rbd ig fusion proteins Search Results


95
Cytoskeleton Inc raf rbd gst fusion protein
Raf Rbd Gst Fusion Protein, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Genentech inc ig-fusion proteins
Ig Fusion Proteins, supplied by Genentech inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rbd+ig+fusion+proteins/us11226339-204-38-28?v=Genentech+inc
Average 90 stars, based on 1 article reviews
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90
Becton Dickinson recombinant soluble dimeric mouse h-2kb–ig fusion protein
Recombinant Soluble Dimeric Mouse H 2kb–Ig Fusion Protein, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rbd+ig+fusion+proteins/pm12533710-59-0-15?v=Becton+Dickinson
Average 90 stars, based on 1 article reviews
recombinant soluble dimeric mouse h-2kb–ig fusion protein - by Bioz Stars, 2026-08
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Becton Dickinson recombinant soluble dimeric mouse cd1d–ig fusion proteins
Recombinant Soluble Dimeric Mouse Cd1d–Ig Fusion Proteins, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rbd+ig+fusion+proteins/pm16785522-68-15-23?v=Becton+Dickinson
Average 90 stars, based on 1 article reviews
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90
United Biomedical ub-612
Ub 612, supplied by United Biomedical, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rbd+ig+fusion+proteins/10__1002_slash_exp__20210082-225-6-40?v=United+Biomedical
Average 90 stars, based on 1 article reviews
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90
ZymoGenetics inc atacicept taci-ig
Antigens targeted by antibodies in multiple myeloma in different stages of preclinical/clinical development.
Atacicept Taci Ig, supplied by ZymoGenetics inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rbd+ig+fusion+proteins/pmc03200112-259-0-2?v=ZymoGenetics+inc
Average 90 stars, based on 1 article reviews
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92
Proteintech f2
Antigens targeted by antibodies in multiple myeloma in different stages of preclinical/clinical development.
F2, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rbd+ig+fusion+proteins/pmc07947712-124-12-26?v=Proteintech
Average 92 stars, based on 1 article reviews
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93
Santa Cruz Biotechnology gst fusion protein
Antigens targeted by antibodies in multiple myeloma in different stages of preclinical/clinical development.
Gst Fusion Protein, supplied by Santa Cruz Biotechnology, 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/product/rbd+ig+fusion+proteins/us08987474-240-17-40?v=Santa+Cruz+Biotechnology
Average 93 stars, based on 1 article reviews
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95
Sino Biological recombinant sars cov 2 rbd fusion
Antigens targeted by antibodies in multiple myeloma in different stages of preclinical/clinical development.
Recombinant Sars Cov 2 Rbd Fusion, supplied by Sino Biological, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rbd+ig+fusion+proteins/us11547673-2759-2-27?v=Sino+Biological
Average 95 stars, based on 1 article reviews
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96
Proteintech α tubulin
A Immunostainings showing nuclear localization of TDP-43 Wt, 12D and 12A in HeLa cells. Endogenous TDP-43 expression was silenced by siRNAs, followed by transient transfection of the indicated siRNA-resistant myc-TDP-43 constructs. After 24 h, localization of TDP-43 Wt, 12D and 12A variants was visualized by TDP-43 immunostaining (mouse anti-TDP-43 antibody, Proteintech). G3BP1 (rabbit anti-G3BP1 antibody, Proteintech) and DAPI signal is shown to visualize the cytoplasm and nuclei, respectively. In the merge (right column), DAPI is show in turquoise, TDP-43 in green, and G3BP1 in magenta. Bar, 30 μm. B Electrophoretic mobility shift assay (EMSA) of TDP-43-MBP-His 6 variants (Wt, 12D and 12A) in a complex with (UG) 12 RNA. C SDS-PAGE followed by TDP-43 Western blot (upper blot) showing efficient siRNA-mediated knockdown of endogenous TDP-43 (running at ~43 kDa) in comparison to control siRNA and re-expression of myc-tagged TDP-43 Wt, 12D and 12A in Hela cells. Equal loading is demonstrated <t>by</t> <t>α-Tubulin</t> Western blot (bottom). TDP-43 was detected using rabbit anti-TDP-43 C-term antibody <t>(Proteintech),</t> <t>α-Tubulin</t> using mouse anti-alpha Tubulin antibody (Proteintech) and Myc-tag using mouse-anti Myc antibody (9E10, Helmholtz Center Munich).
α Tubulin, supplied by Proteintech, 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/rbd+ig+fusion+proteins/bio_rxiv__2021__04__30__442163-281-42-25?v=Proteintech
Average 96 stars, based on 1 article reviews
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96
Proteintech hsp90
A Immunostainings showing nuclear localization of TDP-43 Wt, 12D and 12A in HeLa cells. Endogenous TDP-43 expression was silenced by siRNAs, followed by transient transfection of the indicated siRNA-resistant myc-TDP-43 constructs. After 24 h, localization of TDP-43 Wt, 12D and 12A variants was visualized by TDP-43 immunostaining (mouse anti-TDP-43 antibody, Proteintech). G3BP1 (rabbit anti-G3BP1 antibody, Proteintech) and DAPI signal is shown to visualize the cytoplasm and nuclei, respectively. In the merge (right column), DAPI is show in turquoise, TDP-43 in green, and G3BP1 in magenta. Bar, 30 μm. B Electrophoretic mobility shift assay (EMSA) of TDP-43-MBP-His 6 variants (Wt, 12D and 12A) in a complex with (UG) 12 RNA. C SDS-PAGE followed by TDP-43 Western blot (upper blot) showing efficient siRNA-mediated knockdown of endogenous TDP-43 (running at ~43 kDa) in comparison to control siRNA and re-expression of myc-tagged TDP-43 Wt, 12D and 12A in Hela cells. Equal loading is demonstrated <t>by</t> <t>α-Tubulin</t> Western blot (bottom). TDP-43 was detected using rabbit anti-TDP-43 C-term antibody <t>(Proteintech),</t> <t>α-Tubulin</t> using mouse anti-alpha Tubulin antibody (Proteintech) and Myc-tag using mouse-anti Myc antibody (9E10, Helmholtz Center Munich).
Hsp90, supplied by Proteintech, 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/rbd+ig+fusion+proteins/pmc08983676-207-28-35?v=Proteintech
Average 96 stars, based on 1 article reviews
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96
Proteintech myod
Panel A shows representative Western blots of MyoD1, Myogenin, myosin heavy <t>chain</t> <t>(MHC),</t> and tubulin (as an internal control) in C2C12 cells after myogenic differentiation. Cells were collected 7 days after differentiation for <t>MyoD</t> and MHC or 5 days after differentiation for myogenin. Panel B shows the time course of MyoD1, myogenin, and MHC protein expression after changing the medium for myogenic differentiation. The band density of MyoD, myogenin, or MHC was normalized with that of tubulin. The normalized density was compared with the average of the normalized density in passage 1 just before myogenic differentiation (day 0) in the MyoD and myogenin expressions. Because MHC expression was undetectable on day 0, the normalized density was compared with the average of the normalized density in passage 1, 7 days after myogenic differentiation. Data are presented as means ± SE (n = 4 dishes). *P < 0.05, **P < 0.01 vs. passage 1 at each time point; †P < 0.05, ††P < 0.01 vs. passage 10 at each time point (Tukey–Kramer test).
Myod, supplied by Proteintech, 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/rbd+ig+fusion+proteins/pmc09844915-62-15-17?v=Proteintech
Average 96 stars, based on 1 article reviews
myod - by Bioz Stars, 2026-08
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Image Search Results


Antigens targeted by antibodies in multiple myeloma in different stages of preclinical/clinical development.

Journal: Bone Marrow Research

Article Title: Antibody-Based Therapies in Multiple Myeloma

doi: 10.1155/2011/924058

Figure Lengend Snippet: Antigens targeted by antibodies in multiple myeloma in different stages of preclinical/clinical development.

Article Snippet: Atacicept (TACI-Ig, ZymoGenetics; Serono) acts as a decoy receptor by binding to and neutralizing soluble BAFF and APRIL, and preventing these ligands from binding to their cognate receptors on B-cell tumors, thereby enhancing cytotoxicity.

Techniques: In Vivo, Injection, Binding Assay, Expressing, Recombinant, In Vitro, Conjugation Assay, Variant Assay, Activity Assay

A Immunostainings showing nuclear localization of TDP-43 Wt, 12D and 12A in HeLa cells. Endogenous TDP-43 expression was silenced by siRNAs, followed by transient transfection of the indicated siRNA-resistant myc-TDP-43 constructs. After 24 h, localization of TDP-43 Wt, 12D and 12A variants was visualized by TDP-43 immunostaining (mouse anti-TDP-43 antibody, Proteintech). G3BP1 (rabbit anti-G3BP1 antibody, Proteintech) and DAPI signal is shown to visualize the cytoplasm and nuclei, respectively. In the merge (right column), DAPI is show in turquoise, TDP-43 in green, and G3BP1 in magenta. Bar, 30 μm. B Electrophoretic mobility shift assay (EMSA) of TDP-43-MBP-His 6 variants (Wt, 12D and 12A) in a complex with (UG) 12 RNA. C SDS-PAGE followed by TDP-43 Western blot (upper blot) showing efficient siRNA-mediated knockdown of endogenous TDP-43 (running at ~43 kDa) in comparison to control siRNA and re-expression of myc-tagged TDP-43 Wt, 12D and 12A in Hela cells. Equal loading is demonstrated by α-Tubulin Western blot (bottom). TDP-43 was detected using rabbit anti-TDP-43 C-term antibody (Proteintech), α-Tubulin using mouse anti-alpha Tubulin antibody (Proteintech) and Myc-tag using mouse-anti Myc antibody (9E10, Helmholtz Center Munich).

Journal: bioRxiv

Article Title: Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregation

doi: 10.1101/2021.04.30.442163

Figure Lengend Snippet: A Immunostainings showing nuclear localization of TDP-43 Wt, 12D and 12A in HeLa cells. Endogenous TDP-43 expression was silenced by siRNAs, followed by transient transfection of the indicated siRNA-resistant myc-TDP-43 constructs. After 24 h, localization of TDP-43 Wt, 12D and 12A variants was visualized by TDP-43 immunostaining (mouse anti-TDP-43 antibody, Proteintech). G3BP1 (rabbit anti-G3BP1 antibody, Proteintech) and DAPI signal is shown to visualize the cytoplasm and nuclei, respectively. In the merge (right column), DAPI is show in turquoise, TDP-43 in green, and G3BP1 in magenta. Bar, 30 μm. B Electrophoretic mobility shift assay (EMSA) of TDP-43-MBP-His 6 variants (Wt, 12D and 12A) in a complex with (UG) 12 RNA. C SDS-PAGE followed by TDP-43 Western blot (upper blot) showing efficient siRNA-mediated knockdown of endogenous TDP-43 (running at ~43 kDa) in comparison to control siRNA and re-expression of myc-tagged TDP-43 Wt, 12D and 12A in Hela cells. Equal loading is demonstrated by α-Tubulin Western blot (bottom). TDP-43 was detected using rabbit anti-TDP-43 C-term antibody (Proteintech), α-Tubulin using mouse anti-alpha Tubulin antibody (Proteintech) and Myc-tag using mouse-anti Myc antibody (9E10, Helmholtz Center Munich).

Article Snippet: Knockdown was analyzed 48 h post transfection by immunohistochemistry using mouse anti TDP-43 antibody (Proteintech, Cat.No: 60019-2-Ig) and immunoblotting using rabbit anti TDP-43 C-Term antibody (Proteintech, Cat.No: 12892-1-AP) to detect TDP-43 and mouse anti alpha-Tubulin antibody (Proteintech, Cat.No: 66031-1-Ig) for detection of α-Tubulin as a control.

Techniques: Expressing, Transfection, Construct, Immunostaining, Electrophoretic Mobility Shift Assay, SDS Page, Western Blot

Panel A shows representative Western blots of MyoD1, Myogenin, myosin heavy chain (MHC), and tubulin (as an internal control) in C2C12 cells after myogenic differentiation. Cells were collected 7 days after differentiation for MyoD and MHC or 5 days after differentiation for myogenin. Panel B shows the time course of MyoD1, myogenin, and MHC protein expression after changing the medium for myogenic differentiation. The band density of MyoD, myogenin, or MHC was normalized with that of tubulin. The normalized density was compared with the average of the normalized density in passage 1 just before myogenic differentiation (day 0) in the MyoD and myogenin expressions. Because MHC expression was undetectable on day 0, the normalized density was compared with the average of the normalized density in passage 1, 7 days after myogenic differentiation. Data are presented as means ± SE (n = 4 dishes). *P < 0.05, **P < 0.01 vs. passage 1 at each time point; †P < 0.05, ††P < 0.01 vs. passage 10 at each time point (Tukey–Kramer test).

Journal: PLOS ONE

Article Title: Decrease in the expression of muscle-specific miRNAs, miR-133a and miR-1, in myoblasts with replicative senescence

doi: 10.1371/journal.pone.0280527

Figure Lengend Snippet: Panel A shows representative Western blots of MyoD1, Myogenin, myosin heavy chain (MHC), and tubulin (as an internal control) in C2C12 cells after myogenic differentiation. Cells were collected 7 days after differentiation for MyoD and MHC or 5 days after differentiation for myogenin. Panel B shows the time course of MyoD1, myogenin, and MHC protein expression after changing the medium for myogenic differentiation. The band density of MyoD, myogenin, or MHC was normalized with that of tubulin. The normalized density was compared with the average of the normalized density in passage 1 just before myogenic differentiation (day 0) in the MyoD and myogenin expressions. Because MHC expression was undetectable on day 0, the normalized density was compared with the average of the normalized density in passage 1, 7 days after myogenic differentiation. Data are presented as means ± SE (n = 4 dishes). *P < 0.05, **P < 0.01 vs. passage 1 at each time point; †P < 0.05, ††P < 0.01 vs. passage 10 at each time point (Tukey–Kramer test).

Article Snippet: After transfer, the membranes were incubated with antibodies specific to MHC (Clone MF20, R&D Systems), MyoD (18943-1-AP, Proteintech, Tokyo, Japan), β-tubulin (ab179513, abcam), p16 INK4a (10883-1-ap, Proteintech), or p21 (28248-1-AP, Proteintech).

Techniques: Western Blot, Expressing

Panel A shows the infusion index after 7 days of differentiation in cells transfected with miR-133a, miR-1, or both. Mock cells were transfected with a negative control miRNA. Data are presented as means ± SE (n = 10 dishes). **P < 0.01 (Tukey–Kramer test). Panels B–E show representative blots of MyoD1, myogenin, MHC, and tubulin (B), and quantitative data (C–E) in cells after differentiation for 7 days. The band density of MyoD1, myogenin, or myosin heavy chain (MHC) was normalized with that of tubulin. The normalized density was compared with the average of the normalized density in the mock group. Data are presented as means ± SE (n = 5 dishes). *P < 0.05 (Tukey–Kramer test).

Journal: PLOS ONE

Article Title: Decrease in the expression of muscle-specific miRNAs, miR-133a and miR-1, in myoblasts with replicative senescence

doi: 10.1371/journal.pone.0280527

Figure Lengend Snippet: Panel A shows the infusion index after 7 days of differentiation in cells transfected with miR-133a, miR-1, or both. Mock cells were transfected with a negative control miRNA. Data are presented as means ± SE (n = 10 dishes). **P < 0.01 (Tukey–Kramer test). Panels B–E show representative blots of MyoD1, myogenin, MHC, and tubulin (B), and quantitative data (C–E) in cells after differentiation for 7 days. The band density of MyoD1, myogenin, or myosin heavy chain (MHC) was normalized with that of tubulin. The normalized density was compared with the average of the normalized density in the mock group. Data are presented as means ± SE (n = 5 dishes). *P < 0.05 (Tukey–Kramer test).

Article Snippet: After transfer, the membranes were incubated with antibodies specific to MHC (Clone MF20, R&D Systems), MyoD (18943-1-AP, Proteintech, Tokyo, Japan), β-tubulin (ab179513, abcam), p16 INK4a (10883-1-ap, Proteintech), or p21 (28248-1-AP, Proteintech).

Techniques: Transfection, Negative Control