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PeproTech sdf1a (cxcl12)
Sdf1a (Cxcl12), supplied by PeproTech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sdf1a+(cxcl12)/recombinant+chemokines/pm39623220-157-0-3
Average 90 stars, based on 1 article reviews

sdf1a (cxcl12) - by Bioz Stars, 2026-09

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Article Title: Engineering Extracellular Vesicles Secreted by Human Brain Organoids with Different Regional Identity.
Article Snippet: Get e-Alerts BIOLOGICAL AND MEDICAL APPLICATIONS OF MATERIALS AND INTERFACES | March 3, 2025 Engineering Extracellular Vesicles Secreted by Human Brain Organoids with Different Regional Identity , , , , , , , and ACS Applied Materials & Interfaces Cite this: ACS Appl.. Mater.. Interfaces 2025, 17, 10, 15145–15162 https://doi.org/10.1021/acsami.4c22692 Copyright © 2025 American Chemical Society Request reuse permissions Cite Share Jump to Chang Liu* Xingchi Chen Justice Ene Colin Esmonde Takahisa Kanekiyo Changchun Zeng Li Sun Yan Li* Open PDF Supporting Information (1) Article Views 467 Altmetric Citations 1 Learn about these metrics Published March 3, 2025 5/29/25, 7:49 PM Engineering Extracellular Vesicles Secreted by Human Brain Organoids with Different Regional Identity | ACS Applied Materials & Interf... https://pubs.acs.org/doi/10.1021/acsami.4c22692 2/38 Extracellular vesicles (EVs) are membrane-bound nanovesicles that show signi cance in intercellular communications and high therapeutic potential.

Article Title: Generation and long-term culture of human cerebellar organoids from pluripotent stem cells.
Article Snippet: The advancement of research on human cerebellar development and diseases has been hindered by the lack of a cell-based system that mirrors the cellular diversity and functional characteristics of the human cerebellum.. Here, we describe our protocol for a human pluripotent stem cell-derived human cerebellar organoid (hCerO) model, which successfully replicates the cellular diversity of the fetal cerebellum along with some of its distinct cytoarchitectural features.. Our approach involves the patterning of human pluripotent stem cells, resulting in the generation of both cerebellar excitatory and inhibitory progenitor populations—specifically, the rhombic lip and ventricular zone progenitors, respectively.

Article Title: MIF interacts with CXCR7 to promote receptor internalization, ERK1/2 and ZAP-70 signaling, and lymphocyte chemotaxis.
Article Snippet: Macrophage migration-inhibitory factor (MIF) is a pleiotropic cytokine with chemokine-like functions and is a mediator in numerous inflammatory conditions.. Depending on the context, MIF signals through 1 or more of its receptors cluster of differentiation (CD)74, CXC-motif chemokine receptor (CXCR)2, and CXCR4.. In addition, heteromeric receptor complexes have been identified.

Article Title: A novel disorder involving dyshematopoiesis, inflammation, and HLH due to aberrant CDC42 function
Article Snippet: 600 μl of complete R10 supplemented with 100 ng/ml SDF1a/CXCL12 (300-28A; Peprotech) chemoattractant was plated into a 24-well tissue culture–treated plate.

Article Title: Platelets and mast cells promote pathogenic eosinophil recruitment during invasive fungal infection via the 5-HIAA-GPR35 ligand-receptor system.
Article Snippet: BioLegend Cat# 104428; RRID: AB_830799 PE-conjugated rat anti mouse/human GATA3 (REA174) Miltenyi Cat# 130-100-664; RRID:AB_2651823 Alexa647-conjugated rat anti mouse anti-T-bet (4B10) BioLegend Cat# 644803; RRID: AB_1595573 APC-conjugated anti-mouse IL-4 (11B11) eBioscience Cat# 17-7041-82; RRID: AB_469494 PE/Cy7-conjugated rat anti-mouse IFNg (XMG1.2) BioLegend Cat# 505826; RRID: AB_2295770 APC anti- mouse IFNg (XMG1.2) BioLegend Cat# 505810; RRID: AB_315404 Rabbit polyclonal anti-GPR35 Biomatik N/A AF647-Goat anti-Rabbit IgG (H+L) Highly Cross-Adsorbed Ab Fisher Scientific Cat# A21245; RRID:AB_2535813 Bacterial and virus strains Cryptococcus neoformans (strain KN99) Madhani lab, UCSF N/A Chemicals, peptides, and recombinant proteins 5-HIAA Sigma #H8876 CXCL12 (SDF1a human) Peprotech #300-28A Diphtheria Toxin (DT) Millipore/Sigma #322326 FMS-like tyrosine kinase 3 ligand Peprotech) Peprotech #250-31 IL-5 Peprotech #215-15 IL-3 Peprotech #213-13 IL-6 Peprotech #216-16 Stem Cell Factor Peprotech #250-03 Cell Trace Violet Fisher #C34557 Deep Red Life Tech #C34565 (Continued on next page) Immunity 56, 1548–1560.e1–e5, July 11, 2023 e1

Incubation:

Article Title: Functional role of endothelial adhesion molecules in the early stages of brain metastasis.
Article Snippet: .. For the stimulated conditions, 4T1-GFP cells were incubated with either 55% mouse (BALB/c) plasma in DMEM or 50 ng/mL mouse CXCL12 (SDF1a; PeproTech). .. MDA231BR-GFP cells were incubated with 55% human plasma in DMEM or 50 ng/mL human CXCL12 (SDF1a (PeproTech).

Article Title: Functional role of endothelial adhesion molecules in the early stages of brain metastasis.
Article Snippet: For the stimulated conditions, 4T1-GFP cells were incubated with either 55% mouse (BALB/c) plasma in DMEM or 50 ng/mL mouse CXCL12 (SDF1a; PeproTech). .. MDA231BR-GFP cells were incubated with 55% human plasma in DMEM or 50 ng/mL human CXCL12 (SDF1a (PeproTech). ..

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( A ) GSEA plots of “chemokine signaling pathway” and “chemotaxis” gene sets enriched in MAOB-OE PrSC cells compared with controls. ( B ) ELISA of CXCL12 secretion in the culture media of control and MAOB-KD PrSC cells ( n = 3). ( C ) Representative IHC images and corresponding Pearson’s correlation analysis of stroma-expressed MAOB and CXCL12 protein levels in a PC TMA ( n = 37). Scale bars, 100 μm. ( D ) Pearson’s correlation analysis of MAOB and CXCL12 mRNA levels in patient-derived cultured prostatic stromal cells (left, n = 20) and laser-capture microdissected breast tumor stroma (right, n = 53) from GSE34312 and GSE9014 datasets, respectively. Statistical analysis was performed using one-way ANOVA with Dunnett’s test in (B). Data represent means ± SEM. ** P < 0.01.

Journal: Science Advances

Article Title: Stromal-derived MAOB promotes prostate cancer growth and progression

doi: 10.1126/sciadv.adi4935

Figure Lengend Snippet: ( A ) GSEA plots of “chemokine signaling pathway” and “chemotaxis” gene sets enriched in MAOB-OE PrSC cells compared with controls. ( B ) ELISA of CXCL12 secretion in the culture media of control and MAOB-KD PrSC cells ( n = 3). ( C ) Representative IHC images and corresponding Pearson’s correlation analysis of stroma-expressed MAOB and CXCL12 protein levels in a PC TMA ( n = 37). Scale bars, 100 μm. ( D ) Pearson’s correlation analysis of MAOB and CXCL12 mRNA levels in patient-derived cultured prostatic stromal cells (left, n = 20) and laser-capture microdissected breast tumor stroma (right, n = 53) from GSE34312 and GSE9014 datasets, respectively. Statistical analysis was performed using one-way ANOVA with Dunnett’s test in (B). Data represent means ± SEM. ** P < 0.01.

Article Snippet: TGFβ1 (ELH-TGFb1-1) and CXCL12 (DLH-SDF1a-1) protein levels in cell culture media were quantified by enzyme-linked immunosorbent assay (ELISA) (RayBiotech).

Techniques: Chemotaxis Assay, Enzyme-linked Immunosorbent Assay, Derivative Assay, Cell Culture

( A ) Western blot of Twist1 in control and MAOB-manipulated PrSC cells upon NAC (5 mM, 48 hours) or H 2 O 2 (40 μM, 24 hours) treatment. ( B ) ELISA of CXCL12 secretion in culture media of control and MAOB-OE PrSC cells treated with TWIST1 siRNA or NAC (5 mM, 48 hours) ( n = 3). ( C ) qPCR of CXCL12 in indicated PrSC cells upon NAC treatment (5 mM, 48 hours) or Twist1/ TWIST1 siRNA expression ( n = 3). ( D and E ) Determination of CXCL12 mRNA (D) and 0.7-kb promoter activity (E) in PrSC cells upon Twist1 expression and/or TGFβ1 treatment (10 ng/ml, 12 hours) ( n = 3). ( F ) Schematic diagrams of WT and mutated CXCL12 E-box/SBE-Luc constructs and determination of their activities in PrSC cells upon Twist1 expression and/or TGFβ1 treatment (10 ng/ml, 12 hours) ( n = 3). ( G ) Representative proximity ligation assay staining and quantitation of indicated Twist1-Smad interactions by per-nucleus fluorescence intensity in control and MAOB-OE PrSC cells. Smad antibody incubation alone served as negative control. Numbers of nuclei included for comparisons between groups are denoted. Scale bars, 50 μm. ( H ) Co-IP assays of indicated Twist1-Smad interactions in PrSC cells with coexpression of Twist1 and individual Smads. Immunoglobulin G (IgG) was used in IP as negative control. Ten percent input was blotted as positive control. ( I ) ChIP analysis of chromatin from control and MAOB-OE PrSC cells precipitated with anti-Twist1, anti-Smad4, or a control IgG, followed by qPCR probing the E-box/SBE-centric CXCL12 promoter region ( n = 3). ( J ) ChIP analysis of chromatin from PrSC cells precipitated with anti-Smad4 antibody and then reprecipitated with anti-Twist1 or a control IgG (re-ChIP), followed by qPCR probing the E-box/SBE-encompassing CXCL12 promoter sequence ( n = 3). Statistical analysis was performed using one-way ANOVA with Tukey’s test. Data represent means ± SEM. * P < 0.05, ** P < 0.01; ns, not significant.

Journal: Science Advances

Article Title: Stromal-derived MAOB promotes prostate cancer growth and progression

doi: 10.1126/sciadv.adi4935

Figure Lengend Snippet: ( A ) Western blot of Twist1 in control and MAOB-manipulated PrSC cells upon NAC (5 mM, 48 hours) or H 2 O 2 (40 μM, 24 hours) treatment. ( B ) ELISA of CXCL12 secretion in culture media of control and MAOB-OE PrSC cells treated with TWIST1 siRNA or NAC (5 mM, 48 hours) ( n = 3). ( C ) qPCR of CXCL12 in indicated PrSC cells upon NAC treatment (5 mM, 48 hours) or Twist1/ TWIST1 siRNA expression ( n = 3). ( D and E ) Determination of CXCL12 mRNA (D) and 0.7-kb promoter activity (E) in PrSC cells upon Twist1 expression and/or TGFβ1 treatment (10 ng/ml, 12 hours) ( n = 3). ( F ) Schematic diagrams of WT and mutated CXCL12 E-box/SBE-Luc constructs and determination of their activities in PrSC cells upon Twist1 expression and/or TGFβ1 treatment (10 ng/ml, 12 hours) ( n = 3). ( G ) Representative proximity ligation assay staining and quantitation of indicated Twist1-Smad interactions by per-nucleus fluorescence intensity in control and MAOB-OE PrSC cells. Smad antibody incubation alone served as negative control. Numbers of nuclei included for comparisons between groups are denoted. Scale bars, 50 μm. ( H ) Co-IP assays of indicated Twist1-Smad interactions in PrSC cells with coexpression of Twist1 and individual Smads. Immunoglobulin G (IgG) was used in IP as negative control. Ten percent input was blotted as positive control. ( I ) ChIP analysis of chromatin from control and MAOB-OE PrSC cells precipitated with anti-Twist1, anti-Smad4, or a control IgG, followed by qPCR probing the E-box/SBE-centric CXCL12 promoter region ( n = 3). ( J ) ChIP analysis of chromatin from PrSC cells precipitated with anti-Smad4 antibody and then reprecipitated with anti-Twist1 or a control IgG (re-ChIP), followed by qPCR probing the E-box/SBE-encompassing CXCL12 promoter sequence ( n = 3). Statistical analysis was performed using one-way ANOVA with Tukey’s test. Data represent means ± SEM. * P < 0.05, ** P < 0.01; ns, not significant.

Article Snippet: TGFβ1 (ELH-TGFb1-1) and CXCL12 (DLH-SDF1a-1) protein levels in cell culture media were quantified by enzyme-linked immunosorbent assay (ELISA) (RayBiotech).

Techniques: Western Blot, Enzyme-linked Immunosorbent Assay, Expressing, Activity Assay, Construct, Proximity Ligation Assay, Staining, Quantitation Assay, Fluorescence, Incubation, Negative Control, Co-Immunoprecipitation Assay, Positive Control, Sequencing

( A ) Quantitation of C4-2 and PC-3 PC cells in monoculture and coculture with indicated PrSC fibroblasts upon anti-CXCL12 (0.1 μg/ml) antibody treatment ( n = 3). ( B ) Quantitation of PC cells in coculture with indicated PrSC cells treated with rCXCL12 protein (50 ng/ml; n = 3). ( C ) Western blot of CXCR4 and CXCR7 in control and CXCR4-KD/CXCR7-KD PC cells. ( D and E ) Quantitation of control and CXCR4-KD/CXCR7-KD PC cells in coculture with indicated PrSC cells treated without (D) or with (E) rCXCL12 (50 ng/ml; n = 3). ( F ) Quantitation of PC cells in coculture with indicated PrSC cells treated with 10 nM AMD3100 ( n = 3). ( G ) Representative images and quantitation of PC-3 cell migration and invasion in coculture with indicated PrSC cells upon treatment with anti-CXCL12 antibody (0.1 μg/ml) or 10 nM AMD3100 ( n = 3). Scale bars, 200 μm. ( H ) Representative images and quantitation of PC cell migration in coculture with indicated PrSC cells treated with rCXCL12 (50 ng/ml; n = 3). Scale bars, 100 μm. ( I ) Phospho-antibody array analysis of PC-3 cells treated with indicated PrSC cell CM. All phosphoprotein levels were normalized to their total forms from a single array with six replicate spots, with significantly activated phosphoproteins (fold change > 1.5, P < 0.05) denoted. ( J ) Western blot of p-Src and p-JNK in control and CXCR4-KD PC-3 cells treated with indicated PrSC cell CM. ( K ) Western blot of p-Src and p-JNK in PC-3 cells treated with indicated PrSC cell CM plus rCXCL12 (50 ng/ml). ( L ) Quantitation of PC cells in coculture with indicated PrSC cells following pretreatment with 40 nM Src inhibitor 1 or 10 μM SP600125 for 24 hours ( n = 3). Statistical analysis was performed using one-way ANOVA with Tukey’s test. Data represent means ± SEM. * P < 0.05, ** P < 0.01; ns, not significant.

Journal: Science Advances

Article Title: Stromal-derived MAOB promotes prostate cancer growth and progression

doi: 10.1126/sciadv.adi4935

Figure Lengend Snippet: ( A ) Quantitation of C4-2 and PC-3 PC cells in monoculture and coculture with indicated PrSC fibroblasts upon anti-CXCL12 (0.1 μg/ml) antibody treatment ( n = 3). ( B ) Quantitation of PC cells in coculture with indicated PrSC cells treated with rCXCL12 protein (50 ng/ml; n = 3). ( C ) Western blot of CXCR4 and CXCR7 in control and CXCR4-KD/CXCR7-KD PC cells. ( D and E ) Quantitation of control and CXCR4-KD/CXCR7-KD PC cells in coculture with indicated PrSC cells treated without (D) or with (E) rCXCL12 (50 ng/ml; n = 3). ( F ) Quantitation of PC cells in coculture with indicated PrSC cells treated with 10 nM AMD3100 ( n = 3). ( G ) Representative images and quantitation of PC-3 cell migration and invasion in coculture with indicated PrSC cells upon treatment with anti-CXCL12 antibody (0.1 μg/ml) or 10 nM AMD3100 ( n = 3). Scale bars, 200 μm. ( H ) Representative images and quantitation of PC cell migration in coculture with indicated PrSC cells treated with rCXCL12 (50 ng/ml; n = 3). Scale bars, 100 μm. ( I ) Phospho-antibody array analysis of PC-3 cells treated with indicated PrSC cell CM. All phosphoprotein levels were normalized to their total forms from a single array with six replicate spots, with significantly activated phosphoproteins (fold change > 1.5, P < 0.05) denoted. ( J ) Western blot of p-Src and p-JNK in control and CXCR4-KD PC-3 cells treated with indicated PrSC cell CM. ( K ) Western blot of p-Src and p-JNK in PC-3 cells treated with indicated PrSC cell CM plus rCXCL12 (50 ng/ml). ( L ) Quantitation of PC cells in coculture with indicated PrSC cells following pretreatment with 40 nM Src inhibitor 1 or 10 μM SP600125 for 24 hours ( n = 3). Statistical analysis was performed using one-way ANOVA with Tukey’s test. Data represent means ± SEM. * P < 0.05, ** P < 0.01; ns, not significant.

Article Snippet: TGFβ1 (ELH-TGFb1-1) and CXCL12 (DLH-SDF1a-1) protein levels in cell culture media were quantified by enzyme-linked immunosorbent assay (ELISA) (RayBiotech).

Techniques: Quantitation Assay, Western Blot, Migration, Ab Array

( A ) Quantitation of C4-2 and PC-3 cell proliferation in monoculture and coculture with control and MAOB-OE PrSC cells upon selegiline treatment (10 nM, 72 hours) ( n = 3). ( B ) BLI-based growth curves of Luc-tagged PC-3 tumors grown in the prostates of male NSG mice treated with selegiline at various doses (0.5, 2, and 10 mg/kg) or saline as a vehicle ( n = 5 per group). ( C ) BLI images of mice from each group at the end point. ( D ) Determination of tumor weights ( n = 5). ( E ) Determination of MAOA and MAOB enzymatic activities in mouse liver tissue from each group at the end point ( n = 3). ( F ) Representative images of H&E and IHC staining of tumor-expressed Ki-67, p-Src, and p-JNK and stroma-expressed αSMA and CXCL12 and their quantitation in tumor samples from each group ( n = 5). Scale bars, 100 μm. ( G ) Mouse body weights determined weekly ( n = 5). ( H ) Representative H&E images of mouse liver and kidney tissue from each group. Scale bars, 100 μm. ( I to L ) ELISA of ALT (I), AST (J), BUN (K), and creatinine (L) in mouse sera at the end point ( n = 5). ( M ) Schematic depicting stromal-derived MAOB activation of paracrine CXCL12-CXCR4/Src/JNK signaling through interplay between ROS-dependent Twist1 (via a HIF1α/VEGF-A/AKT/FOXO1 pathway) and TGFβ1/Smads to promote stromal-epithelial interactions for PC growth and progression. Statistical analysis was performed using one-way ANOVA with Tukey’s test in (A), (D) to (F), and (I) to (L) and two-way ANOVA with Tukey’s test in (B) and (G). Data represent means ± SEM. * P < 0.05, ** P < 0.01; ns, not significant.

Journal: Science Advances

Article Title: Stromal-derived MAOB promotes prostate cancer growth and progression

doi: 10.1126/sciadv.adi4935

Figure Lengend Snippet: ( A ) Quantitation of C4-2 and PC-3 cell proliferation in monoculture and coculture with control and MAOB-OE PrSC cells upon selegiline treatment (10 nM, 72 hours) ( n = 3). ( B ) BLI-based growth curves of Luc-tagged PC-3 tumors grown in the prostates of male NSG mice treated with selegiline at various doses (0.5, 2, and 10 mg/kg) or saline as a vehicle ( n = 5 per group). ( C ) BLI images of mice from each group at the end point. ( D ) Determination of tumor weights ( n = 5). ( E ) Determination of MAOA and MAOB enzymatic activities in mouse liver tissue from each group at the end point ( n = 3). ( F ) Representative images of H&E and IHC staining of tumor-expressed Ki-67, p-Src, and p-JNK and stroma-expressed αSMA and CXCL12 and their quantitation in tumor samples from each group ( n = 5). Scale bars, 100 μm. ( G ) Mouse body weights determined weekly ( n = 5). ( H ) Representative H&E images of mouse liver and kidney tissue from each group. Scale bars, 100 μm. ( I to L ) ELISA of ALT (I), AST (J), BUN (K), and creatinine (L) in mouse sera at the end point ( n = 5). ( M ) Schematic depicting stromal-derived MAOB activation of paracrine CXCL12-CXCR4/Src/JNK signaling through interplay between ROS-dependent Twist1 (via a HIF1α/VEGF-A/AKT/FOXO1 pathway) and TGFβ1/Smads to promote stromal-epithelial interactions for PC growth and progression. Statistical analysis was performed using one-way ANOVA with Tukey’s test in (A), (D) to (F), and (I) to (L) and two-way ANOVA with Tukey’s test in (B) and (G). Data represent means ± SEM. * P < 0.05, ** P < 0.01; ns, not significant.

Article Snippet: TGFβ1 (ELH-TGFb1-1) and CXCL12 (DLH-SDF1a-1) protein levels in cell culture media were quantified by enzyme-linked immunosorbent assay (ELISA) (RayBiotech).

Techniques: Quantitation Assay, Saline, Immunohistochemistry, Enzyme-linked Immunosorbent Assay, Derivative Assay, Activation Assay

Fig. 5 CAFs enhance sorafenib resistance of HCC cells through CXCL12 in vivo. a Representative images of tumors in mice of CAFs + AMD3100 group, CAFs group, and NFs group after different treatments. b The tumor volume in different treatment groups. c The tumor proliferation trend in different treatment groups. d Pathological validation of tumors under a microscope (40X), after H&E staining and Immunohistochemistry in tumor tissues. The immunohistochemistry staining to detect the expression of Cleaved Caspase-3 in different treatment groups from the tumor tissues of mice. e The expression level of Cleaved Caspase-3 in different treatment groups from the tumors of mice. The data presented mean ± SEM. **p < 0.001; ***p < 0.0001; ****p < 0.00001

Journal: BMC cancer

Article Title: Cancer-associated fibroblasts induce sorafenib resistance of hepatocellular carcinoma cells through CXCL12/FOLR1.

doi: 10.1186/s12885-023-11613-8

Figure Lengend Snippet: Fig. 5 CAFs enhance sorafenib resistance of HCC cells through CXCL12 in vivo. a Representative images of tumors in mice of CAFs + AMD3100 group, CAFs group, and NFs group after different treatments. b The tumor volume in different treatment groups. c The tumor proliferation trend in different treatment groups. d Pathological validation of tumors under a microscope (40X), after H&E staining and Immunohistochemistry in tumor tissues. The immunohistochemistry staining to detect the expression of Cleaved Caspase-3 in different treatment groups from the tumor tissues of mice. e The expression level of Cleaved Caspase-3 in different treatment groups from the tumors of mice. The data presented mean ± SEM. **p < 0.001; ***p < 0.0001; ****p < 0.00001

Article Snippet: Primary antibodies were used for IHC staining: CXCL12 (Boster, BA1389, 1:100), and α-SMA (Abcam, ab119952, 1:100).

Techniques: In Vivo, Biomarker Discovery, Microscopy, Staining, Immunohistochemistry, Expressing

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sdf1a (cxcl12) (PeproTech)

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