resource source identifier recombinant dna pdcx egfp Search Results


resource source identifier recombinant dna pdcx egfp  (Addgene inc)
96
Addgene inc resource source identifier recombinant dna pdcx egfp
Resource Source Identifier Recombinant Dna Pdcx Egfp, supplied by Addgene inc, 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/resource+source+identifier+recombinant+dna+pdcx+egfp/pSpCas9(BB)-2A-GFP+(PX458)+(Plasmid+%2348138)/pm39626666-214-2-17
Average 96 stars, based on 1 article reviews
resource source identifier recombinant dna pdcx egfp - by Bioz Stars, 2026-09
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recombinant proteins recombinant mouse pd 1  (MedChemExpress)
97
MedChemExpress recombinant proteins recombinant mouse pd 1
Figure 1. Synthesis and characterization of aPD-1-(iRGD)2 (A) The pattern diagram of the structure and chemical synthesis procedures of aPD-1-(iRGD)2. (B) Production of core substrate GDP-fucose-iRGD. (C) ESI-MS characterization of aPD-1-(iRGD)2. (D and E) The binding affinity of aPD-1-(iRGD)2 and unmodified antibody toward human (D) and murine <t>(E)</t> <t>PD-1</t> protein by ELISA.
Recombinant Proteins Recombinant Mouse Pd 1, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/resource+source+identifier+recombinant+dna+pdcx+egfp/PD-1+Antibody/pm38843844-210-93-100
Average 97 stars, based on 1 article reviews
recombinant proteins recombinant mouse pd 1 - by Bioz Stars, 2026-09
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cd274 double nickase plasmid  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology cd274 double nickase plasmid
Figure 1. USP22 is a DUB of <t>CD274.</t> A, Western blot analysis of CD274 expression in 293T cells expressing Flag-CD274 treated with DUB inhibitor PR-619. B, Identification of potential DUB binding to overexpressed Flag-CD274 in 293T cells. C, Endogenous coimmunoprecipitation to validate the USP22–CD274 interaction in HepG2, SMMC-7721, Hepa 1-6, and H22 cells. D, Pulldown assay with purified Flag-USP22 and recombinant N-terminal extracellular domain or C-terminal cytoplasmic tail and transmembrane domain of CD274. E, Western blot analysis of CD274 expression in WT HepG2 cells and three individual USP22 KO clones. F, Western blot analysis of CD274 expression in WT HepG2 cells transfected with dose-increasing Flag-USP22. G, Western blot analysis of CD274 expression in USP22 KO HepG2 cells transfected with WT USP22, USP22 enzymatically inactive mutant (USP22-C185A), and USP22 containing only the UCH domain (USP22-UCH). H, Western blot analysis of CD274 expression in WT and USP22 KO HepG2 cells treated with proteasome inhibitor MG132. I, Western blot analysis of CD274 expression in WT HepG2 cells transfected with Flag-USP22 and treated with MG132. J, Stability analysis of CD274 protein in WT and USP22 KO HepG2 cells treated with CHX. K, Stability analysis of CD274 protein in WT HepG2 cells overexpressing Flag-USP22 and treated with CHX. L, Ubiquitination assay of CD274 in WT and USP22 KO HepG2 cells cotransfected with HA-Ub and Flag-USP22 and treated with MG132. M, In vitro deubiquitination assay of ubiquitinated CD274 protein with purified Flag-USP22, Flag-USP22 CA. All blots in A–M are representative of at least three independent experiments.
Cd274 Double Nickase Plasmid, 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/resource+source+identifier+recombinant+dna+pdcx+egfp/Pdcd-1L1+Double+Nickase+Plasmid/10__1158_slash_2326___6066__cir___18___0910-35-45-51
Average 93 stars, based on 1 article reviews
cd274 double nickase plasmid - by Bioz Stars, 2026-09
93/100 stars
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Image Search Results


Figure 1. Synthesis and characterization of aPD-1-(iRGD)2 (A) The pattern diagram of the structure and chemical synthesis procedures of aPD-1-(iRGD)2. (B) Production of core substrate GDP-fucose-iRGD. (C) ESI-MS characterization of aPD-1-(iRGD)2. (D and E) The binding affinity of aPD-1-(iRGD)2 and unmodified antibody toward human (D) and murine (E) PD-1 protein by ELISA.

Journal: Cell reports. Medicine

Article Title: Glycoengineering-based anti-PD-1-iRGD peptide conjugate boosts antitumor efficacy through T cell engagement.

doi: 10.1016/j.xcrm.2024.101590

Figure Lengend Snippet: Figure 1. Synthesis and characterization of aPD-1-(iRGD)2 (A) The pattern diagram of the structure and chemical synthesis procedures of aPD-1-(iRGD)2. (B) Production of core substrate GDP-fucose-iRGD. (C) ESI-MS characterization of aPD-1-(iRGD)2. (D and E) The binding affinity of aPD-1-(iRGD)2 and unmodified antibody toward human (D) and murine (E) PD-1 protein by ELISA.

Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Anti-mouse NRP-1-PerCP5.5 Biolegend Cat# 145208, RRID:AB_2562034 Anti-mouse PD-L1-PerCP5.5 Biolegend Cat# 124334, RRID:AB_2629831 Anti-mouse CD11b-FITC Biolegend Cat# 101206, RRID:AB_312788 Anti-mouse CD11b-APC Biolegend Cat# 101212, RRID:AB_312795 Anti-mouse CD11c-FITC Biolegend Cat# 117306, RRID:AB_313775 Anti-mouse F4/80-FITC Biolegend Cat# 123108, RRID:AB_893502 Anti-mouse MHC II-APC Biolegend Cat# 107614, RRID:AB_313329 Anti-mouse CD83-PE Biolegend Cat# 121508, RRID:AB_572015 Anti-mouse CD103-PerCP Biolegend Cat# 121406, RRID:AB_1133989 Anti-mouse CD86-PerCP Biolegend Cat# 105028, RRID:AB_893420 Anti-mouse CD163-PE Biolegend Cat# 156704, RRID:AB_2860724 Anti-mouse Ly6G-PE Biolegend Cat# 127608, RRID:AB_1186104 Anti-mouse Ly6G-PC7 Biolegend Cat# 127618, RRID:AB_1877262 Anti-mouse NRP-1 Biolegend Cat# 145201, RRID:AB_2561840 Chemicals, peptides, and recombinant proteins Recombinant Mouse PD-1 (HEK293, His) MCE HY-P73724 Recombinant human PD-1 (HEK293, His) MCE HY-P7396 Blinatumomab MCE HY-P9963 FTY720 MCE HY-12005 Recombinant mouse IL7 Peprotech #210-07 Recombinant mouse IL15 Peprotech #210-15 Dynabeads for T cell activation/expansion TM Mouse T activator CD3/CD28 Gibco #11453D iRGD, c(CRGDKGPDC) Genescript Biotech Corporation N/A BCN-Cy5 Xi’an Ruixi Biological Technology Co., Ltd N/A N3-iRGD Nanjing Yuan Peptide Biotech Ltd. N/A OVA257-264 peptide Genscript Biotech Corporation N/A GP33 peptide Genscript Biotech Corporation N/A NY-ESO-1157-165 Genscript Biotech Corporation N/A collagenase IV Sigma-Aldrich C4-BIOC DNase I Sigma-Aldrich 04536282001 CFSE eBioscience #65-0850-84 Cell Proliferation Dye eFluorTM 670 eBioscience #65-0840-85 Cell Proliferation Dye eFluorTM 450 eBioscience #65-0842-90 CellTrackerTM Blue Invitrogen #C12881 Deep Red cell tracer Invitrogen #C37608 Zombie AquaTM Fixable Viability Kit Biolegend #423101 Critical commercial assays Cytofix/CytopermTM Fixation/Permeabilization Kit BD Biosciences #554714 Foxp3/transcription factor flow cytometry fixed membrane breaking buffer EBioscience #00-5523-00 GEXSCOPE Single Cell RNA-seq Kit Singleron Biotechnologies N/A Deposited data Mouse CD45+ cells single cell RNA-seq data This paper CNGB database: CNP0005642.

Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay

Figure 1. USP22 is a DUB of CD274. A, Western blot analysis of CD274 expression in 293T cells expressing Flag-CD274 treated with DUB inhibitor PR-619. B, Identification of potential DUB binding to overexpressed Flag-CD274 in 293T cells. C, Endogenous coimmunoprecipitation to validate the USP22–CD274 interaction in HepG2, SMMC-7721, Hepa 1-6, and H22 cells. D, Pulldown assay with purified Flag-USP22 and recombinant N-terminal extracellular domain or C-terminal cytoplasmic tail and transmembrane domain of CD274. E, Western blot analysis of CD274 expression in WT HepG2 cells and three individual USP22 KO clones. F, Western blot analysis of CD274 expression in WT HepG2 cells transfected with dose-increasing Flag-USP22. G, Western blot analysis of CD274 expression in USP22 KO HepG2 cells transfected with WT USP22, USP22 enzymatically inactive mutant (USP22-C185A), and USP22 containing only the UCH domain (USP22-UCH). H, Western blot analysis of CD274 expression in WT and USP22 KO HepG2 cells treated with proteasome inhibitor MG132. I, Western blot analysis of CD274 expression in WT HepG2 cells transfected with Flag-USP22 and treated with MG132. J, Stability analysis of CD274 protein in WT and USP22 KO HepG2 cells treated with CHX. K, Stability analysis of CD274 protein in WT HepG2 cells overexpressing Flag-USP22 and treated with CHX. L, Ubiquitination assay of CD274 in WT and USP22 KO HepG2 cells cotransfected with HA-Ub and Flag-USP22 and treated with MG132. M, In vitro deubiquitination assay of ubiquitinated CD274 protein with purified Flag-USP22, Flag-USP22 CA. All blots in A–M are representative of at least three independent experiments.

Journal: Cancer Immunology Research

Article Title: USP22 Deubiquitinates CD274 to Suppress Anticancer Immunity

doi: 10.1158/2326-6066.cir-18-0910

Figure Lengend Snippet: Figure 1. USP22 is a DUB of CD274. A, Western blot analysis of CD274 expression in 293T cells expressing Flag-CD274 treated with DUB inhibitor PR-619. B, Identification of potential DUB binding to overexpressed Flag-CD274 in 293T cells. C, Endogenous coimmunoprecipitation to validate the USP22–CD274 interaction in HepG2, SMMC-7721, Hepa 1-6, and H22 cells. D, Pulldown assay with purified Flag-USP22 and recombinant N-terminal extracellular domain or C-terminal cytoplasmic tail and transmembrane domain of CD274. E, Western blot analysis of CD274 expression in WT HepG2 cells and three individual USP22 KO clones. F, Western blot analysis of CD274 expression in WT HepG2 cells transfected with dose-increasing Flag-USP22. G, Western blot analysis of CD274 expression in USP22 KO HepG2 cells transfected with WT USP22, USP22 enzymatically inactive mutant (USP22-C185A), and USP22 containing only the UCH domain (USP22-UCH). H, Western blot analysis of CD274 expression in WT and USP22 KO HepG2 cells treated with proteasome inhibitor MG132. I, Western blot analysis of CD274 expression in WT HepG2 cells transfected with Flag-USP22 and treated with MG132. J, Stability analysis of CD274 protein in WT and USP22 KO HepG2 cells treated with CHX. K, Stability analysis of CD274 protein in WT HepG2 cells overexpressing Flag-USP22 and treated with CHX. L, Ubiquitination assay of CD274 in WT and USP22 KO HepG2 cells cotransfected with HA-Ub and Flag-USP22 and treated with MG132. M, In vitro deubiquitination assay of ubiquitinated CD274 protein with purified Flag-USP22, Flag-USP22 CA. All blots in A–M are representative of at least three independent experiments.

Article Snippet: Generation of CRISPR/Cas9-mediated knockout and doubleknockout cell lines To generate USP22 knockout (KO), CD274 KO, and USP22/ CD274 double KO (DKO) cell lines, cells were transfected or cotransfected with USP22 Double Nickase Plasmid (human; sc-403660-NIC, Santa Cruz), USP22 Double Nickase Plasmid (mouse; sc-432127-NIC, Santa Cruz), CD274 Double Nickase Plasmid (human; sc-401140-NIC, Santa Cruz), or USP22 Double Nickase Plasmid (human) together with CD274 Double Nickase Plasmid (human), respectively, according to the manufacturer's instructions.

Techniques: Western Blot, Expressing, Binding Assay, Recombinant, Clone Assay, Transfection, Mutagenesis, Ubiquitin Proteomics, In Vitro

Figure 2. USP22 depletion potentiates anticancer immunity. A, TCGA-based correlation analysis of USP22 and CD274 with genetic alterations. B–D, Tumor growth of WT and USP22 KO H22 cells in immunodeficient NCG mice. E–G, Tumor growth of WT and USP22 KO H22 cells in immunocompetent C57BL/6 mice. H–J, Tumor growth of WT and USP22 KO H22 cells inoculated in the same C57BL/6 mice. K–M, Therapeutic efficacy of anti-CD274 antibody on the tumor growth of WT and USP22 KO H22 cells in C57BL/6 mice. N–P, Therapeutic efficacy of CDDP on the tumor growth of WT and USP22 KO H22 cells in C57BL/6 mice. For all mouse experiments (B–P), schematic protocols are shown on the left; tumor growth was monitored at the indicated times and reported as the mean tumor surface size SD; and tumor weight was determined after sacrifice and reported as the mean tumor weight SD. All mice experiments were pooled from at least two rounds of independent experiments (n ¼ 10), and statistically significant differences were determined with an unpaired Student t test: , P < 0.05; , P < 0.01. ns, not significant.

Journal: Cancer Immunology Research

Article Title: USP22 Deubiquitinates CD274 to Suppress Anticancer Immunity

doi: 10.1158/2326-6066.cir-18-0910

Figure Lengend Snippet: Figure 2. USP22 depletion potentiates anticancer immunity. A, TCGA-based correlation analysis of USP22 and CD274 with genetic alterations. B–D, Tumor growth of WT and USP22 KO H22 cells in immunodeficient NCG mice. E–G, Tumor growth of WT and USP22 KO H22 cells in immunocompetent C57BL/6 mice. H–J, Tumor growth of WT and USP22 KO H22 cells inoculated in the same C57BL/6 mice. K–M, Therapeutic efficacy of anti-CD274 antibody on the tumor growth of WT and USP22 KO H22 cells in C57BL/6 mice. N–P, Therapeutic efficacy of CDDP on the tumor growth of WT and USP22 KO H22 cells in C57BL/6 mice. For all mouse experiments (B–P), schematic protocols are shown on the left; tumor growth was monitored at the indicated times and reported as the mean tumor surface size SD; and tumor weight was determined after sacrifice and reported as the mean tumor weight SD. All mice experiments were pooled from at least two rounds of independent experiments (n ¼ 10), and statistically significant differences were determined with an unpaired Student t test: , P < 0.05; , P < 0.01. ns, not significant.

Article Snippet: Generation of CRISPR/Cas9-mediated knockout and doubleknockout cell lines To generate USP22 knockout (KO), CD274 KO, and USP22/ CD274 double KO (DKO) cell lines, cells were transfected or cotransfected with USP22 Double Nickase Plasmid (human; sc-403660-NIC, Santa Cruz), USP22 Double Nickase Plasmid (mouse; sc-432127-NIC, Santa Cruz), CD274 Double Nickase Plasmid (human; sc-401140-NIC, Santa Cruz), or USP22 Double Nickase Plasmid (human) together with CD274 Double Nickase Plasmid (human), respectively, according to the manufacturer's instructions.

Techniques:

Figure 3. USP22 depletion enhances tumor infiltration of lymphocytes. A, Absolute number of CD3þ TILs in tumors derived from WT and USP22 KO H22 cells detected by flow cytometry. B, Relative ratio of CD8þGZMBþ cells in CD3þ TILs in tumors derived from WT and USP22 KO H22 cells detected by flow cytometry. C, Absolute number of CD3þ TILs in tumors derived from mice bearing both WT and USP22 KO H22 tumors as determined by flow cytometry. D, Relative ratio of CD8þGZMBþ cells in CD3þ TILs in tumors derived from mice bearing both WT and USP22 KO H22 tumors as determined by flow cytometry. E, Absolute number of CD3þ TILs in tumors derived from CD274-blocked WT and USP22 KO H22 cells as determined by flow cytometry. F, Relative ratio of CD8þGZMBþ cells in CD3þ TILs in tumors derived from CD274-blocked WT and USP22 KO H22 cells detected by flow cytometry. G, Absolute number of CD3þ

Journal: Cancer Immunology Research

Article Title: USP22 Deubiquitinates CD274 to Suppress Anticancer Immunity

doi: 10.1158/2326-6066.cir-18-0910

Figure Lengend Snippet: Figure 3. USP22 depletion enhances tumor infiltration of lymphocytes. A, Absolute number of CD3þ TILs in tumors derived from WT and USP22 KO H22 cells detected by flow cytometry. B, Relative ratio of CD8þGZMBþ cells in CD3þ TILs in tumors derived from WT and USP22 KO H22 cells detected by flow cytometry. C, Absolute number of CD3þ TILs in tumors derived from mice bearing both WT and USP22 KO H22 tumors as determined by flow cytometry. D, Relative ratio of CD8þGZMBþ cells in CD3þ TILs in tumors derived from mice bearing both WT and USP22 KO H22 tumors as determined by flow cytometry. E, Absolute number of CD3þ TILs in tumors derived from CD274-blocked WT and USP22 KO H22 cells as determined by flow cytometry. F, Relative ratio of CD8þGZMBþ cells in CD3þ TILs in tumors derived from CD274-blocked WT and USP22 KO H22 cells detected by flow cytometry. G, Absolute number of CD3þ

Article Snippet: Generation of CRISPR/Cas9-mediated knockout and doubleknockout cell lines To generate USP22 knockout (KO), CD274 KO, and USP22/ CD274 double KO (DKO) cell lines, cells were transfected or cotransfected with USP22 Double Nickase Plasmid (human; sc-403660-NIC, Santa Cruz), USP22 Double Nickase Plasmid (mouse; sc-432127-NIC, Santa Cruz), CD274 Double Nickase Plasmid (human; sc-401140-NIC, Santa Cruz), or USP22 Double Nickase Plasmid (human) together with CD274 Double Nickase Plasmid (human), respectively, according to the manufacturer's instructions.

Techniques: Derivative Assay, Cytometry

Figure 4. USP22 is a prognostic factor of liver cancer. A, Kaplan–Meier curves of survival analysis of USP22 in liver cancer patients (n ¼ 364). B, Kaplan–Meier curves of survival analysis of USP22 in sorafenib-treated liver cancer patients (n ¼ 29). C, Kaplan–Meier curves of survival analysis of USP22 in liver cancer patients with hepatitis virus (n ¼ 150). D, Kaplan–Meier curves of survival analysis of USP22 in liver cancer patients with alcohol consumption (n ¼ 115). E, HCC tissue microarray analysis of the expression correlation of USP22 and CD274 at protein level (n ¼ 333). F, HCC cDNA bank analysis of the expression correlation of USP22 and CD274 at mRNA level (n ¼ 185). The detailed R, HR, P, log-rank P value were individually shown as indicated, and P value < 0.05 was considered statistically significant.

Journal: Cancer Immunology Research

Article Title: USP22 Deubiquitinates CD274 to Suppress Anticancer Immunity

doi: 10.1158/2326-6066.cir-18-0910

Figure Lengend Snippet: Figure 4. USP22 is a prognostic factor of liver cancer. A, Kaplan–Meier curves of survival analysis of USP22 in liver cancer patients (n ¼ 364). B, Kaplan–Meier curves of survival analysis of USP22 in sorafenib-treated liver cancer patients (n ¼ 29). C, Kaplan–Meier curves of survival analysis of USP22 in liver cancer patients with hepatitis virus (n ¼ 150). D, Kaplan–Meier curves of survival analysis of USP22 in liver cancer patients with alcohol consumption (n ¼ 115). E, HCC tissue microarray analysis of the expression correlation of USP22 and CD274 at protein level (n ¼ 333). F, HCC cDNA bank analysis of the expression correlation of USP22 and CD274 at mRNA level (n ¼ 185). The detailed R, HR, P, log-rank P value were individually shown as indicated, and P value < 0.05 was considered statistically significant.

Article Snippet: Generation of CRISPR/Cas9-mediated knockout and doubleknockout cell lines To generate USP22 knockout (KO), CD274 KO, and USP22/ CD274 double KO (DKO) cell lines, cells were transfected or cotransfected with USP22 Double Nickase Plasmid (human; sc-403660-NIC, Santa Cruz), USP22 Double Nickase Plasmid (mouse; sc-432127-NIC, Santa Cruz), CD274 Double Nickase Plasmid (human; sc-401140-NIC, Santa Cruz), or USP22 Double Nickase Plasmid (human) together with CD274 Double Nickase Plasmid (human), respectively, according to the manufacturer's instructions.

Techniques: Virus, Microarray, Expressing