „dark dark“ Google-data „base“ within 0.3 secs:
Only searchphrase: „| Glycine 0.1M | or also: | Glycine 0.1M quenching agent |
Check: HOFFMAN et al, 2015:
Formaldehyde Crosslinking: A Tool for the Study of Chromatin Complexes
First Published on September 9, 2015 doi: 10.1074/jbc.R115.651679 October 30, 2015 The Journal of Biological Chemistry 290, 26404-26411. FREE FULL TEXT:
http://www.jbc.org/content/290/44/26404.full
Further references:
https://www.researchgate.net/post/Does_anyone_know_what_is_the_purpose_of_glycine_to_blocking_solution_in_ELISA_assay
https://www.researchgate.net/post/Any_advice_for_quenching_formaldehyde_protein-protein_crosslinking_Glycine_or_Tris
http://www.angelfire.com/clone2/fouad/techniques/Confocal_Immunofluorescence_using_PFA_as_a_fixative.pdf
https://ki.mit.edu/files/ki/cfile/sbc/microscopy/immunofluorescence-protocol.pdf
https://www.thermofisher.com/at/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/chemistry-crosslinking.html
http://www.protocol-online.org/biology-forums-2/posts/15808.html
http://www.protocol-online.org/biology-forums/posts/34079.html
https://www.thermofisher.com/at/en/home/life-science/cell-analysis/cellular-imaging/ihc/zymed-buffer-recipes.html
https://www.abcam.com/kits/blocking-for-ihc
https://electron-microscopy.hms.harvard.edu/methods
http://cshprotocols.cshlp.org/content/2008/8/pdb.rec11433.full?text_only=true
https://www.qgelbio.com/wp-content/uploads/2017/08/N.3.1-Cell-Fixation-in-gel-Protocol_QGel-96wp-format_v1.2.pdf
https://en.wikipedia.org/wiki/Glycine
http://europepmc.org/abstract/MED/26314115
Hope, I have made your day, best,
WHM
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VOTE
Dialysis technique you can use
Dialysis technique you can use
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VOTE
dialysis or repeatedly soaking the scaffold in water
dialysis or repeatedly soaking the scaffold in water
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VOTE
Obviously
Obviously
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VOTE
Dear Kubra,
Glutaraldehyde is used as a biocide in medical, industrial, agricultural, oil and natural gas industry, and laboratory settings. Glutaraldehyde degrades rapidly under both aerobic and anaerobic conditions in water and under aerobic conditions in soil.
Glutaraldehyde is hydrophilic and can be removed from the atmosphere by wet deposition. Glutaraldehyde can be deactivated chemically by adding a suitable amount of alkalinating or reducing agents. Heat removal, carbon oxide treatment even water may be also one of major solution for the same. Two options are available, depending on the concentration of glutaraldehyde to be deactivated. With Sodium Bisulfite and With Sodium Hydroxide (Caustic Soda) could be used.
An effective chemical method that can be used to deactivate concentrations of glutaraldehyde (up to 5%) is by addition of sodium bisulfite (SBS). In order to assure rapid, complete inactivation, it is recommended that 2-3 parts (by weight) of SBS be added per part of active glutaraldehyde. Addition of 2-3 parts SBS will rapidly reduce the concentration of glutaraldehyde in solution to less than 2 ppm active within five minutes at room temperature.
Adding a sufficient amount of sodium hydroxide solution to maintain a pH of 12 will reduce the concentration of glutaraldehyde to approximately 20 ppm or less within 8 hours at room temperature. Maintaining the pH at 12 or higher is critical, as a lower pH will result in a significantly slower deactivation of glutaraldehyde. CO2 treatment and heat based removal of glutaraldehyde can be done. CO2 can be used to extract residual glutaraldehyde from crosslinked collagen (Collagen is the most abundant protein in the human body) films. Since CO2 is a nontoxic, nonflammable substance that is relatively inert and can be used to process biomaterials at mild pressures and physiologic temperatures. Collagen scaffolds require crosslinking to improve mechanical strength, requiring agents like glutaraldehyde that have high residual cytotoxicity. First, reduce glutaraldehyde concentration in ppm level or percentage. CO2 treatment can have negligible alteration of thermal stability but can significantly increase film stiffness and tensile strength. However, these changes were minor compared to heat-based removal of glutaraldehyde.
Hope, content is helpful for you.
Ashish
Dear Kubra,
Glutaraldehyde is used as a biocide in medical, industrial, agricultural, oil and natural gas industry, and laboratory settings. Glutaraldehyde degrades rapidly under both aerobic and anaerobic conditions in water and under aerobic conditions in soil.
Glutaraldehyde is hydrophilic and can be removed from the atmosphere by wet deposition. Glutaraldehyde can be deactivated chemically by adding a suitable amount of alkalinating or reducing agents. Heat removal, carbon oxide treatment even water may be also one of major solution for the same. Two options are available, depending on the concentration of glutaraldehyde to be deactivated. With Sodium Bisulfite and With Sodium Hydroxide (Caustic Soda) could be used.
An effective chemical method that can be used to deactivate concentrations of glutaraldehyde (up to 5%) is by addition of sodium bisulfite (SBS). In order to assure rapid, complete inactivation, it is recommended that 2-3 parts (by weight) of SBS be added per part of active glutaraldehyde. Addition of 2-3 parts SBS will rapidly reduce the concentration of glutaraldehyde in solution to less than 2 ppm active within five minutes at room temperature.
Adding a sufficient amount of sodium hydroxide solution to maintain a pH of 12 will reduce the concentration of glutaraldehyde to approximately 20 ppm or less within 8 hours at room temperature. Maintaining the pH at 12 or higher is critical, as a lower pH will result in a significantly slower deactivation of glutaraldehyde. CO2 treatment and heat based removal of glutaraldehyde can be done. CO2 can be used to extract residual glutaraldehyde from crosslinked collagen (Collagen is the most abundant protein in the human body) films. Since CO2 is a nontoxic, nonflammable substance that is relatively inert and can be used to process biomaterials at mild pressures and physiologic temperatures. Collagen scaffolds require crosslinking to improve mechanical strength, requiring agents like glutaraldehyde that have high residual cytotoxicity. First, reduce glutaraldehyde concentration in ppm level or percentage. CO2 treatment can have negligible alteration of thermal stability but can significantly increase film stiffness and tensile strength. However, these changes were minor compared to heat-based removal of glutaraldehyde.
Hope, content is helpful for you.
Ashish
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VOTE
Anything with free amines can be used theoretically. Tris-HCl buffer, Ammonium chloride, and ethanolamine are commonly available good options.
Anything with free amines can be used theoretically. Tris-HCl buffer, Ammonium chloride, and ethanolamine are commonly available good options.
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VOTE
I would like to use 0.1 M glycine. Does anyone have papers to cite - as i would not like to go in blind?
I would like to use 0.1 M glycine. Does anyone have papers to cite - as i would not like to go in blind?
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VOTE