rabbit anti s100a1  (Bioss)

Journal: Cancers

Article Title: Partial Hepatectomy Promotes the Development of KRASG12V-Induced Hepatocellular Carcinoma in Zebrafish

doi: 10.3390/cancers16101793

Figure Lengend Snippet: Comparison of DEGs during kras G12V -induced HCC development and PH-induced liver regeneration in zebrafish. ( A ) Workflow of the differential expression analysis based on the RNA-Seq reads. ( B ) Experimental design for comparing the transcriptomic changes in the kras+ livers with those in the PH livers with the quantification of total DEGs. ( C , D ) Venn diagrams showing the overlaps of ( C ) upregulated genes and ( D ) downregulated genes between the kras+ male liver on Day 5 and the PH male liver on Day 1. ( E , F ) Heatmaps of genes that were significantly ( A ) upregulated and ( B ) downregulated in both the kras+ liver on Day 5 and the PH liver on Day 1 based RNA-seq data. ( G , H ) Expression of ( G ) fgf13b and ( H ) s100a1 in the kras+ male livers 24 h after PH/sham surgery as determined by RT-qPCR ( n = 4). ns p > 0.05, ** p ≤ 0.01.

Article Snippet: The effect of MO- s100a1 -ATG on S100A1 expression was validated in 1-dpf zebrafish embryos with western blotting using the Rabbit-anti-βactin antibody (bs-0061R, Bioss Antibodies, Woburn, MA, USA) (1:5000) and the Rabbit-anti-S100A1 antibody (50266-RP02; Sino Biological, Beijing, China) (1:1000).

Techniques: Comparison, Expressing, RNA Sequencing Assay, Quantitative RT-PCR

Journal: Cancers

Article Title: Partial Hepatectomy Promotes the Development of KRASG12V-Induced Hepatocellular Carcinoma in Zebrafish

doi: 10.3390/cancers16101793

Figure Lengend Snippet: The effect of s100a1 knockdown on the development of kras G12V -induced HCC in zebrafish larvae. ( A ) Experiment design of s100a1 knockdown and oncogene induction in Lipan larvae and kras+ larvae. ( B ) Western blot of S100A1with the total protein extracted from MO-injected zebrafish embryos at 24 hpf. β-actin served as a loading control. Each protein sample was pooled from 15 zebrafish embryos. The quantification of the intensity of S100A1normalized by the intensity of β-actin was at the lower panel. The uncropped image of blots is shown in . ( C ) Fluorescence images of morpholino-treated Lipan and kras+ larvae after 48 h of Dox treatment. ( D ) Measurement of liver size based on the fluorescence in ( B ) ( n ≥ 8). Circles, squares, and triangles indicate values of individual samples ( E ) Expression of sox5, sox9a, and sox9b in the kras+ livers at 24 h after PH/sham surgery as determined by RT-qPCR ( n = 3). Scale Bar = 200 μm. ns p > 0.05, * p ≤ 0.05, ** p ≤ 0.01.

Article Snippet: The effect of MO- s100a1 -ATG on S100A1 expression was validated in 1-dpf zebrafish embryos with western blotting using the Rabbit-anti-βactin antibody (bs-0061R, Bioss Antibodies, Woburn, MA, USA) (1:5000) and the Rabbit-anti-S100A1 antibody (50266-RP02; Sino Biological, Beijing, China) (1:1000).

Techniques: Western Blot, Injection, Fluorescence, Expressing, Quantitative RT-PCR

Journal: Journal of nanobiotechnology

Article Title: Tungsten-based polyoxometalate nanoclusters as ferroptosis inhibitors modulating S100A8/A9-mediated iron metabolism pathway for managing intracerebral haemorrhage.

doi: 10.1186/s12951-025-03149-9

Figure Lengend Snippet: Scheme 1 W-POM NCs for managing intracerebral haemorrhage. Schematic illustration of W-POM NCs inhibiting ferroptosis by modulating the S100A8/ A9-mediated iron metabolism pathway. The nanoclusters targeted oxidative stress and iron dysregulation to manage ICH, demonstrating their potential for neuroprotection and therapeutic efficacy. The figures were created using BioRender.com. ICH, intracerebral haemorrhage; W-POM NCs, tungsten- based polyoxometalate nanoclusters; TFR1, Transferrin Receptor 1; DMT1, Divalent Metal Transporter 1; FPN, Ferroportin; TLR4, Toll-like receptor 4; ROS, Reactive Oxygen Species

Article Snippet: The following primary antibodies were detected via WB: rabbit anti-transferrin receptor 1 (TFR1) polyclonal antibody (1:1000, AF5343, Affbiotech, China), rabbit anti-FPN polyclonal antibody (1:1000, NBP1-21502, Novus, US), rabbit anti-divalent metal transporter 1 (DMT1) polyclonal antibody (1:1000, 20507-1-AP, Proteintech, US), rabbit anti-S100A8/ A9 monoclonal antibody (1:1000, ab288715, Abcam, UK), rabbit anti-hepcidin monoclonal antibody (1:200, ab190775, Abcam, UK), anti-TLR4 polyclonal antibody (1:1000, AF7017, Affbiotech, China).

Techniques: Drug discovery

Journal: Journal of nanobiotechnology

Article Title: Tungsten-based polyoxometalate nanoclusters as ferroptosis inhibitors modulating S100A8/A9-mediated iron metabolism pathway for managing intracerebral haemorrhage.

doi: 10.1186/s12951-025-03149-9

Figure Lengend Snippet: Fig. 5 W-POM NCs inhibit ICH-induced neuroinflammation, oxidative stress and ferroptosis in ICH mice model. (a) Protein expression of iron transport- related proteins (TFR1, FPN, DMT1) assessed using western blot. (b-d) Statistical graph of grayscale values of TFR1, FPN, DMT1 protein expression. (e) Representative TEM images of mitochondrial morphology of the neurons in the perihaematomal area at 72 h after ICH. Red arrows indicate mitochondria. Representative images by Nissl staining (f) and FJB staining (g) in the perihaematomal tissue showing the effects of W-POM NCs on ICH-induced neuronal injury and neurodegeneration. Statistical analysis of Nissl staining (h) and FJB staining (i) results in the perihaematomal tissue. (j) Representative images of immunofluorescent staining for Iba-1 (red) and DAPI (blue) in the perihaematomal area at 72 h after ICH. (l) Quantitative analyses of Iba-1 positive cells in the perihaematomal area at 72 h after ICH. (k) Representative images of immunofluorescent staining for GFAP (red) and DAPI (blue) in the perihaemato mal area at 72 h after ICH. (m) Quantitative analyses of GFAP-positive cells in the perihaematomal area at 72 h after ICH. (*P < 0.05, **P < 0.01, ***P < 0.001, means ± SEM). ICH, intracerebral haemorrhage; TEM, transmission electron microscopy; W-POM NCs, tungsten-based polyoxometalate nanoclusters; TFR1, transferrin receptor 1; DMT1, divalent metal transporter 1; FPN, ferroportin

Article Snippet: The following primary antibodies were detected via WB: rabbit anti-transferrin receptor 1 (TFR1) polyclonal antibody (1:1000, AF5343, Affbiotech, China), rabbit anti-FPN polyclonal antibody (1:1000, NBP1-21502, Novus, US), rabbit anti-divalent metal transporter 1 (DMT1) polyclonal antibody (1:1000, 20507-1-AP, Proteintech, US), rabbit anti-S100A8/ A9 monoclonal antibody (1:1000, ab288715, Abcam, UK), rabbit anti-hepcidin monoclonal antibody (1:200, ab190775, Abcam, UK), anti-TLR4 polyclonal antibody (1:1000, AF7017, Affbiotech, China).

Techniques: Expressing, Western Blot, Staining, Transmission Assay, Electron Microscopy

Journal: Advanced Science

Article Title: On‐Site Melanoma Diagnosis Utilizing a Swellable Microneedle‐Assisted Skin Interstitial Fluid Sampling and a Microfluidic Particle Dam for Visual Quantification of S100A1

doi: 10.1002/advs.202306188

Figure Lengend Snippet: Illustration of a swellable microneedle patch and a self‐powered microfluidic device for melanoma diagnosis. i) Extraction of ISF with the administration of a swellable microneedle patch on the skin. ii) Elution in a centrifuge tube. iii) Reaction between S100A1 and antibody‐conjugated magnetic microparticles (MMPs) and polystyrene microparticles (PMPs). iv) Visual quantification of S100A1 using a microfluidic device with a microfluidic particle dam. With the high concentration of S100A1, MMPs and PMPs simultaneously bind to S100A1 to form the “MMPs‐S100A1‐PMPs” structure, which lessens the number of free PMPs escaping from a magnetic separator, resulting in a short PMP accumulation length that can be visually quantified without an additional instrument. With the lower concentration of S100A1, however, a longer PMP accumulation length is observed due to the insufficient binding between MMPs and PMPs.

Article Snippet: Tissue sections were washed with Phosphate‐Buffered Saline, 0.1% Tween (PBST) buffer, and blocked with 5% goat serum and 2.5% BSA for 2 h. The sections were incubated in 1:500 anti‐S100A1 antibody (Sino Biological, Inc. Beijing, China) in 5% BSA overnight.

Techniques: Extraction, Concentration Assay, Binding Assay

Journal: Advanced Science

Article Title: On‐Site Melanoma Diagnosis Utilizing a Swellable Microneedle‐Assisted Skin Interstitial Fluid Sampling and a Microfluidic Particle Dam for Visual Quantification of S100A1

doi: 10.1002/advs.202306188

Figure Lengend Snippet: Optimization of hydrogel‐based swellable microneedle for extraction of macromolecules. a) Optical image of microneedles (left), the agarose gel before (middle) and after the insertion (right). Scale bar: 1 mm. b) Demonstration of FITC‐dextran (molecular weight: 15 kDa) extraction from the skin model. The control group (left, agarose gel without FITC‐dextran), the 10–100 kDa HA fabricated microneedle group (middle) and the 200–400 kDa HA fabricated microneedle group (right). Scale bar: 500 µm. c) Optical density at wavelength 450 nm to measure the extracted S100A1 concentration in skin model (0, 0.625, 1.25, 2.5, 5, 10, 20, 40, 100, and 200 ng mL −1 ) using HA fabricated microneedles (n = 3). d) Subset data of Figure where the concentration of S100A1 ranges from 0 – 10 ng m −1 L (n = 3).

Article Snippet: Tissue sections were washed with Phosphate‐Buffered Saline, 0.1% Tween (PBST) buffer, and blocked with 5% goat serum and 2.5% BSA for 2 h. The sections were incubated in 1:500 anti‐S100A1 antibody (Sino Biological, Inc. Beijing, China) in 5% BSA overnight.

Techniques: Extraction, Agarose Gel Electrophoresis, Molecular Weight, Concentration Assay

Journal: Advanced Science

Article Title: On‐Site Melanoma Diagnosis Utilizing a Swellable Microneedle‐Assisted Skin Interstitial Fluid Sampling and a Microfluidic Particle Dam for Visual Quantification of S100A1

doi: 10.1002/advs.202306188

Figure Lengend Snippet: Detection of mouse S100A1 standards on microchip. a) Schematic illustration of S100A1 detection using the microfluidic chip. b) Optimization of reaction time (n = 3). c) Optical image of accumulated PMPs. d) PMP accumulation length versus with respect to S100A1 concentrations (n = 3). e) Linear regression with S100A1 concentration ranging from 0 to 50 ng mL −1 . f) Selectivity against potential interfering factors (n = 3). The measured PMP accumulation length showed that only S100A1 (500 ng mL −1 ) shortened the PMP accumulation while other interfering biomarkers with higher concentrations (S100A4, 1 µg mL −1 ; S100A8, 250 µg mL −1 ; S100A13, 1 µg mL −1 ; S100B, 1 mg mL −1 ; LDH‐A, 10 µg mL −1 ; LDH‐B, 10 µg mL −1 ; MIA, 1 mg mL −1 ) did not cause any robust binding between MMPs and PMPs.

Article Snippet: Tissue sections were washed with Phosphate‐Buffered Saline, 0.1% Tween (PBST) buffer, and blocked with 5% goat serum and 2.5% BSA for 2 h. The sections were incubated in 1:500 anti‐S100A1 antibody (Sino Biological, Inc. Beijing, China) in 5% BSA overnight.

Techniques: MicroChIP Assay, Concentration Assay, Binding Assay

Journal: Advanced Science

Article Title: On‐Site Melanoma Diagnosis Utilizing a Swellable Microneedle‐Assisted Skin Interstitial Fluid Sampling and a Microfluidic Particle Dam for Visual Quantification of S100A1

doi: 10.1002/advs.202306188

Figure Lengend Snippet: Standard curves for S100A1 extracted from skin model. a) Schematic illustration of S100A1 extraction using microneedle patch, followed by ELISA and microchip analyses. b) ELISA measurement for S100A1 in the skin model. c) Standard curve of ELISA measurement using non‐linear fitting d) PMP accumulation length in microfluidic chip against S100A1 concentrations in the skin model. e) Standard curve of microchip measurement using the non‐linear fitting. All experiments were repeated twice.

Article Snippet: Tissue sections were washed with Phosphate‐Buffered Saline, 0.1% Tween (PBST) buffer, and blocked with 5% goat serum and 2.5% BSA for 2 h. The sections were incubated in 1:500 anti‐S100A1 antibody (Sino Biological, Inc. Beijing, China) in 5% BSA overnight.

Techniques: Extraction, Enzyme-linked Immunosorbent Assay, MicroChIP Assay

Journal: Advanced Science

Article Title: On‐Site Melanoma Diagnosis Utilizing a Swellable Microneedle‐Assisted Skin Interstitial Fluid Sampling and a Microfluidic Particle Dam for Visual Quantification of S100A1

doi: 10.1002/advs.202306188

Figure Lengend Snippet: In vivo model of melanoma. a–e) Mice with different tumor sizes. Scale bar: 1 mm. f) Microneedle patch administration. Scale bar: 1 mm. g) H&E staining of melanoma tissue and IHC staining of S100A1. Scale bar (H&E staining): 500 µm. Scale bar (IHC): 50 µm. h) IHC staining of S100A1 for tumors with different sizes. Scale bar: 50 µm.

Article Snippet: Tissue sections were washed with Phosphate‐Buffered Saline, 0.1% Tween (PBST) buffer, and blocked with 5% goat serum and 2.5% BSA for 2 h. The sections were incubated in 1:500 anti‐S100A1 antibody (Sino Biological, Inc. Beijing, China) in 5% BSA overnight.

Techniques: In Vivo, Staining, Immunohistochemistry

Journal: Advanced Science

Article Title: On‐Site Melanoma Diagnosis Utilizing a Swellable Microneedle‐Assisted Skin Interstitial Fluid Sampling and a Microfluidic Particle Dam for Visual Quantification of S100A1

doi: 10.1002/advs.202306188

Figure Lengend Snippet: Quantitative measurement of S100A1 based on ELISA and microfluidic chip. a) ELISA measurement of S100A1 extracted from ISF and serum. b) Original concentration of S100A1 in ISF and serum based on the inverse regression. c) Relationship between the tumor size and S100A1 expression level. d) Microchip measurement of S100A1 extracted from ISF (n = 3). e) Original concentration of S100A1 in ISF based on the inverse regression (n = 3). f) Comparison of S100A1 expression levels measured by mouse S100A1 ELISA kit (y‐axis) and microfluidic chips (x‐axis). The correlation was determined on the basis of Lin's concordance correlation coefficient ρ ^ c = 0.916, validating a moderate agreement between the gold standard ELISA and the proposed microfluidic chip.

Article Snippet: Tissue sections were washed with Phosphate‐Buffered Saline, 0.1% Tween (PBST) buffer, and blocked with 5% goat serum and 2.5% BSA for 2 h. The sections were incubated in 1:500 anti‐S100A1 antibody (Sino Biological, Inc. Beijing, China) in 5% BSA overnight.

Techniques: Enzyme-linked Immunosorbent Assay, Concentration Assay, Expressing, MicroChIP Assay, Comparison