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rabbit purified immunoglobulin g conjugated to alkaline phosphatase  (Cedarlane)


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    Cedarlane rabbit purified immunoglobulin g conjugated to alkaline phosphatase
    Antibodies used (listed in alphabetical order) for Western blotting (WB) and (or) immunogold labeling (IGL).
    Rabbit Purified Immunoglobulin G Conjugated To Alkaline Phosphatase, supplied by Cedarlane, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+salmonid+ig/Anti-Salmonid+Ig+(H%2BL)%2C+Purified%2C+(Polyclonal)+(rabbit+IgG)/pmc11763710-49-3-16
    Average 93 stars, based on 7 article reviews
    rabbit purified immunoglobulin g conjugated to alkaline phosphatase - by Bioz Stars, 2026-09
    93/100 stars

    Images

    1) Product Images from "The Passage of Chaperonins to Extracellular Locations in Legionella pneumophila Requires a Functional Dot/Icm System"

    Article Title: The Passage of Chaperonins to Extracellular Locations in Legionella pneumophila Requires a Functional Dot/Icm System

    Journal: Biomolecules

    doi: 10.3390/biom15010091

    Antibodies used (listed in alphabetical order) for Western blotting (WB) and (or) immunogold labeling (IGL).
    Figure Legend Snippet: Antibodies used (listed in alphabetical order) for Western blotting (WB) and (or) immunogold labeling (IGL).

    Techniques Used: Western Blot, Labeling, Recombinant, Cell Culture, Purification

    Immunoblots of SDS-PAGE-resolved proteins from whole bacterial cells treated with trypsin (250 µg trypsin/10 9 bacteria), and immunostained with an HtpB-specific monoclonal antibody and alkaline phosphatase-conjugated rabbit anti-mouse IgG. ( A ) Band patterns produced in the wild-type strain Lp02 and its dotA − derivative JV309. Trypsin-accessible HtpB is evidenced by the immunolabeled degradation products of <60 kDa. The presence of trypsin-accessible HtpB was recovered in the trans -complemented dotA − mutant ( dotA − + C). ( B , C ) Band patterns showing the lack of trypsin-accessible HtpB in two different dotB mutants: dotB − (with a loss-of-function point mutation), and Δ dotB (with a deletion of the dotB gene). A recovery of trypsin-accessible HtpB was observed in trans -complemented dotB mutants ( dotB + C and Δ dotB + C), but not in the mock-complemented mutants carrying an empty vector ( dotB + V and Δ dotB + V). Abbreviations for all panels: “C” = control, trypsin-free sample, “T” = trypsin-treated sample. Arrows at the far left indicate the position of three of the broad-range pre-stained protein size markers (New England Biolabs, Whitby, ON, Canada) corresponding to (from top to bottom) 62, 47 and 37.5 kDa.
    Figure Legend Snippet: Immunoblots of SDS-PAGE-resolved proteins from whole bacterial cells treated with trypsin (250 µg trypsin/10 9 bacteria), and immunostained with an HtpB-specific monoclonal antibody and alkaline phosphatase-conjugated rabbit anti-mouse IgG. ( A ) Band patterns produced in the wild-type strain Lp02 and its dotA − derivative JV309. Trypsin-accessible HtpB is evidenced by the immunolabeled degradation products of <60 kDa. The presence of trypsin-accessible HtpB was recovered in the trans -complemented dotA − mutant ( dotA − + C). ( B , C ) Band patterns showing the lack of trypsin-accessible HtpB in two different dotB mutants: dotB − (with a loss-of-function point mutation), and Δ dotB (with a deletion of the dotB gene). A recovery of trypsin-accessible HtpB was observed in trans -complemented dotB mutants ( dotB + C and Δ dotB + C), but not in the mock-complemented mutants carrying an empty vector ( dotB + V and Δ dotB + V). Abbreviations for all panels: “C” = control, trypsin-free sample, “T” = trypsin-treated sample. Arrows at the far left indicate the position of three of the broad-range pre-stained protein size markers (New England Biolabs, Whitby, ON, Canada) corresponding to (from top to bottom) 62, 47 and 37.5 kDa.

    Techniques Used: Western Blot, SDS Page, Bacteria, Produced, Immunolabeling, Mutagenesis, Plasmid Preparation, Control, Staining

    Related Articles

    Incubation:

    Article Title: Cell death induced by Lepeophtheirus salmonis labial gland protein 3 in salmonid fish leukocytes: A mechanism for disabling host immune responses.
    Article Snippet: .. Thereafter, non-adherent leukocytes were incubated with 1:200 diluted Anti-Salmonid Ig (H), FITC, (Clone IPA5F12, Cat no. 177-CLF004F, Cedarlane) at a cell density of 5 x 106 in PBS +0.5 % BSA in the dark (on ice, 30 min, gentle shaking). ..

    Article Title: Evaluation of Immune Status in Two Cohorts of Atlantic Salmon Raised in Different Aquaculture Systems (Case Study)
    Article Snippet: .. Nunc MaxiSorp plates (Thermo Fisher Scientific, Waltham, MA, USA) were coated with anti-salmonid Ig (heavy chain) monoclonal antibody supernatant (CLF004 from Cedarlane, Burlington, ON, Canada) diluted in carbonate buffer pH = 9.6 to an end concentration of 0.3 μg/mL and incubated for 48 h at 4 °C. .. Plates were washed 3 times with wash buffer (R&D systems) before the addition of blocking buffer (wash buffer + 4% horse serum (in-house) and an incubation for 2 h at RT).

    Gentle:

    Article Title: Cell death induced by Lepeophtheirus salmonis labial gland protein 3 in salmonid fish leukocytes: A mechanism for disabling host immune responses.
    Article Snippet: .. Thereafter, non-adherent leukocytes were incubated with 1:200 diluted Anti-Salmonid Ig (H), FITC, (Clone IPA5F12, Cat no. 177-CLF004F, Cedarlane) at a cell density of 5 x 106 in PBS +0.5 % BSA in the dark (on ice, 30 min, gentle shaking). ..

    Concentration Assay:

    Article Title: Evaluation of Immune Status in Two Cohorts of Atlantic Salmon Raised in Different Aquaculture Systems (Case Study)
    Article Snippet: .. Nunc MaxiSorp plates (Thermo Fisher Scientific, Waltham, MA, USA) were coated with anti-salmonid Ig (heavy chain) monoclonal antibody supernatant (CLF004 from Cedarlane, Burlington, ON, Canada) diluted in carbonate buffer pH = 9.6 to an end concentration of 0.3 μg/mL and incubated for 48 h at 4 °C. .. Plates were washed 3 times with wash buffer (R&D systems) before the addition of blocking buffer (wash buffer + 4% horse serum (in-house) and an incubation for 2 h at RT).



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    Cedarlane rabbit purified immunoglobulin g conjugated to alkaline phosphatase
    Antibodies used (listed in alphabetical order) for Western blotting (WB) and (or) immunogold labeling (IGL).
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    Image Search Results


    Antibodies used (listed in alphabetical order) for Western blotting (WB) and (or) immunogold labeling (IGL).

    Journal: Biomolecules

    Article Title: The Passage of Chaperonins to Extracellular Locations in Legionella pneumophila Requires a Functional Dot/Icm System

    doi: 10.3390/biom15010091

    Figure Lengend Snippet: Antibodies used (listed in alphabetical order) for Western blotting (WB) and (or) immunogold labeling (IGL).

    Article Snippet: αMouseAP , Commercial rabbit purified immunoglobulin G conjugated to alkaline phosphatase. Diluted 1:5000 for WB , Cedarlane Labs 5.

    Techniques: Western Blot, Labeling, Recombinant, Cell Culture, Purification

    Immunoblots of SDS-PAGE-resolved proteins from whole bacterial cells treated with trypsin (250 µg trypsin/10 9 bacteria), and immunostained with an HtpB-specific monoclonal antibody and alkaline phosphatase-conjugated rabbit anti-mouse IgG. ( A ) Band patterns produced in the wild-type strain Lp02 and its dotA − derivative JV309. Trypsin-accessible HtpB is evidenced by the immunolabeled degradation products of <60 kDa. The presence of trypsin-accessible HtpB was recovered in the trans -complemented dotA − mutant ( dotA − + C). ( B , C ) Band patterns showing the lack of trypsin-accessible HtpB in two different dotB mutants: dotB − (with a loss-of-function point mutation), and Δ dotB (with a deletion of the dotB gene). A recovery of trypsin-accessible HtpB was observed in trans -complemented dotB mutants ( dotB + C and Δ dotB + C), but not in the mock-complemented mutants carrying an empty vector ( dotB + V and Δ dotB + V). Abbreviations for all panels: “C” = control, trypsin-free sample, “T” = trypsin-treated sample. Arrows at the far left indicate the position of three of the broad-range pre-stained protein size markers (New England Biolabs, Whitby, ON, Canada) corresponding to (from top to bottom) 62, 47 and 37.5 kDa.

    Journal: Biomolecules

    Article Title: The Passage of Chaperonins to Extracellular Locations in Legionella pneumophila Requires a Functional Dot/Icm System

    doi: 10.3390/biom15010091

    Figure Lengend Snippet: Immunoblots of SDS-PAGE-resolved proteins from whole bacterial cells treated with trypsin (250 µg trypsin/10 9 bacteria), and immunostained with an HtpB-specific monoclonal antibody and alkaline phosphatase-conjugated rabbit anti-mouse IgG. ( A ) Band patterns produced in the wild-type strain Lp02 and its dotA − derivative JV309. Trypsin-accessible HtpB is evidenced by the immunolabeled degradation products of <60 kDa. The presence of trypsin-accessible HtpB was recovered in the trans -complemented dotA − mutant ( dotA − + C). ( B , C ) Band patterns showing the lack of trypsin-accessible HtpB in two different dotB mutants: dotB − (with a loss-of-function point mutation), and Δ dotB (with a deletion of the dotB gene). A recovery of trypsin-accessible HtpB was observed in trans -complemented dotB mutants ( dotB + C and Δ dotB + C), but not in the mock-complemented mutants carrying an empty vector ( dotB + V and Δ dotB + V). Abbreviations for all panels: “C” = control, trypsin-free sample, “T” = trypsin-treated sample. Arrows at the far left indicate the position of three of the broad-range pre-stained protein size markers (New England Biolabs, Whitby, ON, Canada) corresponding to (from top to bottom) 62, 47 and 37.5 kDa.

    Article Snippet: αMouseAP , Commercial rabbit purified immunoglobulin G conjugated to alkaline phosphatase. Diluted 1:5000 for WB , Cedarlane Labs 5.

    Techniques: Western Blot, SDS Page, Bacteria, Produced, Immunolabeling, Mutagenesis, Plasmid Preparation, Control, Staining