anti mouse igg1 gamma chain specific biotin antibody  (Millipore)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86
    Name:
    Anti Mouse IgG1 gamma chain specific Biotin antibody
    Description:
    Immunoglobulin G IgG belongs to the immunoglobulin family and is a widely expressed serum antibody It consists of a γ heavy chain in the constant C region The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa respectively The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains linking the heavy and light chains and resides inside the chains Maternal IgG is the only antibody transported across the placenta to the fetus It passively immunizes the infants IgG is further subdivided into four classes namely IgG1 IgG2 IgG3 and IgG4 with different heavy chains named γ1 γ2 γ3 and γ4 respectively IgG1 is induced due to antibody responses to membrane proteins and soluble protein antigens It is the most abundant subclass of IgG
    Catalog Number:
    SAB3701173
    Price:
    None
    Buy from Supplier


    Structured Review

    Millipore anti mouse igg1 gamma chain specific biotin antibody
    Immunoglobulin G IgG belongs to the immunoglobulin family and is a widely expressed serum antibody It consists of a γ heavy chain in the constant C region The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa respectively The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains linking the heavy and light chains and resides inside the chains Maternal IgG is the only antibody transported across the placenta to the fetus It passively immunizes the infants IgG is further subdivided into four classes namely IgG1 IgG2 IgG3 and IgG4 with different heavy chains named γ1 γ2 γ3 and γ4 respectively IgG1 is induced due to antibody responses to membrane proteins and soluble protein antigens It is the most abundant subclass of IgG
    https://www.bioz.com/result/anti mouse igg1 gamma chain specific biotin antibody/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti mouse igg1 gamma chain specific biotin antibody - by Bioz Stars, 2021-07
    86/100 stars

    Images

    Related Articles

    Staining:

    Article Title: Combinatorial genetics in liver repopulation and carcinogenesis with a novel in vivo CRISPR activation platform
    Article Snippet: For FAH staining we employed rabbit anti-FAH (ab81087, Abcam), and goat anti-rabbit for secondary antibody (Vector Labs). .. The dCas9 has a hemagglutinin (HA) tag, therefore we could stain tissues with a mouse anti-HA antibody (H3663, Sigma-Aldrich), and rabbit anti-mouse IgG1 secondary antibody (SAB3701173, Sigma-Aldrich). .. For MYC we used a rabbit anti-MYC antibody (sc764, Santa Cruz Biotechnology), and goat anti-rabbit as the secondary antibody (Vector Labs).

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93
    Millipore mouse anti rabbit β actin antibody
    Acute effect of BAC on the expression of ZO-1 mRNA and protein in the rabbit corneal epithelium. (A) Corneal epithelial cells isolated from a control eye or from eyes treated with 0.005%, 0.01% or 0.02% BAC were subjected to western blot analysis with antibodies to ZO-1 or <t>β</t> actin (loading control). (B) Qutantitative analysis of ZO-1 band intensity in bolts similar to those shown in (A). Data were normalized by the corresponding β actin band intensity and mean ± SE of values from three eyes per group. (C) Corneal epithelial cells isolated from a control eye or from eyes treated with 0.005%, 0.01% or 0.02% BAC were subjected to RT-PCR analysis of ZO-1 mRNA. (D) Quantitative analysis of ZO-1 band intensity in gel similar to that shown in (A). Data were normalized by the corresponding G3PDH band intensity and are mean±SE of values from three eyes per group. Topical application of BAC had no significant effect on the amount of ZO-1 mRNA and protein (Dunnett test).
    Mouse Anti Rabbit β Actin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti rabbit β actin antibody/product/Millipore
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse anti rabbit β actin antibody - by Bioz Stars, 2021-07
    93/100 stars
      Buy from Supplier

    96
    Millipore fluorescein isothiocyanate fitc conjugated goat anti mouse igg
    Effect of BDNF/NSCs on MAP2 expression in host cells and neuron-like cells with concomitant PKH26 at 2 and 3 weeks after BDNF/NSCs or NSCs transplantation (immunofluorescence staining). Transplanted cells were labeled using PKH26 dye (red), with MAP2 labeled by <t>FITC</t> (green). Merged cells show MAP2 expression in transplanted neuron-like cells with concomitant PKH26. Scale bar: 50 μm. BDNF: Brain-derived neurotrophic factor; NSCs: neural stem cells; MAP2: microtubule-associated protein 2; FITC: fluorescein <t>isothiocyanate.</t>
    Fluorescein Isothiocyanate Fitc Conjugated Goat Anti Mouse Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescein isothiocyanate fitc conjugated goat anti mouse igg/product/Millipore
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fluorescein isothiocyanate fitc conjugated goat anti mouse igg - by Bioz Stars, 2021-07
    96/100 stars
      Buy from Supplier

    91
    Millipore biotin conjugated anti mouse igg1
    Detection of serum antibodies. Mice were immunized as described in . At 15 days after the last immunization, mice were bled for detection of serum antigen-specific <t>IgG1</t> (a) and IgG2a (b) The IgG2a/IgG1 ratio is also shown (c) Results are expressed
    Biotin Conjugated Anti Mouse Igg1, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotin conjugated anti mouse igg1/product/Millipore
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    biotin conjugated anti mouse igg1 - by Bioz Stars, 2021-07
    91/100 stars
      Buy from Supplier


    Image Search Results


    Acute effect of BAC on the expression of ZO-1 mRNA and protein in the rabbit corneal epithelium. (A) Corneal epithelial cells isolated from a control eye or from eyes treated with 0.005%, 0.01% or 0.02% BAC were subjected to western blot analysis with antibodies to ZO-1 or β actin (loading control). (B) Qutantitative analysis of ZO-1 band intensity in bolts similar to those shown in (A). Data were normalized by the corresponding β actin band intensity and mean ± SE of values from three eyes per group. (C) Corneal epithelial cells isolated from a control eye or from eyes treated with 0.005%, 0.01% or 0.02% BAC were subjected to RT-PCR analysis of ZO-1 mRNA. (D) Quantitative analysis of ZO-1 band intensity in gel similar to that shown in (A). Data were normalized by the corresponding G3PDH band intensity and are mean±SE of values from three eyes per group. Topical application of BAC had no significant effect on the amount of ZO-1 mRNA and protein (Dunnett test).

    Journal: PLoS ONE

    Article Title: Localization and Expression of Zonula Occludins-1 in the Rabbit Corneal Epithelium following Exposure to Benzalkonium Chloride

    doi: 10.1371/journal.pone.0040893

    Figure Lengend Snippet: Acute effect of BAC on the expression of ZO-1 mRNA and protein in the rabbit corneal epithelium. (A) Corneal epithelial cells isolated from a control eye or from eyes treated with 0.005%, 0.01% or 0.02% BAC were subjected to western blot analysis with antibodies to ZO-1 or β actin (loading control). (B) Qutantitative analysis of ZO-1 band intensity in bolts similar to those shown in (A). Data were normalized by the corresponding β actin band intensity and mean ± SE of values from three eyes per group. (C) Corneal epithelial cells isolated from a control eye or from eyes treated with 0.005%, 0.01% or 0.02% BAC were subjected to RT-PCR analysis of ZO-1 mRNA. (D) Quantitative analysis of ZO-1 band intensity in gel similar to that shown in (A). Data were normalized by the corresponding G3PDH band intensity and are mean±SE of values from three eyes per group. Topical application of BAC had no significant effect on the amount of ZO-1 mRNA and protein (Dunnett test).

    Article Snippet: Antibodies and Reagent BAC was purchased from Sigma (St. Louis, MO); pentobarbital sodium from Abbott Laboratories (North Chicago, IL); mouse anti-rabbit ZO-1 antibody, mouse anti-rabbit ZO-2 antibody, mouse anti-rabbit claudin-1 and mouse anti-rabbit occludin from Zymed (Carlsbad, CA); rat monoclonal antibodies for Ki67 from DakoCytomation (MIB-1; Glostrup, Denmark); TUNEL apoptosis detection kit was purchased from Roche Diagnostics (Meylen, France); Alexa488-conjugated goat anti-mouse IgG, goat anti-mouse IgG and Alexa594-conjuagated mouse anti-rat IgG from Molecular Probes (Eugene, OR); 4,6-diamidino-2-phenylindole (DAPI) and bovine serum albumin (BSA) from Vector Laboratories (Burlingame CA); Dulbecco modified Eagle medium (DMEM) and Dispase II from Invitrogen Corp (Carlsbad, CA); mouse anti-rabbit β actin antibody from Sigma; Horseradish peroxidase-conjugated goat antibody to mouse immunoglobulin G (IgG), nitrocellulose membranes and an enhanced chemiluminescence (ECL) kit from GE Healthcare UK (Chalfont, UK).

    Techniques: BAC Assay, Expressing, Isolation, Western Blot, Reverse Transcription Polymerase Chain Reaction

    The proteasome inhibitor induces ARNT protein expression. Wild-type MEF cultures were treated with 8 μM MG132 for the indicated times. ARNT and AHR expression were analyzed by immunoblotting using the corresponding primary antibodies. (A) Representative immunoblots obtained for each of the proteins. (B) Quantitative analysis by volumetric integration of the raw data from the immunoblots shown in panel A. Data were normalized by the levels of mouse β-actin expression. The experiment was performed in duplicate with three different MEF preparations.

    Journal: Molecular and Cellular Biology

    Article Title: Proteasome Inhibition Induces Nuclear Translocation and Transcriptional Activation of the Dioxin Receptor in Mouse Embryo Primary Fibroblasts in the Absence of Xenobiotics

    doi: 10.1128/MCB.21.5.1700-1709.2001

    Figure Lengend Snippet: The proteasome inhibitor induces ARNT protein expression. Wild-type MEF cultures were treated with 8 μM MG132 for the indicated times. ARNT and AHR expression were analyzed by immunoblotting using the corresponding primary antibodies. (A) Representative immunoblots obtained for each of the proteins. (B) Quantitative analysis by volumetric integration of the raw data from the immunoblots shown in panel A. Data were normalized by the levels of mouse β-actin expression. The experiment was performed in duplicate with three different MEF preparations.

    Article Snippet: Rabbit antibody against mouse β-actin was obtained from Sigma.

    Techniques: Expressing, Western Blot

    The proteasome inhibitor induces ARNT transcription. Wild-type MEF cultures were treated with 8 μM MG132 for the indicated times. ARNT and AHR mRNA levels were analyzed by RT-PCR using 7 μg of total RNA and oligo (dT) priming. The specific oligonucleotides for PCR amplification of each gene are indicated in Materials and Methods. The control lane corresponds to an RT-PCR reaction performed in the absence of RNA template. Mouse β-actin mRNA expression was analyzed to verify total RNA integrity and concentration. Note that low but detectable levels of ARNT mRNA could be detected constitutively (0 h) and 12 h after proteasome inhibition. ARNT levels increased by about twofold at 3 h of MG132 treatment and by close to fourfold after 6 h of proteasome inhibition. The experiment was done in duplicate with three different MEF preparations.

    Journal: Molecular and Cellular Biology

    Article Title: Proteasome Inhibition Induces Nuclear Translocation and Transcriptional Activation of the Dioxin Receptor in Mouse Embryo Primary Fibroblasts in the Absence of Xenobiotics

    doi: 10.1128/MCB.21.5.1700-1709.2001

    Figure Lengend Snippet: The proteasome inhibitor induces ARNT transcription. Wild-type MEF cultures were treated with 8 μM MG132 for the indicated times. ARNT and AHR mRNA levels were analyzed by RT-PCR using 7 μg of total RNA and oligo (dT) priming. The specific oligonucleotides for PCR amplification of each gene are indicated in Materials and Methods. The control lane corresponds to an RT-PCR reaction performed in the absence of RNA template. Mouse β-actin mRNA expression was analyzed to verify total RNA integrity and concentration. Note that low but detectable levels of ARNT mRNA could be detected constitutively (0 h) and 12 h after proteasome inhibition. ARNT levels increased by about twofold at 3 h of MG132 treatment and by close to fourfold after 6 h of proteasome inhibition. The experiment was done in duplicate with three different MEF preparations.

    Article Snippet: Rabbit antibody against mouse β-actin was obtained from Sigma.

    Techniques: Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction, Amplification, Expressing, Concentration Assay, Inhibition

    CYP1A2 protein induction by xenobiotics and proteasome inhibitors in MEF cultures. (A) MEF cultures from wild-type (lanes 1 to 3) or AHR-null (lanes 4 to 6) mice were treated with the indicated AHR ligands, and total-cell extracts were analyzed by immunoblotting using 10 μg of protein and an anti-CYP1A2 antibody. Total-cell extracts from cultures treated for 12 h with DMSO (lanes 1 and 4), 10 μM BP (lanes 2 and 5), or 10 nM TCDD (lanes 3 and 6) were used. (B) Wild-type MEF cultures were treated with 8 μM MG132 for the indicated times or with 10 nM TCDD for 6 h, and CYP1A2 expression was analyzed by immunoblotting. (C) To determine if CYP1A2 induction was an AHR-dependent process, AHR-null MEF cultures were treated with 8 μM MG132 for the indicated times or with 10 nM TCDD for 6 h and CYP1A2 expression was analyzed by immunoblotting. Expression of mouse β-actin was used as a control for protein loading. Vaccinia-expressed mouse CYP1A2 (r1A2) was used as positive control (lane 7). Experiments were done in duplicate with three different MEF preparations.

    Journal: Molecular and Cellular Biology

    Article Title: Proteasome Inhibition Induces Nuclear Translocation and Transcriptional Activation of the Dioxin Receptor in Mouse Embryo Primary Fibroblasts in the Absence of Xenobiotics

    doi: 10.1128/MCB.21.5.1700-1709.2001

    Figure Lengend Snippet: CYP1A2 protein induction by xenobiotics and proteasome inhibitors in MEF cultures. (A) MEF cultures from wild-type (lanes 1 to 3) or AHR-null (lanes 4 to 6) mice were treated with the indicated AHR ligands, and total-cell extracts were analyzed by immunoblotting using 10 μg of protein and an anti-CYP1A2 antibody. Total-cell extracts from cultures treated for 12 h with DMSO (lanes 1 and 4), 10 μM BP (lanes 2 and 5), or 10 nM TCDD (lanes 3 and 6) were used. (B) Wild-type MEF cultures were treated with 8 μM MG132 for the indicated times or with 10 nM TCDD for 6 h, and CYP1A2 expression was analyzed by immunoblotting. (C) To determine if CYP1A2 induction was an AHR-dependent process, AHR-null MEF cultures were treated with 8 μM MG132 for the indicated times or with 10 nM TCDD for 6 h and CYP1A2 expression was analyzed by immunoblotting. Expression of mouse β-actin was used as a control for protein loading. Vaccinia-expressed mouse CYP1A2 (r1A2) was used as positive control (lane 7). Experiments were done in duplicate with three different MEF preparations.

    Article Snippet: Rabbit antibody against mouse β-actin was obtained from Sigma.

    Techniques: Mouse Assay, Expressing, Positive Control

    The AHR-EGFP fusion protein is transcriptionally active. MEF cultures isolated from AHR-null mouse embryos were transfected with the AHR-EGFP fusion construct as indicated in Materials and Methods. Reporter gene expression was analyzed following CYP1A2 induction by immunoblotting using 10 μg of protein. AHR-null MEF cultures were transfected and treated for 6 h with DMSO (lane 3) or 10 nM TCDD (lane 2). Nontransfected AHR-null MEF cultures were used as a negative control (lane 1). Vacciniavirus-expressed mouse CYP1A2 was included as a positive control (lane 4). Expression of mouse β-actin was included as a control for protein loading. The experiment was done in duplicate with two different AHR-null MEF preparations.

    Journal: Molecular and Cellular Biology

    Article Title: Proteasome Inhibition Induces Nuclear Translocation and Transcriptional Activation of the Dioxin Receptor in Mouse Embryo Primary Fibroblasts in the Absence of Xenobiotics

    doi: 10.1128/MCB.21.5.1700-1709.2001

    Figure Lengend Snippet: The AHR-EGFP fusion protein is transcriptionally active. MEF cultures isolated from AHR-null mouse embryos were transfected with the AHR-EGFP fusion construct as indicated in Materials and Methods. Reporter gene expression was analyzed following CYP1A2 induction by immunoblotting using 10 μg of protein. AHR-null MEF cultures were transfected and treated for 6 h with DMSO (lane 3) or 10 nM TCDD (lane 2). Nontransfected AHR-null MEF cultures were used as a negative control (lane 1). Vacciniavirus-expressed mouse CYP1A2 was included as a positive control (lane 4). Expression of mouse β-actin was included as a control for protein loading. The experiment was done in duplicate with two different AHR-null MEF preparations.

    Article Snippet: Rabbit antibody against mouse β-actin was obtained from Sigma.

    Techniques: Isolation, Transfection, Construct, Expressing, Negative Control, Positive Control

    CYP1A2 induction by proteasome inhibition is due to AHR-dependent transcriptional activation. Wild-type and AHR-null MEF cultures were treated with 8 μM MG132 for the indicated times or with 10 nM TCDD for 6 h, and CYP1A2 mRNA expression was measured by Northern blot analysis as indicated in Materials and Methods. mCYP1A2 mRNA expression steadily increased with time by proteasome inhibition or TCDD treatment in control (Ahr+/+) but not in AHR-null (Ahr−/−) MEF cultures. Note that although AHR-null cells were not responsive for CYP1A2 induction by any of the treatments, their basal CYP1A2 mRNA levels (0 h) appeared to be higher than for wild-type (Ahr+/+) MEF. Expression of mouse β-actin was used as a control for RNA integrity and loading. The experiment was repeated twice with two different MEF preparations.

    Journal: Molecular and Cellular Biology

    Article Title: Proteasome Inhibition Induces Nuclear Translocation and Transcriptional Activation of the Dioxin Receptor in Mouse Embryo Primary Fibroblasts in the Absence of Xenobiotics

    doi: 10.1128/MCB.21.5.1700-1709.2001

    Figure Lengend Snippet: CYP1A2 induction by proteasome inhibition is due to AHR-dependent transcriptional activation. Wild-type and AHR-null MEF cultures were treated with 8 μM MG132 for the indicated times or with 10 nM TCDD for 6 h, and CYP1A2 mRNA expression was measured by Northern blot analysis as indicated in Materials and Methods. mCYP1A2 mRNA expression steadily increased with time by proteasome inhibition or TCDD treatment in control (Ahr+/+) but not in AHR-null (Ahr−/−) MEF cultures. Note that although AHR-null cells were not responsive for CYP1A2 induction by any of the treatments, their basal CYP1A2 mRNA levels (0 h) appeared to be higher than for wild-type (Ahr+/+) MEF. Expression of mouse β-actin was used as a control for RNA integrity and loading. The experiment was repeated twice with two different MEF preparations.

    Article Snippet: Rabbit antibody against mouse β-actin was obtained from Sigma.

    Techniques: Inhibition, Activation Assay, Expressing, Northern Blot

    Effect of BDNF/NSCs on MAP2 expression in host cells and neuron-like cells with concomitant PKH26 at 2 and 3 weeks after BDNF/NSCs or NSCs transplantation (immunofluorescence staining). Transplanted cells were labeled using PKH26 dye (red), with MAP2 labeled by FITC (green). Merged cells show MAP2 expression in transplanted neuron-like cells with concomitant PKH26. Scale bar: 50 μm. BDNF: Brain-derived neurotrophic factor; NSCs: neural stem cells; MAP2: microtubule-associated protein 2; FITC: fluorescein isothiocyanate.

    Journal: Neural Regeneration Research

    Article Title: Neural stem cells over-expressing brain-derived neurotrophic factor promote neuronal survival and cytoskeletal protein expression in traumatic brain injury sites

    doi: 10.4103/1673-5374.202947

    Figure Lengend Snippet: Effect of BDNF/NSCs on MAP2 expression in host cells and neuron-like cells with concomitant PKH26 at 2 and 3 weeks after BDNF/NSCs or NSCs transplantation (immunofluorescence staining). Transplanted cells were labeled using PKH26 dye (red), with MAP2 labeled by FITC (green). Merged cells show MAP2 expression in transplanted neuron-like cells with concomitant PKH26. Scale bar: 50 μm. BDNF: Brain-derived neurotrophic factor; NSCs: neural stem cells; MAP2: microtubule-associated protein 2; FITC: fluorescein isothiocyanate.

    Article Snippet: After washing three times with PBS, sections were incubated with an appropriate secondary antibody for 1 hour at room temperature: goat anti-mouse IgG (1:1,000; ZSGB-Bio, Beijing, China) for NF200 and avidin-biotin complex (Boster), and fluorescein isothiocyanate (FITC)-conjugated goat anti-mouse IgG (1:1,000; Sigma-Aldrich) for MAP2.

    Techniques: Expressing, Transplantation Assay, Immunofluorescence, Staining, Labeling, Derivative Assay

    Detection of serum antibodies. Mice were immunized as described in . At 15 days after the last immunization, mice were bled for detection of serum antigen-specific IgG1 (a) and IgG2a (b) The IgG2a/IgG1 ratio is also shown (c) Results are expressed

    Journal:

    Article Title: Increased levels of interferon-γ primed by culture filtrate proteins antigen and CpG-ODN immunization do not confer significant protection against Mycobacterium tuberculosis infection

    doi: 10.1111/j.1365-2567.2007.02597.x

    Figure Lengend Snippet: Detection of serum antibodies. Mice were immunized as described in . At 15 days after the last immunization, mice were bled for detection of serum antigen-specific IgG1 (a) and IgG2a (b) The IgG2a/IgG1 ratio is also shown (c) Results are expressed

    Article Snippet: After incubating the plates for 2 hr at 37°, biotin-conjugated anti-mouse IgG1 (A85-1; Sigma) and IgG2a (R19-15; Sigma) were added for detection of specific antibodies.

    Techniques: Mouse Assay