Structured Review

Proteintech shp 1
Shp 1, supplied by Proteintech, 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/shp 1/product/Proteintech
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99
shp 1 - by Bioz Stars, 2024-07
86/100 stars

Images


Structured Review

Proteintech shp 2
PSD-A inhibits STAT3 signaling pathway in A549 cells. (a) PSD-A inhibits constitutive STAT3 activation at tyrosine 705. Cells were treated with PSD-A for 24 h, and expression of p-STAT3 and total STAT3 was measured using Western blot. (b) PSD-A inhibits inducible STAT3 activation in A549 cells. A549 cells were pretreated with PSD-A for 4 h and then stimulated with 100 nM TPA and 10 ng/mL IL-6 for 1 h. Extracts were prepared and subjected to Western blot for the expression of p-STAT3 and STAT3. (c) Cells were treated with PSD-A for 24 h, and expressions of phosphatases (STAT3-negative regulators) were determined by Western blot. PSD-A increased the expression of SHP-1 without affecting <t>SHP-2</t> and PTEN. (d) Cells were treated with 25 nM PSD-A in the presence or absence of Na 3 VO 4 (100 μ M) for 24 h. Cell lysates were collected and subjected to Western blot for the expression of p-STAT3 and STAT3. Na 3 VO 4 pretreatment reversed the suppressive effect of PSD-A on STAT3 indicating that tyrosine phosphatases play an important role in PSD-A-mediated STAT3 inhibition. (e) Cells were treated with PSD-A for 4 h, and expressions of tyrosine kinases (p-SRC/SRC and p-JAK2/JAK2) were measured by Western blot. PSD-A suppressed the phosphorylation of SRC but did not affect p-JAK2 expression. (f) Cells were treated with or without PSD-A in the presence or absence of momelotininb (JAK inhibitor) and SP600125 (JNK inhibitor) for 4 h. Proteins were extracted, and expression of p-STAT3 and STAT3 was detected by Western blot. (g) Cells were treated with PSD-A (50 nM) and S31–201 (100 μ M) for 4 h, and expression of p-STAT3 was measured in cell lysates by Western blot. (h) A549 cells were incubated with or without PSD-A for 4 h and then further incubated with IL-6 for 1 h. The nuclear extracts were then collected and assayed for STAT3 DNA-binding activity according to the instructions of the kit. Columns not sharing the same superscript letters within the groups differ significantly ( P < 0.05).
Shp 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/shp 2/product/Proteintech
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
shp 2 - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Proscillaridin A Promotes Oxidative Stress and ER Stress, Inhibits STAT3 Activation, and Induces Apoptosis in A549 Lung Adenocarcinoma Cells"

Article Title: Proscillaridin A Promotes Oxidative Stress and ER Stress, Inhibits STAT3 Activation, and Induces Apoptosis in A549 Lung Adenocarcinoma Cells

Journal: Oxidative Medicine and Cellular Longevity

doi: 10.1155/2018/3853409

PSD-A inhibits STAT3 signaling pathway in A549 cells. (a) PSD-A inhibits constitutive STAT3 activation at tyrosine 705. Cells were treated with PSD-A for 24 h, and expression of p-STAT3 and total STAT3 was measured using Western blot. (b) PSD-A inhibits inducible STAT3 activation in A549 cells. A549 cells were pretreated with PSD-A for 4 h and then stimulated with 100 nM TPA and 10 ng/mL IL-6 for 1 h. Extracts were prepared and subjected to Western blot for the expression of p-STAT3 and STAT3. (c) Cells were treated with PSD-A for 24 h, and expressions of phosphatases (STAT3-negative regulators) were determined by Western blot. PSD-A increased the expression of SHP-1 without affecting SHP-2 and PTEN. (d) Cells were treated with 25 nM PSD-A in the presence or absence of Na 3 VO 4 (100 μ M) for 24 h. Cell lysates were collected and subjected to Western blot for the expression of p-STAT3 and STAT3. Na 3 VO 4 pretreatment reversed the suppressive effect of PSD-A on STAT3 indicating that tyrosine phosphatases play an important role in PSD-A-mediated STAT3 inhibition. (e) Cells were treated with PSD-A for 4 h, and expressions of tyrosine kinases (p-SRC/SRC and p-JAK2/JAK2) were measured by Western blot. PSD-A suppressed the phosphorylation of SRC but did not affect p-JAK2 expression. (f) Cells were treated with or without PSD-A in the presence or absence of momelotininb (JAK inhibitor) and SP600125 (JNK inhibitor) for 4 h. Proteins were extracted, and expression of p-STAT3 and STAT3 was detected by Western blot. (g) Cells were treated with PSD-A (50 nM) and S31–201 (100 μ M) for 4 h, and expression of p-STAT3 was measured in cell lysates by Western blot. (h) A549 cells were incubated with or without PSD-A for 4 h and then further incubated with IL-6 for 1 h. The nuclear extracts were then collected and assayed for STAT3 DNA-binding activity according to the instructions of the kit. Columns not sharing the same superscript letters within the groups differ significantly ( P < 0.05).
Figure Legend Snippet: PSD-A inhibits STAT3 signaling pathway in A549 cells. (a) PSD-A inhibits constitutive STAT3 activation at tyrosine 705. Cells were treated with PSD-A for 24 h, and expression of p-STAT3 and total STAT3 was measured using Western blot. (b) PSD-A inhibits inducible STAT3 activation in A549 cells. A549 cells were pretreated with PSD-A for 4 h and then stimulated with 100 nM TPA and 10 ng/mL IL-6 for 1 h. Extracts were prepared and subjected to Western blot for the expression of p-STAT3 and STAT3. (c) Cells were treated with PSD-A for 24 h, and expressions of phosphatases (STAT3-negative regulators) were determined by Western blot. PSD-A increased the expression of SHP-1 without affecting SHP-2 and PTEN. (d) Cells were treated with 25 nM PSD-A in the presence or absence of Na 3 VO 4 (100 μ M) for 24 h. Cell lysates were collected and subjected to Western blot for the expression of p-STAT3 and STAT3. Na 3 VO 4 pretreatment reversed the suppressive effect of PSD-A on STAT3 indicating that tyrosine phosphatases play an important role in PSD-A-mediated STAT3 inhibition. (e) Cells were treated with PSD-A for 4 h, and expressions of tyrosine kinases (p-SRC/SRC and p-JAK2/JAK2) were measured by Western blot. PSD-A suppressed the phosphorylation of SRC but did not affect p-JAK2 expression. (f) Cells were treated with or without PSD-A in the presence or absence of momelotininb (JAK inhibitor) and SP600125 (JNK inhibitor) for 4 h. Proteins were extracted, and expression of p-STAT3 and STAT3 was detected by Western blot. (g) Cells were treated with PSD-A (50 nM) and S31–201 (100 μ M) for 4 h, and expression of p-STAT3 was measured in cell lysates by Western blot. (h) A549 cells were incubated with or without PSD-A for 4 h and then further incubated with IL-6 for 1 h. The nuclear extracts were then collected and assayed for STAT3 DNA-binding activity according to the instructions of the kit. Columns not sharing the same superscript letters within the groups differ significantly ( P < 0.05).

Techniques Used: Activation Assay, Expressing, Western Blot, Inhibition, Incubation, Binding Assay, Activity Assay


Structured Review

Proteintech shp 1
PSD-A inhibits STAT3 signaling pathway in A549 cells. (a) PSD-A inhibits constitutive STAT3 activation at tyrosine 705. Cells were treated with PSD-A for 24 h, and expression of p-STAT3 and total STAT3 was measured using Western blot. (b) PSD-A inhibits inducible STAT3 activation in A549 cells. A549 cells were pretreated with PSD-A for 4 h and then stimulated with 100 nM TPA and 10 ng/mL IL-6 for 1 h. Extracts were prepared and subjected to Western blot for the expression of p-STAT3 and STAT3. (c) Cells were treated with PSD-A for 24 h, and expressions of phosphatases (STAT3-negative regulators) were determined by Western blot. PSD-A increased the expression of <t>SHP-1</t> without affecting SHP-2 and PTEN. (d) Cells were treated with 25 nM PSD-A in the presence or absence of Na 3 VO 4 (100 μ M) for 24 h. Cell lysates were collected and subjected to Western blot for the expression of p-STAT3 and STAT3. Na 3 VO 4 pretreatment reversed the suppressive effect of PSD-A on STAT3 indicating that tyrosine phosphatases play an important role in PSD-A-mediated STAT3 inhibition. (e) Cells were treated with PSD-A for 4 h, and expressions of tyrosine kinases (p-SRC/SRC and p-JAK2/JAK2) were measured by Western blot. PSD-A suppressed the phosphorylation of SRC but did not affect p-JAK2 expression. (f) Cells were treated with or without PSD-A in the presence or absence of momelotininb (JAK inhibitor) and SP600125 (JNK inhibitor) for 4 h. Proteins were extracted, and expression of p-STAT3 and STAT3 was detected by Western blot. (g) Cells were treated with PSD-A (50 nM) and S31–201 (100 μ M) for 4 h, and expression of p-STAT3 was measured in cell lysates by Western blot. (h) A549 cells were incubated with or without PSD-A for 4 h and then further incubated with IL-6 for 1 h. The nuclear extracts were then collected and assayed for STAT3 DNA-binding activity according to the instructions of the kit. Columns not sharing the same superscript letters within the groups differ significantly ( P < 0.05).
Shp 1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/shp 1/product/Proteintech
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
shp 1 - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Proscillaridin A Promotes Oxidative Stress and ER Stress, Inhibits STAT3 Activation, and Induces Apoptosis in A549 Lung Adenocarcinoma Cells"

Article Title: Proscillaridin A Promotes Oxidative Stress and ER Stress, Inhibits STAT3 Activation, and Induces Apoptosis in A549 Lung Adenocarcinoma Cells

Journal: Oxidative Medicine and Cellular Longevity

doi: 10.1155/2018/3853409

PSD-A inhibits STAT3 signaling pathway in A549 cells. (a) PSD-A inhibits constitutive STAT3 activation at tyrosine 705. Cells were treated with PSD-A for 24 h, and expression of p-STAT3 and total STAT3 was measured using Western blot. (b) PSD-A inhibits inducible STAT3 activation in A549 cells. A549 cells were pretreated with PSD-A for 4 h and then stimulated with 100 nM TPA and 10 ng/mL IL-6 for 1 h. Extracts were prepared and subjected to Western blot for the expression of p-STAT3 and STAT3. (c) Cells were treated with PSD-A for 24 h, and expressions of phosphatases (STAT3-negative regulators) were determined by Western blot. PSD-A increased the expression of SHP-1 without affecting SHP-2 and PTEN. (d) Cells were treated with 25 nM PSD-A in the presence or absence of Na 3 VO 4 (100 μ M) for 24 h. Cell lysates were collected and subjected to Western blot for the expression of p-STAT3 and STAT3. Na 3 VO 4 pretreatment reversed the suppressive effect of PSD-A on STAT3 indicating that tyrosine phosphatases play an important role in PSD-A-mediated STAT3 inhibition. (e) Cells were treated with PSD-A for 4 h, and expressions of tyrosine kinases (p-SRC/SRC and p-JAK2/JAK2) were measured by Western blot. PSD-A suppressed the phosphorylation of SRC but did not affect p-JAK2 expression. (f) Cells were treated with or without PSD-A in the presence or absence of momelotininb (JAK inhibitor) and SP600125 (JNK inhibitor) for 4 h. Proteins were extracted, and expression of p-STAT3 and STAT3 was detected by Western blot. (g) Cells were treated with PSD-A (50 nM) and S31–201 (100 μ M) for 4 h, and expression of p-STAT3 was measured in cell lysates by Western blot. (h) A549 cells were incubated with or without PSD-A for 4 h and then further incubated with IL-6 for 1 h. The nuclear extracts were then collected and assayed for STAT3 DNA-binding activity according to the instructions of the kit. Columns not sharing the same superscript letters within the groups differ significantly ( P < 0.05).
Figure Legend Snippet: PSD-A inhibits STAT3 signaling pathway in A549 cells. (a) PSD-A inhibits constitutive STAT3 activation at tyrosine 705. Cells were treated with PSD-A for 24 h, and expression of p-STAT3 and total STAT3 was measured using Western blot. (b) PSD-A inhibits inducible STAT3 activation in A549 cells. A549 cells were pretreated with PSD-A for 4 h and then stimulated with 100 nM TPA and 10 ng/mL IL-6 for 1 h. Extracts were prepared and subjected to Western blot for the expression of p-STAT3 and STAT3. (c) Cells were treated with PSD-A for 24 h, and expressions of phosphatases (STAT3-negative regulators) were determined by Western blot. PSD-A increased the expression of SHP-1 without affecting SHP-2 and PTEN. (d) Cells were treated with 25 nM PSD-A in the presence or absence of Na 3 VO 4 (100 μ M) for 24 h. Cell lysates were collected and subjected to Western blot for the expression of p-STAT3 and STAT3. Na 3 VO 4 pretreatment reversed the suppressive effect of PSD-A on STAT3 indicating that tyrosine phosphatases play an important role in PSD-A-mediated STAT3 inhibition. (e) Cells were treated with PSD-A for 4 h, and expressions of tyrosine kinases (p-SRC/SRC and p-JAK2/JAK2) were measured by Western blot. PSD-A suppressed the phosphorylation of SRC but did not affect p-JAK2 expression. (f) Cells were treated with or without PSD-A in the presence or absence of momelotininb (JAK inhibitor) and SP600125 (JNK inhibitor) for 4 h. Proteins were extracted, and expression of p-STAT3 and STAT3 was detected by Western blot. (g) Cells were treated with PSD-A (50 nM) and S31–201 (100 μ M) for 4 h, and expression of p-STAT3 was measured in cell lysates by Western blot. (h) A549 cells were incubated with or without PSD-A for 4 h and then further incubated with IL-6 for 1 h. The nuclear extracts were then collected and assayed for STAT3 DNA-binding activity according to the instructions of the kit. Columns not sharing the same superscript letters within the groups differ significantly ( P < 0.05).

Techniques Used: Activation Assay, Expressing, Western Blot, Inhibition, Incubation, Binding Assay, Activity Assay


Structured Review

Proteintech shp 1
<t>SHP-1,</t> STAT3, MCL1, and VEGF were regulated by TMEFF2. Protein expression levels of SHP-1, STAT3 and p-STAT3 were measured by Western blot in ASPC1 pancreatic cancer cells ( A ) and CAPAN1 pancreatic cancer cells ( B ), which overexpressed TMEFF2. The mRNA and protein expression level of MCL1 and VEGF were measured by real-time polymerase chain reaction (RT-PCR) and Western blot in ASPC1 pancreatic cancer cells ( C, D ), and CAPAN1 pancreatic cancer cells ( E, F ), which overexpressed TMEFF2. Control, original ASPC1 or CAPAN1 pancreatic cancer cells; vector, cells transduced with lentivirus containing control vector; TMEFF2, cells transduced with lentivirus expressing TMEFF2. *** P<0.001 vs. control.
Shp 1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/shp 1/product/Proteintech
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
shp 1 - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Expression of TMEFF2 in Human Pancreatic Cancer Tissue and the Effects of TMEFF2 Knockdown on Cell, Proliferation, and Apoptosis in Human Pancreatic Cell Lines"

Article Title: Expression of TMEFF2 in Human Pancreatic Cancer Tissue and the Effects of TMEFF2 Knockdown on Cell, Proliferation, and Apoptosis in Human Pancreatic Cell Lines

Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

doi: 10.12659/MSM.913974

SHP-1, STAT3, MCL1, and VEGF were regulated by TMEFF2. Protein expression levels of SHP-1, STAT3 and p-STAT3 were measured by Western blot in ASPC1 pancreatic cancer cells ( A ) and CAPAN1 pancreatic cancer cells ( B ), which overexpressed TMEFF2. The mRNA and protein expression level of MCL1 and VEGF were measured by real-time polymerase chain reaction (RT-PCR) and Western blot in ASPC1 pancreatic cancer cells ( C, D ), and CAPAN1 pancreatic cancer cells ( E, F ), which overexpressed TMEFF2. Control, original ASPC1 or CAPAN1 pancreatic cancer cells; vector, cells transduced with lentivirus containing control vector; TMEFF2, cells transduced with lentivirus expressing TMEFF2. *** P<0.001 vs. control.
Figure Legend Snippet: SHP-1, STAT3, MCL1, and VEGF were regulated by TMEFF2. Protein expression levels of SHP-1, STAT3 and p-STAT3 were measured by Western blot in ASPC1 pancreatic cancer cells ( A ) and CAPAN1 pancreatic cancer cells ( B ), which overexpressed TMEFF2. The mRNA and protein expression level of MCL1 and VEGF were measured by real-time polymerase chain reaction (RT-PCR) and Western blot in ASPC1 pancreatic cancer cells ( C, D ), and CAPAN1 pancreatic cancer cells ( E, F ), which overexpressed TMEFF2. Control, original ASPC1 or CAPAN1 pancreatic cancer cells; vector, cells transduced with lentivirus containing control vector; TMEFF2, cells transduced with lentivirus expressing TMEFF2. *** P<0.001 vs. control.

Techniques Used: Expressing, Western Blot, Real-time Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Plasmid Preparation, Transduction

TMEFF2 regulated STAT3 via SHP-1. ( A ) The interactions between TMEFF2 and SHP-1 were measured using a co-immunoprecipitation assay. The mRNA ( B ) and protein ( C ) expression level of TMEFF2 were measured in BXPC3 pancreatic cancer cells after transfection with lentivirus containing short-hairpin RNAs (shRNAs) (siTMEFF2-1, −2 and −3) or control shRNA (siNC). The efficiency of SHP-1 overexpression was measured by real-time polymerase chain reaction (RT-PCR) ( D ) and Western blot ( E ) in BXPC3 pancreatic cancer cells, and ( F ) shows the protein expression level of SHP-1, STAT3, and p-STAT3 measured in BXPC3 pancreatic cancer cells transfected by control shRNA together with control vector (siNC + vector), lentivirus expressing siTMEFF2-2 (siTMEFF2), SHP-1 overexpression vector (SHP-1) and siTMEFF2-2 lentivirus with SHP-1 overexpression vector (siTMEFF2 + SHP-1). *** P<0.001 vs. control or siNC + vector; ### P<0.001 vs. siTMEFF2; +++ P<0.001 vs. SHP-1.
Figure Legend Snippet: TMEFF2 regulated STAT3 via SHP-1. ( A ) The interactions between TMEFF2 and SHP-1 were measured using a co-immunoprecipitation assay. The mRNA ( B ) and protein ( C ) expression level of TMEFF2 were measured in BXPC3 pancreatic cancer cells after transfection with lentivirus containing short-hairpin RNAs (shRNAs) (siTMEFF2-1, −2 and −3) or control shRNA (siNC). The efficiency of SHP-1 overexpression was measured by real-time polymerase chain reaction (RT-PCR) ( D ) and Western blot ( E ) in BXPC3 pancreatic cancer cells, and ( F ) shows the protein expression level of SHP-1, STAT3, and p-STAT3 measured in BXPC3 pancreatic cancer cells transfected by control shRNA together with control vector (siNC + vector), lentivirus expressing siTMEFF2-2 (siTMEFF2), SHP-1 overexpression vector (SHP-1) and siTMEFF2-2 lentivirus with SHP-1 overexpression vector (siTMEFF2 + SHP-1). *** P<0.001 vs. control or siNC + vector; ### P<0.001 vs. siTMEFF2; +++ P<0.001 vs. SHP-1.

Techniques Used: Co-Immunoprecipitation Assay, Expressing, Transfection, shRNA, Over Expression, Real-time Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Western Blot, Plasmid Preparation

Effects of TMEFF2 knockdown and SHP-1 overexpression. ( A ) mRNA and ( B ) protein expression level of MCL1 and VEGF followed by ( C ) cell proliferation and ( D ) cell apoptosis were analyzed in BXPC3 cells, which were transfected with control shRNA together with control vector (siNC + vector), lentivirus expressing siTMEFF2-2 (siTMEFF2), SHP-1 overexpression vector (SHP-1) and siTMEFF2-2 lentivirus together with SHP-1 overexpression vector (siTMEFF2 + SHP-1). *** P<0.001 vs. control or siNC + vector; ### P<0.001 vs. siTMEFF2; +++ P<0.001 vs. SHP-1.
Figure Legend Snippet: Effects of TMEFF2 knockdown and SHP-1 overexpression. ( A ) mRNA and ( B ) protein expression level of MCL1 and VEGF followed by ( C ) cell proliferation and ( D ) cell apoptosis were analyzed in BXPC3 cells, which were transfected with control shRNA together with control vector (siNC + vector), lentivirus expressing siTMEFF2-2 (siTMEFF2), SHP-1 overexpression vector (SHP-1) and siTMEFF2-2 lentivirus together with SHP-1 overexpression vector (siTMEFF2 + SHP-1). *** P<0.001 vs. control or siNC + vector; ### P<0.001 vs. siTMEFF2; +++ P<0.001 vs. SHP-1.

Techniques Used: Over Expression, Expressing, Transfection, shRNA, Plasmid Preparation


Structured Review

Proteintech shp 2
PSN-A modulates Bcl-2 family proteins and inhibits STAT3 signaling. (A) LNCaP and DU145 cells were treated with 0, 25 and 50 nM PSN-A for 24 h. Total proteins were extracted and subjected to immunobloting for the expressions of Bax, Bcl-2, cleaved caspases-3 and PARP-1. β-actin was used as loading control. (B) LNCaP and DU145 cells were treated with 0, 25 and 50 nM PSN-A for 24 h. Total cell lysates were extracted and subjected to Western blot for the expressions of SHP-1, <t>SHP-2,</t> PTEN, p-Jak2, Jak2, p-STAT3 and STAT3. β-actin was used as loading control.
Shp 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/shp 2/product/Proteintech
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
shp 2 - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Proscillaridin A induces apoptosis, inhibits STAT3 activation and augments doxorubicin toxicity in prostate cancer cells"

Article Title: Proscillaridin A induces apoptosis, inhibits STAT3 activation and augments doxorubicin toxicity in prostate cancer cells

Journal: International Journal of Medical Sciences

doi: 10.7150/ijms.23270

PSN-A modulates Bcl-2 family proteins and inhibits STAT3 signaling. (A) LNCaP and DU145 cells were treated with 0, 25 and 50 nM PSN-A for 24 h. Total proteins were extracted and subjected to immunobloting for the expressions of Bax, Bcl-2, cleaved caspases-3 and PARP-1. β-actin was used as loading control. (B) LNCaP and DU145 cells were treated with 0, 25 and 50 nM PSN-A for 24 h. Total cell lysates were extracted and subjected to Western blot for the expressions of SHP-1, SHP-2, PTEN, p-Jak2, Jak2, p-STAT3 and STAT3. β-actin was used as loading control.
Figure Legend Snippet: PSN-A modulates Bcl-2 family proteins and inhibits STAT3 signaling. (A) LNCaP and DU145 cells were treated with 0, 25 and 50 nM PSN-A for 24 h. Total proteins were extracted and subjected to immunobloting for the expressions of Bax, Bcl-2, cleaved caspases-3 and PARP-1. β-actin was used as loading control. (B) LNCaP and DU145 cells were treated with 0, 25 and 50 nM PSN-A for 24 h. Total cell lysates were extracted and subjected to Western blot for the expressions of SHP-1, SHP-2, PTEN, p-Jak2, Jak2, p-STAT3 and STAT3. β-actin was used as loading control.

Techniques Used: Western Blot


Structured Review

Proteintech rabbit antibody against shp 2
D1R interacts with <t>Shp-2</t> in the striatal neurons. Notes: Striatal proteins were coimmunoprecipitated with anti-D1R and anti-Shp-2 antibodies ( A and B ). Representative immunoblots showing D1R and Shp-2 interactions in striatal neurons as detected by coimmunoprecipitation. No precipitating antibody, an irrelevant IgG was used in L2, L3, respectively. The D1R antibody (L4A) or Shp-2 antibody (L4B) was used in L4 for normal rats and L5 for LID rats, respectively. No striatal proteins and antibodies were used in L1. Abbreviations: IP, immunoprecipitation; D1R, D1 dopamine receptor; L1, lane 1; L2, lane 2; L3, lane 3; L4, lane 4; L5, lane 5; LID, levodopa-induced dyskinesia.
Rabbit Antibody Against Shp 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit antibody against shp 2/product/Proteintech
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
rabbit antibody against shp 2 - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "The abnormal activation of D1R/Shp-2 complex involved in levodopa-induced dyskinesia in 6-hydroxydopamine-lesioned Parkinson’s rats"

Article Title: The abnormal activation of D1R/Shp-2 complex involved in levodopa-induced dyskinesia in 6-hydroxydopamine-lesioned Parkinson’s rats

Journal: Neuropsychiatric Disease and Treatment

doi: 10.2147/NDT.S162562

D1R interacts with Shp-2 in the striatal neurons. Notes: Striatal proteins were coimmunoprecipitated with anti-D1R and anti-Shp-2 antibodies ( A and B ). Representative immunoblots showing D1R and Shp-2 interactions in striatal neurons as detected by coimmunoprecipitation. No precipitating antibody, an irrelevant IgG was used in L2, L3, respectively. The D1R antibody (L4A) or Shp-2 antibody (L4B) was used in L4 for normal rats and L5 for LID rats, respectively. No striatal proteins and antibodies were used in L1. Abbreviations: IP, immunoprecipitation; D1R, D1 dopamine receptor; L1, lane 1; L2, lane 2; L3, lane 3; L4, lane 4; L5, lane 5; LID, levodopa-induced dyskinesia.
Figure Legend Snippet: D1R interacts with Shp-2 in the striatal neurons. Notes: Striatal proteins were coimmunoprecipitated with anti-D1R and anti-Shp-2 antibodies ( A and B ). Representative immunoblots showing D1R and Shp-2 interactions in striatal neurons as detected by coimmunoprecipitation. No precipitating antibody, an irrelevant IgG was used in L2, L3, respectively. The D1R antibody (L4A) or Shp-2 antibody (L4B) was used in L4 for normal rats and L5 for LID rats, respectively. No striatal proteins and antibodies were used in L1. Abbreviations: IP, immunoprecipitation; D1R, D1 dopamine receptor; L1, lane 1; L2, lane 2; L3, lane 3; L4, lane 4; L5, lane 5; LID, levodopa-induced dyskinesia.

Techniques Used: Western Blot, Immunoprecipitation

Molecular events underlying LID involving D1R/Shp-2 complex and its downstream signaling factors, such as ERK1/2 and mTOR. Notes: The bands represent immunoblot images detected by antibodies against p-Shp-2 ( A ), p-ERK ( B ) and p-mTOR ( C ). Proteins were analyzed from the sham group (1), l -DOPA group (2), SCH23390 + l -DOPA group (3), SKF38393 group (4). Repeated administration of l -DOPA increased the level of p-Shp-2, p-ERK1/2 and p-mTOR. SKF38393 increased the levels similarly. Conversely, SCH23390 plus L-DOPA prevented the increase. Data are presented as mean ± SD. * p < 0.05, versus sham group; # p < 0.05, versus l -DOPA group. Data are statistically analyzed by one-way ANOVA test. Abbreviations: ANOVA, analysis of variance; D1R, D1 dopamine receptor; ERK1/2, extracellular signal-regulated kinases 1 and 2; l -DOPA, l -3,4-dihydroxyphenylalanine; LID, levodopa-induced dyskinesia.
Figure Legend Snippet: Molecular events underlying LID involving D1R/Shp-2 complex and its downstream signaling factors, such as ERK1/2 and mTOR. Notes: The bands represent immunoblot images detected by antibodies against p-Shp-2 ( A ), p-ERK ( B ) and p-mTOR ( C ). Proteins were analyzed from the sham group (1), l -DOPA group (2), SCH23390 + l -DOPA group (3), SKF38393 group (4). Repeated administration of l -DOPA increased the level of p-Shp-2, p-ERK1/2 and p-mTOR. SKF38393 increased the levels similarly. Conversely, SCH23390 plus L-DOPA prevented the increase. Data are presented as mean ± SD. * p < 0.05, versus sham group; # p < 0.05, versus l -DOPA group. Data are statistically analyzed by one-way ANOVA test. Abbreviations: ANOVA, analysis of variance; D1R, D1 dopamine receptor; ERK1/2, extracellular signal-regulated kinases 1 and 2; l -DOPA, l -3,4-dihydroxyphenylalanine; LID, levodopa-induced dyskinesia.

Techniques Used: Western Blot


Structured Review

Proteintech shp 2
In human dNK cells, the <t>2B4/SHP-2/p-P38</t> pathway is involved in 2B4-induced downregulation of TNF-α and IFN-γ after T. gondii infection. A Some inhibitors may induce cell death, so 7-AAD was used to exclude the effect of SHP-2 inhibitor and Fyn inhibitor on dNK cells. B SHP-2 expression in uninfected and infected dNK cells was assessed by PCR (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test). C SHP-2, p-SHP-2, and Fyn expression in uninfected and infected dNK cells as assessed by Western blot (data are presented as the mean ± SD, n = 3, * P < 0.05, ** P < 0.01, by the paired t -test). D Expression of SHP-2, Fyn, p-ERK, p-P38, and 2B4 in infected dNK cells with or without anti-2B4 antibody as assessed by Western blot. E Expression of p-P38, p-ERK, TNF-α, IFN-γ, and 2B4 in the infected group with or without anti-2B4 antibody (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test). F Levels of p-2B4, p-P38, p-ERK, TNF-α, and IFN-γ in the infected group with or without SHP-2 inhibitor treatment. G Expression of SHP-2, p-P38, p-ERK, TNF-α, and IFN-γ in uninfected, infected, infected and treated with a 2B4 antibody groups, and infected with 2B4 antibody and SHP-2 inhibitor groups. H Analysis for Fig. 6g (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test). I Input for SHP-2, 2B4, p-P38, IFN-γ, and TNF-α when we used SHP-2 antibody to pull down 2B4 and p-P38. j 2B4 and p-P38 were synchronously immunoprecipitated by SHP-2 antibody
Shp 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/shp 2/product/Proteintech
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
shp 2 - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "A novel 2B4 receptor leads to worse pregnancy outcomes by facilitating TNF-α and IFN-γ production in dNK cells during Toxoplasma gondii infection"

Article Title: A novel 2B4 receptor leads to worse pregnancy outcomes by facilitating TNF-α and IFN-γ production in dNK cells during Toxoplasma gondii infection

Journal: Parasites & Vectors

doi: 10.1186/s13071-022-05455-9

In human dNK cells, the 2B4/SHP-2/p-P38 pathway is involved in 2B4-induced downregulation of TNF-α and IFN-γ after T. gondii infection. A Some inhibitors may induce cell death, so 7-AAD was used to exclude the effect of SHP-2 inhibitor and Fyn inhibitor on dNK cells. B SHP-2 expression in uninfected and infected dNK cells was assessed by PCR (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test). C SHP-2, p-SHP-2, and Fyn expression in uninfected and infected dNK cells as assessed by Western blot (data are presented as the mean ± SD, n = 3, * P < 0.05, ** P < 0.01, by the paired t -test). D Expression of SHP-2, Fyn, p-ERK, p-P38, and 2B4 in infected dNK cells with or without anti-2B4 antibody as assessed by Western blot. E Expression of p-P38, p-ERK, TNF-α, IFN-γ, and 2B4 in the infected group with or without anti-2B4 antibody (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test). F Levels of p-2B4, p-P38, p-ERK, TNF-α, and IFN-γ in the infected group with or without SHP-2 inhibitor treatment. G Expression of SHP-2, p-P38, p-ERK, TNF-α, and IFN-γ in uninfected, infected, infected and treated with a 2B4 antibody groups, and infected with 2B4 antibody and SHP-2 inhibitor groups. H Analysis for Fig. 6g (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test). I Input for SHP-2, 2B4, p-P38, IFN-γ, and TNF-α when we used SHP-2 antibody to pull down 2B4 and p-P38. j 2B4 and p-P38 were synchronously immunoprecipitated by SHP-2 antibody
Figure Legend Snippet: In human dNK cells, the 2B4/SHP-2/p-P38 pathway is involved in 2B4-induced downregulation of TNF-α and IFN-γ after T. gondii infection. A Some inhibitors may induce cell death, so 7-AAD was used to exclude the effect of SHP-2 inhibitor and Fyn inhibitor on dNK cells. B SHP-2 expression in uninfected and infected dNK cells was assessed by PCR (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test). C SHP-2, p-SHP-2, and Fyn expression in uninfected and infected dNK cells as assessed by Western blot (data are presented as the mean ± SD, n = 3, * P < 0.05, ** P < 0.01, by the paired t -test). D Expression of SHP-2, Fyn, p-ERK, p-P38, and 2B4 in infected dNK cells with or without anti-2B4 antibody as assessed by Western blot. E Expression of p-P38, p-ERK, TNF-α, IFN-γ, and 2B4 in the infected group with or without anti-2B4 antibody (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test). F Levels of p-2B4, p-P38, p-ERK, TNF-α, and IFN-γ in the infected group with or without SHP-2 inhibitor treatment. G Expression of SHP-2, p-P38, p-ERK, TNF-α, and IFN-γ in uninfected, infected, infected and treated with a 2B4 antibody groups, and infected with 2B4 antibody and SHP-2 inhibitor groups. H Analysis for Fig. 6g (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test). I Input for SHP-2, 2B4, p-P38, IFN-γ, and TNF-α when we used SHP-2 antibody to pull down 2B4 and p-P38. j 2B4 and p-P38 were synchronously immunoprecipitated by SHP-2 antibody

Techniques Used: Infection, Expressing, Western Blot, Immunoprecipitation

In human dNK cells, the 2B4/Fyn/p-ERK pathway is involved in 2B4-induced downregulation of TNF-α and IFN-γ after T. gondii infection. A Fyn, p-ERK, TNF-α, p-P38, and IFN-γ expression in the infected group with or without Fyn inhibitor treatment. B Expression of p-ERK, TNF-α, p-P38, and IFN-γ in the infected group, infected group treated with the 2B4 antibody, and the infected group treated with both anti-2B4 antibody and the Fyn inhibitor. C Analysis for Fig. 7b (data are presented as the mean ± SD, n = 3, ** P < 0.01, * P < 0.05, by the paired t -test). D Input for Fyn, p-ERK, 2B4, IFN-γ, and TNF-α when we used Fyn to bind 2B4 and p-ERK. E 2B4 and p-ERK were synchronously immunoprecipitated by Fyn antibody. F Input for 2B4, SHP-2, Fyn, TNF-α, and IFN-γ when we used 2B4 to bind to SHP-2 or Fyn. G SHP-2 and Fyn were synchronously immunoprecipitated by 2B4 antibody. H Expression of TNF-α and IFN-γ in infected dNK cells with or without p-ERK inhibitor or p-P38 inhibitor, respectively. I Analysis of Fig. 7h (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test)
Figure Legend Snippet: In human dNK cells, the 2B4/Fyn/p-ERK pathway is involved in 2B4-induced downregulation of TNF-α and IFN-γ after T. gondii infection. A Fyn, p-ERK, TNF-α, p-P38, and IFN-γ expression in the infected group with or without Fyn inhibitor treatment. B Expression of p-ERK, TNF-α, p-P38, and IFN-γ in the infected group, infected group treated with the 2B4 antibody, and the infected group treated with both anti-2B4 antibody and the Fyn inhibitor. C Analysis for Fig. 7b (data are presented as the mean ± SD, n = 3, ** P < 0.01, * P < 0.05, by the paired t -test). D Input for Fyn, p-ERK, 2B4, IFN-γ, and TNF-α when we used Fyn to bind 2B4 and p-ERK. E 2B4 and p-ERK were synchronously immunoprecipitated by Fyn antibody. F Input for 2B4, SHP-2, Fyn, TNF-α, and IFN-γ when we used 2B4 to bind to SHP-2 or Fyn. G SHP-2 and Fyn were synchronously immunoprecipitated by 2B4 antibody. H Expression of TNF-α and IFN-γ in infected dNK cells with or without p-ERK inhibitor or p-P38 inhibitor, respectively. I Analysis of Fig. 7h (data are presented as the mean ± SD, n = 3, * P < 0.05, by the paired t -test)

Techniques Used: Infection, Expressing, Immunoprecipitation

Working model for the roles of 2B4 in dNK cells following T. gondii infection. A In summary, the expressions of 2B4, SHP-2, p-SHP-2, Fyn, p-ERK, p-P38, TNF-α, and IFN-γ were found in T. gondii -infected dNK cells relative to uninfected dNK cells. B After 2B4 cross-linking, activation of 2B4 can downregulate TNF-α and IFN-γ expression by activating the 2B4/SHP-2/p-P38 pathway and inhibiting the 2B4/Fyn/p-ERK pathway following T. gondii infection
Figure Legend Snippet: Working model for the roles of 2B4 in dNK cells following T. gondii infection. A In summary, the expressions of 2B4, SHP-2, p-SHP-2, Fyn, p-ERK, p-P38, TNF-α, and IFN-γ were found in T. gondii -infected dNK cells relative to uninfected dNK cells. B After 2B4 cross-linking, activation of 2B4 can downregulate TNF-α and IFN-γ expression by activating the 2B4/SHP-2/p-P38 pathway and inhibiting the 2B4/Fyn/p-ERK pathway following T. gondii infection

Techniques Used: Infection, Activation Assay, Expressing


Structured Review

Proteintech anti shp 1
<t>SHP-1,</t> c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.
Anti Shp 1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti shp 1/product/Proteintech
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
anti shp 1 - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Src-homology domain 2 containing protein tyrosine phosphatase-1 (SHP-1) directly binds to proto-oncogene tyrosine-protein kinase Src (c-Src) and promotes the transcriptional activation of connexin 43 (Cx43)"

Article Title: Src-homology domain 2 containing protein tyrosine phosphatase-1 (SHP-1) directly binds to proto-oncogene tyrosine-protein kinase Src (c-Src) and promotes the transcriptional activation of connexin 43 (Cx43)

Journal: Bioengineered

doi: 10.1080/21655979.2022.2079252

SHP-1, c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.
Figure Legend Snippet: SHP-1, c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.

Techniques Used: Expressing, Over Expression, Western Blot, Transfection, Plasmid Preparation

The protein expression after overexpression of SHP-1 was detected by immunofluorescence. (a) The microscopy images of SHP-1, p-c-Src, and Cx43 stained in HL-1 cells were photographed under a fluorescence microscope. (b) The average fluorescence intensity was calculated. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01. Scale bar: 50 μm.
Figure Legend Snippet: The protein expression after overexpression of SHP-1 was detected by immunofluorescence. (a) The microscopy images of SHP-1, p-c-Src, and Cx43 stained in HL-1 cells were photographed under a fluorescence microscope. (b) The average fluorescence intensity was calculated. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01. Scale bar: 50 μm.

Techniques Used: Expressing, Over Expression, Immunofluorescence, Microscopy, Staining, Fluorescence, Transfection, Plasmid Preparation

SHP-1 is directly combined with c-Src. (a) The immunofluorescence co-localization of SHP-1 and c-Src protein in HL-1 cells. Scale bar: 50 μm. (b) Co-IP test was performed with SHP-1 antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input. (c) Co-IP test was performed with c-Src antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input.
Figure Legend Snippet: SHP-1 is directly combined with c-Src. (a) The immunofluorescence co-localization of SHP-1 and c-Src protein in HL-1 cells. Scale bar: 50 μm. (b) Co-IP test was performed with SHP-1 antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input. (c) Co-IP test was performed with c-Src antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input.

Techniques Used: Immunofluorescence, Co-Immunoprecipitation Assay


Structured Review

Proteintech anti shp 1
<t>SHP-1,</t> c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.
Anti Shp 1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti shp 1/product/Proteintech
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
anti shp 1 - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Src-homology domain 2 containing protein tyrosine phosphatase-1 (SHP-1) directly binds to proto-oncogene tyrosine-protein kinase Src (c-Src) and promotes the transcriptional activation of connexin 43 (Cx43)"

Article Title: Src-homology domain 2 containing protein tyrosine phosphatase-1 (SHP-1) directly binds to proto-oncogene tyrosine-protein kinase Src (c-Src) and promotes the transcriptional activation of connexin 43 (Cx43)

Journal: Bioengineered

doi: 10.1080/21655979.2022.2079252

SHP-1, c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.
Figure Legend Snippet: SHP-1, c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.

Techniques Used: Expressing, Over Expression, Western Blot, Transfection, Plasmid Preparation

The protein expression after overexpression of SHP-1 was detected by immunofluorescence. (a) The microscopy images of SHP-1, p-c-Src, and Cx43 stained in HL-1 cells were photographed under a fluorescence microscope. (b) The average fluorescence intensity was calculated. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01. Scale bar: 50 μm.
Figure Legend Snippet: The protein expression after overexpression of SHP-1 was detected by immunofluorescence. (a) The microscopy images of SHP-1, p-c-Src, and Cx43 stained in HL-1 cells were photographed under a fluorescence microscope. (b) The average fluorescence intensity was calculated. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01. Scale bar: 50 μm.

Techniques Used: Expressing, Over Expression, Immunofluorescence, Microscopy, Staining, Fluorescence, Transfection, Plasmid Preparation

SHP-1 is directly combined with c-Src. (a) The immunofluorescence co-localization of SHP-1 and c-Src protein in HL-1 cells. Scale bar: 50 μm. (b) Co-IP test was performed with SHP-1 antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input. (c) Co-IP test was performed with c-Src antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input.
Figure Legend Snippet: SHP-1 is directly combined with c-Src. (a) The immunofluorescence co-localization of SHP-1 and c-Src protein in HL-1 cells. Scale bar: 50 μm. (b) Co-IP test was performed with SHP-1 antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input. (c) Co-IP test was performed with c-Src antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input.

Techniques Used: Immunofluorescence, Co-Immunoprecipitation Assay


Structured Review

Proteintech shp 1
<t>SHP-1,</t> c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.
Shp 1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/shp 1/product/Proteintech
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
shp 1 - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Src-homology domain 2 containing protein tyrosine phosphatase-1 (SHP-1) directly binds to proto-oncogene tyrosine-protein kinase Src (c-Src) and promotes the transcriptional activation of connexin 43 (Cx43)"

Article Title: Src-homology domain 2 containing protein tyrosine phosphatase-1 (SHP-1) directly binds to proto-oncogene tyrosine-protein kinase Src (c-Src) and promotes the transcriptional activation of connexin 43 (Cx43)

Journal: Bioengineered

doi: 10.1080/21655979.2022.2079252

SHP-1, c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.
Figure Legend Snippet: SHP-1, c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.

Techniques Used: Expressing, Over Expression, Western Blot, Transfection, Plasmid Preparation

The protein expression after overexpression of SHP-1 was detected by immunofluorescence. (a) The microscopy images of SHP-1, p-c-Src, and Cx43 stained in HL-1 cells were photographed under a fluorescence microscope. (b) The average fluorescence intensity was calculated. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01. Scale bar: 50 μm.
Figure Legend Snippet: The protein expression after overexpression of SHP-1 was detected by immunofluorescence. (a) The microscopy images of SHP-1, p-c-Src, and Cx43 stained in HL-1 cells were photographed under a fluorescence microscope. (b) The average fluorescence intensity was calculated. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01. Scale bar: 50 μm.

Techniques Used: Expressing, Over Expression, Immunofluorescence, Microscopy, Staining, Fluorescence, Transfection, Plasmid Preparation

SHP-1 is directly combined with c-Src. (a) The immunofluorescence co-localization of SHP-1 and c-Src protein in HL-1 cells. Scale bar: 50 μm. (b) Co-IP test was performed with SHP-1 antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input. (c) Co-IP test was performed with c-Src antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input.
Figure Legend Snippet: SHP-1 is directly combined with c-Src. (a) The immunofluorescence co-localization of SHP-1 and c-Src protein in HL-1 cells. Scale bar: 50 μm. (b) Co-IP test was performed with SHP-1 antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input. (c) Co-IP test was performed with c-Src antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input.

Techniques Used: Immunofluorescence, Co-Immunoprecipitation Assay

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86
    Proteintech shp 1
    Shp 1, supplied by Proteintech, 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/shp 1/product/Proteintech
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    shp 1 - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    93
    Proteintech shp 2
    PSD-A inhibits STAT3 signaling pathway in A549 cells. (a) PSD-A inhibits constitutive STAT3 activation at tyrosine 705. Cells were treated with PSD-A for 24 h, and expression of p-STAT3 and total STAT3 was measured using Western blot. (b) PSD-A inhibits inducible STAT3 activation in A549 cells. A549 cells were pretreated with PSD-A for 4 h and then stimulated with 100 nM TPA and 10 ng/mL IL-6 for 1 h. Extracts were prepared and subjected to Western blot for the expression of p-STAT3 and STAT3. (c) Cells were treated with PSD-A for 24 h, and expressions of phosphatases (STAT3-negative regulators) were determined by Western blot. PSD-A increased the expression of SHP-1 without affecting <t>SHP-2</t> and PTEN. (d) Cells were treated with 25 nM PSD-A in the presence or absence of Na 3 VO 4 (100 μ M) for 24 h. Cell lysates were collected and subjected to Western blot for the expression of p-STAT3 and STAT3. Na 3 VO 4 pretreatment reversed the suppressive effect of PSD-A on STAT3 indicating that tyrosine phosphatases play an important role in PSD-A-mediated STAT3 inhibition. (e) Cells were treated with PSD-A for 4 h, and expressions of tyrosine kinases (p-SRC/SRC and p-JAK2/JAK2) were measured by Western blot. PSD-A suppressed the phosphorylation of SRC but did not affect p-JAK2 expression. (f) Cells were treated with or without PSD-A in the presence or absence of momelotininb (JAK inhibitor) and SP600125 (JNK inhibitor) for 4 h. Proteins were extracted, and expression of p-STAT3 and STAT3 was detected by Western blot. (g) Cells were treated with PSD-A (50 nM) and S31–201 (100 μ M) for 4 h, and expression of p-STAT3 was measured in cell lysates by Western blot. (h) A549 cells were incubated with or without PSD-A for 4 h and then further incubated with IL-6 for 1 h. The nuclear extracts were then collected and assayed for STAT3 DNA-binding activity according to the instructions of the kit. Columns not sharing the same superscript letters within the groups differ significantly ( P < 0.05).
    Shp 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/shp 2/product/Proteintech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    shp 2 - by Bioz Stars, 2024-07
    93/100 stars
      Buy from Supplier

    93
    Proteintech rabbit antibody against shp 2
    D1R interacts with <t>Shp-2</t> in the striatal neurons. Notes: Striatal proteins were coimmunoprecipitated with anti-D1R and anti-Shp-2 antibodies ( A and B ). Representative immunoblots showing D1R and Shp-2 interactions in striatal neurons as detected by coimmunoprecipitation. No precipitating antibody, an irrelevant IgG was used in L2, L3, respectively. The D1R antibody (L4A) or Shp-2 antibody (L4B) was used in L4 for normal rats and L5 for LID rats, respectively. No striatal proteins and antibodies were used in L1. Abbreviations: IP, immunoprecipitation; D1R, D1 dopamine receptor; L1, lane 1; L2, lane 2; L3, lane 3; L4, lane 4; L5, lane 5; LID, levodopa-induced dyskinesia.
    Rabbit Antibody Against Shp 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit antibody against shp 2/product/Proteintech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit antibody against shp 2 - by Bioz Stars, 2024-07
    93/100 stars
      Buy from Supplier

    93
    Proteintech anti shp 1
    <t>SHP-1,</t> c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.
    Anti Shp 1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti shp 1/product/Proteintech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti shp 1 - by Bioz Stars, 2024-07
    93/100 stars
      Buy from Supplier

    Image Search Results


    PSD-A inhibits STAT3 signaling pathway in A549 cells. (a) PSD-A inhibits constitutive STAT3 activation at tyrosine 705. Cells were treated with PSD-A for 24 h, and expression of p-STAT3 and total STAT3 was measured using Western blot. (b) PSD-A inhibits inducible STAT3 activation in A549 cells. A549 cells were pretreated with PSD-A for 4 h and then stimulated with 100 nM TPA and 10 ng/mL IL-6 for 1 h. Extracts were prepared and subjected to Western blot for the expression of p-STAT3 and STAT3. (c) Cells were treated with PSD-A for 24 h, and expressions of phosphatases (STAT3-negative regulators) were determined by Western blot. PSD-A increased the expression of SHP-1 without affecting SHP-2 and PTEN. (d) Cells were treated with 25 nM PSD-A in the presence or absence of Na 3 VO 4 (100 μ M) for 24 h. Cell lysates were collected and subjected to Western blot for the expression of p-STAT3 and STAT3. Na 3 VO 4 pretreatment reversed the suppressive effect of PSD-A on STAT3 indicating that tyrosine phosphatases play an important role in PSD-A-mediated STAT3 inhibition. (e) Cells were treated with PSD-A for 4 h, and expressions of tyrosine kinases (p-SRC/SRC and p-JAK2/JAK2) were measured by Western blot. PSD-A suppressed the phosphorylation of SRC but did not affect p-JAK2 expression. (f) Cells were treated with or without PSD-A in the presence or absence of momelotininb (JAK inhibitor) and SP600125 (JNK inhibitor) for 4 h. Proteins were extracted, and expression of p-STAT3 and STAT3 was detected by Western blot. (g) Cells were treated with PSD-A (50 nM) and S31–201 (100 μ M) for 4 h, and expression of p-STAT3 was measured in cell lysates by Western blot. (h) A549 cells were incubated with or without PSD-A for 4 h and then further incubated with IL-6 for 1 h. The nuclear extracts were then collected and assayed for STAT3 DNA-binding activity according to the instructions of the kit. Columns not sharing the same superscript letters within the groups differ significantly ( P < 0.05).

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Proscillaridin A Promotes Oxidative Stress and ER Stress, Inhibits STAT3 Activation, and Induces Apoptosis in A549 Lung Adenocarcinoma Cells

    doi: 10.1155/2018/3853409

    Figure Lengend Snippet: PSD-A inhibits STAT3 signaling pathway in A549 cells. (a) PSD-A inhibits constitutive STAT3 activation at tyrosine 705. Cells were treated with PSD-A for 24 h, and expression of p-STAT3 and total STAT3 was measured using Western blot. (b) PSD-A inhibits inducible STAT3 activation in A549 cells. A549 cells were pretreated with PSD-A for 4 h and then stimulated with 100 nM TPA and 10 ng/mL IL-6 for 1 h. Extracts were prepared and subjected to Western blot for the expression of p-STAT3 and STAT3. (c) Cells were treated with PSD-A for 24 h, and expressions of phosphatases (STAT3-negative regulators) were determined by Western blot. PSD-A increased the expression of SHP-1 without affecting SHP-2 and PTEN. (d) Cells were treated with 25 nM PSD-A in the presence or absence of Na 3 VO 4 (100 μ M) for 24 h. Cell lysates were collected and subjected to Western blot for the expression of p-STAT3 and STAT3. Na 3 VO 4 pretreatment reversed the suppressive effect of PSD-A on STAT3 indicating that tyrosine phosphatases play an important role in PSD-A-mediated STAT3 inhibition. (e) Cells were treated with PSD-A for 4 h, and expressions of tyrosine kinases (p-SRC/SRC and p-JAK2/JAK2) were measured by Western blot. PSD-A suppressed the phosphorylation of SRC but did not affect p-JAK2 expression. (f) Cells were treated with or without PSD-A in the presence or absence of momelotininb (JAK inhibitor) and SP600125 (JNK inhibitor) for 4 h. Proteins were extracted, and expression of p-STAT3 and STAT3 was detected by Western blot. (g) Cells were treated with PSD-A (50 nM) and S31–201 (100 μ M) for 4 h, and expression of p-STAT3 was measured in cell lysates by Western blot. (h) A549 cells were incubated with or without PSD-A for 4 h and then further incubated with IL-6 for 1 h. The nuclear extracts were then collected and assayed for STAT3 DNA-binding activity according to the instructions of the kit. Columns not sharing the same superscript letters within the groups differ significantly ( P < 0.05).

    Article Snippet: The primary antibodies for cleaved caspases (3 and 9), cleaved PARP, p-STAT3 (Tyr705), STAT3, p-SRC, and SRC were obtained from Cell Signaling Technology (Beverly, MA) while primary antibodies for Bax, Bcl-2, Bcl-xl, Xiap, survivin, ATF4, eIF2 α , GRP78, GRP98, GAPDH, SHP-1, SHP-2, PTEN, and TrxR1 were obtained from Proteintech (Wuhan, China).

    Techniques: Activation Assay, Expressing, Western Blot, Inhibition, Incubation, Binding Assay, Activity Assay

    D1R interacts with Shp-2 in the striatal neurons. Notes: Striatal proteins were coimmunoprecipitated with anti-D1R and anti-Shp-2 antibodies ( A and B ). Representative immunoblots showing D1R and Shp-2 interactions in striatal neurons as detected by coimmunoprecipitation. No precipitating antibody, an irrelevant IgG was used in L2, L3, respectively. The D1R antibody (L4A) or Shp-2 antibody (L4B) was used in L4 for normal rats and L5 for LID rats, respectively. No striatal proteins and antibodies were used in L1. Abbreviations: IP, immunoprecipitation; D1R, D1 dopamine receptor; L1, lane 1; L2, lane 2; L3, lane 3; L4, lane 4; L5, lane 5; LID, levodopa-induced dyskinesia.

    Journal: Neuropsychiatric Disease and Treatment

    Article Title: The abnormal activation of D1R/Shp-2 complex involved in levodopa-induced dyskinesia in 6-hydroxydopamine-lesioned Parkinson’s rats

    doi: 10.2147/NDT.S162562

    Figure Lengend Snippet: D1R interacts with Shp-2 in the striatal neurons. Notes: Striatal proteins were coimmunoprecipitated with anti-D1R and anti-Shp-2 antibodies ( A and B ). Representative immunoblots showing D1R and Shp-2 interactions in striatal neurons as detected by coimmunoprecipitation. No precipitating antibody, an irrelevant IgG was used in L2, L3, respectively. The D1R antibody (L4A) or Shp-2 antibody (L4B) was used in L4 for normal rats and L5 for LID rats, respectively. No striatal proteins and antibodies were used in L1. Abbreviations: IP, immunoprecipitation; D1R, D1 dopamine receptor; L1, lane 1; L2, lane 2; L3, lane 3; L4, lane 4; L5, lane 5; LID, levodopa-induced dyskinesia.

    Article Snippet: Samples were incubated with a mouse antibody against D1R (EMD Millipore, Billerica, MA, USA) or a rabbit antibody against Shp-2 (Proteintech, Rosemont, IL, USA) overnight at 4°C.

    Techniques: Western Blot, Immunoprecipitation

    Molecular events underlying LID involving D1R/Shp-2 complex and its downstream signaling factors, such as ERK1/2 and mTOR. Notes: The bands represent immunoblot images detected by antibodies against p-Shp-2 ( A ), p-ERK ( B ) and p-mTOR ( C ). Proteins were analyzed from the sham group (1), l -DOPA group (2), SCH23390 + l -DOPA group (3), SKF38393 group (4). Repeated administration of l -DOPA increased the level of p-Shp-2, p-ERK1/2 and p-mTOR. SKF38393 increased the levels similarly. Conversely, SCH23390 plus L-DOPA prevented the increase. Data are presented as mean ± SD. * p < 0.05, versus sham group; # p < 0.05, versus l -DOPA group. Data are statistically analyzed by one-way ANOVA test. Abbreviations: ANOVA, analysis of variance; D1R, D1 dopamine receptor; ERK1/2, extracellular signal-regulated kinases 1 and 2; l -DOPA, l -3,4-dihydroxyphenylalanine; LID, levodopa-induced dyskinesia.

    Journal: Neuropsychiatric Disease and Treatment

    Article Title: The abnormal activation of D1R/Shp-2 complex involved in levodopa-induced dyskinesia in 6-hydroxydopamine-lesioned Parkinson’s rats

    doi: 10.2147/NDT.S162562

    Figure Lengend Snippet: Molecular events underlying LID involving D1R/Shp-2 complex and its downstream signaling factors, such as ERK1/2 and mTOR. Notes: The bands represent immunoblot images detected by antibodies against p-Shp-2 ( A ), p-ERK ( B ) and p-mTOR ( C ). Proteins were analyzed from the sham group (1), l -DOPA group (2), SCH23390 + l -DOPA group (3), SKF38393 group (4). Repeated administration of l -DOPA increased the level of p-Shp-2, p-ERK1/2 and p-mTOR. SKF38393 increased the levels similarly. Conversely, SCH23390 plus L-DOPA prevented the increase. Data are presented as mean ± SD. * p < 0.05, versus sham group; # p < 0.05, versus l -DOPA group. Data are statistically analyzed by one-way ANOVA test. Abbreviations: ANOVA, analysis of variance; D1R, D1 dopamine receptor; ERK1/2, extracellular signal-regulated kinases 1 and 2; l -DOPA, l -3,4-dihydroxyphenylalanine; LID, levodopa-induced dyskinesia.

    Article Snippet: Samples were incubated with a mouse antibody against D1R (EMD Millipore, Billerica, MA, USA) or a rabbit antibody against Shp-2 (Proteintech, Rosemont, IL, USA) overnight at 4°C.

    Techniques: Western Blot

    SHP-1, c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.

    Journal: Bioengineered

    Article Title: Src-homology domain 2 containing protein tyrosine phosphatase-1 (SHP-1) directly binds to proto-oncogene tyrosine-protein kinase Src (c-Src) and promotes the transcriptional activation of connexin 43 (Cx43)

    doi: 10.1080/21655979.2022.2079252

    Figure Lengend Snippet: SHP-1, c-Src, p-c-Src, and Cx43 expression after overexpression of SHP-1 was detected by qPCR and western blot. (a) qPCR was used to detect the gene expression of SHP-1 and Cx43 in HL-1 cells. (b) The expression of SHP-1, c-Src, p-c-Src, and Cx43 in HL-1 cells was detected by WB, and semi-quantitative analysis based on gray value was performed. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01.

    Article Snippet: The primary antibody used was as follows: anti-Cx43 (1:500, Abcam), anti-p-c-Src (1:500, CST), and anti-SHP-1 (1:500, Proteintech).

    Techniques: Expressing, Over Expression, Western Blot, Transfection, Plasmid Preparation

    The protein expression after overexpression of SHP-1 was detected by immunofluorescence. (a) The microscopy images of SHP-1, p-c-Src, and Cx43 stained in HL-1 cells were photographed under a fluorescence microscope. (b) The average fluorescence intensity was calculated. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01. Scale bar: 50 μm.

    Journal: Bioengineered

    Article Title: Src-homology domain 2 containing protein tyrosine phosphatase-1 (SHP-1) directly binds to proto-oncogene tyrosine-protein kinase Src (c-Src) and promotes the transcriptional activation of connexin 43 (Cx43)

    doi: 10.1080/21655979.2022.2079252

    Figure Lengend Snippet: The protein expression after overexpression of SHP-1 was detected by immunofluorescence. (a) The microscopy images of SHP-1, p-c-Src, and Cx43 stained in HL-1 cells were photographed under a fluorescence microscope. (b) The average fluorescence intensity was calculated. OE-SHP-1, HL-1 cells transfected with SHP-1 overexpression lentivirus. NC, HL-1 cells transfected with lentivirus vector. ##, p < 0.01. Scale bar: 50 μm.

    Article Snippet: The primary antibody used was as follows: anti-Cx43 (1:500, Abcam), anti-p-c-Src (1:500, CST), and anti-SHP-1 (1:500, Proteintech).

    Techniques: Expressing, Over Expression, Immunofluorescence, Microscopy, Staining, Fluorescence, Transfection, Plasmid Preparation

    SHP-1 is directly combined with c-Src. (a) The immunofluorescence co-localization of SHP-1 and c-Src protein in HL-1 cells. Scale bar: 50 μm. (b) Co-IP test was performed with SHP-1 antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input. (c) Co-IP test was performed with c-Src antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input.

    Journal: Bioengineered

    Article Title: Src-homology domain 2 containing protein tyrosine phosphatase-1 (SHP-1) directly binds to proto-oncogene tyrosine-protein kinase Src (c-Src) and promotes the transcriptional activation of connexin 43 (Cx43)

    doi: 10.1080/21655979.2022.2079252

    Figure Lengend Snippet: SHP-1 is directly combined with c-Src. (a) The immunofluorescence co-localization of SHP-1 and c-Src protein in HL-1 cells. Scale bar: 50 μm. (b) Co-IP test was performed with SHP-1 antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input. (c) Co-IP test was performed with c-Src antibody and cell extract co-precipitated IgG polyclonal antibody was used as control, and the cell extract was set as an input.

    Article Snippet: The primary antibody used was as follows: anti-Cx43 (1:500, Abcam), anti-p-c-Src (1:500, CST), and anti-SHP-1 (1:500, Proteintech).

    Techniques: Immunofluorescence, Co-Immunoprecipitation Assay