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sds page 1x running buffer  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology sds page 1x running buffer
    Sds Page 1x Running Buffer, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 567 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sds+page+1x+running+buffer/bio_rxiv__2023__06__06__543873-222-11-28?v=Santa+Cruz+Biotechnology
    Average 95 stars, based on 567 article reviews
    sds page 1x running buffer - by Bioz Stars, 2026-08
    95/100 stars

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    (A) Western blot probed for total PLCγ1 content. Cells were transfected with either a Gads expression vector (“PLCγ1-mNG Null”, left lane) or PLCγ1-mNG vector (middle and rightmost lanes). PLCγ1-mNG lysates were loaded after either 0 min (middle) or 60 min (right) at RT to determine the stability of PLCγ1-mNG against degradation. Each lane was loaded with 1 µL of lysate. (B) Relative blot intensities (background corrected) for endogenous PLCγ1 (left, grey) versus transfected PLCγ1-mNG (right, green) normalized to endogenous levels (same lane) (n=2). (C) Western blot probed for pY783 with a series of time points and different kinase conditions. Phosphorylation reactions were conducted in 10 µL volumes containing 1 µL of PLCγ1-mNG lysate each, ATP, phosphatase inhibitor, and kinase in buffer. Reactions were kept at RT for the designated time, then quenched <t>with</t> <t>SDS-PAGE</t> loading buffer. Either no kinase, his6-Hck, or BTK-KD (Kinase Domain) was used. (D) Blot intensities (background corrected) of pPLCγ1-mNG relative to non-specific pY bands.
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    (A) Western blot probed for total PLCγ1 content. Cells were transfected with either a Gads expression vector (“PLCγ1-mNG Null”, left lane) or PLCγ1-mNG vector (middle and rightmost lanes). PLCγ1-mNG lysates were loaded after either 0 min (middle) or 60 min (right) at RT to determine the stability of PLCγ1-mNG against degradation. Each lane was loaded with 1 µL of lysate. (B) Relative blot intensities (background corrected) for endogenous PLCγ1 (left, grey) versus transfected PLCγ1-mNG (right, green) normalized to endogenous levels (same lane) (n=2). (C) Western blot probed for pY783 with a series of time points and different kinase conditions. Phosphorylation reactions were conducted in 10 µL volumes containing 1 µL of PLCγ1-mNG lysate each, ATP, phosphatase inhibitor, and kinase in buffer. Reactions were kept at RT for the designated time, then quenched <t>with</t> <t>SDS-PAGE</t> loading buffer. Either no kinase, his6-Hck, or BTK-KD (Kinase Domain) was used. (D) Blot intensities (background corrected) of pPLCγ1-mNG relative to non-specific pY bands.
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    (A) Western blot probed for total PLCγ1 content. Cells were transfected with either a Gads expression vector (“PLCγ1-mNG Null”, left lane) or PLCγ1-mNG vector (middle and rightmost lanes). PLCγ1-mNG lysates were loaded after either 0 min (middle) or 60 min (right) at RT to determine the stability of PLCγ1-mNG against degradation. Each lane was loaded with 1 µL of lysate. (B) Relative blot intensities (background corrected) for endogenous PLCγ1 (left, grey) versus transfected PLCγ1-mNG (right, green) normalized to endogenous levels (same lane) (n=2). (C) Western blot probed for pY783 with a series of time points and different kinase conditions. Phosphorylation reactions were conducted in 10 µL volumes containing 1 µL of PLCγ1-mNG lysate each, ATP, phosphatase inhibitor, and kinase in buffer. Reactions were kept at RT for the designated time, then quenched <t>with</t> <t>SDS-PAGE</t> loading buffer. Either no kinase, his6-Hck, or BTK-KD (Kinase Domain) was used. (D) Blot intensities (background corrected) of pPLCγ1-mNG relative to non-specific pY bands.
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    sds page 1x running buffer  (Santa Cruz Biotechnology)
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    (A) Western blot probed for total PLCγ1 content. Cells were transfected with either a Gads expression vector (“PLCγ1-mNG Null”, left lane) or PLCγ1-mNG vector (middle and rightmost lanes). PLCγ1-mNG lysates were loaded after either 0 min (middle) or 60 min (right) at RT to determine the stability of PLCγ1-mNG against degradation. Each lane was loaded with 1 µL of lysate. (B) Relative blot intensities (background corrected) for endogenous PLCγ1 (left, grey) versus transfected PLCγ1-mNG (right, green) normalized to endogenous levels (same lane) (n=2). (C) Western blot probed for pY783 with a series of time points and different kinase conditions. Phosphorylation reactions were conducted in 10 µL volumes containing 1 µL of PLCγ1-mNG lysate each, ATP, phosphatase inhibitor, and kinase in buffer. Reactions were kept at RT for the designated time, then quenched <t>with</t> <t>SDS-PAGE</t> loading buffer. Either no kinase, his6-Hck, or BTK-KD (Kinase Domain) was used. (D) Blot intensities (background corrected) of pPLCγ1-mNG relative to non-specific pY bands.
    Sds Page 1x Running Buffer, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (A) Western blot probed for total PLCγ1 content. Cells were transfected with either a Gads expression vector (“PLCγ1-mNG Null”, left lane) or PLCγ1-mNG vector (middle and rightmost lanes). PLCγ1-mNG lysates were loaded after either 0 min (middle) or 60 min (right) at RT to determine the stability of PLCγ1-mNG against degradation. Each lane was loaded with 1 µL of lysate. (B) Relative blot intensities (background corrected) for endogenous PLCγ1 (left, grey) versus transfected PLCγ1-mNG (right, green) normalized to endogenous levels (same lane) (n=2). (C) Western blot probed for pY783 with a series of time points and different kinase conditions. Phosphorylation reactions were conducted in 10 µL volumes containing 1 µL of PLCγ1-mNG lysate each, ATP, phosphatase inhibitor, and kinase in buffer. Reactions were kept at RT for the designated time, then quenched <t>with</t> <t>SDS-PAGE</t> loading buffer. Either no kinase, his6-Hck, or BTK-KD (Kinase Domain) was used. (D) Blot intensities (background corrected) of pPLCγ1-mNG relative to non-specific pY bands.
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    (A) Western blot probed for total PLCγ1 content. Cells were transfected with either a Gads expression vector (“PLCγ1-mNG Null”, left lane) or PLCγ1-mNG vector (middle and rightmost lanes). PLCγ1-mNG lysates were loaded after either 0 min (middle) or 60 min (right) at RT to determine the stability of PLCγ1-mNG against degradation. Each lane was loaded with 1 µL of lysate. (B) Relative blot intensities (background corrected) for endogenous PLCγ1 (left, grey) versus transfected PLCγ1-mNG (right, green) normalized to endogenous levels (same lane) (n=2). (C) Western blot probed for pY783 with a series of time points and different kinase conditions. Phosphorylation reactions were conducted in 10 µL volumes containing 1 µL of PLCγ1-mNG lysate each, ATP, phosphatase inhibitor, and kinase in buffer. Reactions were kept at RT for the designated time, then quenched <t>with</t> <t>SDS-PAGE</t> loading buffer. Either no kinase, his6-Hck, or BTK-KD (Kinase Domain) was used. (D) Blot intensities (background corrected) of pPLCγ1-mNG relative to non-specific pY bands.
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    Image Search Results


    (A) Western blot probed for total PLCγ1 content. Cells were transfected with either a Gads expression vector (“PLCγ1-mNG Null”, left lane) or PLCγ1-mNG vector (middle and rightmost lanes). PLCγ1-mNG lysates were loaded after either 0 min (middle) or 60 min (right) at RT to determine the stability of PLCγ1-mNG against degradation. Each lane was loaded with 1 µL of lysate. (B) Relative blot intensities (background corrected) for endogenous PLCγ1 (left, grey) versus transfected PLCγ1-mNG (right, green) normalized to endogenous levels (same lane) (n=2). (C) Western blot probed for pY783 with a series of time points and different kinase conditions. Phosphorylation reactions were conducted in 10 µL volumes containing 1 µL of PLCγ1-mNG lysate each, ATP, phosphatase inhibitor, and kinase in buffer. Reactions were kept at RT for the designated time, then quenched with SDS-PAGE loading buffer. Either no kinase, his6-Hck, or BTK-KD (Kinase Domain) was used. (D) Blot intensities (background corrected) of pPLCγ1-mNG relative to non-specific pY bands.

    Journal: bioRxiv

    Article Title: Supported membrane assay probes PLCγ1 activity in LAT condensates

    doi: 10.64898/2026.01.23.701188

    Figure Lengend Snippet: (A) Western blot probed for total PLCγ1 content. Cells were transfected with either a Gads expression vector (“PLCγ1-mNG Null”, left lane) or PLCγ1-mNG vector (middle and rightmost lanes). PLCγ1-mNG lysates were loaded after either 0 min (middle) or 60 min (right) at RT to determine the stability of PLCγ1-mNG against degradation. Each lane was loaded with 1 µL of lysate. (B) Relative blot intensities (background corrected) for endogenous PLCγ1 (left, grey) versus transfected PLCγ1-mNG (right, green) normalized to endogenous levels (same lane) (n=2). (C) Western blot probed for pY783 with a series of time points and different kinase conditions. Phosphorylation reactions were conducted in 10 µL volumes containing 1 µL of PLCγ1-mNG lysate each, ATP, phosphatase inhibitor, and kinase in buffer. Reactions were kept at RT for the designated time, then quenched with SDS-PAGE loading buffer. Either no kinase, his6-Hck, or BTK-KD (Kinase Domain) was used. (D) Blot intensities (background corrected) of pPLCγ1-mNG relative to non-specific pY bands.

    Article Snippet: 1 μL of lysate per lane was thawed, treated as stated, and run on SurePAGE 4-12% Bis-Tris SDS–PAGE gels (GenScript) in 1X MES SDS-PAGE buffer and transferred to nitrocellulose membranes (Invitrogen) in 1X NuPAGE Transfer Buffer (Invitrogen).

    Techniques: Western Blot, Transfection, Expressing, Plasmid Preparation, Phospho-proteomics, SDS Page