human cxcr1  (Santa Cruz Biotechnology)

 
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    Name:
    IL 8RA siRNA
    Description:
    Gene Silencers generally consist of pools of three to five target specific 19 25 nucleotide sequences in length For independent verification of IL 8RA gene silencing results individual duplex components or plasmids are also available upon request Suitable control antibody IL 8RA Antibody B 1 sc 7303 is recommended as control antibody for monitoring of IL 8RA expression knockdown by Western blotting or immunofluorescence
    Catalog Number:
    SC-40026
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    None
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    Gene Editing siRNA shRNA Gene Silencers Membrane Receptor IL 8RA siRNA shRNA Plasmid and Lentiviral Particle Gene Silencers IL 8RA siRNA and shRNA Plasmids h
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    Structured Review

    Santa Cruz Biotechnology human cxcr1
    Increased internalization of <t>CXCR1</t> in MMA(III)-exposed UROtsa cells. Flow cytometry analysis showed that the cells exposed to 50 nM MMA(III) for 3 or more months had an increased internalization of the IL-8 receptor CXCR1. The bars represent the mean
    Gene Silencers generally consist of pools of three to five target specific 19 25 nucleotide sequences in length For independent verification of IL 8RA gene silencing results individual duplex components or plasmids are also available upon request Suitable control antibody IL 8RA Antibody B 1 sc 7303 is recommended as control antibody for monitoring of IL 8RA expression knockdown by Western blotting or immunofluorescence
    https://www.bioz.com/result/human cxcr1/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    86/100 stars

    Images

    1) Product Images from "Interleukin-8 (IL-8) over-production and autocrine cell activation are key factors in monomethylarsonous acid [MMA(III)]-induced malignant transformation of urothelial cells"

    Article Title: Interleukin-8 (IL-8) over-production and autocrine cell activation are key factors in monomethylarsonous acid [MMA(III)]-induced malignant transformation of urothelial cells

    Journal: Toxicology and Applied Pharmacology

    doi: 10.1016/j.taap.2011.10.002

    Increased internalization of CXCR1 in MMA(III)-exposed UROtsa cells. Flow cytometry analysis showed that the cells exposed to 50 nM MMA(III) for 3 or more months had an increased internalization of the IL-8 receptor CXCR1. The bars represent the mean
    Figure Legend Snippet: Increased internalization of CXCR1 in MMA(III)-exposed UROtsa cells. Flow cytometry analysis showed that the cells exposed to 50 nM MMA(III) for 3 or more months had an increased internalization of the IL-8 receptor CXCR1. The bars represent the mean

    Techniques Used: Flow Cytometry, Cytometry

    UROtsa cells constitutively express CXCR1 and CXCR2. Untreated UROtsa cells were processed to determine the expression of surface and intracellular CXCR1 and CXCR2. The receptors were found to be mainly intracellular, suggesting IL-8 autocrine activation.
    Figure Legend Snippet: UROtsa cells constitutively express CXCR1 and CXCR2. Untreated UROtsa cells were processed to determine the expression of surface and intracellular CXCR1 and CXCR2. The receptors were found to be mainly intracellular, suggesting IL-8 autocrine activation.

    Techniques Used: Expressing, Activation Assay

    2) Product Images from "CXCL8 derived from tumor-associated macrophages and esophageal squamous cell carcinomas contributes to tumor progression by promoting migration and invasion of cancer cells"

    Article Title: CXCL8 derived from tumor-associated macrophages and esophageal squamous cell carcinomas contributes to tumor progression by promoting migration and invasion of cancer cells

    Journal: Oncotarget

    doi: 10.18632/oncotarget.22526

    A high expression of CXCL8 in human ESCC tissues is associated with the poor prognosis of ESCC patients (A) A double immunofluorescence analysis was performed using anti-CXCL8 (green) and anti-CD11b (red) antibodies on human ESCC tissue. Nuclei were stained with DAPI (blue). Not only CD11b-positive macrophages but also the cancer nest was stained by CXCL8 in human ESCC tissue. Scale bar, 100 μm. (B) Immunohistochemical staining for CXCL8 in human ESCC tissue. Typical images of CXCL8 are shown: negative ( left ), low-intensity ( center ) and high-intensity ( right) compared to the corresponding normal esophageal epithelia. Scale bar, 100 μm. (C) Immunohistochemical staining for CXCR1 in human ESCC tissue. Typical images are shown: low-intensity ( left ) and high-intensity ( right ) compared to the corresponding normal esophageal epithelia. Scale bar, 100 μm. (D) Immunohistochemical staining for CXCR2 in human ESCC tissue. Typical images are shown: low-intensity ( left ) and high-intensity ( right ) compared to the corresponding normal esophageal epithelia. Scale bar, 100 μm. (E) Kaplan-Meier analysis of ESCC patients divided into three groups according to their expression of CXCL8: CXCL8-Negative group (n = 14), CXCL8-Low group (n = 43) and CXCL8-High group (n = 13). The log-rank test was performed to determine significance. * p
    Figure Legend Snippet: A high expression of CXCL8 in human ESCC tissues is associated with the poor prognosis of ESCC patients (A) A double immunofluorescence analysis was performed using anti-CXCL8 (green) and anti-CD11b (red) antibodies on human ESCC tissue. Nuclei were stained with DAPI (blue). Not only CD11b-positive macrophages but also the cancer nest was stained by CXCL8 in human ESCC tissue. Scale bar, 100 μm. (B) Immunohistochemical staining for CXCL8 in human ESCC tissue. Typical images of CXCL8 are shown: negative ( left ), low-intensity ( center ) and high-intensity ( right) compared to the corresponding normal esophageal epithelia. Scale bar, 100 μm. (C) Immunohistochemical staining for CXCR1 in human ESCC tissue. Typical images are shown: low-intensity ( left ) and high-intensity ( right ) compared to the corresponding normal esophageal epithelia. Scale bar, 100 μm. (D) Immunohistochemical staining for CXCR2 in human ESCC tissue. Typical images are shown: low-intensity ( left ) and high-intensity ( right ) compared to the corresponding normal esophageal epithelia. Scale bar, 100 μm. (E) Kaplan-Meier analysis of ESCC patients divided into three groups according to their expression of CXCL8: CXCL8-Negative group (n = 14), CXCL8-Low group (n = 43) and CXCL8-High group (n = 13). The log-rank test was performed to determine significance. * p

    Techniques Used: Expressing, Immunofluorescence, Staining, Immunohistochemistry

    Akt and Erk1/2 were phosphorylated by CXCL8 through CXCR1 and CXCR2 in the ESCC cell lines (A) The mRNA levels of CXCR1 and CXCR2 in the ESCC cell lines were quantified by RT-PCR. (B) The protein level of CXCR1 and CXCR2 in the ESCC cell lines was confirmed by western blotting. Anti-CXCR1, CXCR2 and β-actin antibodies were used. (C) TE-8, TE-9 and TE-15 cells in serum-free conditions were treated with 10 ng/ml rhCXCL8 for 0, 10, 30 and 60 min. Western blotting was conducted with total protein extracted from ESCC cell lines using specific antibodies against Akt, p-Akt (Ser473), p-Akt (Thr308), Erk1/2, p-Erk1/2 (Thr202/Tyr204) and β-actin. Densitometric analysis of bands was performed with ImageJ (National Institutes of Health, Maryland, USA). The results are mean ± SEM. * p
    Figure Legend Snippet: Akt and Erk1/2 were phosphorylated by CXCL8 through CXCR1 and CXCR2 in the ESCC cell lines (A) The mRNA levels of CXCR1 and CXCR2 in the ESCC cell lines were quantified by RT-PCR. (B) The protein level of CXCR1 and CXCR2 in the ESCC cell lines was confirmed by western blotting. Anti-CXCR1, CXCR2 and β-actin antibodies were used. (C) TE-8, TE-9 and TE-15 cells in serum-free conditions were treated with 10 ng/ml rhCXCL8 for 0, 10, 30 and 60 min. Western blotting was conducted with total protein extracted from ESCC cell lines using specific antibodies against Akt, p-Akt (Ser473), p-Akt (Thr308), Erk1/2, p-Erk1/2 (Thr202/Tyr204) and β-actin. Densitometric analysis of bands was performed with ImageJ (National Institutes of Health, Maryland, USA). The results are mean ± SEM. * p

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Western Blot

    CXCL8 promoted the migration and invasion of the TE-8 cells (A) (i) For the transwell migration assay, TE-8 cells were plated on the transwell in serum-free RPMI-1640 at 5.0 × 10 5 cells/well. rhCXCL8 was added in the upper chamber at 10 ng/ml. The cell inserts were set on 24-well plates in RPMI-1640 with 1% FBS for 24 h. The migrated cells on the underside of the membrane were stained by Diff-Quik and counted. The results are mean ± SEM. Scale bar, 100 μm. (ii) For the transwell invasion assay, TE-8 cells were seeded on a transwell coated with matrigel in serum-free RPMI-1640 at 5.0 × 10 5 cells/well. Recombinant human CXCL8 was added in the transwell at 100 ng/ml. The cell inserts were set on 24-well plates in RPMI-1640 with 1% FBS for 48 h. The invaded cells on the underside of the membrane were stained by Diff-Quik and counted. (B) (i) TE-8 cells were plated on the upper chamber with or without rhCXCL8 at 10 ng/ml combined with the inhibitor against PI3K (LY294002, 10 μM) or MEK1/2 (PD98059, 10 μM). DMSO (0.2 μl/ml) was added to negative control. After 24 h, the migrated cells were counted. (ii) TE-8 cells were plated on the upper transwell coated with matrigel. rhCXCL8 was added in the transwell combined with LY294002 (10 μM) or PD98059 (10 μM). DMSO (0.2 μl/ml) was added to negative control. After 48 h, the invaded cells were counted. (C) TE-8 cells were transfected with 20 nM siRNA targeting CXCR1 and CXCR2 . siNC was transfected to TE-8 as negative control. Effective knockdown of CXCR1 and CXCR2 was confirmed by western blotting using antibodies against CXCR1 and CXCR2. (D) (i) CXCR1 - or CXCR2- silenced TE-8 cells were plated on the upper transwell with rhCXCL8 at 10 ng/ml. After 24 h, the migrated cells were counted. (ii) CXCR1 - or CXCR2 -silenced TE-8 cells were plated on the upper transwell coated with matrigel. rhCXCL8 was added in the transwell at 100 ng/ml. After 48 h, the invaded cells were counted. (E) (i) TE-8 cells were plated on the upper transwell with rhCXCL8 at 10 ng/ml combined with the neutralizing antibody against CXCR1 (0.2 μg/ml) or CXCR2 (1.0 μg/ml). Mouse IgG was added to negative control. The concentrations of neutralizing antibodies were based on the manufacturer's instructions. (ii) TE-8 cells were plated on the upper transwell coated with matrigel. rhCXCL8 was added in the upper transwell at 100 ng/ml combined with the neutralizing antibody against CXCR1 (0.2 μg/ml) or CXCR2 (1.0 μg/ml). Mouse IgG was added to negative control. After 48 h, the invaded cells were counted. NS, not significant; * p
    Figure Legend Snippet: CXCL8 promoted the migration and invasion of the TE-8 cells (A) (i) For the transwell migration assay, TE-8 cells were plated on the transwell in serum-free RPMI-1640 at 5.0 × 10 5 cells/well. rhCXCL8 was added in the upper chamber at 10 ng/ml. The cell inserts were set on 24-well plates in RPMI-1640 with 1% FBS for 24 h. The migrated cells on the underside of the membrane were stained by Diff-Quik and counted. The results are mean ± SEM. Scale bar, 100 μm. (ii) For the transwell invasion assay, TE-8 cells were seeded on a transwell coated with matrigel in serum-free RPMI-1640 at 5.0 × 10 5 cells/well. Recombinant human CXCL8 was added in the transwell at 100 ng/ml. The cell inserts were set on 24-well plates in RPMI-1640 with 1% FBS for 48 h. The invaded cells on the underside of the membrane were stained by Diff-Quik and counted. (B) (i) TE-8 cells were plated on the upper chamber with or without rhCXCL8 at 10 ng/ml combined with the inhibitor against PI3K (LY294002, 10 μM) or MEK1/2 (PD98059, 10 μM). DMSO (0.2 μl/ml) was added to negative control. After 24 h, the migrated cells were counted. (ii) TE-8 cells were plated on the upper transwell coated with matrigel. rhCXCL8 was added in the transwell combined with LY294002 (10 μM) or PD98059 (10 μM). DMSO (0.2 μl/ml) was added to negative control. After 48 h, the invaded cells were counted. (C) TE-8 cells were transfected with 20 nM siRNA targeting CXCR1 and CXCR2 . siNC was transfected to TE-8 as negative control. Effective knockdown of CXCR1 and CXCR2 was confirmed by western blotting using antibodies against CXCR1 and CXCR2. (D) (i) CXCR1 - or CXCR2- silenced TE-8 cells were plated on the upper transwell with rhCXCL8 at 10 ng/ml. After 24 h, the migrated cells were counted. (ii) CXCR1 - or CXCR2 -silenced TE-8 cells were plated on the upper transwell coated with matrigel. rhCXCL8 was added in the transwell at 100 ng/ml. After 48 h, the invaded cells were counted. (E) (i) TE-8 cells were plated on the upper transwell with rhCXCL8 at 10 ng/ml combined with the neutralizing antibody against CXCR1 (0.2 μg/ml) or CXCR2 (1.0 μg/ml). Mouse IgG was added to negative control. The concentrations of neutralizing antibodies were based on the manufacturer's instructions. (ii) TE-8 cells were plated on the upper transwell coated with matrigel. rhCXCL8 was added in the upper transwell at 100 ng/ml combined with the neutralizing antibody against CXCR1 (0.2 μg/ml) or CXCR2 (1.0 μg/ml). Mouse IgG was added to negative control. After 48 h, the invaded cells were counted. NS, not significant; * p

    Techniques Used: Migration, Transwell Migration Assay, Staining, Diff-Quik, Transwell Invasion Assay, Recombinant, Negative Control, Transfection, Western Blot

    TAM-like PBMo-derived macrophages induced the migration and invasion of TE-8 cells by activating PI3K and MEK1/2 signals through CXCL8 and CXCR1/2 interaction (A) PBMos (1.0 × 10 5 cells/well) were seeded on the lower chamber of 24-well plates with M-CSF (25 ng/ml) for 6 days to induce PBMo-derived macrophages, then incubated with 50% TE-8 CM to induce TAM-like PBMo-derived macrophages. After 2 days, the media were replaced with serum-free media. (i) TE-8 cells were plated on the upper transwell at 5.0 × 10 5 cells/well and set on the plate. After 24 h, the migrated cells were counted. (ii) TE-8 cells were plated on the upper transwell coated with matrigel at 5.0 × 10 5 cells/well and set on the plate. After 48 h, the invaded cells were counted. Scale bar, 100 μm. (B) (i) TE-8 cells were plated on the upper transwell with the inhibitor against PI3K (LY294002, 10 nM) or MEK1/2 (PD98059, 10 nM). DMSO (0.2 μl/ml) was added to negative control. After 24 h, the migrated cells were counted. (ii) TE-8 cells were plated on the upper matrigel-coated transwell with LY294002 (10 nM) or PD98059 (10 nM). DMSO (0.2 μl/ml) was added to negative control. After 48 h, the invaded cells were counted. (C) (i) TE-8 cells were plated on the upper transwell with the neutralizing antibodies against CXCR1 (0.2 μg/ml), CXCR2 (1.0 μg/ml) or CXCL8 (1.0 μg/ml). Mouse IgG was added to negative control. After 24 h, the migrated cells were counted. The concentrations of neutralizing antibody were based on manufacturer's instructions. (ii) TE-8 cells were plated on the upper matrigel-coated transwell with the neutralizing antibodies against CXCR1 (0.2 μg/ml), CXCR2 (1.0 μg/ml) or CXCL8 (1.0 μg/ml). Mouse IgG was added to negative control. After 48 h, the invaded cells were counted. The results are mean ± SEM. * p
    Figure Legend Snippet: TAM-like PBMo-derived macrophages induced the migration and invasion of TE-8 cells by activating PI3K and MEK1/2 signals through CXCL8 and CXCR1/2 interaction (A) PBMos (1.0 × 10 5 cells/well) were seeded on the lower chamber of 24-well plates with M-CSF (25 ng/ml) for 6 days to induce PBMo-derived macrophages, then incubated with 50% TE-8 CM to induce TAM-like PBMo-derived macrophages. After 2 days, the media were replaced with serum-free media. (i) TE-8 cells were plated on the upper transwell at 5.0 × 10 5 cells/well and set on the plate. After 24 h, the migrated cells were counted. (ii) TE-8 cells were plated on the upper transwell coated with matrigel at 5.0 × 10 5 cells/well and set on the plate. After 48 h, the invaded cells were counted. Scale bar, 100 μm. (B) (i) TE-8 cells were plated on the upper transwell with the inhibitor against PI3K (LY294002, 10 nM) or MEK1/2 (PD98059, 10 nM). DMSO (0.2 μl/ml) was added to negative control. After 24 h, the migrated cells were counted. (ii) TE-8 cells were plated on the upper matrigel-coated transwell with LY294002 (10 nM) or PD98059 (10 nM). DMSO (0.2 μl/ml) was added to negative control. After 48 h, the invaded cells were counted. (C) (i) TE-8 cells were plated on the upper transwell with the neutralizing antibodies against CXCR1 (0.2 μg/ml), CXCR2 (1.0 μg/ml) or CXCL8 (1.0 μg/ml). Mouse IgG was added to negative control. After 24 h, the migrated cells were counted. The concentrations of neutralizing antibody were based on manufacturer's instructions. (ii) TE-8 cells were plated on the upper matrigel-coated transwell with the neutralizing antibodies against CXCR1 (0.2 μg/ml), CXCR2 (1.0 μg/ml) or CXCL8 (1.0 μg/ml). Mouse IgG was added to negative control. After 48 h, the invaded cells were counted. The results are mean ± SEM. * p

    Techniques Used: Derivative Assay, Migration, Incubation, Negative Control

    A proposed model of the interaction between ESCC cells and TAMs through CXCL8 in tumor microenvironment Many humoral factors, including IL-4, induced macrophages into TAMs. Then, expression level of CXCL8 was up-regulated in TAMs. CXCL8 secreted from TAMs, as well as from ESCC cells, contributed ESCC cells' migration and invasion by activating Akt and Erk1/2 signals through CXCR1/CXCR2 of ESCC cells.
    Figure Legend Snippet: A proposed model of the interaction between ESCC cells and TAMs through CXCL8 in tumor microenvironment Many humoral factors, including IL-4, induced macrophages into TAMs. Then, expression level of CXCL8 was up-regulated in TAMs. CXCL8 secreted from TAMs, as well as from ESCC cells, contributed ESCC cells' migration and invasion by activating Akt and Erk1/2 signals through CXCR1/CXCR2 of ESCC cells.

    Techniques Used: Expressing, Migration

    Related Articles

    Small Interfering RNA:

    Article Title: CXCL8 derived from tumor-associated macrophages and esophageal squamous cell carcinomas contributes to tumor progression by promoting migration and invasion of cancer cells
    Article Snippet: Transwell migration and invasion assays were performed as described above. .. CXCR1 and CXCR2 knockdown by small interfering RNA Cancer cell lines were transfected with 20 nM small interfering RNA (siRNA) targeting human CXCR1 (IL-8RA siRNA, sc-40026, Santa Cruz) and CXCR2 (IL-8RB siRNA, sc-40028, Santa Cruz) using Lipofectamine® RNAiMAX (Invitrogen). .. Control siRNA (Sigma-Aldrich) was used as the negative control.

    Transfection:

    Article Title: CXCL8 derived from tumor-associated macrophages and esophageal squamous cell carcinomas contributes to tumor progression by promoting migration and invasion of cancer cells
    Article Snippet: Transwell migration and invasion assays were performed as described above. .. CXCR1 and CXCR2 knockdown by small interfering RNA Cancer cell lines were transfected with 20 nM small interfering RNA (siRNA) targeting human CXCR1 (IL-8RA siRNA, sc-40026, Santa Cruz) and CXCR2 (IL-8RB siRNA, sc-40028, Santa Cruz) using Lipofectamine® RNAiMAX (Invitrogen). .. Control siRNA (Sigma-Aldrich) was used as the negative control.

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    Santa Cruz Biotechnology goat anti human cxcr2
    Staphopain A inhibits calcium mobilization of <t>U937-CXCR2</t> cells. Fluo-3-labelled U937-CXCR2 cells were preincubated with buffer, or 0.5 μM Staphopain A with and without 1 μM Staphostatin A for 15 min at 37°C. After washing, cells were stimulated with different concentrations of CXCL1 ( A ), CXCL7 ( B ) and CXCL8 ( C ). All figures represent the mean±s.e. of three separate experiments. The relative calcium mobilization was calculated by dividing the fluorescence after stimulation by the baseline fluorescence. * P
    Goat Anti Human Cxcr2, 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
    https://www.bioz.com/result/goat anti human cxcr2/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    92
    Santa Cruz Biotechnology antibodies against human cxcr1
    Suppression of BZ-induced IL-8 augments BZ cytotoxic and anti-proliferative effect in TNBC cells. (A) RT-PCR of <t>CXCR1</t> and CXCR2 mRNA levels in MDA-MB-231 cells treated with increasing BZ for 24 h. (B) Western analysis of CXCR1, CXCR2, and control actin protein levels in whole cell extracts (WCE) of MDA-MB-231 cells treated with increasing BZ for 24 h. The bottom panel represents densitometric evaluation of CXCR1 and CXCR2 protein levels shown in the top panel. The CXCR1/2 densities were normalized to actin, and expressed relative to untreated cells. (C) RT-PCR of IL-8 mRNA in MDA-MB-231 cells transfected with control or IL-8 siRNA and incubated 24 h with increasing BZ. (D) IL-8 release measured by ELISA in supernatant of MDA-MB-231 cells transfected with control or IL-8 siRNA and incubated 24 h with increasing BZ. (E) Viability of MDA-MB-231 cells transfected with control or IL-8 siRNA, and incubated 24 h with increasing BZ, measured be Trypan Blue exclusion. (F) Proliferation of MDA-MB-231 cells transfected with control or IL-8 siRNA, and incubated 24 h with BZ, measured by CellTiter 96 One Solution Cell Proliferation Assay. (G) Viability of MDA-MB-231 cells incubated 24 h with increasing BZ in the presence of control pre-immune IgG or IL-8 neutralizing monoclonal antibody. (H) Proliferation of MDA-MB-231 cells incubated 24 h with increasing BZ in the presence of control pre-immune IgG or IL-8 neutralizing monoclonal antibody. The values represent the mean +/− SE of four experiments; asterisks denote a statistically significant change compared to control.
    Antibodies Against Human Cxcr1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibodies against human cxcr1/product/Santa Cruz Biotechnology
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibodies against human cxcr1 - by Bioz Stars, 2021-07
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    93
    Santa Cruz Biotechnology anti human cxcr4
    SDF-1 released by activated LSCs is the key paracrine factor to recruit stromal fibroblasts. ( a ) Protein array showing differential cytokine release by activated LSCs (ALSC) when co-cultured with fibroblasts. ( b ) The mRNA relative levels of different cytokines confirm their upregulation in ALSCs. ( c ) Time-lapse tracing of fibroblast (red) recruitment by LSCs (green) in lung explants. Scale bars, 200 μm. ( d ) Serial sections images captured at day 4 showing expression of SDF-1 (white) and <t>CXCR4</t> (purple) by LSCs and fibroblasts, respectively. Scale bars, 50 μm. ( e ) Fibroblast migration induced by conditioned medium (CM) from ALSCs (expressing control shRNA) (line 4) is prevented by addition of an anti-SDF-1 antibody (line 5) or by using CM from LSCs lacking SDF-1 (ALSC-KD) (line 6). Addition of SDF-1 recombinant protein into CM from ALSC-KD cells rescued their potential to recruit fibroblasts (line 7). Scale bar, 200 μm. All results ( b and e ) are the mean±s.e.m. of 4–5 triplicate experiments. P
    Anti Human Cxcr4, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Staphopain A inhibits calcium mobilization of U937-CXCR2 cells. Fluo-3-labelled U937-CXCR2 cells were preincubated with buffer, or 0.5 μM Staphopain A with and without 1 μM Staphostatin A for 15 min at 37°C. After washing, cells were stimulated with different concentrations of CXCL1 ( A ), CXCL7 ( B ) and CXCL8 ( C ). All figures represent the mean±s.e. of three separate experiments. The relative calcium mobilization was calculated by dividing the fluorescence after stimulation by the baseline fluorescence. * P

    Journal: The EMBO Journal

    Article Title: Staphylococcus aureus Staphopain A inhibits CXCR2-dependent neutrophil activation and chemotaxis

    doi: 10.1038/emboj.2012.212

    Figure Lengend Snippet: Staphopain A inhibits calcium mobilization of U937-CXCR2 cells. Fluo-3-labelled U937-CXCR2 cells were preincubated with buffer, or 0.5 μM Staphopain A with and without 1 μM Staphostatin A for 15 min at 37°C. After washing, cells were stimulated with different concentrations of CXCL1 ( A ), CXCL7 ( B ) and CXCL8 ( C ). All figures represent the mean±s.e. of three separate experiments. The relative calcium mobilization was calculated by dividing the fluorescence after stimulation by the baseline fluorescence. * P

    Article Snippet: After washing, cells were incubated with mouse anti-human CXCR2 (clone 19, Abcam, directed against the N-terminus), goat anti-human CXCR2 (sc-22661, Santa Cruz, directed against the extracellular domain) or mouse anti-human CXCR1 (R & D, directed against the N-terminus) for 30 min on ice.

    Techniques: Fluorescence

    Staphopain A inhibits CXCR2-mediated calcium mobilization of neutrophils. Fluo-3-labelled neutrophils were preincubated with buffer or 0.5 μM Staphopain A with or without 1 μM Staphostatin A, for 15 min at 37°C. After washing, cells were stimulated with different concentrations of CXCL1 ( A ), CXCL7 ( B ), CXCL8 ( C ), fMLF ( D ), C5a ( E ) or a fixed concentration (3 × 10 −9 M) of CXCL2, CXCL3, CXCL5 and CXCL6 ( F ). To determine the IC 50 (50% of inhibition), Fluo-3-labelled neutrophils were preincubated with different concentrations of Staphopain A for 15 min at 37°C and subsequently stimulated with 3 × 10 −9 M CXCL1 ( G ) or 1 × 10 −8 M CXCL7 ( H ). The IC 50 for CXCL1 and CXCL7 was calculated with the formulas y =−4 E +10 −7 x +4.1314 and y =−3 E +10 −7 x +4.0248, respectively. All figures represent the mean±s.e. of three separate experiments using different donors. The relative calcium mobilization was calculated by dividing the fluorescence after stimulation by the baseline fluorescence. * P

    Journal: The EMBO Journal

    Article Title: Staphylococcus aureus Staphopain A inhibits CXCR2-dependent neutrophil activation and chemotaxis

    doi: 10.1038/emboj.2012.212

    Figure Lengend Snippet: Staphopain A inhibits CXCR2-mediated calcium mobilization of neutrophils. Fluo-3-labelled neutrophils were preincubated with buffer or 0.5 μM Staphopain A with or without 1 μM Staphostatin A, for 15 min at 37°C. After washing, cells were stimulated with different concentrations of CXCL1 ( A ), CXCL7 ( B ), CXCL8 ( C ), fMLF ( D ), C5a ( E ) or a fixed concentration (3 × 10 −9 M) of CXCL2, CXCL3, CXCL5 and CXCL6 ( F ). To determine the IC 50 (50% of inhibition), Fluo-3-labelled neutrophils were preincubated with different concentrations of Staphopain A for 15 min at 37°C and subsequently stimulated with 3 × 10 −9 M CXCL1 ( G ) or 1 × 10 −8 M CXCL7 ( H ). The IC 50 for CXCL1 and CXCL7 was calculated with the formulas y =−4 E +10 −7 x +4.1314 and y =−3 E +10 −7 x +4.0248, respectively. All figures represent the mean±s.e. of three separate experiments using different donors. The relative calcium mobilization was calculated by dividing the fluorescence after stimulation by the baseline fluorescence. * P

    Article Snippet: After washing, cells were incubated with mouse anti-human CXCR2 (clone 19, Abcam, directed against the N-terminus), goat anti-human CXCR2 (sc-22661, Santa Cruz, directed against the extracellular domain) or mouse anti-human CXCR1 (R & D, directed against the N-terminus) for 30 min on ice.

    Techniques: Concentration Assay, Inhibition, Fluorescence

    Staphopain A specifically cleaves the N-terminus of CXCR2. ( A ) Western blot analysis of U937-CXCR2 cells incubated with buffer, 0.5 μM Staphopain A, 0.5 μM Staphopain A plus 1 μM Staphostatin A for 15 min at 37°C. Whole-cell lysates were analysed by western blotting using an mAb against the N-terminus of CXCR2. Figure represents three independent experiments. ( B ) Confocal images of HEK cells transfected with human CXCR1 or CXCR2 fused to a C-terminal YFP tag. Cells were incubated with buffer or 0.5 μM Staphopain A for 30 min at 37°C. The N-termini were stained with mAbs and subsequent Alexa633-labelled anti-mouse antibodies. YFP was artificially coloured green. Images are representatives of three independent experiments. ( C ) Flow cytometry analysis of human neutrophils treated with 0.5 μM Staphopain A or 40 nM PMA for 15 min at 37°C. Cells were first stained with antibodies against the N-terminus of CXCR2, the extracellular loop of CXCR2 or the N-terminus of CXCR1 and subsequently with FITC-labelled secondary antibodies. Antibody binding is expressed in percentages, calculated by dividing the fluorescence of treated cells by fluorescence of buffer-treated cells and multiplying with 100. Figure represents the mean±s.e. of three separate experiments using different donors. ** P

    Journal: The EMBO Journal

    Article Title: Staphylococcus aureus Staphopain A inhibits CXCR2-dependent neutrophil activation and chemotaxis

    doi: 10.1038/emboj.2012.212

    Figure Lengend Snippet: Staphopain A specifically cleaves the N-terminus of CXCR2. ( A ) Western blot analysis of U937-CXCR2 cells incubated with buffer, 0.5 μM Staphopain A, 0.5 μM Staphopain A plus 1 μM Staphostatin A for 15 min at 37°C. Whole-cell lysates were analysed by western blotting using an mAb against the N-terminus of CXCR2. Figure represents three independent experiments. ( B ) Confocal images of HEK cells transfected with human CXCR1 or CXCR2 fused to a C-terminal YFP tag. Cells were incubated with buffer or 0.5 μM Staphopain A for 30 min at 37°C. The N-termini were stained with mAbs and subsequent Alexa633-labelled anti-mouse antibodies. YFP was artificially coloured green. Images are representatives of three independent experiments. ( C ) Flow cytometry analysis of human neutrophils treated with 0.5 μM Staphopain A or 40 nM PMA for 15 min at 37°C. Cells were first stained with antibodies against the N-terminus of CXCR2, the extracellular loop of CXCR2 or the N-terminus of CXCR1 and subsequently with FITC-labelled secondary antibodies. Antibody binding is expressed in percentages, calculated by dividing the fluorescence of treated cells by fluorescence of buffer-treated cells and multiplying with 100. Figure represents the mean±s.e. of three separate experiments using different donors. ** P

    Article Snippet: After washing, cells were incubated with mouse anti-human CXCR2 (clone 19, Abcam, directed against the N-terminus), goat anti-human CXCR2 (sc-22661, Santa Cruz, directed against the extracellular domain) or mouse anti-human CXCR1 (R & D, directed against the N-terminus) for 30 min on ice.

    Techniques: Western Blot, Incubation, Transfection, Staining, Flow Cytometry, Cytometry, Binding Assay, Fluorescence

    Determination of the Staphopain A cleavage site in CXCR2. ( A ) Staphopain A cleaves the CXCR2 1–48 -GB1-His protein. Different concentrations of Staphopain A were incubated with 6.75 μM CXCR2 1–48 -GB1-His protein for 15 min at 37°C. Samples were analysed by SDS–PAGE and Instant blue staining. Lane 6: CXCR2 1–48 -GB1-His plus 150 nM Staphopain A plus 1 μM Staphostatin A; lane 7: Staphostatin A alone. ( B ) N-terminal sequencing of the CXCR2 cleavage product generated by incubation of 6.75 μM CXCR2 1–48 -GB1-His protein with 150 nM Staphopain A for 15 min at 37°C. Sequencing was performed once. ( C ) Staphopain A cleavage of CXCR2 1–48 -GB1-His (left, LLDA) or CXCR2 1–48 -GB1-His mutated with a Proline at position 34 (right, LPDA). CXCR2 protein at 6.75 μM, 15 min at 37°C; proteins were stained using Instant Blue. ( D ) Staphopain A cleaves CXCR2 in the presence of plasma. CXCR2 1–48 -GB1-His (1.5 μM) was incubated with Staphopain A with or without 10% human plasma for 30 min at 37°C. CXCR2 was visualized by immunoblotting using anti-CXCR2 (N-terminus specific) antibodies. ( A , C and D ) Representatives of three separate experiments are shown.

    Journal: The EMBO Journal

    Article Title: Staphylococcus aureus Staphopain A inhibits CXCR2-dependent neutrophil activation and chemotaxis

    doi: 10.1038/emboj.2012.212

    Figure Lengend Snippet: Determination of the Staphopain A cleavage site in CXCR2. ( A ) Staphopain A cleaves the CXCR2 1–48 -GB1-His protein. Different concentrations of Staphopain A were incubated with 6.75 μM CXCR2 1–48 -GB1-His protein for 15 min at 37°C. Samples were analysed by SDS–PAGE and Instant blue staining. Lane 6: CXCR2 1–48 -GB1-His plus 150 nM Staphopain A plus 1 μM Staphostatin A; lane 7: Staphostatin A alone. ( B ) N-terminal sequencing of the CXCR2 cleavage product generated by incubation of 6.75 μM CXCR2 1–48 -GB1-His protein with 150 nM Staphopain A for 15 min at 37°C. Sequencing was performed once. ( C ) Staphopain A cleavage of CXCR2 1–48 -GB1-His (left, LLDA) or CXCR2 1–48 -GB1-His mutated with a Proline at position 34 (right, LPDA). CXCR2 protein at 6.75 μM, 15 min at 37°C; proteins were stained using Instant Blue. ( D ) Staphopain A cleaves CXCR2 in the presence of plasma. CXCR2 1–48 -GB1-His (1.5 μM) was incubated with Staphopain A with or without 10% human plasma for 30 min at 37°C. CXCR2 was visualized by immunoblotting using anti-CXCR2 (N-terminus specific) antibodies. ( A , C and D ) Representatives of three separate experiments are shown.

    Article Snippet: After washing, cells were incubated with mouse anti-human CXCR2 (clone 19, Abcam, directed against the N-terminus), goat anti-human CXCR2 (sc-22661, Santa Cruz, directed against the extracellular domain) or mouse anti-human CXCR1 (R & D, directed against the N-terminus) for 30 min on ice.

    Techniques: Incubation, SDS Page, Staining, Sequencing, Generated

    Staphopain A inhibits antibody binding to CXCR2 on neutrophils. ( A ) Neutrophils were incubated with 0.5 μM Staphopain A or buffer for 15 min at 37°C. After washing, cells were stained with a panel of blocking antibodies against surface-expressed receptors. The relative expression was calculated by dividing the mean fluorescence of Staphopain-treated cells by Buffer-treated cells. ( B ) Staphopain A blocks antibody binding in a dose-dependent manner. Neutrophils were incubated with various concentrations of Staphopain A for 15 min at 37°C and stained with an antibody recognizing the N-terminal domain of human CXCR2. Inlay: Representative histogram of the CXCR2 expression on neutrophils treated with 0.5 μM Staphopain A compared to buffer. ( C ) Protease activity is required for antibody inhibition. Neutrophils were treated with 0.5 μM Staphopain A with or without 1 μM Staphostatin A or 10 μM E64. All figures represent the mean±s.e. of three separate experiments using different donors. Background was determined using an isotype control. ( A , B ) * P

    Journal: The EMBO Journal

    Article Title: Staphylococcus aureus Staphopain A inhibits CXCR2-dependent neutrophil activation and chemotaxis

    doi: 10.1038/emboj.2012.212

    Figure Lengend Snippet: Staphopain A inhibits antibody binding to CXCR2 on neutrophils. ( A ) Neutrophils were incubated with 0.5 μM Staphopain A or buffer for 15 min at 37°C. After washing, cells were stained with a panel of blocking antibodies against surface-expressed receptors. The relative expression was calculated by dividing the mean fluorescence of Staphopain-treated cells by Buffer-treated cells. ( B ) Staphopain A blocks antibody binding in a dose-dependent manner. Neutrophils were incubated with various concentrations of Staphopain A for 15 min at 37°C and stained with an antibody recognizing the N-terminal domain of human CXCR2. Inlay: Representative histogram of the CXCR2 expression on neutrophils treated with 0.5 μM Staphopain A compared to buffer. ( C ) Protease activity is required for antibody inhibition. Neutrophils were treated with 0.5 μM Staphopain A with or without 1 μM Staphostatin A or 10 μM E64. All figures represent the mean±s.e. of three separate experiments using different donors. Background was determined using an isotype control. ( A , B ) * P

    Article Snippet: After washing, cells were incubated with mouse anti-human CXCR2 (clone 19, Abcam, directed against the N-terminus), goat anti-human CXCR2 (sc-22661, Santa Cruz, directed against the extracellular domain) or mouse anti-human CXCR1 (R & D, directed against the N-terminus) for 30 min on ice.

    Techniques: Binding Assay, Incubation, Staining, Blocking Assay, Expressing, Fluorescence, Activity Assay, Inhibition

    Staphopain A detection in bacterial supernatants. ( A ) S. aureus strain USA300 (WT) and its isogenic mutant (Δ scpA ) were grown in TSB media and supernatants were collected at different time points. Above: OD 600 measurements taken at different time points; Below: cleavage of 1 μM CXCR2 1–48 -GB1-His protein by undiluted supernatants collected at different points (incubation for 30 min at 37°C unless otherwise noted). The CXCR2 1–48 -GB1-His protein was detected using western blotting with an antibody against the His tag. ( B ) Time-dependent cleavage of CXCR2 1–48 -GB1-His protein (1 μM) by 3 h supernatants (undiluted) of USA300 (WT), its isogenic mutant (Δ scpA ) and a complemented mutant (Δ scpA Comp). ( C ) CXCR2 cleavage by WT supernatant is inhibited by Staphostatin A (MBP-ScpB). CXCR2 1–48 -GB1-His protein (1 μM) was incubated with 3 h supernatants (undiluted) of USA300 (WT) in the presence of various concentrations of MBP-tagged ScpB. MBP is maltose binding protein. ( A – C) Representative blots of three separate experiments are shown.

    Journal: The EMBO Journal

    Article Title: Staphylococcus aureus Staphopain A inhibits CXCR2-dependent neutrophil activation and chemotaxis

    doi: 10.1038/emboj.2012.212

    Figure Lengend Snippet: Staphopain A detection in bacterial supernatants. ( A ) S. aureus strain USA300 (WT) and its isogenic mutant (Δ scpA ) were grown in TSB media and supernatants were collected at different time points. Above: OD 600 measurements taken at different time points; Below: cleavage of 1 μM CXCR2 1–48 -GB1-His protein by undiluted supernatants collected at different points (incubation for 30 min at 37°C unless otherwise noted). The CXCR2 1–48 -GB1-His protein was detected using western blotting with an antibody against the His tag. ( B ) Time-dependent cleavage of CXCR2 1–48 -GB1-His protein (1 μM) by 3 h supernatants (undiluted) of USA300 (WT), its isogenic mutant (Δ scpA ) and a complemented mutant (Δ scpA Comp). ( C ) CXCR2 cleavage by WT supernatant is inhibited by Staphostatin A (MBP-ScpB). CXCR2 1–48 -GB1-His protein (1 μM) was incubated with 3 h supernatants (undiluted) of USA300 (WT) in the presence of various concentrations of MBP-tagged ScpB. MBP is maltose binding protein. ( A – C) Representative blots of three separate experiments are shown.

    Article Snippet: After washing, cells were incubated with mouse anti-human CXCR2 (clone 19, Abcam, directed against the N-terminus), goat anti-human CXCR2 (sc-22661, Santa Cruz, directed against the extracellular domain) or mouse anti-human CXCR1 (R & D, directed against the N-terminus) for 30 min on ice.

    Techniques: Mutagenesis, Incubation, Western Blot, Binding Assay

    Suppression of BZ-induced IL-8 augments BZ cytotoxic and anti-proliferative effect in TNBC cells. (A) RT-PCR of CXCR1 and CXCR2 mRNA levels in MDA-MB-231 cells treated with increasing BZ for 24 h. (B) Western analysis of CXCR1, CXCR2, and control actin protein levels in whole cell extracts (WCE) of MDA-MB-231 cells treated with increasing BZ for 24 h. The bottom panel represents densitometric evaluation of CXCR1 and CXCR2 protein levels shown in the top panel. The CXCR1/2 densities were normalized to actin, and expressed relative to untreated cells. (C) RT-PCR of IL-8 mRNA in MDA-MB-231 cells transfected with control or IL-8 siRNA and incubated 24 h with increasing BZ. (D) IL-8 release measured by ELISA in supernatant of MDA-MB-231 cells transfected with control or IL-8 siRNA and incubated 24 h with increasing BZ. (E) Viability of MDA-MB-231 cells transfected with control or IL-8 siRNA, and incubated 24 h with increasing BZ, measured be Trypan Blue exclusion. (F) Proliferation of MDA-MB-231 cells transfected with control or IL-8 siRNA, and incubated 24 h with BZ, measured by CellTiter 96 One Solution Cell Proliferation Assay. (G) Viability of MDA-MB-231 cells incubated 24 h with increasing BZ in the presence of control pre-immune IgG or IL-8 neutralizing monoclonal antibody. (H) Proliferation of MDA-MB-231 cells incubated 24 h with increasing BZ in the presence of control pre-immune IgG or IL-8 neutralizing monoclonal antibody. The values represent the mean +/− SE of four experiments; asterisks denote a statistically significant change compared to control.

    Journal: PLoS ONE

    Article Title: Proteasome inhibition induces IKK-dependent interleukin-8 expression in triple negative breast cancer cells: Opportunity for combination therapy

    doi: 10.1371/journal.pone.0201858

    Figure Lengend Snippet: Suppression of BZ-induced IL-8 augments BZ cytotoxic and anti-proliferative effect in TNBC cells. (A) RT-PCR of CXCR1 and CXCR2 mRNA levels in MDA-MB-231 cells treated with increasing BZ for 24 h. (B) Western analysis of CXCR1, CXCR2, and control actin protein levels in whole cell extracts (WCE) of MDA-MB-231 cells treated with increasing BZ for 24 h. The bottom panel represents densitometric evaluation of CXCR1 and CXCR2 protein levels shown in the top panel. The CXCR1/2 densities were normalized to actin, and expressed relative to untreated cells. (C) RT-PCR of IL-8 mRNA in MDA-MB-231 cells transfected with control or IL-8 siRNA and incubated 24 h with increasing BZ. (D) IL-8 release measured by ELISA in supernatant of MDA-MB-231 cells transfected with control or IL-8 siRNA and incubated 24 h with increasing BZ. (E) Viability of MDA-MB-231 cells transfected with control or IL-8 siRNA, and incubated 24 h with increasing BZ, measured be Trypan Blue exclusion. (F) Proliferation of MDA-MB-231 cells transfected with control or IL-8 siRNA, and incubated 24 h with BZ, measured by CellTiter 96 One Solution Cell Proliferation Assay. (G) Viability of MDA-MB-231 cells incubated 24 h with increasing BZ in the presence of control pre-immune IgG or IL-8 neutralizing monoclonal antibody. (H) Proliferation of MDA-MB-231 cells incubated 24 h with increasing BZ in the presence of control pre-immune IgG or IL-8 neutralizing monoclonal antibody. The values represent the mean +/− SE of four experiments; asterisks denote a statistically significant change compared to control.

    Article Snippet: Antibodies against human CXCR1 (sc-7303), CXCR2 (sc-7304), IKKα (sc-7218), IKKβ (sc-8014), IKKε (sc-376114), p65 NFκB (sc-372), IκBα (sc-371), and histone H3 (sc-8654) were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Reverse Transcription Polymerase Chain Reaction, Multiple Displacement Amplification, Western Blot, Transfection, Incubation, Enzyme-linked Immunosorbent Assay, Proliferation Assay

    SDF-1 released by activated LSCs is the key paracrine factor to recruit stromal fibroblasts. ( a ) Protein array showing differential cytokine release by activated LSCs (ALSC) when co-cultured with fibroblasts. ( b ) The mRNA relative levels of different cytokines confirm their upregulation in ALSCs. ( c ) Time-lapse tracing of fibroblast (red) recruitment by LSCs (green) in lung explants. Scale bars, 200 μm. ( d ) Serial sections images captured at day 4 showing expression of SDF-1 (white) and CXCR4 (purple) by LSCs and fibroblasts, respectively. Scale bars, 50 μm. ( e ) Fibroblast migration induced by conditioned medium (CM) from ALSCs (expressing control shRNA) (line 4) is prevented by addition of an anti-SDF-1 antibody (line 5) or by using CM from LSCs lacking SDF-1 (ALSC-KD) (line 6). Addition of SDF-1 recombinant protein into CM from ALSC-KD cells rescued their potential to recruit fibroblasts (line 7). Scale bar, 200 μm. All results ( b and e ) are the mean±s.e.m. of 4–5 triplicate experiments. P

    Journal: Nature Communications

    Article Title: A paracrine network regulates the cross-talk between human lung stem cells and the stroma

    doi: 10.1038/ncomms4175

    Figure Lengend Snippet: SDF-1 released by activated LSCs is the key paracrine factor to recruit stromal fibroblasts. ( a ) Protein array showing differential cytokine release by activated LSCs (ALSC) when co-cultured with fibroblasts. ( b ) The mRNA relative levels of different cytokines confirm their upregulation in ALSCs. ( c ) Time-lapse tracing of fibroblast (red) recruitment by LSCs (green) in lung explants. Scale bars, 200 μm. ( d ) Serial sections images captured at day 4 showing expression of SDF-1 (white) and CXCR4 (purple) by LSCs and fibroblasts, respectively. Scale bars, 50 μm. ( e ) Fibroblast migration induced by conditioned medium (CM) from ALSCs (expressing control shRNA) (line 4) is prevented by addition of an anti-SDF-1 antibody (line 5) or by using CM from LSCs lacking SDF-1 (ALSC-KD) (line 6). Addition of SDF-1 recombinant protein into CM from ALSC-KD cells rescued their potential to recruit fibroblasts (line 7). Scale bar, 200 μm. All results ( b and e ) are the mean±s.e.m. of 4–5 triplicate experiments. P

    Article Snippet: The following primary antibodies were used: anti-human CC10 (1/1,000, Santa Cruz, sc-365992), anti-human SPC (1/1,000, Santa Cruz, sc-7705), anti-human AQP5 (1/500, Santa Cruz, sc-9890), anti-human LGR6 (1/1,000, Santa Cruz, SC-48236), anti-human SDF-1 (1/500, Santa Cruz, sc-6193), anti-human CXCR4 (1/500, Santa Cruz, sc-9046), anti-GFP (1/1,000, Abcam, ab-13970), anti-RFP (1/1,000, Abcam, ab-62341), anti-CD73 (1/1,000, Abcam, ab-54217), anti-mouse Vimentin (1/1,000, BD Pharmigen, #550513), anti-human Nuclei antibody (1/1,000, Millipore, MAB1281).

    Techniques: Protein Array, Cell Culture, Expressing, Migration, shRNA, Recombinant