bsa  (Gold Biotechnology Inc)


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    Structured Review

    Gold Biotechnology Inc bsa
    Treatments effect mTORC1 activation in the stomach. Representative Western blot of the pattern observed in REDD and HFD treated (A) males and (B) females comparing the expression of the mTORC1 pathway in the stomach. Actin was used as an internal control. All samples were run in parallel. Images were minimally adjusted in contrast and brightness. Relative quantification of (C) pAKT-T308 for male (top) and female (bottom), (D) pAKT-S473 for male (top) and female (bottom), and (E) pS6K for male (left) and female (right) by densitometry analysis of Western blots. Proteins were extracted by homogenizing tissue in RIPA buffer. A <t>Bradford</t> curve using <t>BSA</t> as a standard was used for protein quantification and 30 μg of protein was separated on a 12.5% SDS-PAGE gel. Actin was used an as internal standard to ensure consistent loading and to normalize all samples. ImageJ was used to quantify intensity of bands. Phosphorylation levels were calculated by dividing the phosphorylation by the unphosphorylated and the phosphorylated form of the protein. Numerical data are summarized as means ± SEM. ∗ p
    Bsa, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 94/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 22 article reviews
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    Images

    1) Product Images from "Sex Modulates Lactobacillus johnsonii N6.2 and Phytophenol Effectiveness in Reducing High Fat Diet Induced mTOR Activation in Sprague-Dawley Rats"

    Article Title: Sex Modulates Lactobacillus johnsonii N6.2 and Phytophenol Effectiveness in Reducing High Fat Diet Induced mTOR Activation in Sprague-Dawley Rats

    Journal: Frontiers in Microbiology

    doi: 10.3389/fmicb.2018.02649

    Treatments effect mTORC1 activation in the stomach. Representative Western blot of the pattern observed in REDD and HFD treated (A) males and (B) females comparing the expression of the mTORC1 pathway in the stomach. Actin was used as an internal control. All samples were run in parallel. Images were minimally adjusted in contrast and brightness. Relative quantification of (C) pAKT-T308 for male (top) and female (bottom), (D) pAKT-S473 for male (top) and female (bottom), and (E) pS6K for male (left) and female (right) by densitometry analysis of Western blots. Proteins were extracted by homogenizing tissue in RIPA buffer. A Bradford curve using BSA as a standard was used for protein quantification and 30 μg of protein was separated on a 12.5% SDS-PAGE gel. Actin was used an as internal standard to ensure consistent loading and to normalize all samples. ImageJ was used to quantify intensity of bands. Phosphorylation levels were calculated by dividing the phosphorylation by the unphosphorylated and the phosphorylated form of the protein. Numerical data are summarized as means ± SEM. ∗ p
    Figure Legend Snippet: Treatments effect mTORC1 activation in the stomach. Representative Western blot of the pattern observed in REDD and HFD treated (A) males and (B) females comparing the expression of the mTORC1 pathway in the stomach. Actin was used as an internal control. All samples were run in parallel. Images were minimally adjusted in contrast and brightness. Relative quantification of (C) pAKT-T308 for male (top) and female (bottom), (D) pAKT-S473 for male (top) and female (bottom), and (E) pS6K for male (left) and female (right) by densitometry analysis of Western blots. Proteins were extracted by homogenizing tissue in RIPA buffer. A Bradford curve using BSA as a standard was used for protein quantification and 30 μg of protein was separated on a 12.5% SDS-PAGE gel. Actin was used an as internal standard to ensure consistent loading and to normalize all samples. ImageJ was used to quantify intensity of bands. Phosphorylation levels were calculated by dividing the phosphorylation by the unphosphorylated and the phosphorylated form of the protein. Numerical data are summarized as means ± SEM. ∗ p

    Techniques Used: Activation Assay, Western Blot, Expressing, SDS Page

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    Gold Biotechnology Inc bsa
    Treatments effect mTORC1 activation in the stomach. Representative Western blot of the pattern observed in REDD and HFD treated (A) males and (B) females comparing the expression of the mTORC1 pathway in the stomach. Actin was used as an internal control. All samples were run in parallel. Images were minimally adjusted in contrast and brightness. Relative quantification of (C) pAKT-T308 for male (top) and female (bottom), (D) pAKT-S473 for male (top) and female (bottom), and (E) pS6K for male (left) and female (right) by densitometry analysis of Western blots. Proteins were extracted by homogenizing tissue in RIPA buffer. A <t>Bradford</t> curve using <t>BSA</t> as a standard was used for protein quantification and 30 μg of protein was separated on a 12.5% SDS-PAGE gel. Actin was used an as internal standard to ensure consistent loading and to normalize all samples. ImageJ was used to quantify intensity of bands. Phosphorylation levels were calculated by dividing the phosphorylation by the unphosphorylated and the phosphorylated form of the protein. Numerical data are summarized as means ± SEM. ∗ p
    Bsa, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bsa/product/Gold Biotechnology Inc
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    Gold Biotechnology Inc blasticidin
    IgM facilitates Leishmania parasites clumping which promotes hybrid formation in vitro. ( a ) Leishmania hybrids genotyping by PCR targeting parental selectable drug markers HYG (Hygromycin) and BSD <t>(Blasticidin).</t> ( b ) Phase contrast image of L. major in culture media containing 20% fetal bovine serum (FBS) without (bottom panel) or with 5% adult inactivated dog serum (top panel). Images taken 30 min after cells were seeded in fresh media. Scale bars = 20 µm. ( c ) Human IgM eluted from a HiTrap® IgM column. Leishmania clumping activity was observed in fractions F4-F8 corresponding to elution of IgM. (d) Presence (+) or absence (−) of L. major clumping activity in inactivated adult sera from different vertebrate species, FBS, or immunoglobulins (IgM, IgG, IgA) purified from adult bovine or human sera. ( e ) Western blot to detect IgM in FBS and adult bovine serum (ABS). Serum purified bovine IgM, positive control; serum albumin, loading control. ( f ) Phase contrast image of L. major in culture media containing 20% FBS with bovine IgM at 50 µg/mL after 24h and ( g ) with peanut agglutinin (PNA) at 50 µg/mL after 24h. Scale bars = 50 µm. ( h ) Phase contrast image of L. major in culture media containing 20% FBS with bovine IgM (pentameric form) at 50 µg/mL after 24h or ( i ) with bovine IgM (monomeric form) at 50 µg/mL after 24h. ( j ) Clumping activity of various Leishmania species in the presence of bovine IgM at 50 µg/mL. ( k ) (top) Workflow for in vitro crossing of L. major parental lines. Mating wells were established with 50 µg/mL IgM in complete Schneider’s media. Double drug resistant hybrid parasites were cloned before genotyping. (bottom) Summary of data from in vitro crossing of parental lines. 1×2 (n=30), 1×3 (n=40), 2×3 (n=7). ( l ) Leishmania major hybrids genotyping by PCR targeting parental selectable drug markers HYG (Hygromycin), BSD (Blasticidin) and SAT (Nourseothricin). Parental 1, WR-SSU-HYG; Parental 2, FVI-FKP40-BSD; parental 3, FVI-FTL-SAT; ntc, no template control; L, 1kb plus ladder (Invitrogen).
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    Gold Biotechnology Inc streptomycin b sulfate
    IgM facilitates Leishmania parasites clumping which promotes hybrid formation in vitro. ( a ) Leishmania hybrids genotyping by PCR targeting parental selectable drug markers HYG (Hygromycin) and BSD <t>(Blasticidin).</t> ( b ) Phase contrast image of L. major in culture media containing 20% fetal bovine serum (FBS) without (bottom panel) or with 5% adult inactivated dog serum (top panel). Images taken 30 min after cells were seeded in fresh media. Scale bars = 20 µm. ( c ) Human IgM eluted from a HiTrap® IgM column. Leishmania clumping activity was observed in fractions F4-F8 corresponding to elution of IgM. (d) Presence (+) or absence (−) of L. major clumping activity in inactivated adult sera from different vertebrate species, FBS, or immunoglobulins (IgM, IgG, IgA) purified from adult bovine or human sera. ( e ) Western blot to detect IgM in FBS and adult bovine serum (ABS). Serum purified bovine IgM, positive control; serum albumin, loading control. ( f ) Phase contrast image of L. major in culture media containing 20% FBS with bovine IgM at 50 µg/mL after 24h and ( g ) with peanut agglutinin (PNA) at 50 µg/mL after 24h. Scale bars = 50 µm. ( h ) Phase contrast image of L. major in culture media containing 20% FBS with bovine IgM (pentameric form) at 50 µg/mL after 24h or ( i ) with bovine IgM (monomeric form) at 50 µg/mL after 24h. ( j ) Clumping activity of various Leishmania species in the presence of bovine IgM at 50 µg/mL. ( k ) (top) Workflow for in vitro crossing of L. major parental lines. Mating wells were established with 50 µg/mL IgM in complete Schneider’s media. Double drug resistant hybrid parasites were cloned before genotyping. (bottom) Summary of data from in vitro crossing of parental lines. 1×2 (n=30), 1×3 (n=40), 2×3 (n=7). ( l ) Leishmania major hybrids genotyping by PCR targeting parental selectable drug markers HYG (Hygromycin), BSD (Blasticidin) and SAT (Nourseothricin). Parental 1, WR-SSU-HYG; Parental 2, FVI-FKP40-BSD; parental 3, FVI-FTL-SAT; ntc, no template control; L, 1kb plus ladder (Invitrogen).
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    Image Search Results


    Treatments effect mTORC1 activation in the stomach. Representative Western blot of the pattern observed in REDD and HFD treated (A) males and (B) females comparing the expression of the mTORC1 pathway in the stomach. Actin was used as an internal control. All samples were run in parallel. Images were minimally adjusted in contrast and brightness. Relative quantification of (C) pAKT-T308 for male (top) and female (bottom), (D) pAKT-S473 for male (top) and female (bottom), and (E) pS6K for male (left) and female (right) by densitometry analysis of Western blots. Proteins were extracted by homogenizing tissue in RIPA buffer. A Bradford curve using BSA as a standard was used for protein quantification and 30 μg of protein was separated on a 12.5% SDS-PAGE gel. Actin was used an as internal standard to ensure consistent loading and to normalize all samples. ImageJ was used to quantify intensity of bands. Phosphorylation levels were calculated by dividing the phosphorylation by the unphosphorylated and the phosphorylated form of the protein. Numerical data are summarized as means ± SEM. ∗ p

    Journal: Frontiers in Microbiology

    Article Title: Sex Modulates Lactobacillus johnsonii N6.2 and Phytophenol Effectiveness in Reducing High Fat Diet Induced mTOR Activation in Sprague-Dawley Rats

    doi: 10.3389/fmicb.2018.02649

    Figure Lengend Snippet: Treatments effect mTORC1 activation in the stomach. Representative Western blot of the pattern observed in REDD and HFD treated (A) males and (B) females comparing the expression of the mTORC1 pathway in the stomach. Actin was used as an internal control. All samples were run in parallel. Images were minimally adjusted in contrast and brightness. Relative quantification of (C) pAKT-T308 for male (top) and female (bottom), (D) pAKT-S473 for male (top) and female (bottom), and (E) pS6K for male (left) and female (right) by densitometry analysis of Western blots. Proteins were extracted by homogenizing tissue in RIPA buffer. A Bradford curve using BSA as a standard was used for protein quantification and 30 μg of protein was separated on a 12.5% SDS-PAGE gel. Actin was used an as internal standard to ensure consistent loading and to normalize all samples. ImageJ was used to quantify intensity of bands. Phosphorylation levels were calculated by dividing the phosphorylation by the unphosphorylated and the phosphorylated form of the protein. Numerical data are summarized as means ± SEM. ∗ p

    Article Snippet: Briefly, membranes probing for unphosphorylated markers were blocked in 5% non-fat dry milk, while membranes probing for phosphorylated markers were blocked in 5% BSA (Gold Biotechnology, St. Louis, MO, United States) for 1 h at 4°C.

    Techniques: Activation Assay, Western Blot, Expressing, SDS Page

    IgM facilitates Leishmania parasites clumping which promotes hybrid formation in vitro. ( a ) Leishmania hybrids genotyping by PCR targeting parental selectable drug markers HYG (Hygromycin) and BSD (Blasticidin). ( b ) Phase contrast image of L. major in culture media containing 20% fetal bovine serum (FBS) without (bottom panel) or with 5% adult inactivated dog serum (top panel). Images taken 30 min after cells were seeded in fresh media. Scale bars = 20 µm. ( c ) Human IgM eluted from a HiTrap® IgM column. Leishmania clumping activity was observed in fractions F4-F8 corresponding to elution of IgM. (d) Presence (+) or absence (−) of L. major clumping activity in inactivated adult sera from different vertebrate species, FBS, or immunoglobulins (IgM, IgG, IgA) purified from adult bovine or human sera. ( e ) Western blot to detect IgM in FBS and adult bovine serum (ABS). Serum purified bovine IgM, positive control; serum albumin, loading control. ( f ) Phase contrast image of L. major in culture media containing 20% FBS with bovine IgM at 50 µg/mL after 24h and ( g ) with peanut agglutinin (PNA) at 50 µg/mL after 24h. Scale bars = 50 µm. ( h ) Phase contrast image of L. major in culture media containing 20% FBS with bovine IgM (pentameric form) at 50 µg/mL after 24h or ( i ) with bovine IgM (monomeric form) at 50 µg/mL after 24h. ( j ) Clumping activity of various Leishmania species in the presence of bovine IgM at 50 µg/mL. ( k ) (top) Workflow for in vitro crossing of L. major parental lines. Mating wells were established with 50 µg/mL IgM in complete Schneider’s media. Double drug resistant hybrid parasites were cloned before genotyping. (bottom) Summary of data from in vitro crossing of parental lines. 1×2 (n=30), 1×3 (n=40), 2×3 (n=7). ( l ) Leishmania major hybrids genotyping by PCR targeting parental selectable drug markers HYG (Hygromycin), BSD (Blasticidin) and SAT (Nourseothricin). Parental 1, WR-SSU-HYG; Parental 2, FVI-FKP40-BSD; parental 3, FVI-FTL-SAT; ntc, no template control; L, 1kb plus ladder (Invitrogen).

    Journal: bioRxiv

    Article Title: Genetic exchange in Leishmania is facilitated by IgM natural antibodies

    doi: 10.1101/2022.06.09.495557

    Figure Lengend Snippet: IgM facilitates Leishmania parasites clumping which promotes hybrid formation in vitro. ( a ) Leishmania hybrids genotyping by PCR targeting parental selectable drug markers HYG (Hygromycin) and BSD (Blasticidin). ( b ) Phase contrast image of L. major in culture media containing 20% fetal bovine serum (FBS) without (bottom panel) or with 5% adult inactivated dog serum (top panel). Images taken 30 min after cells were seeded in fresh media. Scale bars = 20 µm. ( c ) Human IgM eluted from a HiTrap® IgM column. Leishmania clumping activity was observed in fractions F4-F8 corresponding to elution of IgM. (d) Presence (+) or absence (−) of L. major clumping activity in inactivated adult sera from different vertebrate species, FBS, or immunoglobulins (IgM, IgG, IgA) purified from adult bovine or human sera. ( e ) Western blot to detect IgM in FBS and adult bovine serum (ABS). Serum purified bovine IgM, positive control; serum albumin, loading control. ( f ) Phase contrast image of L. major in culture media containing 20% FBS with bovine IgM at 50 µg/mL after 24h and ( g ) with peanut agglutinin (PNA) at 50 µg/mL after 24h. Scale bars = 50 µm. ( h ) Phase contrast image of L. major in culture media containing 20% FBS with bovine IgM (pentameric form) at 50 µg/mL after 24h or ( i ) with bovine IgM (monomeric form) at 50 µg/mL after 24h. ( j ) Clumping activity of various Leishmania species in the presence of bovine IgM at 50 µg/mL. ( k ) (top) Workflow for in vitro crossing of L. major parental lines. Mating wells were established with 50 µg/mL IgM in complete Schneider’s media. Double drug resistant hybrid parasites were cloned before genotyping. (bottom) Summary of data from in vitro crossing of parental lines. 1×2 (n=30), 1×3 (n=40), 2×3 (n=7). ( l ) Leishmania major hybrids genotyping by PCR targeting parental selectable drug markers HYG (Hygromycin), BSD (Blasticidin) and SAT (Nourseothricin). Parental 1, WR-SSU-HYG; Parental 2, FVI-FKP40-BSD; parental 3, FVI-FTL-SAT; ntc, no template control; L, 1kb plus ladder (Invitrogen).

    Article Snippet: The concentration used for each selective drug was as follows: Hygromycin B - 100 µg/mL (Goldbio, H270); Blasticidin - 10 µg/mL (Goldbio, B-800-500); Nourseothricin - 100 µg/mL (Goldbio, N-500-100).

    Techniques: In Vitro, Genotyping Assay, Polymerase Chain Reaction, Activity Assay, Purification, Western Blot, Positive Control, Clone Assay