Journal: Journal of Neuroinflammation

Article Title: IL-37 suppresses CNS autoimmunity by increasing the frequency of Treg cells and reducing CD4 + T cell-derived IL-10 production

doi: 10.1186/s12974-024-03295-1

Figure Lengend Snippet: IL-37 treatment ameliorated EAE at both priming and ongoing phases. ( A ) C57BL/6 mice were immunized to induce EAE and treated i.p. with IL-37 (1 µg/ dose; n = 5) and PBS ( n = 4) at days 1, 4, and 7 p.i. The clinical scores were evaluated daily for 21 days p.i. Mean clinical scores for IL-37-treated and PBS-treated groups were calculated as the sum of daily scores for each mouse divided by the number of days per group. ( B-C ) EAE mice were treated i.p. with 1 µg of rhIL-37b/ day when they showed the first symptoms of EAE. PBS was administered i.p. to the control group in the same way. Clinical scores were followed for 20 days p.i. (peak; n = 7 per group) ( B ) and 26 days p.i. (chronic; n = 4 per group) ( C ), and mean clinical scores were compared between IL-37-treated mice and control. Clinical scores were analyzed by multiple unpaired t-tests. Mean clinical scores were analyzed by Student’s t-test. Data shown as mean ± SEM. Values of p < 0.05 (*), p < 0.01 (**) and p < 0.001 (***) were considered significant. Ns: not significant

Article Snippet: Recombinant human IL-37b (rhIL-37b) (R&D Systems) was reconstituted in phosphate-buffered saline (PBS) at 200 μg/mL.

Techniques: Control

Journal: Journal of Neuroinflammation

Article Title: IL-37 suppresses CNS autoimmunity by increasing the frequency of Treg cells and reducing CD4 + T cell-derived IL-10 production

doi: 10.1186/s12974-024-03295-1

Figure Lengend Snippet: IL-37 enhanced MBP expression. ( A ) The lumbar section of the spinal cord was harvested from EAE mice treated with PBS (left) or rhIL-37b (middle) at the peak of disease ( n = 4 mice in each group). Naïve mice (right) are illustrated as a control to show healthy spinal cord. ( B ) Mean fluorescent intensity of MBP expression in both groups was measured using FIJI software. Unpaired t-test was performed to analyze these two groups. Data shown as mean ± SEM. Values of p < 0.05 (*), p < 0.01 (**) and p < 0.001 (***) were considered significant. Ns: not significant

Article Snippet: Recombinant human IL-37b (rhIL-37b) (R&D Systems) was reconstituted in phosphate-buffered saline (PBS) at 200 μg/mL.

Techniques: Expressing, Control, Software

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: Human (h) and SD‐Rat (r) qRT‐PCR primers used in this study

Article Snippet: After seeding the cells in the culture plates, the chondrocytes were pre‐treated with human recombinant IL‐37b (0.1 ng/mL; SinoBiological) for 2 hours followed by stimulation with pro‐inflammatory factor IL‐1β (10 ng/mL).

Techniques:

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b suppresses IL‐1β‐induced expression of inflammatory‐related genes in chondrocytes. A, RT‐PCR analysis of five splice variants of IL‐37 gene (IL37a–e) in the chondrocytes. B, The mRNA expression of IL‐6, IL‐8, MMP1, MMP3, MMP9, MMP13 and ADAMTS4 was determined by qRT‐PCR. C, MMP1, MMP9 and MMP13 protein expression levels in human chondrocytes pre‐treated with IL‐37b for 2 h followed by induction with IL‐1β for 48 h; one‐way ANOVA followed by Tukey's test. P values < .05 were considered significant, n = 3. All data are expressed as the mean ± SD

Article Snippet: After seeding the cells in the culture plates, the chondrocytes were pre‐treated with human recombinant IL‐37b (0.1 ng/mL; SinoBiological) for 2 hours followed by stimulation with pro‐inflammatory factor IL‐1β (10 ng/mL).

Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Quantitative RT-PCR

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b reduces the activation levels of MAPKs and NF‐κB p65 in an IL‐R8 dependent manner. A, Chondrocytes were transfected with small interfering RNA (siRNA) for IL‐1R8 or negative control siRNA (scrambled), and IL‐1R8 mRNA levels were analysed by qRT‐PCR. B, After transfection with IL‐1R8 siRNA or negative control siRNA for 48 h, chondrocytes were incubated with or without IL‐37b (0.1 ng/mL) for 2 h followed by stimulation with IL‐1β, and gene expression levels of IL‐6 and IL‐8 were then assessed by qRT‐PCR at 24 h. C, The p‐p38, p‐ERK and p‐JNK were detected by Western blot. D, Semi‐quantitative analysis of Western blot. E. NF‐κB p65 translocation was determined by immunofluorescence. P values < .05 were considered significant, n = 3. One‐way ANOVA followed by Tukey test. All data are expressed as the mean ± SD

Article Snippet: After seeding the cells in the culture plates, the chondrocytes were pre‐treated with human recombinant IL‐37b (0.1 ng/mL; SinoBiological) for 2 hours followed by stimulation with pro‐inflammatory factor IL‐1β (10 ng/mL).

Techniques: Activation Assay, Transfection, Small Interfering RNA, Negative Control, Quantitative RT-PCR, Incubation, Expressing, Western Blot, Translocation Assay, Immunofluorescence

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b alleviates condyle degeneration in disc‐perforation‐induced inflammation in SD rats. A, The surgical procedure of disc perforation. D: disc, B: ball‐shaped burr, P: perforation, A: anterior disc. B, Representative morphological features of the condyle in control, model and treatment group. C, Condylar height changes in the three groups. C: condylar surface; N: condylar neck. D, Safranin O and fast green staining analyses of glycosaminoglycan in the TMJ. E, Cartilage layers OARSI grades. F, Immunohistochemical analyses of Col I and Col II in the condylar cartilage. The P values < .05 were considered significant; one‐way ANOVA followed by Tukey's test, n = 6 per group. All data are expressed as the mean ± SD. NC: negative control group. P: disc perforation model group. IL‐37b: treatment group

Article Snippet: After seeding the cells in the culture plates, the chondrocytes were pre‐treated with human recombinant IL‐37b (0.1 ng/mL; SinoBiological) for 2 hours followed by stimulation with pro‐inflammatory factor IL‐1β (10 ng/mL).

Techniques: Staining, Immunohistochemical staining, Negative Control

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b protects condyle degradation by suppressing pro‐inflammatory cytokine expression. A, Immunohistochemical analyses of MMP1, MMP9 and MMP13 in the condylar cartilage (n = 6). B, The mRNA expression of IL‐1β, IL‐6, MMP9 and MMP13 in condylar cartilage was analysed by RT‐qPCR P values < .05 were considered significant; one‐way ANOVA followed by Tukey test, n = 6 per group. All data are expressed as the mean ± SD

Article Snippet: After seeding the cells in the culture plates, the chondrocytes were pre‐treated with human recombinant IL‐37b (0.1 ng/mL; SinoBiological) for 2 hours followed by stimulation with pro‐inflammatory factor IL‐1β (10 ng/mL).

Techniques: Expressing, Immunohistochemical staining, Quantitative RT-PCR

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b reduces subchondral bone loss in disc‐perforation TMJ. A, Quantitative analysis of the structural parameters of subchondral bone by micro‐CT. B, Three‐dimensional image of the condyle. C, TRAP staining of the TMJ subchondral bone and quantitative analysis. OC.N/area: the number of TRAP‐positive cells (per 400 × magnification). P values < .05 were considered significant; One‐way ANOVA followed by Tukey's test. All data are expressed as the mean ± SD, n = 6 per group

Article Snippet: After seeding the cells in the culture plates, the chondrocytes were pre‐treated with human recombinant IL‐37b (0.1 ng/mL; SinoBiological) for 2 hours followed by stimulation with pro‐inflammatory factor IL‐1β (10 ng/mL).

Techniques: Micro-CT, Staining

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: Human (h) and SD‐Rat (r) qRT‐PCR primers used in this study

Article Snippet: Then, the treatment group was treated with a volume of 50 μL human recombinant IL‐37b (Sino Biological) at a dose of 20 µg/mL (twice per week).

Techniques:

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b suppresses IL‐1β‐induced expression of inflammatory‐related genes in chondrocytes. A, RT‐PCR analysis of five splice variants of IL‐37 gene (IL37a–e) in the chondrocytes. B, The mRNA expression of IL‐6, IL‐8, MMP1, MMP3, MMP9, MMP13 and ADAMTS4 was determined by qRT‐PCR. C, MMP1, MMP9 and MMP13 protein expression levels in human chondrocytes pre‐treated with IL‐37b for 2 h followed by induction with IL‐1β for 48 h; one‐way ANOVA followed by Tukey's test. P values < .05 were considered significant, n = 3. All data are expressed as the mean ± SD

Article Snippet: Then, the treatment group was treated with a volume of 50 μL human recombinant IL‐37b (Sino Biological) at a dose of 20 µg/mL (twice per week).

Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Quantitative RT-PCR

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b reduces the activation levels of MAPKs and NF‐κB p65 in an IL‐R8 dependent manner. A, Chondrocytes were transfected with small interfering RNA (siRNA) for IL‐1R8 or negative control siRNA (scrambled), and IL‐1R8 mRNA levels were analysed by qRT‐PCR. B, After transfection with IL‐1R8 siRNA or negative control siRNA for 48 h, chondrocytes were incubated with or without IL‐37b (0.1 ng/mL) for 2 h followed by stimulation with IL‐1β, and gene expression levels of IL‐6 and IL‐8 were then assessed by qRT‐PCR at 24 h. C, The p‐p38, p‐ERK and p‐JNK were detected by Western blot. D, Semi‐quantitative analysis of Western blot. E. NF‐κB p65 translocation was determined by immunofluorescence. P values < .05 were considered significant, n = 3. One‐way ANOVA followed by Tukey test. All data are expressed as the mean ± SD

Article Snippet: Then, the treatment group was treated with a volume of 50 μL human recombinant IL‐37b (Sino Biological) at a dose of 20 µg/mL (twice per week).

Techniques: Activation Assay, Transfection, Small Interfering RNA, Negative Control, Quantitative RT-PCR, Incubation, Expressing, Western Blot, Translocation Assay, Immunofluorescence

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b alleviates condyle degeneration in disc‐perforation‐induced inflammation in SD rats. A, The surgical procedure of disc perforation. D: disc, B: ball‐shaped burr, P: perforation, A: anterior disc. B, Representative morphological features of the condyle in control, model and treatment group. C, Condylar height changes in the three groups. C: condylar surface; N: condylar neck. D, Safranin O and fast green staining analyses of glycosaminoglycan in the TMJ. E, Cartilage layers OARSI grades. F, Immunohistochemical analyses of Col I and Col II in the condylar cartilage. The P values < .05 were considered significant; one‐way ANOVA followed by Tukey's test, n = 6 per group. All data are expressed as the mean ± SD. NC: negative control group. P: disc perforation model group. IL‐37b: treatment group

Article Snippet: Then, the treatment group was treated with a volume of 50 μL human recombinant IL‐37b (Sino Biological) at a dose of 20 µg/mL (twice per week).

Techniques: Staining, Immunohistochemical staining, Negative Control

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b protects condyle degradation by suppressing pro‐inflammatory cytokine expression. A, Immunohistochemical analyses of MMP1, MMP9 and MMP13 in the condylar cartilage (n = 6). B, The mRNA expression of IL‐1β, IL‐6, MMP9 and MMP13 in condylar cartilage was analysed by RT‐qPCR P values < .05 were considered significant; one‐way ANOVA followed by Tukey test, n = 6 per group. All data are expressed as the mean ± SD

Article Snippet: Then, the treatment group was treated with a volume of 50 μL human recombinant IL‐37b (Sino Biological) at a dose of 20 µg/mL (twice per week).

Techniques: Expressing, Immunohistochemical staining, Quantitative RT-PCR

Journal: Cell Proliferation

Article Title: IL‐37b alleviates inflammation in the temporomandibular joint cartilage via IL‐1R8 pathway

doi: 10.1111/cpr.12692

Figure Lengend Snippet: IL‐37b reduces subchondral bone loss in disc‐perforation TMJ. A, Quantitative analysis of the structural parameters of subchondral bone by micro‐CT. B, Three‐dimensional image of the condyle. C, TRAP staining of the TMJ subchondral bone and quantitative analysis. OC.N/area: the number of TRAP‐positive cells (per 400 × magnification). P values < .05 were considered significant; One‐way ANOVA followed by Tukey's test. All data are expressed as the mean ± SD, n = 6 per group

Article Snippet: Then, the treatment group was treated with a volume of 50 μL human recombinant IL‐37b (Sino Biological) at a dose of 20 µg/mL (twice per week).

Techniques: Micro-CT, Staining

Journal: Microbiology Spectrum

Article Title: Identification and characterization of a novel small viral peptide (VSP59) encoded by Bombyx mori cypovirus (BmCPV) that negatively regulates viral replication

doi: 10.1128/spectrum.00826-24

Figure Lengend Snippet: Sequence of siRNAs

Article Snippet: The primary antibodies were anti-dsRed (Thermo Fisher Scientific, Massachusetts, USA), anti-VSP59, anti-Polh, anti-active caspase 3 (Affinity, Melbourne, Germany), anti-prohibitin 2 (PHB2) (Proteintech, Chicago, USA), anti-VP7( ) and anti-VP4 , and the secondary antibodies were horseradish peroxidase (HRP)-labeled goat anti-rabbit IgG (Servicebio, Wuhan, China) or HRP-labeled goat anti-mouse IgG (Servicebio, Wuhan, China).

Techniques: Sequencing

Journal: Microbiology Spectrum

Article Title: Identification and characterization of a novel small viral peptide (VSP59) encoded by Bombyx mori cypovirus (BmCPV) that negatively regulates viral replication

doi: 10.1128/spectrum.00826-24

Figure Lengend Snippet: The effects of overexpression of vsp59 on the gene expression level. ( A ) The expression level of active caspase3 in the BmN cells transfected pIZT-V5/His, pIZT-vsp59, and pIZT-vsp59 mut . The BmN cells were transfected with 4 µg of plasmids. The expression level of active caspase3 in the transfected cells was determined by Western blotting at 48 h post-transfection. Upper, Western blotting; under, grayscale scanning analysis of Western blotting signal bands. ( B ) The expression level of active caspase3 and PHB2 was increased in a VSP59-dependent manner. The BmN cells (1 × 10 6 ) were transfected with 2, 4, and 8 µg of pIZT-vsp59, and the cells were collected at 48 h post-transfection to determine the expression level of active caspase3 and PHB2. The cells transfected with pIZT-V5/His were used as controls. Upper, Western blotting; below left, grayscale scanning analysis of active caspase3 signal bands; below right, grayscale scanning analysis of PHB2 signal bands. ( C and D ) The effects of vsp59 overexpression on the expression levels of the genes related to innate immunity signaling pathways (C) and apoptosis signaling pathway ( D ). The BmN cells were transfected with 4 µg of pIZT-vsp59. The expression level of active caspase3 in the transfected cells was determined by RT-qPCR at 48 h post-transfection. The BmN cells transfected with pIZT-V5/His were used as control. * P < 0.05, ** P < 0.01, *** P < 0.001, and ns: P > 0.05.

Article Snippet: The primary antibodies were anti-dsRed (Thermo Fisher Scientific, Massachusetts, USA), anti-VSP59, anti-Polh, anti-active caspase 3 (Affinity, Melbourne, Germany), anti-prohibitin 2 (PHB2) (Proteintech, Chicago, USA), anti-VP7( ) and anti-VP4 , and the secondary antibodies were horseradish peroxidase (HRP)-labeled goat anti-rabbit IgG (Servicebio, Wuhan, China) or HRP-labeled goat anti-mouse IgG (Servicebio, Wuhan, China).

Techniques: Over Expression, Gene Expression, Expressing, Transfection, Western Blot, Protein-Protein interactions, Quantitative RT-PCR, Control

Journal: Microbiology Spectrum

Article Title: Identification and characterization of a novel small viral peptide (VSP59) encoded by Bombyx mori cypovirus (BmCPV) that negatively regulates viral replication

doi: 10.1128/spectrum.00826-24

Figure Lengend Snippet: VSP59 induced apoptosis through interaction with PHB2. ( A ) Screening candidate proteins interacting with VSP59 through IP. The total proteins extracted from the infected BmN cells at 48 h post-infection were used for IP with specific anti-VSP59 and pre-immune IgG, and the generated IP complex was analyzed by SDS-PAGE. ( B ) Co-IP assay. BmN cells (1 × 10 7 ) were infected with BmCPV (MOI = 2), and 48 h later, the cells were collected and lysed for Co-IP. Co-IP was performed with 5 µg of anti-PHB2, anti-vsp59, and pre-immune IgG. The obtained Co-IP complexes were separated by SDS-PAGE, and Western blotting was performed using anti-vsp59 and anti-PHB2. ( C ) The analysis of co-localization between VSP59 (green) and PHB2 (red) in BmCPV-infected cells. ( D ) The expression level of PHB2 was increased by overexpression of vsp59. The BmN cells (1 × 10 6 ) were transfected with 4 µg of pIZT-vsp59. The expression level of PHB2 in the transfected cells was determined by Western blotting at 48 h post-transfection. The BmN cells transfected with the pIZT-V5/His and pIZT-vsp59 mut were used as control. Upper, Western blotting; under, grayscale scanning analysis of Western blotting signal bands. * P < 0.05, ** P < 0.01, and ns: P > 0.05.

Article Snippet: The primary antibodies were anti-dsRed (Thermo Fisher Scientific, Massachusetts, USA), anti-VSP59, anti-Polh, anti-active caspase 3 (Affinity, Melbourne, Germany), anti-prohibitin 2 (PHB2) (Proteintech, Chicago, USA), anti-VP7( ) and anti-VP4 , and the secondary antibodies were horseradish peroxidase (HRP)-labeled goat anti-rabbit IgG (Servicebio, Wuhan, China) or HRP-labeled goat anti-mouse IgG (Servicebio, Wuhan, China).

Techniques: Infection, Generated, SDS Page, Co-Immunoprecipitation Assay, Western Blot, Expressing, Over Expression, Transfection, Control

Journal: Microbiology Spectrum

Article Title: Identification and characterization of a novel small viral peptide (VSP59) encoded by Bombyx mori cypovirus (BmCPV) that negatively regulates viral replication

doi: 10.1128/spectrum.00826-24

Figure Lengend Snippet: VSP59 attenuated BmCPV replication by induction of apoptosis through interaction with PHB2. ( A ) The replication of BmCPV in the transfected cells with pIZT-vsp59 was assessed by Western blotting and ( B ) real-time PCR. BmN cells (1 × 10 6 ) were transfected with 4 µg of pIZT-vsp59 vector and pIZT-V5/His vector (as control). At 48 h post-transfection, the cells were inoculated with BmCPV (MOI = 2). At 48 hpi, the cells were collected. The total proteins extracted were used for Western blotting ( A ) to determine the expression levels of VP7 and VP4 viral proteins. Upper, Western blotting; under, grayscale scanning analysis of Western blotting signal bands. The total RNAs extracted were used for RT-qPCR ( B ) to determine the vp1 gene expression level. ( C ) The recombinant BmCPV (rBmCPV) and vsp59 mutant virus rBmCPV-VSP59null were constructed using a reverse genetic system. The replication of S1 RNA segment in the BmCPV-infected cells was determined by RT-qPCR. ( D ) The silencing efficiencies of siRNAs to the PHB2 gene were determined by real-time PCR. BmN cells (1 × 10 6 ) were transfected with 5 µmol/L of PHB2-siRNA-245, PHB2-siRNA-637 , PHB2-siRNA-750, or NC-siRNA. At 48 hpi, the cells were collected. The total RNAs extracted were used for RT-qPCR to determine the PHB2 gene expression level. TIF-4A gene was used as an internal reference. ( E ) The effects of silencing PHB2 on the expression level of VP7 and active caspase3 were determined by Western blotting. BmN cells (1 × 10 6 ) were transfected with 4 µg of pIZT-vsp59 plasmid for 48 h, then 5 µL of BmCPV (MOI = 2) was inoculated for 48 h, and then, respectively, transfected with PHB2-siRNA-245 at a final concentration of 5 µmol/L. Meanwhile, the inoculated cells transfected with NC-siRNA were used as a control. After 48 h, the protein was extracted and detected by Western blotting (upper). The primary antibodies were VP7 antibody (mouse, 1:1,000), active caspase3 (rabbit, 1:2,000) antibody, and α-tubulin antibody (mouse, 1:2,000), the secondary antibody is HRP-conjugated goat anti-rabbit/mouse antibody (1:5,000). The amount of protein loaded in each lane is 50 µg. Grayscale scanning analysis of Western blotting signal bands was conducted to determine the relative expression level (under). * P < 0.05, ** P < 0.01, and *** P < 0.001.

Article Snippet: The primary antibodies were anti-dsRed (Thermo Fisher Scientific, Massachusetts, USA), anti-VSP59, anti-Polh, anti-active caspase 3 (Affinity, Melbourne, Germany), anti-prohibitin 2 (PHB2) (Proteintech, Chicago, USA), anti-VP7( ) and anti-VP4 , and the secondary antibodies were horseradish peroxidase (HRP)-labeled goat anti-rabbit IgG (Servicebio, Wuhan, China) or HRP-labeled goat anti-mouse IgG (Servicebio, Wuhan, China).

Techniques: Transfection, Western Blot, Real-time Polymerase Chain Reaction, Plasmid Preparation, Control, Expressing, Quantitative RT-PCR, Gene Expression, Recombinant, Mutagenesis, Virus, Construct, Infection, Concentration Assay

Journal: bioRxiv

Article Title: Identification of a novel interaction between Theileria Prohibitin ( Ta PHB-1) and bovine RUVBL-1

doi: 10.1101/2022.02.14.480320

Figure Lengend Snippet: A. Ana2014 and BoMac cell lysates were probed with prohibitin antibody and β–tubulin was used as loading control. B. Western blotting of the bacterial lysate of recombinant Ta PHB-1 probed with commercial prohibitin antibodies. C. Ta PHB-1 localized majorly in the host cell cytoplasm and bovine PHB in host cell nucleus. TOMM was used to locate mitochondria. Scale bar-5 μm.

Article Snippet: Antibodies against β-tubulin, Prohibitin and myc-tag were obtained from Santa Cruz Biotechnology.

Techniques: Control, Western Blot, Recombinant