Review



mouse igg1 tshr mab  (Bio-Rad)


Bioz Verified Symbol Bio-Rad is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 96
      Buy from Supplier

    Structured Review

    Bio-Rad mouse igg1 tshr mab
    Figure 1 <t>TSHR</t> structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
    Mouse Igg1 Tshr Mab, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1546 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+igg1+tshr+mab/10__1677_slash_joe___07___0058-37-3-12?v=Bio-Rad
    Average 96 stars, based on 1546 article reviews
    mouse igg1 tshr mab - by Bioz Stars, 2026-08
    96/100 stars

    Images

    1) Product Images from "Antibody-induced modulation of TSH receptor post-translational processing"

    Article Title: Antibody-induced modulation of TSH receptor post-translational processing

    Journal: Journal of Endocrinology

    doi: 10.1677/joe-07-0058

    Figure 1 TSHR structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
    Figure Legend Snippet: Figure 1 TSHR structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.

    Techniques Used: Membrane

    Figure 2 Recognition of the TSHR cleaved region by sera from a hamster model of Graves’ disease. TSHR-Abs to the cleaved region in sera from a hamster model of GD as determined by TSHR peptide ELISAs. The numbers shown below each column indicate the initial AA of each synthetic peptide as described in the Materials and Methods section. Immunoreactivity (OD) was compared with peptide 382 and an irrelevant control mAb (data are mean of duplicate measurements). *P!0.05 and **P!0.01.
    Figure Legend Snippet: Figure 2 Recognition of the TSHR cleaved region by sera from a hamster model of Graves’ disease. TSHR-Abs to the cleaved region in sera from a hamster model of GD as determined by TSHR peptide ELISAs. The numbers shown below each column indicate the initial AA of each synthetic peptide as described in the Materials and Methods section. Immunoreactivity (OD) was compared with peptide 382 and an irrelevant control mAb (data are mean of duplicate measurements). *P!0.05 and **P!0.01.

    Techniques Used: Control

    Figure 7 TSHR expression by immunoblot. Membranes prepared from TSH- and antibody-treated cells were resolved on 10% SDS-PAGE and blotted on to PVDF. The membrane was probed with an amino terminal TSHR-mAb (A10; Morgenthaler et al. 1997) at 1:5000 dilution. (A) Lane 1, untreated cells; lane 2, treated with TAb-8 antibody (2 mg/ml) for 24 h; and lane 3, treated with TSH (1000 mU/ml) for 24 h. *P!0.01. (B) Densitometric representation of the TSH holoreceptor bands indicated in (A).
    Figure Legend Snippet: Figure 7 TSHR expression by immunoblot. Membranes prepared from TSH- and antibody-treated cells were resolved on 10% SDS-PAGE and blotted on to PVDF. The membrane was probed with an amino terminal TSHR-mAb (A10; Morgenthaler et al. 1997) at 1:5000 dilution. (A) Lane 1, untreated cells; lane 2, treated with TAb-8 antibody (2 mg/ml) for 24 h; and lane 3, treated with TSH (1000 mU/ml) for 24 h. *P!0.01. (B) Densitometric representation of the TSH holoreceptor bands indicated in (A).

    Techniques Used: Expressing, Western Blot, SDS Page, Membrane



    Similar Products

    mouse igg1 tshr mab  (Bio-Rad)
    96
    Bio-Rad mouse igg1 tshr mab
    Figure 1 <t>TSHR</t> structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.
    Mouse Igg1 Tshr Mab, supplied by Bio-Rad, 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/product/mouse+igg1+tshr+mab/10__1677_slash_joe___07___0058-37-3-12?v=Bio-Rad
    Average 96 stars, based on 1 article reviews
    mouse igg1 tshr mab - by Bioz Stars, 2026-08
    96/100 stars
    		  Buy from Supplier

    Image Search Results


    Figure 1 TSHR structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.

    Journal: Journal of Endocrinology

    Article Title: Antibody-induced modulation of TSH receptor post-translational processing

    doi: 10.1677/joe-07-0058

    Figure Lengend Snippet: Figure 1 TSHR structure, post-translational processing, and epitope geography. (A) Three forms of the TSHR: the TSH holoreceptor undergoes cleavage and loses residues w316–366. This results in the formation of a two subunit structure (a and b) connected by disulfide bonds and is referred to as the cleaved TSHR. Upon reduction, the a subunit (making up much of the ectodomain) is shed from the cell surface and leaves the b subunits on the membrane. This processing of the TSHR is constitutive and irreversible (adapted from Davies et al. 2002). (B) Schematic representation of the structure of the TSHR and the epitopes recognized by TSHR- mAbs. A w50 AA region removed by TSHR cleavage (cleaved region) is shown in white. The capital letters (A–C) indicate the three major epitopes recognized in a hamster model of GD (Ando et al. 2004a). Epitopes shown as oval indicate conformational recognition, and squares indicate linear recognition regions. Note that the ectodomain consists of more than just the TSHR a subunit.

    Article Snippet: 2C11 was a mouse IgG1 TSHR-mAb (Shepherd et al. 1999) purchased from Serotec (Raleigh, NC, USA).

    Techniques: Membrane

    Figure 2 Recognition of the TSHR cleaved region by sera from a hamster model of Graves’ disease. TSHR-Abs to the cleaved region in sera from a hamster model of GD as determined by TSHR peptide ELISAs. The numbers shown below each column indicate the initial AA of each synthetic peptide as described in the Materials and Methods section. Immunoreactivity (OD) was compared with peptide 382 and an irrelevant control mAb (data are mean of duplicate measurements). *P!0.05 and **P!0.01.

    Journal: Journal of Endocrinology

    Article Title: Antibody-induced modulation of TSH receptor post-translational processing

    doi: 10.1677/joe-07-0058

    Figure Lengend Snippet: Figure 2 Recognition of the TSHR cleaved region by sera from a hamster model of Graves’ disease. TSHR-Abs to the cleaved region in sera from a hamster model of GD as determined by TSHR peptide ELISAs. The numbers shown below each column indicate the initial AA of each synthetic peptide as described in the Materials and Methods section. Immunoreactivity (OD) was compared with peptide 382 and an irrelevant control mAb (data are mean of duplicate measurements). *P!0.05 and **P!0.01.

    Article Snippet: 2C11 was a mouse IgG1 TSHR-mAb (Shepherd et al. 1999) purchased from Serotec (Raleigh, NC, USA).

    Techniques: Control

    Figure 7 TSHR expression by immunoblot. Membranes prepared from TSH- and antibody-treated cells were resolved on 10% SDS-PAGE and blotted on to PVDF. The membrane was probed with an amino terminal TSHR-mAb (A10; Morgenthaler et al. 1997) at 1:5000 dilution. (A) Lane 1, untreated cells; lane 2, treated with TAb-8 antibody (2 mg/ml) for 24 h; and lane 3, treated with TSH (1000 mU/ml) for 24 h. *P!0.01. (B) Densitometric representation of the TSH holoreceptor bands indicated in (A).

    Journal: Journal of Endocrinology

    Article Title: Antibody-induced modulation of TSH receptor post-translational processing

    doi: 10.1677/joe-07-0058

    Figure Lengend Snippet: Figure 7 TSHR expression by immunoblot. Membranes prepared from TSH- and antibody-treated cells were resolved on 10% SDS-PAGE and blotted on to PVDF. The membrane was probed with an amino terminal TSHR-mAb (A10; Morgenthaler et al. 1997) at 1:5000 dilution. (A) Lane 1, untreated cells; lane 2, treated with TAb-8 antibody (2 mg/ml) for 24 h; and lane 3, treated with TSH (1000 mU/ml) for 24 h. *P!0.01. (B) Densitometric representation of the TSH holoreceptor bands indicated in (A).

    Article Snippet: 2C11 was a mouse IgG1 TSHR-mAb (Shepherd et al. 1999) purchased from Serotec (Raleigh, NC, USA).

    Techniques: Expressing, Western Blot, SDS Page, Membrane