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blocking buffer iii bsa  (Applichem inc)

 
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    Applichem inc blocking buffer iii bsa
    Recombinant CspZ bound to human factor H (FH) and inactivated human alternative complement pathway in a variant-specific manner. A , recombinant GST-tagged proteins and GST (5 ng/μl each) were immobilized and incubated with 5 ng/μl of purified FH. Protein complexes were detected using an anti-FH antibody (1:1000 dilution). Data represent means and standard deviation of at least <t>three</t> independent experiments, each conducted in duplicate. ∗ p ≤ 0.0001, ns, no statistical significance, one-way ANOVA with post hoc Bonferroni multiple comparison test (confidence interval = 95%). B , the indicated untagged CspZ variants from Borrelia burgdorferi ( Bb ), Borrelia afzelii ( Ba ), or Borrelia garinii ( Bg ) were flowed in PBS buffer over the chip surface, conjugated with human FH. Binding was measured in response units (R.U.) by SPR. The k on , k off , and K D values were determined from the average of three experiments ( <xref ref-type=Table 1 ). Shown is one representative experiment. C , schematic representation showing the disulfide-linked α-, β-, and the γ-chains of C3b, with molecular weight presented, and the sites of α-chain cleavage by FH and FI indicated by arrows . D , microtiter plates coated in triplicate with BSA (“Ctrl,” control), GST, or purified GST-tagged CspZ proteins (1 μg each) were incubated with FH (1 μg) (two wells) or without FH (one well). Reaction mixtures only containing C3b (10 μg/μl) plus FI (20 μg/μl) or C3b were also included. Supernatants from the ELISA plate wells were immunoblotted with polyclonal anti-C3 antibody to detect cleavage products. BSA, bovine serum albumin; FI, factor I; GST, glutathione- S -transferase; SPR, surface plasmon resonance. " width="250" height="auto" />
    Blocking Buffer Iii Bsa, supplied by Applichem inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/blocking+buffer+iii+bsa/pmc11773018-220-17-20?v=Applichem+inc
    Average 90 stars, based on 1 article reviews
    blocking buffer iii bsa - by Bioz Stars, 2026-08
    90/100 stars

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    1) Product Images from "CspZ variant–specific interaction with factor H incorporates a metal site to support Lyme borreliae complement evasion"

    Article Title: CspZ variant–specific interaction with factor H incorporates a metal site to support Lyme borreliae complement evasion

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2024.108083

    Recombinant CspZ bound to human factor H (FH) and inactivated human alternative complement pathway in a variant-specific manner. A , recombinant GST-tagged proteins and GST (5 ng/μl each) were immobilized and incubated with 5 ng/μl of purified FH. Protein complexes were detected using an anti-FH antibody (1:1000 dilution). Data represent means and standard deviation of at least three independent experiments, each conducted in duplicate. ∗ p ≤ 0.0001, ns, no statistical significance, one-way ANOVA with post hoc Bonferroni multiple comparison test (confidence interval = 95%). B , the indicated untagged CspZ variants from Borrelia burgdorferi ( Bb ), Borrelia afzelii ( Ba ), or Borrelia garinii ( Bg ) were flowed in PBS buffer over the chip surface, conjugated with human FH. Binding was measured in response units (R.U.) by SPR. The k on , k off , and K D values were determined from the average of three experiments ( <xref ref-type=Table 1 ). Shown is one representative experiment. C , schematic representation showing the disulfide-linked α-, β-, and the γ-chains of C3b, with molecular weight presented, and the sites of α-chain cleavage by FH and FI indicated by arrows . D , microtiter plates coated in triplicate with BSA (“Ctrl,” control), GST, or purified GST-tagged CspZ proteins (1 μg each) were incubated with FH (1 μg) (two wells) or without FH (one well). Reaction mixtures only containing C3b (10 μg/μl) plus FI (20 μg/μl) or C3b were also included. Supernatants from the ELISA plate wells were immunoblotted with polyclonal anti-C3 antibody to detect cleavage products. BSA, bovine serum albumin; FI, factor I; GST, glutathione- S -transferase; SPR, surface plasmon resonance. " title="... represent means and standard deviation of at least three independent experiments, each conducted in duplicate. ∗ p ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Recombinant CspZ bound to human factor H (FH) and inactivated human alternative complement pathway in a variant-specific manner. A , recombinant GST-tagged proteins and GST (5 ng/μl each) were immobilized and incubated with 5 ng/μl of purified FH. Protein complexes were detected using an anti-FH antibody (1:1000 dilution). Data represent means and standard deviation of at least three independent experiments, each conducted in duplicate. ∗ p ≤ 0.0001, ns, no statistical significance, one-way ANOVA with post hoc Bonferroni multiple comparison test (confidence interval = 95%). B , the indicated untagged CspZ variants from Borrelia burgdorferi ( Bb ), Borrelia afzelii ( Ba ), or Borrelia garinii ( Bg ) were flowed in PBS buffer over the chip surface, conjugated with human FH. Binding was measured in response units (R.U.) by SPR. The k on , k off , and K D values were determined from the average of three experiments ( Table 1 ). Shown is one representative experiment. C , schematic representation showing the disulfide-linked α-, β-, and the γ-chains of C3b, with molecular weight presented, and the sites of α-chain cleavage by FH and FI indicated by arrows . D , microtiter plates coated in triplicate with BSA (“Ctrl,” control), GST, or purified GST-tagged CspZ proteins (1 μg each) were incubated with FH (1 μg) (two wells) or without FH (one well). Reaction mixtures only containing C3b (10 μg/μl) plus FI (20 μg/μl) or C3b were also included. Supernatants from the ELISA plate wells were immunoblotted with polyclonal anti-C3 antibody to detect cleavage products. BSA, bovine serum albumin; FI, factor I; GST, glutathione- S -transferase; SPR, surface plasmon resonance.

    Techniques Used: Recombinant, Variant Assay, Incubation, Purification, Standard Deviation, Comparison, Binding Assay, Molecular Weight, Control, Enzyme-linked Immunosorbent Assay, SPR Assay



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    blocking buffer iii bsa  (Applichem inc)
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    Recombinant CspZ bound to human factor H (FH) and inactivated human alternative complement pathway in a variant-specific manner. A , recombinant GST-tagged proteins and GST (5 ng/μl each) were immobilized and incubated with 5 ng/μl of purified FH. Protein complexes were detected using an anti-FH antibody (1:1000 dilution). Data represent means and standard deviation of at least three independent experiments, each conducted in duplicate. ∗ p ≤ 0.0001, ns, no statistical significance, one-way ANOVA with post hoc Bonferroni multiple comparison test (confidence interval = 95%). B , the indicated untagged CspZ variants from Borrelia burgdorferi ( Bb ), Borrelia afzelii ( Ba ), or Borrelia garinii ( Bg ) were flowed in PBS buffer over the chip surface, conjugated with human FH. Binding was measured in response units (R.U.) by SPR. The k on , k off , and K D values were determined from the average of three experiments ( <xref ref-type=Table 1 ). Shown is one representative experiment. C , schematic representation showing the disulfide-linked α-, β-, and the γ-chains of C3b, with molecular weight presented, and the sites of α-chain cleavage by FH and FI indicated by arrows . D , microtiter plates coated in triplicate with BSA (“Ctrl,” control), GST, or purified GST-tagged CspZ proteins (1 μg each) were incubated with FH (1 μg) (two wells) or without FH (one well). Reaction mixtures only containing C3b (10 μg/μl) plus FI (20 μg/μl) or C3b were also included. Supernatants from the ELISA plate wells were immunoblotted with polyclonal anti-C3 antibody to detect cleavage products. BSA, bovine serum albumin; FI, factor I; GST, glutathione- S -transferase; SPR, surface plasmon resonance. " width="100%" height="100%">

    Journal: The Journal of Biological Chemistry

    Article Title: CspZ variant–specific interaction with factor H incorporates a metal site to support Lyme borreliae complement evasion

    doi: 10.1016/j.jbc.2024.108083

    Figure Lengend Snippet: Recombinant CspZ bound to human factor H (FH) and inactivated human alternative complement pathway in a variant-specific manner. A , recombinant GST-tagged proteins and GST (5 ng/μl each) were immobilized and incubated with 5 ng/μl of purified FH. Protein complexes were detected using an anti-FH antibody (1:1000 dilution). Data represent means and standard deviation of at least three independent experiments, each conducted in duplicate. ∗ p ≤ 0.0001, ns, no statistical significance, one-way ANOVA with post hoc Bonferroni multiple comparison test (confidence interval = 95%). B , the indicated untagged CspZ variants from Borrelia burgdorferi ( Bb ), Borrelia afzelii ( Ba ), or Borrelia garinii ( Bg ) were flowed in PBS buffer over the chip surface, conjugated with human FH. Binding was measured in response units (R.U.) by SPR. The k on , k off , and K D values were determined from the average of three experiments ( Table 1 ). Shown is one representative experiment. C , schematic representation showing the disulfide-linked α-, β-, and the γ-chains of C3b, with molecular weight presented, and the sites of α-chain cleavage by FH and FI indicated by arrows . D , microtiter plates coated in triplicate with BSA (“Ctrl,” control), GST, or purified GST-tagged CspZ proteins (1 μg each) were incubated with FH (1 μg) (two wells) or without FH (one well). Reaction mixtures only containing C3b (10 μg/μl) plus FI (20 μg/μl) or C3b were also included. Supernatants from the ELISA plate wells were immunoblotted with polyclonal anti-C3 antibody to detect cleavage products. BSA, bovine serum albumin; FI, factor I; GST, glutathione- S -transferase; SPR, surface plasmon resonance.

    Article Snippet: Wells were washed three times with PBS containing 0.05% (v/v) Tween-20 (PBS-T) and then blocked with Blocking Buffer III BSA (AppliChem).

    Techniques: Recombinant, Variant Assay, Incubation, Purification, Standard Deviation, Comparison, Binding Assay, Molecular Weight, Control, Enzyme-linked Immunosorbent Assay, SPR Assay