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  • 99
    Thermo Fisher anti ha
    Anti Ha, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1685 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti ha
    Anti Ha, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 6148 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti ha antibody
    Anti Ha Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 5181 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Covance anti ha
    LUBEL catalyzes the synthesis of linear Ub chains In vitro ubiquitination assays of LUBEL‐RBR‐C WT or catalytically dead C2704A in combination with Ube1 and two different Drosophila E2s, UbcD10, or Effete/UbcD1. Reactions were terminated at indicated times, and synthesized Ub chains were detected by immunoblotting using anti‐linear Ub antibody. Total protein loading was visualized by Ponceau S staining. *: nonspecific band. In vitro deubiquitination of Ub chains synthesized by HOIP‐ and LUBEL‐RBR‐C. Ub chains produced by RBR‐C (human or Drosophila ) with UbcH7, UbcD10 or Effete were incubated with a linear linkage‐specific DUB, OTULIN (WT or catalytically dead C129A (C/A) mutant), or a Lys‐linkage‐specific DUB, vOTU. The DUB‐treated samples were subjected to Coomassie staining or immunoblotting using anti‐Ub antibody. *: nonspecific band. Thioester formation assay using Atto647‐labeled Ub. Ubiquitination assay using LUBEL‐RBR‐C WT (left panel) or C2704A (right panel): lanes 1/2 Atto‐Ub + E1, lanes 3/4 + ATP, lanes 5/6 + E2, lanes 7/8 + E3, and lanes 9/10 + Ub‐His 6 . In the presence of N‐terminally tagged Atto‐Ub and C‐terminally tagged Ub‐His 6 , only Ub 2 product can be synthesized and longer chain formation is restricted. Samples are run without or with DTT in odd or even numbered lanes, respectively. The gels monitor the Atto‐labeled Ub. The linear Ub chain formation activity of LUBEL‐LDD mutants. Recombinant proteins of RBR‐C WT, C2704A mutant, and LDD mutants (R2754A and D2755A) were assessed for their activity by in vitro ubiquitination assay. The samples were resolved on a gel and stained with Coomassie or immunoblotted using anti‐linear Ub antibody. Linear Ub chain formation by full‐length LUBEL transient expression in insect cells. Full‐length Myc‐LUBEL was transiently expressed in Drosophila Schneider 2 (S2) cells, and Myc‐HOIP alone or with HA‐HOIL‐1L in HEK293T cells. Total cell lysates (TCL) of control and transfected samples were incubated with immobilized GST‐Linear‐Tandem Ub binding entity (Linear‐TUBE) containing three tandem repeats of ABIN‐1‐UBAN. Pulldown samples were blotted with anti‐linear Ub antibody, while TCL were blotted with anti‐Myc antibody for exogenous LUBEL and HOIP, <t>anti‐HA</t> antibody for HOIL‐1L, and anti‐tubulin antibody for loading. Input of GST proteins was analyzed by Ponceau S staining. *: nonspecific band.
    Anti Ha, supplied by Covance, used in various techniques. Bioz Stars score: 94/100, based on 5844 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore monoclonal anti ha antibody
    LUBEL catalyzes the synthesis of linear Ub chains In vitro ubiquitination assays of LUBEL‐RBR‐C WT or catalytically dead C2704A in combination with Ube1 and two different Drosophila E2s, UbcD10, or Effete/UbcD1. Reactions were terminated at indicated times, and synthesized Ub chains were detected by immunoblotting using anti‐linear Ub antibody. Total protein loading was visualized by Ponceau S staining. *: nonspecific band. In vitro deubiquitination of Ub chains synthesized by HOIP‐ and LUBEL‐RBR‐C. Ub chains produced by RBR‐C (human or Drosophila ) with UbcH7, UbcD10 or Effete were incubated with a linear linkage‐specific DUB, OTULIN (WT or catalytically dead C129A (C/A) mutant), or a Lys‐linkage‐specific DUB, vOTU. The DUB‐treated samples were subjected to Coomassie staining or immunoblotting using anti‐Ub antibody. *: nonspecific band. Thioester formation assay using Atto647‐labeled Ub. Ubiquitination assay using LUBEL‐RBR‐C WT (left panel) or C2704A (right panel): lanes 1/2 Atto‐Ub + E1, lanes 3/4 + ATP, lanes 5/6 + E2, lanes 7/8 + E3, and lanes 9/10 + Ub‐His 6 . In the presence of N‐terminally tagged Atto‐Ub and C‐terminally tagged Ub‐His 6 , only Ub 2 product can be synthesized and longer chain formation is restricted. Samples are run without or with DTT in odd or even numbered lanes, respectively. The gels monitor the Atto‐labeled Ub. The linear Ub chain formation activity of LUBEL‐LDD mutants. Recombinant proteins of RBR‐C WT, C2704A mutant, and LDD mutants (R2754A and D2755A) were assessed for their activity by in vitro ubiquitination assay. The samples were resolved on a gel and stained with Coomassie or immunoblotted using anti‐linear Ub antibody. Linear Ub chain formation by full‐length LUBEL transient expression in insect cells. Full‐length Myc‐LUBEL was transiently expressed in Drosophila Schneider 2 (S2) cells, and Myc‐HOIP alone or with HA‐HOIL‐1L in HEK293T cells. Total cell lysates (TCL) of control and transfected samples were incubated with immobilized GST‐Linear‐Tandem Ub binding entity (Linear‐TUBE) containing three tandem repeats of ABIN‐1‐UBAN. Pulldown samples were blotted with anti‐linear Ub antibody, while TCL were blotted with anti‐Myc antibody for exogenous LUBEL and HOIP, <t>anti‐HA</t> antibody for HOIL‐1L, and anti‐tubulin antibody for loading. Input of GST proteins was analyzed by Ponceau S staining. *: nonspecific band.
    Monoclonal Anti Ha Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4731 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Santa Cruz Biotechnology anti ha
    At SIZ 1 is monosumoylated or disumoylated  in vivo . (A)  SUMO  conjugates were purified from 10‐day‐old plants carrying  XVE ‐His 6 ‐ HA 4 ‐ SUMO 1  and detected by western blot analysis with an anti‐ HA  antibody. (B) The same eluted fractions were examined by western blot analysis with an anti‐At SIZ 1 antibody.
    Anti Ha, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 5576 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Covance mouse anti ha
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Mouse Anti Ha, supplied by Covance, used in various techniques. Bioz Stars score: 93/100, based on 2661 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc anti ha
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Anti Ha, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 2266 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Abcam anti ha
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Anti Ha, supplied by Abcam, used in various techniques. Bioz Stars score: 96/100, based on 1679 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore monoclonal anti ha agarose antibody
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Monoclonal Anti Ha Agarose Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1974 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti ha
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Rabbit Anti Ha, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1207 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore ezview red anti ha affinity gel
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Ezview Red Anti Ha Affinity Gel, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1647 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore mouse anti ha
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Mouse Anti Ha, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1340 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Santa Cruz Biotechnology rabbit anti ha
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Rabbit Anti Ha, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1150 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher anti ha magnetic beads
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Anti Ha Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1240 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Covance anti ha monoclonal antibody
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Anti Ha Monoclonal Antibody, supplied by Covance, used in various techniques. Bioz Stars score: 93/100, based on 709 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam anti ha antibody
    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Anti Ha Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 1154 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Generation and Characterization of Clstn3 tm1a/tm1a <t>Mice.</t> (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with <t>HA-tagged</t> Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with <t>anti-Clstn1</t> (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p
    Mouse Anti Ha, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1021 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    LUBEL catalyzes the synthesis of linear Ub chains In vitro ubiquitination assays of LUBEL‐RBR‐C WT or catalytically dead C2704A in combination with Ube1 and two different Drosophila E2s, UbcD10, or Effete/UbcD1. Reactions were terminated at indicated times, and synthesized Ub chains were detected by immunoblotting using anti‐linear Ub antibody. Total protein loading was visualized by Ponceau S staining. *: nonspecific band. In vitro deubiquitination of Ub chains synthesized by HOIP‐ and LUBEL‐RBR‐C. Ub chains produced by RBR‐C (human or Drosophila ) with UbcH7, UbcD10 or Effete were incubated with a linear linkage‐specific DUB, OTULIN (WT or catalytically dead C129A (C/A) mutant), or a Lys‐linkage‐specific DUB, vOTU. The DUB‐treated samples were subjected to Coomassie staining or immunoblotting using anti‐Ub antibody. *: nonspecific band. Thioester formation assay using Atto647‐labeled Ub. Ubiquitination assay using LUBEL‐RBR‐C WT (left panel) or C2704A (right panel): lanes 1/2 Atto‐Ub + E1, lanes 3/4 + ATP, lanes 5/6 + E2, lanes 7/8 + E3, and lanes 9/10 + Ub‐His 6 . In the presence of N‐terminally tagged Atto‐Ub and C‐terminally tagged Ub‐His 6 , only Ub 2 product can be synthesized and longer chain formation is restricted. Samples are run without or with DTT in odd or even numbered lanes, respectively. The gels monitor the Atto‐labeled Ub. The linear Ub chain formation activity of LUBEL‐LDD mutants. Recombinant proteins of RBR‐C WT, C2704A mutant, and LDD mutants (R2754A and D2755A) were assessed for their activity by in vitro ubiquitination assay. The samples were resolved on a gel and stained with Coomassie or immunoblotted using anti‐linear Ub antibody. Linear Ub chain formation by full‐length LUBEL transient expression in insect cells. Full‐length Myc‐LUBEL was transiently expressed in Drosophila Schneider 2 (S2) cells, and Myc‐HOIP alone or with HA‐HOIL‐1L in HEK293T cells. Total cell lysates (TCL) of control and transfected samples were incubated with immobilized GST‐Linear‐Tandem Ub binding entity (Linear‐TUBE) containing three tandem repeats of ABIN‐1‐UBAN. Pulldown samples were blotted with anti‐linear Ub antibody, while TCL were blotted with anti‐Myc antibody for exogenous LUBEL and HOIP, anti‐HA antibody for HOIL‐1L, and anti‐tubulin antibody for loading. Input of GST proteins was analyzed by Ponceau S staining. *: nonspecific band.

    Journal: EMBO Reports

    Article Title: Linear ubiquitination by LUBEL has a role in Drosophila heat stress response

    doi: 10.15252/embr.201642378

    Figure Lengend Snippet: LUBEL catalyzes the synthesis of linear Ub chains In vitro ubiquitination assays of LUBEL‐RBR‐C WT or catalytically dead C2704A in combination with Ube1 and two different Drosophila E2s, UbcD10, or Effete/UbcD1. Reactions were terminated at indicated times, and synthesized Ub chains were detected by immunoblotting using anti‐linear Ub antibody. Total protein loading was visualized by Ponceau S staining. *: nonspecific band. In vitro deubiquitination of Ub chains synthesized by HOIP‐ and LUBEL‐RBR‐C. Ub chains produced by RBR‐C (human or Drosophila ) with UbcH7, UbcD10 or Effete were incubated with a linear linkage‐specific DUB, OTULIN (WT or catalytically dead C129A (C/A) mutant), or a Lys‐linkage‐specific DUB, vOTU. The DUB‐treated samples were subjected to Coomassie staining or immunoblotting using anti‐Ub antibody. *: nonspecific band. Thioester formation assay using Atto647‐labeled Ub. Ubiquitination assay using LUBEL‐RBR‐C WT (left panel) or C2704A (right panel): lanes 1/2 Atto‐Ub + E1, lanes 3/4 + ATP, lanes 5/6 + E2, lanes 7/8 + E3, and lanes 9/10 + Ub‐His 6 . In the presence of N‐terminally tagged Atto‐Ub and C‐terminally tagged Ub‐His 6 , only Ub 2 product can be synthesized and longer chain formation is restricted. Samples are run without or with DTT in odd or even numbered lanes, respectively. The gels monitor the Atto‐labeled Ub. The linear Ub chain formation activity of LUBEL‐LDD mutants. Recombinant proteins of RBR‐C WT, C2704A mutant, and LDD mutants (R2754A and D2755A) were assessed for their activity by in vitro ubiquitination assay. The samples were resolved on a gel and stained with Coomassie or immunoblotted using anti‐linear Ub antibody. Linear Ub chain formation by full‐length LUBEL transient expression in insect cells. Full‐length Myc‐LUBEL was transiently expressed in Drosophila Schneider 2 (S2) cells, and Myc‐HOIP alone or with HA‐HOIL‐1L in HEK293T cells. Total cell lysates (TCL) of control and transfected samples were incubated with immobilized GST‐Linear‐Tandem Ub binding entity (Linear‐TUBE) containing three tandem repeats of ABIN‐1‐UBAN. Pulldown samples were blotted with anti‐linear Ub antibody, while TCL were blotted with anti‐Myc antibody for exogenous LUBEL and HOIP, anti‐HA antibody for HOIL‐1L, and anti‐tubulin antibody for loading. Input of GST proteins was analyzed by Ponceau S staining. *: nonspecific band.

    Article Snippet: Antibodies and reagents Antibodies used in this study are as follows: anti‐Myc antibody (clone 9E10; Covance, Princeton, NJ), anti‐Flag antibody (clone M2; Sigma, St. Louis, MO), anti‐HA antibody (HA.11 clone 16B12, Covance, Princeton, NJ), anti‐Alpha‐tubulin antibody (ab15246, Abcam, Cambridge, UK), anti‐Linear Ub antibody (LUB9; Life Sensors, Malvern, PA), anti‐Lys 63‐Ub antibody (Apu3; Merck Millipore, Darmstadt, Germany), anti‐Lys 48‐Ub antibody (Apu2; Merck Millipore), and anti‐Ub antibody (clone P4D1; Santa Cruz Biotechnology, Santa Cruz, CA).

    Techniques: In Vitro, Synthesized, Staining, Produced, Incubation, Mutagenesis, Tube Formation Assay, Labeling, Ubiquitin Assay, Activity Assay, Recombinant, Expressing, Transfection, Binding Assay

    At SIZ 1 is monosumoylated or disumoylated  in vivo . (A)  SUMO  conjugates were purified from 10‐day‐old plants carrying  XVE ‐His 6 ‐ HA 4 ‐ SUMO 1  and detected by western blot analysis with an anti‐ HA  antibody. (B) The same eluted fractions were examined by western blot analysis with an anti‐At SIZ 1 antibody.

    Journal: FEBS Open Bio

    Article Title: Post‐translational modifications of Arabidopsis E3 SUMO ligase At SIZ1 are controlled by environmental conditions

    doi: 10.1002/2211-5463.12309

    Figure Lengend Snippet: At SIZ 1 is monosumoylated or disumoylated in vivo . (A) SUMO conjugates were purified from 10‐day‐old plants carrying XVE ‐His 6 ‐ HA 4 ‐ SUMO 1 and detected by western blot analysis with an anti‐ HA antibody. (B) The same eluted fractions were examined by western blot analysis with an anti‐At SIZ 1 antibody.

    Article Snippet: Eluted proteins were detected by western blot analysis with an anti‐HA antibody (Santa Cruz Biotechnology) or an anti‐AtSIZ1 antibody .

    Techniques: In Vivo, Purification, Western Blot

    Heat‐induced At SIZ 1 modification is regulated by  COP 1 and  ESD 4 activity. (A) Transgenic  XVE ‐ COP 1‐Myc 6  plants were incubated in liquid medium with β‐estradiol to induce  COP 1 expression. After incubation for 15 h, the plants were treated with liquid  MS  medium preheated to 37 °C. Samples were collected after treatment for 30 min, and At SIZ 1 and  COP 1‐Myc 6  were detected by western blot analysis with anti‐At SIZ 1 or anti‐Myc antibodies. Tubulin was used as a loading control. (B) Transgenic  XVE ‐ DN ‐ COP 1‐Myc 6  plants were incubated in liquid medium with β‐estradiol to induce  DN ‐ COP 1 expression. After incubation for 15 h, the plants were treated with liquid  MS  medium preheated to 37 °C. Samples were collected after treatment for 0, 10, and 30 min, and At SIZ 1 and  DN ‐ COP 1‐Myc 6  were detected by western blot analysis with anti‐At SIZ 1 or anti‐Myc antibodies. Tubulin was used as a loading control. (C) Ten‐day‐old wild‐type and  ESD 4‐overexpressing transgenic plants grown in  MS  medium were treated with liquid  MS  medium preheated at 37 °C. After treatment for 30 min, total proteins were extracted and At SIZ 1 was detected by western blot analysis with anti‐At SIZ 1 or anti‐ HA  antibodies. Tubulin was used as a loading control.

    Journal: FEBS Open Bio

    Article Title: Post‐translational modifications of Arabidopsis E3 SUMO ligase At SIZ1 are controlled by environmental conditions

    doi: 10.1002/2211-5463.12309

    Figure Lengend Snippet: Heat‐induced At SIZ 1 modification is regulated by COP 1 and ESD 4 activity. (A) Transgenic XVE ‐ COP 1‐Myc 6 plants were incubated in liquid medium with β‐estradiol to induce COP 1 expression. After incubation for 15 h, the plants were treated with liquid MS medium preheated to 37 °C. Samples were collected after treatment for 30 min, and At SIZ 1 and COP 1‐Myc 6 were detected by western blot analysis with anti‐At SIZ 1 or anti‐Myc antibodies. Tubulin was used as a loading control. (B) Transgenic XVE ‐ DN ‐ COP 1‐Myc 6 plants were incubated in liquid medium with β‐estradiol to induce DN ‐ COP 1 expression. After incubation for 15 h, the plants were treated with liquid MS medium preheated to 37 °C. Samples were collected after treatment for 0, 10, and 30 min, and At SIZ 1 and DN ‐ COP 1‐Myc 6 were detected by western blot analysis with anti‐At SIZ 1 or anti‐Myc antibodies. Tubulin was used as a loading control. (C) Ten‐day‐old wild‐type and ESD 4‐overexpressing transgenic plants grown in MS medium were treated with liquid MS medium preheated at 37 °C. After treatment for 30 min, total proteins were extracted and At SIZ 1 was detected by western blot analysis with anti‐At SIZ 1 or anti‐ HA antibodies. Tubulin was used as a loading control.

    Article Snippet: Eluted proteins were detected by western blot analysis with an anti‐HA antibody (Santa Cruz Biotechnology) or an anti‐AtSIZ1 antibody .

    Techniques: Modification, Activity Assay, Transgenic Assay, Incubation, Expressing, Mass Spectrometry, Western Blot

    Generation and Characterization of Clstn3 tm1a/tm1a Mice. (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with HA-tagged Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with anti-Clstn1 (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p

    Journal: bioRxiv

    Article Title: Calsyntenin-3 directly interacts with neurexins to orchestrate excitatory synapse development in the hippocampus

    doi: 10.1101/2020.01.24.918722

    Figure Lengend Snippet: Generation and Characterization of Clstn3 tm1a/tm1a Mice. (A) Strategy used to generate Clstn3 tm1a/tm1a mice. Arrows flanking the neomycin gene and FLP recombinant target (FRT) or exon 8 (E8) indicate loxP sites. Note that lacZ and neo are two separate markers. (B) PCR genotyping of Clstn3 tm1a/tm1a (KO), Clstn3 tm1a/+ (Het) and WT mice. (C) Immunoblot analyses of Clstn3 antibodies (JK091 and JK001) using lysates from HEK293T cells, untransfected or transfected with HA-tagged Clstn3, and rat brain crude synaptosomal fractions (P2). Br., brain; Unt., untransfected HEK293T cell lysates; Trans., transfected HEK293T cell lysates. (D) Cross-reactivity of the Clstn antibodies used in the current study. HEK293T cells, untransfected or transfected with the indicated Clstn3 expression vectors, were immunoblotted with anti-Clstn1 (JK025), anti-Clstn2 (JK028), or anti-Clstn3 (JK091 and JK001) antibodies. The expression of HA-tagged Clstn constructs was confirmed by immunoblotting with anti-HA antibodies. An anti-β-actin antibody was used for normalization. (E and F) Representative immunoblots ( E ) and summary graphs of synaptic protein levels ( F ) in crude synaptosomal fractions of P42 WT and Clstn3 tm1a/tm1a brains (3–5 pairs), analyzed by semiquantitative immunoblotting. Data are means ± SEMs (*** p

    Article Snippet: The following commercially available antibodies were used: mouse monoclonal anti-HA (clone HA-7; Covance), mouse monoclonal anti-FLAG M2 (Sigma-Aldrich, St. Louis, MO, USA), rabbit polyclonal anti-FLAG (Sigma-Aldrich), goat polyclonal anti-EGFP (Rockland Immunochemicals), mouse monoclonal anti-NL1 (clone N97A/31; NeuroMab), rabbit polyclonal anti-NL2 (Synaptic Systems, Göttingen, Germany), rabbit monoclonal anti-TrkC (clone C44H5; Cell Signaling Technology), guinea pig polyclonal anti-VGLUT1 (Millipore), mouse monoclonal anti-GAD67 (clone 1G10.2; Millipore), mouse monoclonal anti-PSD-95 (clone K28/43; Thermo-Fisher), mouse monoclonal anti-β-actin (clone AC-74; Sigma-Aldrich), mouse monoclonal anti-parvalbumin (clone PARV-19; Millipore), mouse monoclonal anti-gephyrin (clone 3B11; Synaptic Systems), rabbit polyclonal anti-GABAA receptor γ2 (Synaptic Systems); mouse monoclonal anti-GluN1 (clone 54.1; Millipore), rabbit polyclonal anti-GluN2A (Millipore), rabbit polyclonal anti-GluN2B (Millipore), goat anti-human IgG-peroxidase (Sigma-Aldrich), and mouse monoclonal anti-NeuN (clone A60; Millipore).

    Techniques: Mouse Assay, Recombinant, Polymerase Chain Reaction, Transfection, Expressing, Construct, Western Blot