neuropeptide y porcine  (Echelon Biosciences)


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    Echelon Biosciences neuropeptide y porcine
    ELISA demonstration of complement-mediated  formation of complexes of Aβ  with C3 activation fragments ( a– d   ). Complexes were captured,  detected, and quantitated as described in Materials and Methods. NHS or purified ACP proteins only do not contain Aβ. ( a )  Preaggregated Aβ 1–42 (100  μM and 50 μM) was incubated  in NHS, captured with mAb to  C3b, and detected with rabbit  Ab to Aβ. ( b ) Two preaggregated Aβ 1–42 preparations (Aβ  1 and Aβ 2, at 20 μM) were incubated in NHS, captured with  mAb to iC3b, and detected with  rabbit Ab to Aβ. ( c ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, or in NHS  containing 10 mM EDTA, captured with mAb to Aβ, and detected with rabbit Ab to C3. ( d   ) Preaggregated Aβ 1–42 was incubated in NHS at the indicated final concentrations, captured with mAb to Aβ, and  detected with rabbit Ab to C3. ( e ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, factor B–depleted NHS ( B-dpl   ), or C1q-depleted NHS  ( C1q-dpl   ), captured with mAb to Aβ, and detected with rabbit Ab to C3. ( f    ) Preaggregated Aβ 1–42 (58 μM) was incubated with the six purified ACP  proteins ( PAP ) or NHS, captured with mAb to Aβ, and detected with rabbit Ab to C3. Background levels obtained in EDTA controls containing Aβ  and purified ACP proteins or NHS, in the various experiments described above, were subtracted. (   g ) Specificity of complement activation. Preaggregated  Aβ preparations (20 μM) and the same concentrations of monomeric Aβ ( mono ), insulin B chain ( Ins.B ), neuropeptide Y-porcine ( NPY ), urotensin I  ( Uro. ), exendin 3 ( Exen ), amyloid precursor peptide 657–676 ( APP-pep. ), and adenovirus penton base 50-residue peptide ( PB50 ) were incubated with  NHS. Complement activation was assessed by the CH50 method. Correlation coefficients for the CH50 determinations ranged from 0.995 to 1.000.
    Neuropeptide Y Porcine, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/neuropeptide y porcine/product/Echelon Biosciences
    Average 80 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    neuropeptide y porcine - by Bioz Stars, 2022-12
    80/100 stars

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    1) Product Images from "Complement-dependent Proinflammatory Properties of the Alzheimer's Disease ?-Peptide "

    Article Title: Complement-dependent Proinflammatory Properties of the Alzheimer's Disease ?-Peptide

    Journal: The Journal of Experimental Medicine

    doi:

    ELISA demonstration of complement-mediated  formation of complexes of Aβ  with C3 activation fragments ( a– d   ). Complexes were captured,  detected, and quantitated as described in Materials and Methods. NHS or purified ACP proteins only do not contain Aβ. ( a )  Preaggregated Aβ 1–42 (100  μM and 50 μM) was incubated  in NHS, captured with mAb to  C3b, and detected with rabbit  Ab to Aβ. ( b ) Two preaggregated Aβ 1–42 preparations (Aβ  1 and Aβ 2, at 20 μM) were incubated in NHS, captured with  mAb to iC3b, and detected with  rabbit Ab to Aβ. ( c ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, or in NHS  containing 10 mM EDTA, captured with mAb to Aβ, and detected with rabbit Ab to C3. ( d   ) Preaggregated Aβ 1–42 was incubated in NHS at the indicated final concentrations, captured with mAb to Aβ, and  detected with rabbit Ab to C3. ( e ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, factor B–depleted NHS ( B-dpl   ), or C1q-depleted NHS  ( C1q-dpl   ), captured with mAb to Aβ, and detected with rabbit Ab to C3. ( f    ) Preaggregated Aβ 1–42 (58 μM) was incubated with the six purified ACP  proteins ( PAP ) or NHS, captured with mAb to Aβ, and detected with rabbit Ab to C3. Background levels obtained in EDTA controls containing Aβ  and purified ACP proteins or NHS, in the various experiments described above, were subtracted. (   g ) Specificity of complement activation. Preaggregated  Aβ preparations (20 μM) and the same concentrations of monomeric Aβ ( mono ), insulin B chain ( Ins.B ), neuropeptide Y-porcine ( NPY ), urotensin I  ( Uro. ), exendin 3 ( Exen ), amyloid precursor peptide 657–676 ( APP-pep. ), and adenovirus penton base 50-residue peptide ( PB50 ) were incubated with  NHS. Complement activation was assessed by the CH50 method. Correlation coefficients for the CH50 determinations ranged from 0.995 to 1.000.
    Figure Legend Snippet: ELISA demonstration of complement-mediated formation of complexes of Aβ with C3 activation fragments ( a– d   ). Complexes were captured, detected, and quantitated as described in Materials and Methods. NHS or purified ACP proteins only do not contain Aβ. ( a ) Preaggregated Aβ 1–42 (100 μM and 50 μM) was incubated in NHS, captured with mAb to C3b, and detected with rabbit Ab to Aβ. ( b ) Two preaggregated Aβ 1–42 preparations (Aβ 1 and Aβ 2, at 20 μM) were incubated in NHS, captured with mAb to iC3b, and detected with rabbit Ab to Aβ. ( c ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, or in NHS containing 10 mM EDTA, captured with mAb to Aβ, and detected with rabbit Ab to C3. ( d   ) Preaggregated Aβ 1–42 was incubated in NHS at the indicated final concentrations, captured with mAb to Aβ, and detected with rabbit Ab to C3. ( e ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, factor B–depleted NHS ( B-dpl   ), or C1q-depleted NHS ( C1q-dpl   ), captured with mAb to Aβ, and detected with rabbit Ab to C3. ( f    ) Preaggregated Aβ 1–42 (58 μM) was incubated with the six purified ACP proteins ( PAP ) or NHS, captured with mAb to Aβ, and detected with rabbit Ab to C3. Background levels obtained in EDTA controls containing Aβ and purified ACP proteins or NHS, in the various experiments described above, were subtracted. (   g ) Specificity of complement activation. Preaggregated Aβ preparations (20 μM) and the same concentrations of monomeric Aβ ( mono ), insulin B chain ( Ins.B ), neuropeptide Y-porcine ( NPY ), urotensin I ( Uro. ), exendin 3 ( Exen ), amyloid precursor peptide 657–676 ( APP-pep. ), and adenovirus penton base 50-residue peptide ( PB50 ) were incubated with NHS. Complement activation was assessed by the CH50 method. Correlation coefficients for the CH50 determinations ranged from 0.995 to 1.000.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Activation Assay, Purification, Incubation

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    Echelon Biosciences neuropeptide y porcine
    ELISA demonstration of complement-mediated  formation of complexes of Aβ  with C3 activation fragments ( a– d   ). Complexes were captured,  detected, and quantitated as described in Materials and Methods. NHS or purified ACP proteins only do not contain Aβ. ( a )  Preaggregated Aβ 1–42 (100  μM and 50 μM) was incubated  in NHS, captured with mAb to  C3b, and detected with rabbit  Ab to Aβ. ( b ) Two preaggregated Aβ 1–42 preparations (Aβ  1 and Aβ 2, at 20 μM) were incubated in NHS, captured with  mAb to iC3b, and detected with  rabbit Ab to Aβ. ( c ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, or in NHS  containing 10 mM EDTA, captured with mAb to Aβ, and detected with rabbit Ab to C3. ( d   ) Preaggregated Aβ 1–42 was incubated in NHS at the indicated final concentrations, captured with mAb to Aβ, and  detected with rabbit Ab to C3. ( e ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, factor B–depleted NHS ( B-dpl   ), or C1q-depleted NHS  ( C1q-dpl   ), captured with mAb to Aβ, and detected with rabbit Ab to C3. ( f    ) Preaggregated Aβ 1–42 (58 μM) was incubated with the six purified ACP  proteins ( PAP ) or NHS, captured with mAb to Aβ, and detected with rabbit Ab to C3. Background levels obtained in EDTA controls containing Aβ  and purified ACP proteins or NHS, in the various experiments described above, were subtracted. (   g ) Specificity of complement activation. Preaggregated  Aβ preparations (20 μM) and the same concentrations of monomeric Aβ ( mono ), insulin B chain ( Ins.B ), neuropeptide Y-porcine ( NPY ), urotensin I  ( Uro. ), exendin 3 ( Exen ), amyloid precursor peptide 657–676 ( APP-pep. ), and adenovirus penton base 50-residue peptide ( PB50 ) were incubated with  NHS. Complement activation was assessed by the CH50 method. Correlation coefficients for the CH50 determinations ranged from 0.995 to 1.000.
    Neuropeptide Y Porcine, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/neuropeptide y porcine/product/Echelon Biosciences
    Average 80 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    neuropeptide y porcine - by Bioz Stars, 2022-12
    80/100 stars
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    ELISA demonstration of complement-mediated  formation of complexes of Aβ  with C3 activation fragments ( a– d   ). Complexes were captured,  detected, and quantitated as described in Materials and Methods. NHS or purified ACP proteins only do not contain Aβ. ( a )  Preaggregated Aβ 1–42 (100  μM and 50 μM) was incubated  in NHS, captured with mAb to  C3b, and detected with rabbit  Ab to Aβ. ( b ) Two preaggregated Aβ 1–42 preparations (Aβ  1 and Aβ 2, at 20 μM) were incubated in NHS, captured with  mAb to iC3b, and detected with  rabbit Ab to Aβ. ( c ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, or in NHS  containing 10 mM EDTA, captured with mAb to Aβ, and detected with rabbit Ab to C3. ( d   ) Preaggregated Aβ 1–42 was incubated in NHS at the indicated final concentrations, captured with mAb to Aβ, and  detected with rabbit Ab to C3. ( e ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, factor B–depleted NHS ( B-dpl   ), or C1q-depleted NHS  ( C1q-dpl   ), captured with mAb to Aβ, and detected with rabbit Ab to C3. ( f    ) Preaggregated Aβ 1–42 (58 μM) was incubated with the six purified ACP  proteins ( PAP ) or NHS, captured with mAb to Aβ, and detected with rabbit Ab to C3. Background levels obtained in EDTA controls containing Aβ  and purified ACP proteins or NHS, in the various experiments described above, were subtracted. (   g ) Specificity of complement activation. Preaggregated  Aβ preparations (20 μM) and the same concentrations of monomeric Aβ ( mono ), insulin B chain ( Ins.B ), neuropeptide Y-porcine ( NPY ), urotensin I  ( Uro. ), exendin 3 ( Exen ), amyloid precursor peptide 657–676 ( APP-pep. ), and adenovirus penton base 50-residue peptide ( PB50 ) were incubated with  NHS. Complement activation was assessed by the CH50 method. Correlation coefficients for the CH50 determinations ranged from 0.995 to 1.000.

    Journal: The Journal of Experimental Medicine

    Article Title: Complement-dependent Proinflammatory Properties of the Alzheimer's Disease ?-Peptide

    doi:

    Figure Lengend Snippet: ELISA demonstration of complement-mediated formation of complexes of Aβ with C3 activation fragments ( a– d   ). Complexes were captured, detected, and quantitated as described in Materials and Methods. NHS or purified ACP proteins only do not contain Aβ. ( a ) Preaggregated Aβ 1–42 (100 μM and 50 μM) was incubated in NHS, captured with mAb to C3b, and detected with rabbit Ab to Aβ. ( b ) Two preaggregated Aβ 1–42 preparations (Aβ 1 and Aβ 2, at 20 μM) were incubated in NHS, captured with mAb to iC3b, and detected with rabbit Ab to Aβ. ( c ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, or in NHS containing 10 mM EDTA, captured with mAb to Aβ, and detected with rabbit Ab to C3. ( d   ) Preaggregated Aβ 1–42 was incubated in NHS at the indicated final concentrations, captured with mAb to Aβ, and detected with rabbit Ab to C3. ( e ) Preaggregated Aβ 1–42 (58 μM) was incubated in NHS, factor B–depleted NHS ( B-dpl   ), or C1q-depleted NHS ( C1q-dpl   ), captured with mAb to Aβ, and detected with rabbit Ab to C3. ( f    ) Preaggregated Aβ 1–42 (58 μM) was incubated with the six purified ACP proteins ( PAP ) or NHS, captured with mAb to Aβ, and detected with rabbit Ab to C3. Background levels obtained in EDTA controls containing Aβ and purified ACP proteins or NHS, in the various experiments described above, were subtracted. (   g ) Specificity of complement activation. Preaggregated Aβ preparations (20 μM) and the same concentrations of monomeric Aβ ( mono ), insulin B chain ( Ins.B ), neuropeptide Y-porcine ( NPY ), urotensin I ( Uro. ), exendin 3 ( Exen ), amyloid precursor peptide 657–676 ( APP-pep. ), and adenovirus penton base 50-residue peptide ( PB50 ) were incubated with NHS. Complement activation was assessed by the CH50 method. Correlation coefficients for the CH50 determinations ranged from 0.995 to 1.000.

    Article Snippet: In some experiments, neuropeptide Y-porcine, urotensin I, or exendin 3 (all from California Peptide Research, Inc.); insulin B chain ( Sigma Chemical Co. ); amyloid precursor protein peptide (657– 676 (Bachem California); and adenovirus penton base 50-residue fragment (residues 317–366; reference ), as well as preaggregated Aβ 1–42 preparations and monomeric Aβ 1–42, were dissolved in DMSO or ddH2 O and aged at room temperature, exactly as described above for Aβ.

    Techniques: Enzyme-linked Immunosorbent Assay, Activation Assay, Purification, Incubation