econopac protein a kit Search Results


econopac protein a kit  (Bio-Rad)
93
Bio-Rad econopac protein a kit
Econopac Protein A Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/econopac+protein+a+kit/Econo-Pac+Protein+A+Kit/pm37662014-90-13-17
Average 93 stars, based on 1 article reviews
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econopac 10dg columns  (Bio-Rad)
96
Bio-Rad econopac 10dg columns
Econopac 10dg Columns, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/econopac+protein+a+kit/Econo-Pac+10DG+Desalting+Columns/pm12469910-65-13-16
Average 96 stars, based on 1 article reviews
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gel filtration  (Bio-Rad)
96
Bio-Rad gel filtration
FIG. 6. Identification of tTG substrates in the E-extract of bone. (A) Three micrograms of in- tramembranous bone E-extract was run in a 10% gel by SDS-PAGE and transferred onto a PVDF membrane for immunodetection with antibodies against AHSG, BAG-75, BSP, FN, ON, and OPN. Of these proteins, AHSG, BSP, and OPN appeared in two forms; both monomeric and high molecular weight forms. Two high molec- ular weight regions/bands of blotted bone E-extract—a band 211 kDa and a band be- tween 150 and 200 kDa—were subjected to N-terminal sequencing in which the results are presented in the panel at the right. Sequence data identifying AHSG, BSP, and OPN was obtained from the high molecular weight regions. (B) One milligram of endochondral bone E-extract was incubated overnight at 37°C in the presence of 3 mM CaCl2, 1 mM DTT, 1 mM bPA, and 0.4 U tTG. Free biotin label was removed from the reaction mixture by gel filtration before loading the preparation onto a monomeric avidin affinity column. Proteins were eluted with 0.1 M glycine buffer, at pH 2.8, and protein-containing frac- tions (monitored at 280 nm) were pooled and concentrated. (C) Five micrograms of the prep- aration was run in 10% gels and biotin (bPA) incorporation was detected with ExtrAvidin- HRP and after stripping of the membrane, AHSG, OPN, and BSP were immunodetected. Membranes were developed using ECL. SDS- PAGE with silver staining of 1 g of the prep- aration is presented on the left. Molecular weight markers are indicated on the left. Arrowheads indicate the top of the running gel.
Gel Filtration, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/econopac+protein+a+kit/Gel+Filtration+Standard/pm12469910-65-10-16
Average 96 stars, based on 1 article reviews
gel filtration - by Bioz Stars, 2026-08
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f shape  (Greiner Bio)
96
Greiner Bio f shape
FIG. 6. Identification of tTG substrates in the E-extract of bone. (A) Three micrograms of in- tramembranous bone E-extract was run in a 10% gel by SDS-PAGE and transferred onto a PVDF membrane for immunodetection with antibodies against AHSG, BAG-75, BSP, FN, ON, and OPN. Of these proteins, AHSG, BSP, and OPN appeared in two forms; both monomeric and high molecular weight forms. Two high molec- ular weight regions/bands of blotted bone E-extract—a band 211 kDa and a band be- tween 150 and 200 kDa—were subjected to N-terminal sequencing in which the results are presented in the panel at the right. Sequence data identifying AHSG, BSP, and OPN was obtained from the high molecular weight regions. (B) One milligram of endochondral bone E-extract was incubated overnight at 37°C in the presence of 3 mM CaCl2, 1 mM DTT, 1 mM bPA, and 0.4 U tTG. Free biotin label was removed from the reaction mixture by gel filtration before loading the preparation onto a monomeric avidin affinity column. Proteins were eluted with 0.1 M glycine buffer, at pH 2.8, and protein-containing frac- tions (monitored at 280 nm) were pooled and concentrated. (C) Five micrograms of the prep- aration was run in 10% gels and biotin (bPA) incorporation was detected with ExtrAvidin- HRP and after stripping of the membrane, AHSG, OPN, and BSP were immunodetected. Membranes were developed using ECL. SDS- PAGE with silver staining of 1 g of the prep- aration is presented on the left. Molecular weight markers are indicated on the left. Arrowheads indicate the top of the running gel.
F Shape, supplied by Greiner Bio, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/econopac+protein+a+kit/Microplate+384+Well+Pp+F-Bottom/pm35235790-271-109-112
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pp microplate 384  (Greiner Bio)
95
Greiner Bio pp microplate 384
FIG. 6. Identification of tTG substrates in the E-extract of bone. (A) Three micrograms of in- tramembranous bone E-extract was run in a 10% gel by SDS-PAGE and transferred onto a PVDF membrane for immunodetection with antibodies against AHSG, BAG-75, BSP, FN, ON, and OPN. Of these proteins, AHSG, BSP, and OPN appeared in two forms; both monomeric and high molecular weight forms. Two high molec- ular weight regions/bands of blotted bone E-extract—a band 211 kDa and a band be- tween 150 and 200 kDa—were subjected to N-terminal sequencing in which the results are presented in the panel at the right. Sequence data identifying AHSG, BSP, and OPN was obtained from the high molecular weight regions. (B) One milligram of endochondral bone E-extract was incubated overnight at 37°C in the presence of 3 mM CaCl2, 1 mM DTT, 1 mM bPA, and 0.4 U tTG. Free biotin label was removed from the reaction mixture by gel filtration before loading the preparation onto a monomeric avidin affinity column. Proteins were eluted with 0.1 M glycine buffer, at pH 2.8, and protein-containing frac- tions (monitored at 280 nm) were pooled and concentrated. (C) Five micrograms of the prep- aration was run in 10% gels and biotin (bPA) incorporation was detected with ExtrAvidin- HRP and after stripping of the membrane, AHSG, OPN, and BSP were immunodetected. Membranes were developed using ECL. SDS- PAGE with silver staining of 1 g of the prep- aration is presented on the left. Molecular weight markers are indicated on the left. Arrowheads indicate the top of the running gel.
Pp Microplate 384, supplied by Greiner Bio, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/econopac+protein+a+kit/Microplate+384+Well+Pp+V-Bottom/pm35235790-271-105-112
Average 95 stars, based on 1 article reviews
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c2272 blotting grade blocker contains bsa biorad  (Bio-Rad)
96
Bio-Rad c2272 blotting grade blocker contains bsa biorad
FIG. 6. Identification of tTG substrates in the E-extract of bone. (A) Three micrograms of in- tramembranous bone E-extract was run in a 10% gel by SDS-PAGE and transferred onto a PVDF membrane for immunodetection with antibodies against AHSG, BAG-75, BSP, FN, ON, and OPN. Of these proteins, AHSG, BSP, and OPN appeared in two forms; both monomeric and high molecular weight forms. Two high molec- ular weight regions/bands of blotted bone E-extract—a band 211 kDa and a band be- tween 150 and 200 kDa—were subjected to N-terminal sequencing in which the results are presented in the panel at the right. Sequence data identifying AHSG, BSP, and OPN was obtained from the high molecular weight regions. (B) One milligram of endochondral bone E-extract was incubated overnight at 37°C in the presence of 3 mM CaCl2, 1 mM DTT, 1 mM bPA, and 0.4 U tTG. Free biotin label was removed from the reaction mixture by gel filtration before loading the preparation onto a monomeric avidin affinity column. Proteins were eluted with 0.1 M glycine buffer, at pH 2.8, and protein-containing frac- tions (monitored at 280 nm) were pooled and concentrated. (C) Five micrograms of the prep- aration was run in 10% gels and biotin (bPA) incorporation was detected with ExtrAvidin- HRP and after stripping of the membrane, AHSG, OPN, and BSP were immunodetected. Membranes were developed using ECL. SDS- PAGE with silver staining of 1 g of the prep- aration is presented on the left. Molecular weight markers are indicated on the left. Arrowheads indicate the top of the running gel.
C2272 Blotting Grade Blocker Contains Bsa Biorad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/econopac+protein+a+kit/Blotting-Grade+Blocker/pm35235790-271-47-52
Average 96 stars, based on 1 article reviews
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Image Search Results


FIG. 6. Identification of tTG substrates in the E-extract of bone. (A) Three micrograms of in- tramembranous bone E-extract was run in a 10% gel by SDS-PAGE and transferred onto a PVDF membrane for immunodetection with antibodies against AHSG, BAG-75, BSP, FN, ON, and OPN. Of these proteins, AHSG, BSP, and OPN appeared in two forms; both monomeric and high molecular weight forms. Two high molec- ular weight regions/bands of blotted bone E-extract—a band 211 kDa and a band be- tween 150 and 200 kDa—were subjected to N-terminal sequencing in which the results are presented in the panel at the right. Sequence data identifying AHSG, BSP, and OPN was obtained from the high molecular weight regions. (B) One milligram of endochondral bone E-extract was incubated overnight at 37°C in the presence of 3 mM CaCl2, 1 mM DTT, 1 mM bPA, and 0.4 U tTG. Free biotin label was removed from the reaction mixture by gel filtration before loading the preparation onto a monomeric avidin affinity column. Proteins were eluted with 0.1 M glycine buffer, at pH 2.8, and protein-containing frac- tions (monitored at 280 nm) were pooled and concentrated. (C) Five micrograms of the prep- aration was run in 10% gels and biotin (bPA) incorporation was detected with ExtrAvidin- HRP and after stripping of the membrane, AHSG, OPN, and BSP were immunodetected. Membranes were developed using ECL. SDS- PAGE with silver staining of 1 g of the prep- aration is presented on the left. Molecular weight markers are indicated on the left. Arrowheads indicate the top of the running gel.

Journal: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research

Article Title: Tissue transglutaminase and its substrates in bone.

doi: 10.1359/jbmr.2002.17.12.2161

Figure Lengend Snippet: FIG. 6. Identification of tTG substrates in the E-extract of bone. (A) Three micrograms of in- tramembranous bone E-extract was run in a 10% gel by SDS-PAGE and transferred onto a PVDF membrane for immunodetection with antibodies against AHSG, BAG-75, BSP, FN, ON, and OPN. Of these proteins, AHSG, BSP, and OPN appeared in two forms; both monomeric and high molecular weight forms. Two high molec- ular weight regions/bands of blotted bone E-extract—a band 211 kDa and a band be- tween 150 and 200 kDa—were subjected to N-terminal sequencing in which the results are presented in the panel at the right. Sequence data identifying AHSG, BSP, and OPN was obtained from the high molecular weight regions. (B) One milligram of endochondral bone E-extract was incubated overnight at 37°C in the presence of 3 mM CaCl2, 1 mM DTT, 1 mM bPA, and 0.4 U tTG. Free biotin label was removed from the reaction mixture by gel filtration before loading the preparation onto a monomeric avidin affinity column. Proteins were eluted with 0.1 M glycine buffer, at pH 2.8, and protein-containing frac- tions (monitored at 280 nm) were pooled and concentrated. (C) Five micrograms of the prep- aration was run in 10% gels and biotin (bPA) incorporation was detected with ExtrAvidin- HRP and after stripping of the membrane, AHSG, OPN, and BSP were immunodetected. Membranes were developed using ECL. SDS- PAGE with silver staining of 1 g of the prep- aration is presented on the left. Molecular weight markers are indicated on the left. Arrowheads indicate the top of the running gel.

Article Snippet: Biotinylated proteins were separated from the free bPA label by gel filtration using EconoPac 10DG columns (BioRad Laboratories) and PBS (Buph from Immunopure Immobilized Monomeric Avidin Kit; Pierce) as a buffer.

Techniques: SDS Page, Membrane, Immunodetection, High Molecular Weight, Sequencing, Incubation, Avidin-Biotin Assay, Stripping Membranes, Silver Staining, Molecular Weight