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bio rad econo pac serum igg purification kit  (Bio-Rad)


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    Bio-Rad bio rad econo pac serum igg purification kit
    Fig. 3. Fractionation of amyloid precursor protein (APP)-specific a-secretase activity in cord blood serum (CBS). To purify and eventually identify the a-secretase activity in CBS, the <t>Econo-Pac</t> Serum IgG <t>Purification</t> Kit <t>(Bio-Rad,</t> Philadelphia, PA, USA) was initially employed to remove highly abundant IgG. CBS was then desalted using Econo-Pac 10DG columns. The desalted serum was applied to DEAE Affi-Gel Blue columns to remove residual IgG and collect 20 additional protein fractions, by eluting with an increasing ionic strength gradient of NaCl buffer ranging from 0.1 M to 2.0 M. The remaining proteins on the column were eluted by the regen- eration buffer included in the kit and collected as the regeneration fraction (Reg). (A) Chinese hamster ovary cells stably expressing wild-type human APP (CHO/APPwt) cells were cultured in 24-well plates and treated with 10 mL of each protein fraction for 2 h. Conditioned media were then collected and analyzed by soluble amyloid precursor protein a (sAPPa) Western blot (upper panel) and ELISA (lower panel). 10 mL CBS, desalted CBS, and phosphate- buffered saline (PBS; Ctrl) were included under the same cell cul- ture conditions as positive and negative controls, respectively. Cell lysates were also prepared from each fraction-treated cell culture as an additional reference to evaluate sAPPa production levels (data not shown). (B) Protein concentration of each fraction. (C) CHO/ APPwt cells were treated with the 0.6 to 1.0 M NaCl-eluted fractions from 10 different CBS lots, as well as whole CBS and PBS (Ctrl), for 2 h and the conditioned media were collected for sAPPa ELISA. The results were presented as mean (+SD) sAPPa produced (ng/mg protein). In addition, each protein fraction was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis to assess total protein fractionation (C, right panel).
    Bio Rad Econo Pac Serum Igg Purification Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/bio+rad+econo+pac+serum+igg+purification+kit/Econo-Pac+Serum+IgG+Purification+Kit/pm29560732-143-11-11
    Average 93 stars, based on 93 article reviews
    bio rad econo pac serum igg purification kit - by Bioz Stars, 2026-10
    93/100 stars

    Images

    1) Product Images from "Human Umbilical Cord Blood Serum-derived α-Secretase: Functional Testing in Alzheimer's Disease Mouse Models."

    Article Title: Human Umbilical Cord Blood Serum-derived α-Secretase: Functional Testing in Alzheimer's Disease Mouse Models.

    Journal: Cell transplantation

    doi: 10.1177/0963689718759473

    Fig. 3. Fractionation of amyloid precursor protein (APP)-specific a-secretase activity in cord blood serum (CBS). To purify and eventually identify the a-secretase activity in CBS, the Econo-Pac Serum IgG Purification Kit (Bio-Rad, Philadelphia, PA, USA) was initially employed to remove highly abundant IgG. CBS was then desalted using Econo-Pac 10DG columns. The desalted serum was applied to DEAE Affi-Gel Blue columns to remove residual IgG and collect 20 additional protein fractions, by eluting with an increasing ionic strength gradient of NaCl buffer ranging from 0.1 M to 2.0 M. The remaining proteins on the column were eluted by the regen- eration buffer included in the kit and collected as the regeneration fraction (Reg). (A) Chinese hamster ovary cells stably expressing wild-type human APP (CHO/APPwt) cells were cultured in 24-well plates and treated with 10 mL of each protein fraction for 2 h. Conditioned media were then collected and analyzed by soluble amyloid precursor protein a (sAPPa) Western blot (upper panel) and ELISA (lower panel). 10 mL CBS, desalted CBS, and phosphate- buffered saline (PBS; Ctrl) were included under the same cell cul- ture conditions as positive and negative controls, respectively. Cell lysates were also prepared from each fraction-treated cell culture as an additional reference to evaluate sAPPa production levels (data not shown). (B) Protein concentration of each fraction. (C) CHO/ APPwt cells were treated with the 0.6 to 1.0 M NaCl-eluted fractions from 10 different CBS lots, as well as whole CBS and PBS (Ctrl), for 2 h and the conditioned media were collected for sAPPa ELISA. The results were presented as mean (+SD) sAPPa produced (ng/mg protein). In addition, each protein fraction was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis to assess total protein fractionation (C, right panel).
    Figure Legend Snippet: Fig. 3. Fractionation of amyloid precursor protein (APP)-specific a-secretase activity in cord blood serum (CBS). To purify and eventually identify the a-secretase activity in CBS, the Econo-Pac Serum IgG Purification Kit (Bio-Rad, Philadelphia, PA, USA) was initially employed to remove highly abundant IgG. CBS was then desalted using Econo-Pac 10DG columns. The desalted serum was applied to DEAE Affi-Gel Blue columns to remove residual IgG and collect 20 additional protein fractions, by eluting with an increasing ionic strength gradient of NaCl buffer ranging from 0.1 M to 2.0 M. The remaining proteins on the column were eluted by the regen- eration buffer included in the kit and collected as the regeneration fraction (Reg). (A) Chinese hamster ovary cells stably expressing wild-type human APP (CHO/APPwt) cells were cultured in 24-well plates and treated with 10 mL of each protein fraction for 2 h. Conditioned media were then collected and analyzed by soluble amyloid precursor protein a (sAPPa) Western blot (upper panel) and ELISA (lower panel). 10 mL CBS, desalted CBS, and phosphate- buffered saline (PBS; Ctrl) were included under the same cell cul- ture conditions as positive and negative controls, respectively. Cell lysates were also prepared from each fraction-treated cell culture as an additional reference to evaluate sAPPa production levels (data not shown). (B) Protein concentration of each fraction. (C) CHO/ APPwt cells were treated with the 0.6 to 1.0 M NaCl-eluted fractions from 10 different CBS lots, as well as whole CBS and PBS (Ctrl), for 2 h and the conditioned media were collected for sAPPa ELISA. The results were presented as mean (+SD) sAPPa produced (ng/mg protein). In addition, each protein fraction was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis to assess total protein fractionation (C, right panel).

    Techniques Used: Fractionation, Activity Assay, Purification, Stable Transfection, Expressing, Cell Culture, Western Blot, Enzyme-linked Immunosorbent Assay, Saline, Protein Concentration, Produced, Polyacrylamide Gel Electrophoresis

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    Article Snippet: An amperometric immunosensor for the specific detection of Ricinus communis is reported.. Screen printed electrodes (SPEs) were modified with gold nanoparticles (GNPs) loaded multiwalled carbon nanotubes (MWCNTs)–chitosan (Ch) film.. The ratio of MWCNT and GNP was optimised to get best electrochemically active electrode.

    Article Title: Human Umbilical Cord Blood Serum-derived α-Secretase: Functional Testing in Alzheimer's Disease Mouse Models.
    Article Snippet: .. Initially, removal of highly abundant immunoglobulins and desalting were performed using Bio-Rad Econo-Pac Serum IgG Purification Kit and 10DG columns. ..

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    Article Snippet: Ricin is a glycoprotein from Ricinus communis seeds.. It is known to have diverse toxic effects on cells of different visceral organs.. In the present study, we purified and denatured ricin in a boiling water bath for different time intervals.

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    Article Snippet: Antibody was produced in rabbits by Cocalico Biologicals. .. The antibody was IgG purified using the Bio-Rad Econo-Pac Serum IgG Purification kit. ..

    Article Title: Human Umbilical Cord Blood Serum–derived α-Secretase
    Article Snippet: .. Initially, removal of highly abundant immunoglobulins and desalting were performed using Bio-Rad Econo-Pac Serum IgG Purification Kit and 10DG columns. ..

    Article Title: Anti-mu opioid antiserum against the third external loop of the cloned mu-opioid receptor acts as a mu receptor neutral antagonist.
    Article Snippet: The region from the third external loop to the C terminus of MOR-1 appeared to be critical to the selective binding of MOR-1 ligands as DAMGO and morphine to MOR-1.. To study the pharmacological properties of the third extracellular loop an antibody was raised in rabbits against the sequence 304–316 which is unique to MOR-1 and includes the third external loop; the anti-MOR-1 antibody was affinity purified against the immunogen sequence and characterized by [H]DAMGO and Western blotting; [H]DPDPE binding assay remained unchanged in the presence of the antibody.. Anti-MOR-1 IgGwas characterized as a neutral antagonist in Chinese hamster ovary (CHO) cells hyperexpressing constitutively active MOR-1s; in fact, anti-MOR-1 IgG completely reversed the inhibition induced by the MOR-1 agonist endomorphin1, endomorphin2, DAMGO and morphine on forskolin stimulated cyclic AMP (cAMP) accumulation and attenuated both the action of the selectiveMOR-1 agonist DAMGO to increase [S]GTPgS binding and the action of theMOR-1 inverse agonist beta-chlornaltrexamine (CNA) to decrease [S]GTPgS binding.



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    bio rad econo pac serum igg purification kit  (Bio-Rad)
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    Bio-Rad bio rad econo pac serum igg purification kit
    Fig. 3. Fractionation of amyloid precursor protein (APP)-specific a-secretase activity in cord blood serum (CBS). To purify and eventually identify the a-secretase activity in CBS, the <t>Econo-Pac</t> Serum IgG <t>Purification</t> Kit <t>(Bio-Rad,</t> Philadelphia, PA, USA) was initially employed to remove highly abundant IgG. CBS was then desalted using Econo-Pac 10DG columns. The desalted serum was applied to DEAE Affi-Gel Blue columns to remove residual IgG and collect 20 additional protein fractions, by eluting with an increasing ionic strength gradient of NaCl buffer ranging from 0.1 M to 2.0 M. The remaining proteins on the column were eluted by the regen- eration buffer included in the kit and collected as the regeneration fraction (Reg). (A) Chinese hamster ovary cells stably expressing wild-type human APP (CHO/APPwt) cells were cultured in 24-well plates and treated with 10 mL of each protein fraction for 2 h. Conditioned media were then collected and analyzed by soluble amyloid precursor protein a (sAPPa) Western blot (upper panel) and ELISA (lower panel). 10 mL CBS, desalted CBS, and phosphate- buffered saline (PBS; Ctrl) were included under the same cell cul- ture conditions as positive and negative controls, respectively. Cell lysates were also prepared from each fraction-treated cell culture as an additional reference to evaluate sAPPa production levels (data not shown). (B) Protein concentration of each fraction. (C) CHO/ APPwt cells were treated with the 0.6 to 1.0 M NaCl-eluted fractions from 10 different CBS lots, as well as whole CBS and PBS (Ctrl), for 2 h and the conditioned media were collected for sAPPa ELISA. The results were presented as mean (+SD) sAPPa produced (ng/mg protein). In addition, each protein fraction was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis to assess total protein fractionation (C, right panel).
    Bio Rad Econo Pac Serum Igg Purification 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/bio+rad+econo+pac+serum+igg+purification+kit/Econo-Pac+Serum+IgG+Purification+Kit/pm29560732-143-11-11
    Average 93 stars, based on 1 article reviews
    bio rad econo pac serum igg purification kit - by Bioz Stars, 2026-10
    93/100 stars
    		  Buy from Supplier

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    Fig. 3. Fractionation of amyloid precursor protein (APP)-specific a-secretase activity in cord blood serum (CBS). To purify and eventually identify the a-secretase activity in CBS, the Econo-Pac Serum IgG Purification Kit (Bio-Rad, Philadelphia, PA, USA) was initially employed to remove highly abundant IgG. CBS was then desalted using Econo-Pac 10DG columns. The desalted serum was applied to DEAE Affi-Gel Blue columns to remove residual IgG and collect 20 additional protein fractions, by eluting with an increasing ionic strength gradient of NaCl buffer ranging from 0.1 M to 2.0 M. The remaining proteins on the column were eluted by the regen- eration buffer included in the kit and collected as the regeneration fraction (Reg). (A) Chinese hamster ovary cells stably expressing wild-type human APP (CHO/APPwt) cells were cultured in 24-well plates and treated with 10 mL of each protein fraction for 2 h. Conditioned media were then collected and analyzed by soluble amyloid precursor protein a (sAPPa) Western blot (upper panel) and ELISA (lower panel). 10 mL CBS, desalted CBS, and phosphate- buffered saline (PBS; Ctrl) were included under the same cell cul- ture conditions as positive and negative controls, respectively. Cell lysates were also prepared from each fraction-treated cell culture as an additional reference to evaluate sAPPa production levels (data not shown). (B) Protein concentration of each fraction. (C) CHO/ APPwt cells were treated with the 0.6 to 1.0 M NaCl-eluted fractions from 10 different CBS lots, as well as whole CBS and PBS (Ctrl), for 2 h and the conditioned media were collected for sAPPa ELISA. The results were presented as mean (+SD) sAPPa produced (ng/mg protein). In addition, each protein fraction was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis to assess total protein fractionation (C, right panel).

    Journal: Cell transplantation

    Article Title: Human Umbilical Cord Blood Serum-derived α-Secretase: Functional Testing in Alzheimer's Disease Mouse Models.

    doi: 10.1177/0963689718759473

    Figure Lengend Snippet: Fig. 3. Fractionation of amyloid precursor protein (APP)-specific a-secretase activity in cord blood serum (CBS). To purify and eventually identify the a-secretase activity in CBS, the Econo-Pac Serum IgG Purification Kit (Bio-Rad, Philadelphia, PA, USA) was initially employed to remove highly abundant IgG. CBS was then desalted using Econo-Pac 10DG columns. The desalted serum was applied to DEAE Affi-Gel Blue columns to remove residual IgG and collect 20 additional protein fractions, by eluting with an increasing ionic strength gradient of NaCl buffer ranging from 0.1 M to 2.0 M. The remaining proteins on the column were eluted by the regen- eration buffer included in the kit and collected as the regeneration fraction (Reg). (A) Chinese hamster ovary cells stably expressing wild-type human APP (CHO/APPwt) cells were cultured in 24-well plates and treated with 10 mL of each protein fraction for 2 h. Conditioned media were then collected and analyzed by soluble amyloid precursor protein a (sAPPa) Western blot (upper panel) and ELISA (lower panel). 10 mL CBS, desalted CBS, and phosphate- buffered saline (PBS; Ctrl) were included under the same cell cul- ture conditions as positive and negative controls, respectively. Cell lysates were also prepared from each fraction-treated cell culture as an additional reference to evaluate sAPPa production levels (data not shown). (B) Protein concentration of each fraction. (C) CHO/ APPwt cells were treated with the 0.6 to 1.0 M NaCl-eluted fractions from 10 different CBS lots, as well as whole CBS and PBS (Ctrl), for 2 h and the conditioned media were collected for sAPPa ELISA. The results were presented as mean (+SD) sAPPa produced (ng/mg protein). In addition, each protein fraction was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis to assess total protein fractionation (C, right panel).

    Article Snippet: Initially, removal of highly abundant immunoglobulins and desalting were performed using Bio-Rad Econo-Pac Serum IgG Purification Kit and 10DG columns.

    Techniques: Fractionation, Activity Assay, Purification, Stable Transfection, Expressing, Cell Culture, Western Blot, Enzyme-linked Immunosorbent Assay, Saline, Protein Concentration, Produced, Polyacrylamide Gel Electrophoresis