mouse antiha tag Search Results


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Santa Cruz Biotechnology immunoprecipitation antiha
FIGURE 5 AD-associated variants R47H and D87N impair TREM2 multimerization in vitro. (A) Experimental design for <t>co-immunoprecipitation</t> experiments in this figure. Constructs containing the same variant were generated with either an HA or FLAG tag and transfected into HEK-293T cells. The tag of interest was immunoprecipitated from the lysate, and antibodies specific to both tags were used to IB. Immunoprecipitation of TREM2 constructs that multimerize should yield bands immunoreactive with both tags, whereas immunoprecipitation of TREM2 constructs with impaired multimerization should yield primarily bands immunoreactive with the tag pulled down and less of the other tag. (B) Representative images of co-immunoprecipitations of TREM2-CV, TREM2-R47H, or TREM2-D87N tagged with either HA or FLAG show the expected pattern, with bands for the pulled down tag visible for all, but bands of the non-targeted tag lost in the lanes containing AD-associated variants. (C, D) Quantification of three independent experiments like that shown in (B). Pulldown efficiencies are calculated as the ratio between the tag that was not pulled down by immunoprecipitation (FLAG in C, HA in D) over the tag that was pulled down (HA in C, FLAG in D). n = 3 independent transfections and pull-downs per group, **p < 0.01, ***p < 0.001. IB, immunoblot. IP, immunoprecipitation.
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FIGURE 5 AD-associated variants R47H and D87N impair TREM2 multimerization in vitro. (A) Experimental design for <t>co-immunoprecipitation</t> experiments in this figure. Constructs containing the same variant were generated with either an HA or FLAG tag and transfected into HEK-293T cells. The tag of interest was immunoprecipitated from the lysate, and antibodies specific to both tags were used to IB. Immunoprecipitation of TREM2 constructs that multimerize should yield bands immunoreactive with both tags, whereas immunoprecipitation of TREM2 constructs with impaired multimerization should yield primarily bands immunoreactive with the tag pulled down and less of the other tag. (B) Representative images of co-immunoprecipitations of TREM2-CV, TREM2-R47H, or TREM2-D87N tagged with either HA or FLAG show the expected pattern, with bands for the pulled down tag visible for all, but bands of the non-targeted tag lost in the lanes containing AD-associated variants. (C, D) Quantification of three independent experiments like that shown in (B). Pulldown efficiencies are calculated as the ratio between the tag that was not pulled down by immunoprecipitation (FLAG in C, HA in D) over the tag that was pulled down (HA in C, FLAG in D). n = 3 independent transfections and pull-downs per group, **p < 0.01, ***p < 0.001. IB, immunoblot. IP, immunoprecipitation.
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Qiagen mouse antihis-tag antibody
FIGURE 5 AD-associated variants R47H and D87N impair TREM2 multimerization in vitro. (A) Experimental design for <t>co-immunoprecipitation</t> experiments in this figure. Constructs containing the same variant were generated with either an HA or FLAG tag and transfected into HEK-293T cells. The tag of interest was immunoprecipitated from the lysate, and antibodies specific to both tags were used to IB. Immunoprecipitation of TREM2 constructs that multimerize should yield bands immunoreactive with both tags, whereas immunoprecipitation of TREM2 constructs with impaired multimerization should yield primarily bands immunoreactive with the tag pulled down and less of the other tag. (B) Representative images of co-immunoprecipitations of TREM2-CV, TREM2-R47H, or TREM2-D87N tagged with either HA or FLAG show the expected pattern, with bands for the pulled down tag visible for all, but bands of the non-targeted tag lost in the lanes containing AD-associated variants. (C, D) Quantification of three independent experiments like that shown in (B). Pulldown efficiencies are calculated as the ratio between the tag that was not pulled down by immunoprecipitation (FLAG in C, HA in D) over the tag that was pulled down (HA in C, FLAG in D). n = 3 independent transfections and pull-downs per group, **p < 0.01, ***p < 0.001. IB, immunoblot. IP, immunoprecipitation.
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Millipore mouse monoclonal anti-myoglobin antibody
FIGURE 5 AD-associated variants R47H and D87N impair TREM2 multimerization in vitro. (A) Experimental design for <t>co-immunoprecipitation</t> experiments in this figure. Constructs containing the same variant were generated with either an HA or FLAG tag and transfected into HEK-293T cells. The tag of interest was immunoprecipitated from the lysate, and antibodies specific to both tags were used to IB. Immunoprecipitation of TREM2 constructs that multimerize should yield bands immunoreactive with both tags, whereas immunoprecipitation of TREM2 constructs with impaired multimerization should yield primarily bands immunoreactive with the tag pulled down and less of the other tag. (B) Representative images of co-immunoprecipitations of TREM2-CV, TREM2-R47H, or TREM2-D87N tagged with either HA or FLAG show the expected pattern, with bands for the pulled down tag visible for all, but bands of the non-targeted tag lost in the lanes containing AD-associated variants. (C, D) Quantification of three independent experiments like that shown in (B). Pulldown efficiencies are calculated as the ratio between the tag that was not pulled down by immunoprecipitation (FLAG in C, HA in D) over the tag that was pulled down (HA in C, FLAG in D). n = 3 independent transfections and pull-downs per group, **p < 0.01, ***p < 0.001. IB, immunoblot. IP, immunoprecipitation.
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Covance antiha tag 16b12
FIGURE 5 AD-associated variants R47H and D87N impair TREM2 multimerization in vitro. (A) Experimental design for <t>co-immunoprecipitation</t> experiments in this figure. Constructs containing the same variant were generated with either an HA or FLAG tag and transfected into HEK-293T cells. The tag of interest was immunoprecipitated from the lysate, and antibodies specific to both tags were used to IB. Immunoprecipitation of TREM2 constructs that multimerize should yield bands immunoreactive with both tags, whereas immunoprecipitation of TREM2 constructs with impaired multimerization should yield primarily bands immunoreactive with the tag pulled down and less of the other tag. (B) Representative images of co-immunoprecipitations of TREM2-CV, TREM2-R47H, or TREM2-D87N tagged with either HA or FLAG show the expected pattern, with bands for the pulled down tag visible for all, but bands of the non-targeted tag lost in the lanes containing AD-associated variants. (C, D) Quantification of three independent experiments like that shown in (B). Pulldown efficiencies are calculated as the ratio between the tag that was not pulled down by immunoprecipitation (FLAG in C, HA in D) over the tag that was pulled down (HA in C, FLAG in D). n = 3 independent transfections and pull-downs per group, **p < 0.01, ***p < 0.001. IB, immunoblot. IP, immunoprecipitation.
Antiha Tag 16b12, supplied by Covance, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


FIGURE 5 AD-associated variants R47H and D87N impair TREM2 multimerization in vitro. (A) Experimental design for co-immunoprecipitation experiments in this figure. Constructs containing the same variant were generated with either an HA or FLAG tag and transfected into HEK-293T cells. The tag of interest was immunoprecipitated from the lysate, and antibodies specific to both tags were used to IB. Immunoprecipitation of TREM2 constructs that multimerize should yield bands immunoreactive with both tags, whereas immunoprecipitation of TREM2 constructs with impaired multimerization should yield primarily bands immunoreactive with the tag pulled down and less of the other tag. (B) Representative images of co-immunoprecipitations of TREM2-CV, TREM2-R47H, or TREM2-D87N tagged with either HA or FLAG show the expected pattern, with bands for the pulled down tag visible for all, but bands of the non-targeted tag lost in the lanes containing AD-associated variants. (C, D) Quantification of three independent experiments like that shown in (B). Pulldown efficiencies are calculated as the ratio between the tag that was not pulled down by immunoprecipitation (FLAG in C, HA in D) over the tag that was pulled down (HA in C, FLAG in D). n = 3 independent transfections and pull-downs per group, **p < 0.01, ***p < 0.001. IB, immunoblot. IP, immunoprecipitation.

Journal: Alzheimer's & dementia : the journal of the Alzheimer's Association

Article Title: Multimerization of TREM2 is impaired by Alzheimer's disease-associated variants.

doi: 10.1002/alz.14124

Figure Lengend Snippet: FIGURE 5 AD-associated variants R47H and D87N impair TREM2 multimerization in vitro. (A) Experimental design for co-immunoprecipitation experiments in this figure. Constructs containing the same variant were generated with either an HA or FLAG tag and transfected into HEK-293T cells. The tag of interest was immunoprecipitated from the lysate, and antibodies specific to both tags were used to IB. Immunoprecipitation of TREM2 constructs that multimerize should yield bands immunoreactive with both tags, whereas immunoprecipitation of TREM2 constructs with impaired multimerization should yield primarily bands immunoreactive with the tag pulled down and less of the other tag. (B) Representative images of co-immunoprecipitations of TREM2-CV, TREM2-R47H, or TREM2-D87N tagged with either HA or FLAG show the expected pattern, with bands for the pulled down tag visible for all, but bands of the non-targeted tag lost in the lanes containing AD-associated variants. (C, D) Quantification of three independent experiments like that shown in (B). Pulldown efficiencies are calculated as the ratio between the tag that was not pulled down by immunoprecipitation (FLAG in C, HA in D) over the tag that was pulled down (HA in C, FLAG in D). n = 3 independent transfections and pull-downs per group, **p < 0.01, ***p < 0.001. IB, immunoblot. IP, immunoprecipitation.

Article Snippet: Primary antibodies to distinguish the differentially tagged TREM2 for the western blot were the same as those used for the immunoprecipitation: antiHA (mouse monoclonal [F-7], #sc-7392, Santa Cruz Biotechnology) or anti-DYKDDDDK (rabbitmonoclonal [D6W5B], #14793,Cell Signaling Technology).

Techniques: In Vitro, Immunoprecipitation, Construct, Variant Assay, Generated, FLAG-tag, Transfection, Western Blot