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Santa Cruz Biotechnology human enigma protein
Human Enigma Protein, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology human hif 1 alpha protein
HIF-1α expression in liver tissue. mRNA expression levels of HIF-1α ( A ), inducers of HIF-1α ( B ) and inhibitors ( C ) in the cholestatic model (BDL) causing chronic liver disease (CLD, n = 5); acute-on-chronic liver failure was induced by intravenous lipopolysaccharide injection ( n = 4). Respective mRNA expression levels in the CCl 4 model causing CLD ( n = 8 with CLD, n = 14 with ACLF) ( D – F ). Increased HIF-1α protein expression was confirmed by Western blotting, and signs of NFκB1 pathway activation were reflected by increased expression of IκB and pIκB ( G ). Effects on mRNA expression levels of downstream genes of HIF are depicted in ( H ). Note: ( G ) For the detection of HIF-1α expression via Western blotting, 30 ng of recombinant Human <t>HIF-1</t> alpha protein (#ab154478, Abcam, Cambridge, MA, USA) as a positive control (pos+), 50 µg of HeLa whole-cell extract as a negative control (neg−) and 100 µg of whole-protein extract from mouse liver tissues (CTRL, CLD and ACLF, respectively) were analyzed. For IκB and pIκB detection, 50 µg of HEK293T cell extract was used (positive control for IκB and pIκB) instead of HeLa extract, and only 50 µg of whole-protein extract from mouse liver tissues was used (CTRL, CLD, ACLF). * p < 0.05, ** p < 0.01, *** p < 0.001.
Human Hif 1 Alpha Protein, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "The Role of Hypoxia-Inducible Factor 1 Alpha in Acute-on-Chronic Liver Failure"

Article Title: The Role of Hypoxia-Inducible Factor 1 Alpha in Acute-on-Chronic Liver Failure

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms25031542

HIF-1α expression in liver tissue. mRNA expression levels of HIF-1α ( A ), inducers of HIF-1α ( B ) and inhibitors ( C ) in the cholestatic model (BDL) causing chronic liver disease (CLD, n = 5); acute-on-chronic liver failure was induced by intravenous lipopolysaccharide injection ( n = 4). Respective mRNA expression levels in the CCl 4 model causing CLD ( n = 8 with CLD, n = 14 with ACLF) ( D – F ). Increased HIF-1α protein expression was confirmed by Western blotting, and signs of NFκB1 pathway activation were reflected by increased expression of IκB and pIκB ( G ). Effects on mRNA expression levels of downstream genes of HIF are depicted in ( H ). Note: ( G ) For the detection of HIF-1α expression via Western blotting, 30 ng of recombinant Human HIF-1 alpha protein (#ab154478, Abcam, Cambridge, MA, USA) as a positive control (pos+), 50 µg of HeLa whole-cell extract as a negative control (neg−) and 100 µg of whole-protein extract from mouse liver tissues (CTRL, CLD and ACLF, respectively) were analyzed. For IκB and pIκB detection, 50 µg of HEK293T cell extract was used (positive control for IκB and pIκB) instead of HeLa extract, and only 50 µg of whole-protein extract from mouse liver tissues was used (CTRL, CLD, ACLF). * p < 0.05, ** p < 0.01, *** p < 0.001.
Figure Legend Snippet: HIF-1α expression in liver tissue. mRNA expression levels of HIF-1α ( A ), inducers of HIF-1α ( B ) and inhibitors ( C ) in the cholestatic model (BDL) causing chronic liver disease (CLD, n = 5); acute-on-chronic liver failure was induced by intravenous lipopolysaccharide injection ( n = 4). Respective mRNA expression levels in the CCl 4 model causing CLD ( n = 8 with CLD, n = 14 with ACLF) ( D – F ). Increased HIF-1α protein expression was confirmed by Western blotting, and signs of NFκB1 pathway activation were reflected by increased expression of IκB and pIκB ( G ). Effects on mRNA expression levels of downstream genes of HIF are depicted in ( H ). Note: ( G ) For the detection of HIF-1α expression via Western blotting, 30 ng of recombinant Human HIF-1 alpha protein (#ab154478, Abcam, Cambridge, MA, USA) as a positive control (pos+), 50 µg of HeLa whole-cell extract as a negative control (neg−) and 100 µg of whole-protein extract from mouse liver tissues (CTRL, CLD and ACLF, respectively) were analyzed. For IκB and pIκB detection, 50 µg of HEK293T cell extract was used (positive control for IκB and pIκB) instead of HeLa extract, and only 50 µg of whole-protein extract from mouse liver tissues was used (CTRL, CLD, ACLF). * p < 0.05, ** p < 0.01, *** p < 0.001.

Techniques Used: Expressing, Injection, Western Blot, Activation Assay, Recombinant, Positive Control, Negative Control

HIF-1α expression in liver tissue of the additional ACLF models. mRNA expression levels of HIF-1α ( A ), inducers of HIF-1α ( B ) and inhibitors ( C ) in the autoimmune hepatitis model causing chronic liver disease (CLD); acute-on-chronic liver failure was induced by systemic infection via intraperitoneal stool injection ( n = 6 for each group). Respective mRNA expression levels in the CCl 4 model with (CLD, n = 5) and without (CLD*, n = 5) additional alcohol ( D – F ); ACLF was induced by alcohol binges ( n = 4). Immunohistochemistry from rat liver tissue showed that HIF-1α was mainly localized in hepatocytes, and increased nuclear HIF-1α could be detected in ACLF ( G ). Immunohistochemistry of human tissue samples from patients with CLD, ACLF and healthy controls showed markedly elevated hepatic HIF-1α expression in ACLF specimens and areas of increased HIF-1α expression in CLD (darker brownish staining), while expression was less pronounced in healthy controls ( H ). * p < 0.05, ** p < 0.01, *** p < 0.001.
Figure Legend Snippet: HIF-1α expression in liver tissue of the additional ACLF models. mRNA expression levels of HIF-1α ( A ), inducers of HIF-1α ( B ) and inhibitors ( C ) in the autoimmune hepatitis model causing chronic liver disease (CLD); acute-on-chronic liver failure was induced by systemic infection via intraperitoneal stool injection ( n = 6 for each group). Respective mRNA expression levels in the CCl 4 model with (CLD, n = 5) and without (CLD*, n = 5) additional alcohol ( D – F ); ACLF was induced by alcohol binges ( n = 4). Immunohistochemistry from rat liver tissue showed that HIF-1α was mainly localized in hepatocytes, and increased nuclear HIF-1α could be detected in ACLF ( G ). Immunohistochemistry of human tissue samples from patients with CLD, ACLF and healthy controls showed markedly elevated hepatic HIF-1α expression in ACLF specimens and areas of increased HIF-1α expression in CLD (darker brownish staining), while expression was less pronounced in healthy controls ( H ). * p < 0.05, ** p < 0.01, *** p < 0.001.

Techniques Used: Expressing, Infection, Injection, Immunohistochemistry, Staining

HIF-1α mRNA expression in extrahepatic organs of the BDL model. Heat maps of HIF-1α and inducers and inhibitors of HIF-1α in transcriptome analysis of extrahepatic organs (control vs. CLD and CLD vs. ACLF) ( A ), mRNA expression levels of HIF-1α ( B ), inducers of HIF-1a ( C ) and inhibitors ( D ) in specimens from small bowel. Respective mRNA expression levels in specimens from skeletal muscle tissue ( E – G ). * p < 0.05, ** p < 0.01.
Figure Legend Snippet: HIF-1α mRNA expression in extrahepatic organs of the BDL model. Heat maps of HIF-1α and inducers and inhibitors of HIF-1α in transcriptome analysis of extrahepatic organs (control vs. CLD and CLD vs. ACLF) ( A ), mRNA expression levels of HIF-1α ( B ), inducers of HIF-1a ( C ) and inhibitors ( D ) in specimens from small bowel. Respective mRNA expression levels in specimens from skeletal muscle tissue ( E – G ). * p < 0.05, ** p < 0.01.

Techniques Used: Expressing


Structured Review

Santa Cruz Biotechnology human cd276 ecd protein
(A) Amino acid substitutions in m276-SL. (B) Chemical structure of m276-SL-PBD linker and warhead: maleimide (green), PEG-4 spacer (blue), and cathepsin-B-cleavablevaline-alanine dipeptide (red). The gray cloud indicates the cleavable amide group. (C–E) Cell viability assays were used to measure the activity of m276-SL-PBD and m276-glyco-PBD against the parent 293 <t>(CD276</t> wild type) or 293-CD276 KO (CD276 knockout) (C), HCT116 colon cancer (D), or UACC melanoma cells (E). Error bars denote SD. (F–I) Subcutaneous growth of HCT-116 (F) and UACC (H) tumors and corresponding Kaplan-Meier survival curves (HCT116, G; UACC, I). ADC treatments were initiated when tumors reached an average size of ~750 mm 3 and were administered on the days shown (red arrows); n = 8–30/group; p values: t test (F and H) and log-rank test (G and I). Median survival is indicated for arms with <50% of animals alive at study end. Error bars denote SEM. n.s., non-significant.
Human Cd276 Ecd Protein, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Engineering CD276/B7-H3-targeted antibody-drug conjugates with enhanced cancer-eradicating capability"

Article Title: Engineering CD276/B7-H3-targeted antibody-drug conjugates with enhanced cancer-eradicating capability

Journal: Cell reports

doi: 10.1016/j.celrep.2023.113503

(A) Amino acid substitutions in m276-SL. (B) Chemical structure of m276-SL-PBD linker and warhead: maleimide (green), PEG-4 spacer (blue), and cathepsin-B-cleavablevaline-alanine dipeptide (red). The gray cloud indicates the cleavable amide group. (C–E) Cell viability assays were used to measure the activity of m276-SL-PBD and m276-glyco-PBD against the parent 293 (CD276 wild type) or 293-CD276 KO (CD276 knockout) (C), HCT116 colon cancer (D), or UACC melanoma cells (E). Error bars denote SD. (F–I) Subcutaneous growth of HCT-116 (F) and UACC (H) tumors and corresponding Kaplan-Meier survival curves (HCT116, G; UACC, I). ADC treatments were initiated when tumors reached an average size of ~750 mm 3 and were administered on the days shown (red arrows); n = 8–30/group; p values: t test (F and H) and log-rank test (G and I). Median survival is indicated for arms with <50% of animals alive at study end. Error bars denote SEM. n.s., non-significant.
Figure Legend Snippet: (A) Amino acid substitutions in m276-SL. (B) Chemical structure of m276-SL-PBD linker and warhead: maleimide (green), PEG-4 spacer (blue), and cathepsin-B-cleavablevaline-alanine dipeptide (red). The gray cloud indicates the cleavable amide group. (C–E) Cell viability assays were used to measure the activity of m276-SL-PBD and m276-glyco-PBD against the parent 293 (CD276 wild type) or 293-CD276 KO (CD276 knockout) (C), HCT116 colon cancer (D), or UACC melanoma cells (E). Error bars denote SD. (F–I) Subcutaneous growth of HCT-116 (F) and UACC (H) tumors and corresponding Kaplan-Meier survival curves (HCT116, G; UACC, I). ADC treatments were initiated when tumors reached an average size of ~750 mm 3 and were administered on the days shown (red arrows); n = 8–30/group; p values: t test (F and H) and log-rank test (G and I). Median survival is indicated for arms with <50% of animals alive at study end. Error bars denote SEM. n.s., non-significant.

Techniques Used: Activity Assay, Knock-Out

(A) In vivo fluorescence imaging of Cy7-labeled m276 antibodies in JIMT tumor-bearing mice at 4, 24, 48, and 72 h post injection. Side-view images of the tumor flank are shown. An example of tumor and liver fluorescence is highlighted (white and yellow regions of interest [ROIs], respectively). (B) SEC monitoring of m276-SL-PBD samples with high-aggregate (HA) and low-aggregate (LA) composition pre- and post purification by SEC. Size standards are shown at the top. (C) Body weights in CD276-WT and -KO mice after three treatments (red arrows) with 2 mg/kg of LA and HA ADC samples from (B). Student’s t test; *p < 0.05 for m276-SL-PBD-LA in WT versus KO and m276-SL-PBD-HA in WT versus KO; n = 8–15/group. (D and E) Cell viability assays measured the activity of m276-SL-PBD pre- and post-HIC purification against HEK293 CD276-WT, CD276-KO (D), or CD276 + SUM159 breast cancer cells (E). HIC-enriched DAR1, DAR2, and DAR2-tail fractions were tested (see ). Error bars denote SD.
Figure Legend Snippet: (A) In vivo fluorescence imaging of Cy7-labeled m276 antibodies in JIMT tumor-bearing mice at 4, 24, 48, and 72 h post injection. Side-view images of the tumor flank are shown. An example of tumor and liver fluorescence is highlighted (white and yellow regions of interest [ROIs], respectively). (B) SEC monitoring of m276-SL-PBD samples with high-aggregate (HA) and low-aggregate (LA) composition pre- and post purification by SEC. Size standards are shown at the top. (C) Body weights in CD276-WT and -KO mice after three treatments (red arrows) with 2 mg/kg of LA and HA ADC samples from (B). Student’s t test; *p < 0.05 for m276-SL-PBD-LA in WT versus KO and m276-SL-PBD-HA in WT versus KO; n = 8–15/group. (D and E) Cell viability assays measured the activity of m276-SL-PBD pre- and post-HIC purification against HEK293 CD276-WT, CD276-KO (D), or CD276 + SUM159 breast cancer cells (E). HIC-enriched DAR1, DAR2, and DAR2-tail fractions were tested (see ). Error bars denote SD.

Techniques Used: In Vivo, Fluorescence, Imaging, Labeling, Injection, Purification, Activity Assay

(A) PET imaging at ~4, 24, 48, 72, 120, and 168 h post injection of 0.5 mg/kg [ 89 Zr]Zr-DFO-m276-SL-PBD ADC into mice with 9464D-CD276-WT (right flank) and 9464D-CD276-KO (left flank) tumors. (B) Quantification of tumor/liver labeling ratios from the PET study in (A). Error bars denote SD. (C) Biodistribution analysis 48 h post intravenous injection of [ 89 Zr]Zr-DFO-m276-SL antibody or [ 89 Zr] Zr-DFO-m276-SL-PBD ADC in CD276-wild-type (+/+) or -knockout (−/−) C57BL/6 mice. 9464D CD276-WT (right flank) and CD276-KO (left flank) tumors from the same mice were included for comparison. A one-way ANOVA determined p values between groups. Error bars denote SD. (D) Biodistribution analysis 48 h post injection of [ 89 Zr]Zr-DFO-m276-SL-PBD ADC in athymic nude mice with ES4-CD276-WT (right flank, R) and ES4-CD276-KO (left flank, L) Ewing’s tumors. T test determined p values between WT and KO ES4 tumors. Error bars denote SD. (E) Subcutaneous growth of ES4-CD276-WT (right flank, R) or ES4-CD276-KO (left flank, L) Ewing’s tumors after m276-SL-PBD treatment. Treatments (blue arrows) were initiated when tumors reached an average size of ~750 mm 3 ; n = 6–9/group. A t test determined p values between WT and KO ES4 tumors at the indicated time points. Error bars denote SEM. p values for (C)–(E): *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, and ****p ≤ 0.0001.
Figure Legend Snippet: (A) PET imaging at ~4, 24, 48, 72, 120, and 168 h post injection of 0.5 mg/kg [ 89 Zr]Zr-DFO-m276-SL-PBD ADC into mice with 9464D-CD276-WT (right flank) and 9464D-CD276-KO (left flank) tumors. (B) Quantification of tumor/liver labeling ratios from the PET study in (A). Error bars denote SD. (C) Biodistribution analysis 48 h post intravenous injection of [ 89 Zr]Zr-DFO-m276-SL antibody or [ 89 Zr] Zr-DFO-m276-SL-PBD ADC in CD276-wild-type (+/+) or -knockout (−/−) C57BL/6 mice. 9464D CD276-WT (right flank) and CD276-KO (left flank) tumors from the same mice were included for comparison. A one-way ANOVA determined p values between groups. Error bars denote SD. (D) Biodistribution analysis 48 h post injection of [ 89 Zr]Zr-DFO-m276-SL-PBD ADC in athymic nude mice with ES4-CD276-WT (right flank, R) and ES4-CD276-KO (left flank, L) Ewing’s tumors. T test determined p values between WT and KO ES4 tumors. Error bars denote SD. (E) Subcutaneous growth of ES4-CD276-WT (right flank, R) or ES4-CD276-KO (left flank, L) Ewing’s tumors after m276-SL-PBD treatment. Treatments (blue arrows) were initiated when tumors reached an average size of ~750 mm 3 ; n = 6–9/group. A t test determined p values between WT and KO ES4 tumors at the indicated time points. Error bars denote SEM. p values for (C)–(E): *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, and ****p ≤ 0.0001.

Techniques Used: Imaging, Injection, Labeling, Knock-Out, Comparison

(A and B) Cell viability assays measured m276-SL-PBD activity against glioblastoma/neuroblastoma (A) and pancreatic/breast cancer (B) cell lines. IC 50 values are in the key. Error bars were omitted for clarity; SD was always <10%. (C) Table of IC 50 values from cell viability assays showing the relative sensitivity of cancer cell lines to m276-SL-PBD. (D) CD276 mRNA expression in CD276-low B cell lymphocytic leukemia (BLL) and CD276-high glioblastoma (GBM), neuroblastoma (NB), pancreatic cancer (PC), and breast cancer (BC) cell lines using the database: DepMap mRNA expression. The number of cancer cell lines in each group is indicated in parentheses. Sensitive (blue dots) and resistant (back dot) cell lines used in the cell viability assays (A and B) are highlighted. (E and F) Tables showing glioblastoma/neuroblastoma (E) or pancreatic/breast cancer (F) cell line sensitivity (IC 50 values from cell viability assays) after SGD-1882-free drug treatment and CD276 surface expression levels (mean fluorescence intensity; MFI) as measured by flow cytometry. (G) Subcutaneous (IMR5) and orthotopic (SUM159 and MDA-MB-231) tumor volumes following ADC treatment. Treatments with 0.5 mg/kg m276-SL-PBD (blue arrows) were initiated when tumors reached ~1,000 mm 3 ; n = 8–10/group. Error bars denote SEM. (H) Bioluminescence imaging monitored systemic MDA-MB-231-luc tumor burden following intravenous injection into NRG mice, followed by randomization and treatment with vehicle or m276-SL-PBD. Representative mice shown (n = 15/group; DPI, days post inoculation). (I) Quantification of tumor burden from the MDA-MB-231 metastasis study in (H). Error bars denote SD. (J) Kaplan-Meier survival curves for the MDA-MB-231-luc metastases study in (H).
Figure Legend Snippet: (A and B) Cell viability assays measured m276-SL-PBD activity against glioblastoma/neuroblastoma (A) and pancreatic/breast cancer (B) cell lines. IC 50 values are in the key. Error bars were omitted for clarity; SD was always <10%. (C) Table of IC 50 values from cell viability assays showing the relative sensitivity of cancer cell lines to m276-SL-PBD. (D) CD276 mRNA expression in CD276-low B cell lymphocytic leukemia (BLL) and CD276-high glioblastoma (GBM), neuroblastoma (NB), pancreatic cancer (PC), and breast cancer (BC) cell lines using the database: DepMap mRNA expression. The number of cancer cell lines in each group is indicated in parentheses. Sensitive (blue dots) and resistant (back dot) cell lines used in the cell viability assays (A and B) are highlighted. (E and F) Tables showing glioblastoma/neuroblastoma (E) or pancreatic/breast cancer (F) cell line sensitivity (IC 50 values from cell viability assays) after SGD-1882-free drug treatment and CD276 surface expression levels (mean fluorescence intensity; MFI) as measured by flow cytometry. (G) Subcutaneous (IMR5) and orthotopic (SUM159 and MDA-MB-231) tumor volumes following ADC treatment. Treatments with 0.5 mg/kg m276-SL-PBD (blue arrows) were initiated when tumors reached ~1,000 mm 3 ; n = 8–10/group. Error bars denote SEM. (H) Bioluminescence imaging monitored systemic MDA-MB-231-luc tumor burden following intravenous injection into NRG mice, followed by randomization and treatment with vehicle or m276-SL-PBD. Representative mice shown (n = 15/group; DPI, days post inoculation). (I) Quantification of tumor burden from the MDA-MB-231 metastasis study in (H). Error bars denote SD. (J) Kaplan-Meier survival curves for the MDA-MB-231-luc metastases study in (H).

Techniques Used: Activity Assay, Expressing, Fluorescence, Flow Cytometry, Imaging, Injection

(A) Western blot analysis of CD276 and HER2 levels in JIMT and DU4475 breast cancer cells. (B and C) Cell viability assays measured trastuzumab-SL-PBD and m276-SL-PBD activity against JIMT (B) and DU4475 (C) breast cancer cells. Non-specific IgG-SL-PBD served as a non-binding control. Error bars denote SD. (D and E) Orthotopic growth of JIMT (D) and DU4475 (E) breast tumors in response to trastuzumab-SL-PBD and m276-SL-PBD treatment. ADC treatments (0.5 mg/kg) were initiated when tumor volumes reached ~750–1,000 mm 3 and administered on the days shown (green arrows). Relapsed tumors in the m276-SL-PBD group were re-treated five times with ADC (blue arrows) when tumor volumes reached an average of ~750 mm 3 ; n = 5–8/group. Error bars denote SEM.
Figure Legend Snippet: (A) Western blot analysis of CD276 and HER2 levels in JIMT and DU4475 breast cancer cells. (B and C) Cell viability assays measured trastuzumab-SL-PBD and m276-SL-PBD activity against JIMT (B) and DU4475 (C) breast cancer cells. Non-specific IgG-SL-PBD served as a non-binding control. Error bars denote SD. (D and E) Orthotopic growth of JIMT (D) and DU4475 (E) breast tumors in response to trastuzumab-SL-PBD and m276-SL-PBD treatment. ADC treatments (0.5 mg/kg) were initiated when tumor volumes reached ~750–1,000 mm 3 and administered on the days shown (green arrows). Relapsed tumors in the m276-SL-PBD group were re-treated five times with ADC (blue arrows) when tumor volumes reached an average of ~750 mm 3 ; n = 5–8/group. Error bars denote SEM.

Techniques Used: Western Blot, Activity Assay, Binding Assay

(A and B) Immunofluorescence staining for CD276 (green) in BCM-5471, BCM-4013, and BCM-4272 (B) breast cancer PDX models. Tumor endothelium was co-stained with CD31 (red), confirming CD276 expression in both tumor cells and tumor vasculature. Non-specific IgG (A) served as a non-binding control. Scale bars in (A) and (B), 50 μm. (C–E) Orthotopic growth of BCM-5471 (C), BCM-4013 (D), and BCM-4272 (E) breast tumors following treatment with vehicle (control) or 50 or 100 μg/kg m276-SL-PBD. Treatments with m276-SL-PBD were initiated when tumor volumes reached ~1,000 mm 3 and were administered on the days shown (blue arrows); n = 7–8/group. Error bars denote SEM.
Figure Legend Snippet: (A and B) Immunofluorescence staining for CD276 (green) in BCM-5471, BCM-4013, and BCM-4272 (B) breast cancer PDX models. Tumor endothelium was co-stained with CD31 (red), confirming CD276 expression in both tumor cells and tumor vasculature. Non-specific IgG (A) served as a non-binding control. Scale bars in (A) and (B), 50 μm. (C–E) Orthotopic growth of BCM-5471 (C), BCM-4013 (D), and BCM-4272 (E) breast tumors following treatment with vehicle (control) or 50 or 100 μg/kg m276-SL-PBD. Treatments with m276-SL-PBD were initiated when tumor volumes reached ~1,000 mm 3 and were administered on the days shown (blue arrows); n = 7–8/group. Error bars denote SEM.

Techniques Used: Immunofluorescence, Staining, Expressing, Binding Assay

KEY RESOURCES TABLE
Figure Legend Snippet: KEY RESOURCES TABLE

Techniques Used: Recombinant, Fluorescence, Blocking Assay, Plasmid Preparation, Expressing, Software


Structured Review

Santa Cruz Biotechnology stromal cells50 human protein atlas
Stromal Cells50 Human Protein Atlas, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology human cd276 ecd protein
Human Cd276 Ecd Protein, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology length human mog protein
Length Human Mog Protein, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology antibodies against human proteins
Antibodies Against Human Proteins, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology antibodies against human proteins
Antibodies Against Human Proteins, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti human lysosomal associated membrane protein 1 lamp1  (Santa Cruz Biotechnology)

 
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    Structured Review

    Santa Cruz Biotechnology mouse anti human lysosomal associated membrane protein 1 lamp1
    A , B Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and tested for p-AMPKα and AMPKα by Western blot and flow cytometry. Mean ± SEM from 5 individuals in each group. C Co-localization of AMPK with <t>LAMP1</t> + lysosomes detected by confocal microscopy. A representative from 3 individuals per group. Scale bar, 5 μm. Mean ± SEM from 30 individuals in each group. D , E Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and detected for p-S6 and p-AKT. Mean ± SEM from 5 individuals in each group. F , G A549 cell pre-conditioned CD4 + T cells were activated with anti-CD3/CD28 beads for 3 days in the presence or absence of AMPK inhibitor Compound C (10 μM), followed by detection of T cell differentiation. Mean ± SEM from 5 individuals in each group. * p < 0.05, ** p < 0.01 with paired student t -test ( A – E ) and ANOVA plus Tukey method ( F , G ).
    Mouse Anti Human Lysosomal Associated Membrane Protein 1 Lamp1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Cancer CD39 drives metabolic adaption and mal-differentiation of CD4 + T cells in patients with non-small-cell lung cancer"

    Article Title: Cancer CD39 drives metabolic adaption and mal-differentiation of CD4 + T cells in patients with non-small-cell lung cancer

    Journal: Cell Death & Disease

    doi: 10.1038/s41419-023-06336-4

    A , B Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and tested for p-AMPKα and AMPKα by Western blot and flow cytometry. Mean ± SEM from 5 individuals in each group. C Co-localization of AMPK with LAMP1 + lysosomes detected by confocal microscopy. A representative from 3 individuals per group. Scale bar, 5 μm. Mean ± SEM from 30 individuals in each group. D , E Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and detected for p-S6 and p-AKT. Mean ± SEM from 5 individuals in each group. F , G A549 cell pre-conditioned CD4 + T cells were activated with anti-CD3/CD28 beads for 3 days in the presence or absence of AMPK inhibitor Compound C (10 μM), followed by detection of T cell differentiation. Mean ± SEM from 5 individuals in each group. * p < 0.05, ** p < 0.01 with paired student t -test ( A – E ) and ANOVA plus Tukey method ( F , G ).
    Figure Legend Snippet: A , B Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and tested for p-AMPKα and AMPKα by Western blot and flow cytometry. Mean ± SEM from 5 individuals in each group. C Co-localization of AMPK with LAMP1 + lysosomes detected by confocal microscopy. A representative from 3 individuals per group. Scale bar, 5 μm. Mean ± SEM from 30 individuals in each group. D , E Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and detected for p-S6 and p-AKT. Mean ± SEM from 5 individuals in each group. F , G A549 cell pre-conditioned CD4 + T cells were activated with anti-CD3/CD28 beads for 3 days in the presence or absence of AMPK inhibitor Compound C (10 μM), followed by detection of T cell differentiation. Mean ± SEM from 5 individuals in each group. * p < 0.05, ** p < 0.01 with paired student t -test ( A – E ) and ANOVA plus Tukey method ( F , G ).

    Techniques Used: Western Blot, Flow Cytometry, Confocal Microscopy, Cell Differentiation


    Structured Review

    Santa Cruz Biotechnology recombinant human semaphorin 7a fc chimera protein
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    Santa Cruz Biotechnology human enigma protein
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    (A) Amino acid substitutions in m276-SL. (B) Chemical structure of m276-SL-PBD linker and warhead: maleimide (green), PEG-4 spacer (blue), and cathepsin-B-cleavablevaline-alanine dipeptide (red). The gray cloud indicates the cleavable amide group. (C–E) Cell viability assays were used to measure the activity of m276-SL-PBD and m276-glyco-PBD against the parent 293 <t>(CD276</t> wild type) or 293-CD276 KO (CD276 knockout) (C), HCT116 colon cancer (D), or UACC melanoma cells (E). Error bars denote SD. (F–I) Subcutaneous growth of HCT-116 (F) and UACC (H) tumors and corresponding Kaplan-Meier survival curves (HCT116, G; UACC, I). ADC treatments were initiated when tumors reached an average size of ~750 mm 3 and were administered on the days shown (red arrows); n = 8–30/group; p values: t test (F and H) and log-rank test (G and I). Median survival is indicated for arms with <50% of animals alive at study end. Error bars denote SEM. n.s., non-significant.
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    (A) Amino acid substitutions in m276-SL. (B) Chemical structure of m276-SL-PBD linker and warhead: maleimide (green), PEG-4 spacer (blue), and cathepsin-B-cleavablevaline-alanine dipeptide (red). The gray cloud indicates the cleavable amide group. (C–E) Cell viability assays were used to measure the activity of m276-SL-PBD and m276-glyco-PBD against the parent 293 <t>(CD276</t> wild type) or 293-CD276 KO (CD276 knockout) (C), HCT116 colon cancer (D), or UACC melanoma cells (E). Error bars denote SD. (F–I) Subcutaneous growth of HCT-116 (F) and UACC (H) tumors and corresponding Kaplan-Meier survival curves (HCT116, G; UACC, I). ADC treatments were initiated when tumors reached an average size of ~750 mm 3 and were administered on the days shown (red arrows); n = 8–30/group; p values: t test (F and H) and log-rank test (G and I). Median survival is indicated for arms with <50% of animals alive at study end. Error bars denote SEM. n.s., non-significant.
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    HIF-1α expression in liver tissue. mRNA expression levels of HIF-1α ( A ), inducers of HIF-1α ( B ) and inhibitors ( C ) in the cholestatic model (BDL) causing chronic liver disease (CLD, n = 5); acute-on-chronic liver failure was induced by intravenous lipopolysaccharide injection ( n = 4). Respective mRNA expression levels in the CCl 4 model causing CLD ( n = 8 with CLD, n = 14 with ACLF) ( D – F ). Increased HIF-1α protein expression was confirmed by Western blotting, and signs of NFκB1 pathway activation were reflected by increased expression of IκB and pIκB ( G ). Effects on mRNA expression levels of downstream genes of HIF are depicted in ( H ). Note: ( G ) For the detection of HIF-1α expression via Western blotting, 30 ng of recombinant Human HIF-1 alpha protein (#ab154478, Abcam, Cambridge, MA, USA) as a positive control (pos+), 50 µg of HeLa whole-cell extract as a negative control (neg−) and 100 µg of whole-protein extract from mouse liver tissues (CTRL, CLD and ACLF, respectively) were analyzed. For IκB and pIκB detection, 50 µg of HEK293T cell extract was used (positive control for IκB and pIκB) instead of HeLa extract, and only 50 µg of whole-protein extract from mouse liver tissues was used (CTRL, CLD, ACLF). * p < 0.05, ** p < 0.01, *** p < 0.001.

    Journal: International Journal of Molecular Sciences

    Article Title: The Role of Hypoxia-Inducible Factor 1 Alpha in Acute-on-Chronic Liver Failure

    doi: 10.3390/ijms25031542

    Figure Lengend Snippet: HIF-1α expression in liver tissue. mRNA expression levels of HIF-1α ( A ), inducers of HIF-1α ( B ) and inhibitors ( C ) in the cholestatic model (BDL) causing chronic liver disease (CLD, n = 5); acute-on-chronic liver failure was induced by intravenous lipopolysaccharide injection ( n = 4). Respective mRNA expression levels in the CCl 4 model causing CLD ( n = 8 with CLD, n = 14 with ACLF) ( D – F ). Increased HIF-1α protein expression was confirmed by Western blotting, and signs of NFκB1 pathway activation were reflected by increased expression of IκB and pIκB ( G ). Effects on mRNA expression levels of downstream genes of HIF are depicted in ( H ). Note: ( G ) For the detection of HIF-1α expression via Western blotting, 30 ng of recombinant Human HIF-1 alpha protein (#ab154478, Abcam, Cambridge, MA, USA) as a positive control (pos+), 50 µg of HeLa whole-cell extract as a negative control (neg−) and 100 µg of whole-protein extract from mouse liver tissues (CTRL, CLD and ACLF, respectively) were analyzed. For IκB and pIκB detection, 50 µg of HEK293T cell extract was used (positive control for IκB and pIκB) instead of HeLa extract, and only 50 µg of whole-protein extract from mouse liver tissues was used (CTRL, CLD, ACLF). * p < 0.05, ** p < 0.01, *** p < 0.001.

    Article Snippet: For the detection of IκB, as well as pIκB, 30 ng of recombinant Human HIF-1 alpha protein, 50 µg of HEK293T whole-cell extract (as endogenous expression of IκB has been described for HEK293T cells, Santa Cruz, Dallas, TX, USA) [ ] and 50 µg of whole-protein extract from liver tissues were used.

    Techniques: Expressing, Injection, Western Blot, Activation Assay, Recombinant, Positive Control, Negative Control

    HIF-1α expression in liver tissue of the additional ACLF models. mRNA expression levels of HIF-1α ( A ), inducers of HIF-1α ( B ) and inhibitors ( C ) in the autoimmune hepatitis model causing chronic liver disease (CLD); acute-on-chronic liver failure was induced by systemic infection via intraperitoneal stool injection ( n = 6 for each group). Respective mRNA expression levels in the CCl 4 model with (CLD, n = 5) and without (CLD*, n = 5) additional alcohol ( D – F ); ACLF was induced by alcohol binges ( n = 4). Immunohistochemistry from rat liver tissue showed that HIF-1α was mainly localized in hepatocytes, and increased nuclear HIF-1α could be detected in ACLF ( G ). Immunohistochemistry of human tissue samples from patients with CLD, ACLF and healthy controls showed markedly elevated hepatic HIF-1α expression in ACLF specimens and areas of increased HIF-1α expression in CLD (darker brownish staining), while expression was less pronounced in healthy controls ( H ). * p < 0.05, ** p < 0.01, *** p < 0.001.

    Journal: International Journal of Molecular Sciences

    Article Title: The Role of Hypoxia-Inducible Factor 1 Alpha in Acute-on-Chronic Liver Failure

    doi: 10.3390/ijms25031542

    Figure Lengend Snippet: HIF-1α expression in liver tissue of the additional ACLF models. mRNA expression levels of HIF-1α ( A ), inducers of HIF-1α ( B ) and inhibitors ( C ) in the autoimmune hepatitis model causing chronic liver disease (CLD); acute-on-chronic liver failure was induced by systemic infection via intraperitoneal stool injection ( n = 6 for each group). Respective mRNA expression levels in the CCl 4 model with (CLD, n = 5) and without (CLD*, n = 5) additional alcohol ( D – F ); ACLF was induced by alcohol binges ( n = 4). Immunohistochemistry from rat liver tissue showed that HIF-1α was mainly localized in hepatocytes, and increased nuclear HIF-1α could be detected in ACLF ( G ). Immunohistochemistry of human tissue samples from patients with CLD, ACLF and healthy controls showed markedly elevated hepatic HIF-1α expression in ACLF specimens and areas of increased HIF-1α expression in CLD (darker brownish staining), while expression was less pronounced in healthy controls ( H ). * p < 0.05, ** p < 0.01, *** p < 0.001.

    Article Snippet: For the detection of IκB, as well as pIκB, 30 ng of recombinant Human HIF-1 alpha protein, 50 µg of HEK293T whole-cell extract (as endogenous expression of IκB has been described for HEK293T cells, Santa Cruz, Dallas, TX, USA) [ ] and 50 µg of whole-protein extract from liver tissues were used.

    Techniques: Expressing, Infection, Injection, Immunohistochemistry, Staining

    HIF-1α mRNA expression in extrahepatic organs of the BDL model. Heat maps of HIF-1α and inducers and inhibitors of HIF-1α in transcriptome analysis of extrahepatic organs (control vs. CLD and CLD vs. ACLF) ( A ), mRNA expression levels of HIF-1α ( B ), inducers of HIF-1a ( C ) and inhibitors ( D ) in specimens from small bowel. Respective mRNA expression levels in specimens from skeletal muscle tissue ( E – G ). * p < 0.05, ** p < 0.01.

    Journal: International Journal of Molecular Sciences

    Article Title: The Role of Hypoxia-Inducible Factor 1 Alpha in Acute-on-Chronic Liver Failure

    doi: 10.3390/ijms25031542

    Figure Lengend Snippet: HIF-1α mRNA expression in extrahepatic organs of the BDL model. Heat maps of HIF-1α and inducers and inhibitors of HIF-1α in transcriptome analysis of extrahepatic organs (control vs. CLD and CLD vs. ACLF) ( A ), mRNA expression levels of HIF-1α ( B ), inducers of HIF-1a ( C ) and inhibitors ( D ) in specimens from small bowel. Respective mRNA expression levels in specimens from skeletal muscle tissue ( E – G ). * p < 0.05, ** p < 0.01.

    Article Snippet: For the detection of IκB, as well as pIκB, 30 ng of recombinant Human HIF-1 alpha protein, 50 µg of HEK293T whole-cell extract (as endogenous expression of IκB has been described for HEK293T cells, Santa Cruz, Dallas, TX, USA) [ ] and 50 µg of whole-protein extract from liver tissues were used.

    Techniques: Expressing

    (A) Amino acid substitutions in m276-SL. (B) Chemical structure of m276-SL-PBD linker and warhead: maleimide (green), PEG-4 spacer (blue), and cathepsin-B-cleavablevaline-alanine dipeptide (red). The gray cloud indicates the cleavable amide group. (C–E) Cell viability assays were used to measure the activity of m276-SL-PBD and m276-glyco-PBD against the parent 293 (CD276 wild type) or 293-CD276 KO (CD276 knockout) (C), HCT116 colon cancer (D), or UACC melanoma cells (E). Error bars denote SD. (F–I) Subcutaneous growth of HCT-116 (F) and UACC (H) tumors and corresponding Kaplan-Meier survival curves (HCT116, G; UACC, I). ADC treatments were initiated when tumors reached an average size of ~750 mm 3 and were administered on the days shown (red arrows); n = 8–30/group; p values: t test (F and H) and log-rank test (G and I). Median survival is indicated for arms with <50% of animals alive at study end. Error bars denote SEM. n.s., non-significant.

    Journal: Cell reports

    Article Title: Engineering CD276/B7-H3-targeted antibody-drug conjugates with enhanced cancer-eradicating capability

    doi: 10.1016/j.celrep.2023.113503

    Figure Lengend Snippet: (A) Amino acid substitutions in m276-SL. (B) Chemical structure of m276-SL-PBD linker and warhead: maleimide (green), PEG-4 spacer (blue), and cathepsin-B-cleavablevaline-alanine dipeptide (red). The gray cloud indicates the cleavable amide group. (C–E) Cell viability assays were used to measure the activity of m276-SL-PBD and m276-glyco-PBD against the parent 293 (CD276 wild type) or 293-CD276 KO (CD276 knockout) (C), HCT116 colon cancer (D), or UACC melanoma cells (E). Error bars denote SD. (F–I) Subcutaneous growth of HCT-116 (F) and UACC (H) tumors and corresponding Kaplan-Meier survival curves (HCT116, G; UACC, I). ADC treatments were initiated when tumors reached an average size of ~750 mm 3 and were administered on the days shown (red arrows); n = 8–30/group; p values: t test (F and H) and log-rank test (G and I). Median survival is indicated for arms with <50% of animals alive at study end. Error bars denote SEM. n.s., non-significant.

    Article Snippet: To compare m276-SL and m276SL-PBD binding to CD276, human CD276 ECD protein was coated onto a high-binding ELISA plate (Santa Cruz, #sc-204463) at 100 ng/well overnight at 4°C.

    Techniques: Activity Assay, Knock-Out

    (A) In vivo fluorescence imaging of Cy7-labeled m276 antibodies in JIMT tumor-bearing mice at 4, 24, 48, and 72 h post injection. Side-view images of the tumor flank are shown. An example of tumor and liver fluorescence is highlighted (white and yellow regions of interest [ROIs], respectively). (B) SEC monitoring of m276-SL-PBD samples with high-aggregate (HA) and low-aggregate (LA) composition pre- and post purification by SEC. Size standards are shown at the top. (C) Body weights in CD276-WT and -KO mice after three treatments (red arrows) with 2 mg/kg of LA and HA ADC samples from (B). Student’s t test; *p < 0.05 for m276-SL-PBD-LA in WT versus KO and m276-SL-PBD-HA in WT versus KO; n = 8–15/group. (D and E) Cell viability assays measured the activity of m276-SL-PBD pre- and post-HIC purification against HEK293 CD276-WT, CD276-KO (D), or CD276 + SUM159 breast cancer cells (E). HIC-enriched DAR1, DAR2, and DAR2-tail fractions were tested (see ). Error bars denote SD.

    Journal: Cell reports

    Article Title: Engineering CD276/B7-H3-targeted antibody-drug conjugates with enhanced cancer-eradicating capability

    doi: 10.1016/j.celrep.2023.113503

    Figure Lengend Snippet: (A) In vivo fluorescence imaging of Cy7-labeled m276 antibodies in JIMT tumor-bearing mice at 4, 24, 48, and 72 h post injection. Side-view images of the tumor flank are shown. An example of tumor and liver fluorescence is highlighted (white and yellow regions of interest [ROIs], respectively). (B) SEC monitoring of m276-SL-PBD samples with high-aggregate (HA) and low-aggregate (LA) composition pre- and post purification by SEC. Size standards are shown at the top. (C) Body weights in CD276-WT and -KO mice after three treatments (red arrows) with 2 mg/kg of LA and HA ADC samples from (B). Student’s t test; *p < 0.05 for m276-SL-PBD-LA in WT versus KO and m276-SL-PBD-HA in WT versus KO; n = 8–15/group. (D and E) Cell viability assays measured the activity of m276-SL-PBD pre- and post-HIC purification against HEK293 CD276-WT, CD276-KO (D), or CD276 + SUM159 breast cancer cells (E). HIC-enriched DAR1, DAR2, and DAR2-tail fractions were tested (see ). Error bars denote SD.

    Article Snippet: To compare m276-SL and m276SL-PBD binding to CD276, human CD276 ECD protein was coated onto a high-binding ELISA plate (Santa Cruz, #sc-204463) at 100 ng/well overnight at 4°C.

    Techniques: In Vivo, Fluorescence, Imaging, Labeling, Injection, Purification, Activity Assay

    (A) PET imaging at ~4, 24, 48, 72, 120, and 168 h post injection of 0.5 mg/kg [ 89 Zr]Zr-DFO-m276-SL-PBD ADC into mice with 9464D-CD276-WT (right flank) and 9464D-CD276-KO (left flank) tumors. (B) Quantification of tumor/liver labeling ratios from the PET study in (A). Error bars denote SD. (C) Biodistribution analysis 48 h post intravenous injection of [ 89 Zr]Zr-DFO-m276-SL antibody or [ 89 Zr] Zr-DFO-m276-SL-PBD ADC in CD276-wild-type (+/+) or -knockout (−/−) C57BL/6 mice. 9464D CD276-WT (right flank) and CD276-KO (left flank) tumors from the same mice were included for comparison. A one-way ANOVA determined p values between groups. Error bars denote SD. (D) Biodistribution analysis 48 h post injection of [ 89 Zr]Zr-DFO-m276-SL-PBD ADC in athymic nude mice with ES4-CD276-WT (right flank, R) and ES4-CD276-KO (left flank, L) Ewing’s tumors. T test determined p values between WT and KO ES4 tumors. Error bars denote SD. (E) Subcutaneous growth of ES4-CD276-WT (right flank, R) or ES4-CD276-KO (left flank, L) Ewing’s tumors after m276-SL-PBD treatment. Treatments (blue arrows) were initiated when tumors reached an average size of ~750 mm 3 ; n = 6–9/group. A t test determined p values between WT and KO ES4 tumors at the indicated time points. Error bars denote SEM. p values for (C)–(E): *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, and ****p ≤ 0.0001.

    Journal: Cell reports

    Article Title: Engineering CD276/B7-H3-targeted antibody-drug conjugates with enhanced cancer-eradicating capability

    doi: 10.1016/j.celrep.2023.113503

    Figure Lengend Snippet: (A) PET imaging at ~4, 24, 48, 72, 120, and 168 h post injection of 0.5 mg/kg [ 89 Zr]Zr-DFO-m276-SL-PBD ADC into mice with 9464D-CD276-WT (right flank) and 9464D-CD276-KO (left flank) tumors. (B) Quantification of tumor/liver labeling ratios from the PET study in (A). Error bars denote SD. (C) Biodistribution analysis 48 h post intravenous injection of [ 89 Zr]Zr-DFO-m276-SL antibody or [ 89 Zr] Zr-DFO-m276-SL-PBD ADC in CD276-wild-type (+/+) or -knockout (−/−) C57BL/6 mice. 9464D CD276-WT (right flank) and CD276-KO (left flank) tumors from the same mice were included for comparison. A one-way ANOVA determined p values between groups. Error bars denote SD. (D) Biodistribution analysis 48 h post injection of [ 89 Zr]Zr-DFO-m276-SL-PBD ADC in athymic nude mice with ES4-CD276-WT (right flank, R) and ES4-CD276-KO (left flank, L) Ewing’s tumors. T test determined p values between WT and KO ES4 tumors. Error bars denote SD. (E) Subcutaneous growth of ES4-CD276-WT (right flank, R) or ES4-CD276-KO (left flank, L) Ewing’s tumors after m276-SL-PBD treatment. Treatments (blue arrows) were initiated when tumors reached an average size of ~750 mm 3 ; n = 6–9/group. A t test determined p values between WT and KO ES4 tumors at the indicated time points. Error bars denote SEM. p values for (C)–(E): *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, and ****p ≤ 0.0001.

    Article Snippet: To compare m276-SL and m276SL-PBD binding to CD276, human CD276 ECD protein was coated onto a high-binding ELISA plate (Santa Cruz, #sc-204463) at 100 ng/well overnight at 4°C.

    Techniques: Imaging, Injection, Labeling, Knock-Out, Comparison

    (A and B) Cell viability assays measured m276-SL-PBD activity against glioblastoma/neuroblastoma (A) and pancreatic/breast cancer (B) cell lines. IC 50 values are in the key. Error bars were omitted for clarity; SD was always <10%. (C) Table of IC 50 values from cell viability assays showing the relative sensitivity of cancer cell lines to m276-SL-PBD. (D) CD276 mRNA expression in CD276-low B cell lymphocytic leukemia (BLL) and CD276-high glioblastoma (GBM), neuroblastoma (NB), pancreatic cancer (PC), and breast cancer (BC) cell lines using the database: DepMap mRNA expression. The number of cancer cell lines in each group is indicated in parentheses. Sensitive (blue dots) and resistant (back dot) cell lines used in the cell viability assays (A and B) are highlighted. (E and F) Tables showing glioblastoma/neuroblastoma (E) or pancreatic/breast cancer (F) cell line sensitivity (IC 50 values from cell viability assays) after SGD-1882-free drug treatment and CD276 surface expression levels (mean fluorescence intensity; MFI) as measured by flow cytometry. (G) Subcutaneous (IMR5) and orthotopic (SUM159 and MDA-MB-231) tumor volumes following ADC treatment. Treatments with 0.5 mg/kg m276-SL-PBD (blue arrows) were initiated when tumors reached ~1,000 mm 3 ; n = 8–10/group. Error bars denote SEM. (H) Bioluminescence imaging monitored systemic MDA-MB-231-luc tumor burden following intravenous injection into NRG mice, followed by randomization and treatment with vehicle or m276-SL-PBD. Representative mice shown (n = 15/group; DPI, days post inoculation). (I) Quantification of tumor burden from the MDA-MB-231 metastasis study in (H). Error bars denote SD. (J) Kaplan-Meier survival curves for the MDA-MB-231-luc metastases study in (H).

    Journal: Cell reports

    Article Title: Engineering CD276/B7-H3-targeted antibody-drug conjugates with enhanced cancer-eradicating capability

    doi: 10.1016/j.celrep.2023.113503

    Figure Lengend Snippet: (A and B) Cell viability assays measured m276-SL-PBD activity against glioblastoma/neuroblastoma (A) and pancreatic/breast cancer (B) cell lines. IC 50 values are in the key. Error bars were omitted for clarity; SD was always <10%. (C) Table of IC 50 values from cell viability assays showing the relative sensitivity of cancer cell lines to m276-SL-PBD. (D) CD276 mRNA expression in CD276-low B cell lymphocytic leukemia (BLL) and CD276-high glioblastoma (GBM), neuroblastoma (NB), pancreatic cancer (PC), and breast cancer (BC) cell lines using the database: DepMap mRNA expression. The number of cancer cell lines in each group is indicated in parentheses. Sensitive (blue dots) and resistant (back dot) cell lines used in the cell viability assays (A and B) are highlighted. (E and F) Tables showing glioblastoma/neuroblastoma (E) or pancreatic/breast cancer (F) cell line sensitivity (IC 50 values from cell viability assays) after SGD-1882-free drug treatment and CD276 surface expression levels (mean fluorescence intensity; MFI) as measured by flow cytometry. (G) Subcutaneous (IMR5) and orthotopic (SUM159 and MDA-MB-231) tumor volumes following ADC treatment. Treatments with 0.5 mg/kg m276-SL-PBD (blue arrows) were initiated when tumors reached ~1,000 mm 3 ; n = 8–10/group. Error bars denote SEM. (H) Bioluminescence imaging monitored systemic MDA-MB-231-luc tumor burden following intravenous injection into NRG mice, followed by randomization and treatment with vehicle or m276-SL-PBD. Representative mice shown (n = 15/group; DPI, days post inoculation). (I) Quantification of tumor burden from the MDA-MB-231 metastasis study in (H). Error bars denote SD. (J) Kaplan-Meier survival curves for the MDA-MB-231-luc metastases study in (H).

    Article Snippet: To compare m276-SL and m276SL-PBD binding to CD276, human CD276 ECD protein was coated onto a high-binding ELISA plate (Santa Cruz, #sc-204463) at 100 ng/well overnight at 4°C.

    Techniques: Activity Assay, Expressing, Fluorescence, Flow Cytometry, Imaging, Injection

    (A) Western blot analysis of CD276 and HER2 levels in JIMT and DU4475 breast cancer cells. (B and C) Cell viability assays measured trastuzumab-SL-PBD and m276-SL-PBD activity against JIMT (B) and DU4475 (C) breast cancer cells. Non-specific IgG-SL-PBD served as a non-binding control. Error bars denote SD. (D and E) Orthotopic growth of JIMT (D) and DU4475 (E) breast tumors in response to trastuzumab-SL-PBD and m276-SL-PBD treatment. ADC treatments (0.5 mg/kg) were initiated when tumor volumes reached ~750–1,000 mm 3 and administered on the days shown (green arrows). Relapsed tumors in the m276-SL-PBD group were re-treated five times with ADC (blue arrows) when tumor volumes reached an average of ~750 mm 3 ; n = 5–8/group. Error bars denote SEM.

    Journal: Cell reports

    Article Title: Engineering CD276/B7-H3-targeted antibody-drug conjugates with enhanced cancer-eradicating capability

    doi: 10.1016/j.celrep.2023.113503

    Figure Lengend Snippet: (A) Western blot analysis of CD276 and HER2 levels in JIMT and DU4475 breast cancer cells. (B and C) Cell viability assays measured trastuzumab-SL-PBD and m276-SL-PBD activity against JIMT (B) and DU4475 (C) breast cancer cells. Non-specific IgG-SL-PBD served as a non-binding control. Error bars denote SD. (D and E) Orthotopic growth of JIMT (D) and DU4475 (E) breast tumors in response to trastuzumab-SL-PBD and m276-SL-PBD treatment. ADC treatments (0.5 mg/kg) were initiated when tumor volumes reached ~750–1,000 mm 3 and administered on the days shown (green arrows). Relapsed tumors in the m276-SL-PBD group were re-treated five times with ADC (blue arrows) when tumor volumes reached an average of ~750 mm 3 ; n = 5–8/group. Error bars denote SEM.

    Article Snippet: To compare m276-SL and m276SL-PBD binding to CD276, human CD276 ECD protein was coated onto a high-binding ELISA plate (Santa Cruz, #sc-204463) at 100 ng/well overnight at 4°C.

    Techniques: Western Blot, Activity Assay, Binding Assay

    (A and B) Immunofluorescence staining for CD276 (green) in BCM-5471, BCM-4013, and BCM-4272 (B) breast cancer PDX models. Tumor endothelium was co-stained with CD31 (red), confirming CD276 expression in both tumor cells and tumor vasculature. Non-specific IgG (A) served as a non-binding control. Scale bars in (A) and (B), 50 μm. (C–E) Orthotopic growth of BCM-5471 (C), BCM-4013 (D), and BCM-4272 (E) breast tumors following treatment with vehicle (control) or 50 or 100 μg/kg m276-SL-PBD. Treatments with m276-SL-PBD were initiated when tumor volumes reached ~1,000 mm 3 and were administered on the days shown (blue arrows); n = 7–8/group. Error bars denote SEM.

    Journal: Cell reports

    Article Title: Engineering CD276/B7-H3-targeted antibody-drug conjugates with enhanced cancer-eradicating capability

    doi: 10.1016/j.celrep.2023.113503

    Figure Lengend Snippet: (A and B) Immunofluorescence staining for CD276 (green) in BCM-5471, BCM-4013, and BCM-4272 (B) breast cancer PDX models. Tumor endothelium was co-stained with CD31 (red), confirming CD276 expression in both tumor cells and tumor vasculature. Non-specific IgG (A) served as a non-binding control. Scale bars in (A) and (B), 50 μm. (C–E) Orthotopic growth of BCM-5471 (C), BCM-4013 (D), and BCM-4272 (E) breast tumors following treatment with vehicle (control) or 50 or 100 μg/kg m276-SL-PBD. Treatments with m276-SL-PBD were initiated when tumor volumes reached ~1,000 mm 3 and were administered on the days shown (blue arrows); n = 7–8/group. Error bars denote SEM.

    Article Snippet: To compare m276-SL and m276SL-PBD binding to CD276, human CD276 ECD protein was coated onto a high-binding ELISA plate (Santa Cruz, #sc-204463) at 100 ng/well overnight at 4°C.

    Techniques: Immunofluorescence, Staining, Expressing, Binding Assay

    KEY RESOURCES TABLE

    Journal: Cell reports

    Article Title: Engineering CD276/B7-H3-targeted antibody-drug conjugates with enhanced cancer-eradicating capability

    doi: 10.1016/j.celrep.2023.113503

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: To compare m276-SL and m276SL-PBD binding to CD276, human CD276 ECD protein was coated onto a high-binding ELISA plate (Santa Cruz, #sc-204463) at 100 ng/well overnight at 4°C.

    Techniques: Recombinant, Fluorescence, Blocking Assay, Plasmid Preparation, Expressing, Software

    A , B Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and tested for p-AMPKα and AMPKα by Western blot and flow cytometry. Mean ± SEM from 5 individuals in each group. C Co-localization of AMPK with LAMP1 + lysosomes detected by confocal microscopy. A representative from 3 individuals per group. Scale bar, 5 μm. Mean ± SEM from 30 individuals in each group. D , E Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and detected for p-S6 and p-AKT. Mean ± SEM from 5 individuals in each group. F , G A549 cell pre-conditioned CD4 + T cells were activated with anti-CD3/CD28 beads for 3 days in the presence or absence of AMPK inhibitor Compound C (10 μM), followed by detection of T cell differentiation. Mean ± SEM from 5 individuals in each group. * p < 0.05, ** p < 0.01 with paired student t -test ( A – E ) and ANOVA plus Tukey method ( F , G ).

    Journal: Cell Death & Disease

    Article Title: Cancer CD39 drives metabolic adaption and mal-differentiation of CD4 + T cells in patients with non-small-cell lung cancer

    doi: 10.1038/s41419-023-06336-4

    Figure Lengend Snippet: A , B Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and tested for p-AMPKα and AMPKα by Western blot and flow cytometry. Mean ± SEM from 5 individuals in each group. C Co-localization of AMPK with LAMP1 + lysosomes detected by confocal microscopy. A representative from 3 individuals per group. Scale bar, 5 μm. Mean ± SEM from 30 individuals in each group. D , E Healthy CD4 + T cells were pre-conditioned with A549 cells for 12 h, activated with anti-CD3/CD28 beads for 3 days, and detected for p-S6 and p-AKT. Mean ± SEM from 5 individuals in each group. F , G A549 cell pre-conditioned CD4 + T cells were activated with anti-CD3/CD28 beads for 3 days in the presence or absence of AMPK inhibitor Compound C (10 μM), followed by detection of T cell differentiation. Mean ± SEM from 5 individuals in each group. * p < 0.05, ** p < 0.01 with paired student t -test ( A – E ) and ANOVA plus Tukey method ( F , G ).

    Article Snippet: Lysosomes were labeled with mouse anti-human lysosomal-associated membrane protein 1 (LAMP1) (Santa Cruz Biotechnology, sc-20011, 1:100) followed by Alexa Fluor® 488-labeled anti-mouse IgG (Abcam, ab150113, 1:200).

    Techniques: Western Blot, Flow Cytometry, Confocal Microscopy, Cell Differentiation