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Invitrogen

PPAP2B Monoclonal Antibody (ZV002)

Advanced Verification

7 Published Figures

View all (8) PPAP2B antibodies

Questions & Answers

Catalog # 39-1000

Price (TWD)

16,640.00

線上優惠

Ends: 30-Jun-2025

21,200.00

Save 4,560.00 (22%)

100 µg

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Questions & Answers

Application

PPAP2B Antibody in Immunocytochemistry (ICC/IF)

FIGURE: 1 / 10

PPAP2B Antibody (39-1000) in ICC/IF

Immunofluorescence analysis of PPAP2B was performed using 70% confluent log phase HeLa cells treated with 50 ng/mL EGF for 12 h. The cells were fixed with 4% paraformaldehyde for 10 minutes, permeabilized with 0.1% Triton™ X-100 for 10 minutes, and blocked with 1% BSA for 1 hour at room temperature. The cells were labeled with PPAP2B (ZV002) Mouse Monoclonal Antibody (Product # 39-1000) at 2 µg/mL in 0.1% BSA and incubated for 3 hours at room temperature and then labeled with Goat anti-Mouse IgG (H+L) Superclonal™ Secondary Antibody, Alexa... View More

PPAP2B Antibody in Immunocytochemistry (ICC/IF)

PPAP2B Antibody in Immunohistochemistry (IHC)

PPAP2B Antibody in Western Blot (WB)

PPAP2B Antibody in Western Blot (WB)

PPAP2B Antibody in Western Blot, Flow Cytometry (WB, Flow)

PPAP2B Antibody in Western Blot (WB)

PPAP2B Antibody in Western Blot (WB)

PPAP2B Antibody in Western Blot (WB)

PPAP2B Antibody

PPAP2B Antibody

Product Image Gallery

PPAP2B Antibody in Immunocytochemistry (ICC/IF) — Immunofluorescence analysis of PPAP2B was performed using 70% confluent log phase HeLa cells treated with 50 ng/mL EGF for 12 h. The cells were fixed with 4% paraformaldehyde for 10 minutes, permeabilized with 0.1% Triton™ X-100 for 10 minutes, and blocked with 1% BSA for 1 hour at room temperature. The cells were labeled with PPAP2B (ZV002) Mouse Monoclonal Antibody (Product # 39-1000) at 2 µg/mL in 0.1% BSA and incubated for 3 hours at room temperature and then labeled with Goat anti-Mouse IgG (H+L) Superclonal™ Secondary Antibody, Alexa Fluor® 488 conjugate (Product # A28175) at a dilution of 1:2000 for 45 minutes at room temperature (Panel a: green). Nuclei (Panel b: blue) were stained with SlowFade® Gold Antifade Mountant with DAPI (Product # S36938). F-actin (Panel c: red) was stained with Alexa Fluor® 555 Rhodamine Phalloidin (Product # R415, 1:300). Panel d represents the merged image showing punctate cytoplasmic localization. Panel e shows the untreated cells. Panel f shows the control without primary antibody. The images were captured at 60X magnification.

PPAP2B Antibody in Immunohistochemistry (IHC) — Figure 2 Immunohistochemistry of primary tumors . (A) A representative serial section of human glioblastoma was stained with hematoxylin and eosin (H&E), white arrows indicate microvascular proliferation, and (B) black arrows indicate anti-LPP3-RGD positive glioblastoma cells. Scale bars, 100 mum. (C) Anti-LPP3 staining in normal pancreas show cytosolic expression in both endocrine (Islet of Langerhans-arrow) and exocrine components. (D, E) In pancreatic endocrine tumors, 65% of the tumors show cytosolic staining. Inset: Nuclear localization of LPP3 is also detected in 40% of cases. (F) An example of LPP3-negative tumor cells. All experiments are representative of those obtained in at least three separate experiments, with similar results.

PPAP2B Antibody in Western Blot (WB) — Figure 6 LPP3- knockdown results in increased vascular endothelial cell permeability. ( A ) Timeline of the knockdown, beta-catenin cDNA transfection, and TER assay. ( B ) LPP3-depletion results in decreased TER and increased LMVECs barrier disruption, whereas no change was observed in LMVECs receiving control shRNA . Following transfection of beta-catenin cDNA into LPP3-depleted LMVECs, the TER level was restored nearly to control group, while the transfection with p120-catenin cDNA into LPP3-depleted LMVECs had only a modest effect. Experiments were carried out in triplicates and repeated at least three times; * P < 0.05. ( C ) The efficiency of Lpp3 -knockdown was assessed by WB with the indicated antibodies. Experiments were repeated at least three times with similar results.

PPAP2B Antibody in Western Blot (WB) — Published figure using PPAP2B monoclonal antibody (Product # 39-1000) in Western Blot

PPAP2B Antibody in Western Blot, Flow Cytometry (WB, Flow) — Figure 3 LPP3 regulates glioblastoma cell proliferation . (A) The time line indicates when glioblastoma cell lines were plated, shRNA (retrovirus) mediated knockdown was conducted, cells were growth factor and serum starved, fresh medium was added, BrdU (1.0 mug/ml) was added, and the proliferation assay was performed. (B) Quantification of glioblastoma cell proliferation assay. The data represent the mean +- s.e.m. n = 5-7 from five to seven independent experiments, Y= P < 0.05 vs. control untreated; P P < 0.05 vs. control shRNA treated group. (C-F) Representative images of the BrdU assay. Arrows indicate BrdU positive cells. Scale bar, 150 mum. (G) The efficiency of knockdown of LPP3 was assessed by western blotting with the indicated antibodies. Figure 3G (top panel, last lane, anti-LPP3), a partial band is likely produced by over flow from the neighboring well. All experiments are representative of those obtained in at least three separate experiments with similar results.

PPAP2B Antibody in Western Blot (WB) — Figure 5 LPP3 regulates glioblastoma tumor growth . (A) Stable clones of U87 and U118 were selected and efficiency of knockdown was determined by western blotting with the indicated antibodies. LPP3 -knockdown decreased total beta-catenin, CYCLIN-D1, and CD133 proteins, whereas it had no effect on LPP2 or GAPDH. (B) Conditioned media were collected and subjected to ELISA for VEGF, IL-8, and TIMP-2. LPP3 -knockdown in U87 and U118 cells reduced the concentration of VEGF and IL-8, whereas TIMP-2 was unaffected. (C) In the xenograft assay, mice receiving cells that expressed control shRNA showed increased tumor growth (n = 12, Y= P < 0.05) after 14 and 28 days. LPP3 -knockdown reduced U87 and U118 tumor growth (n = 12, P P < 0.05). (D) Representative images from the xenograft assay. Dotted circles indicate the location of tumor implants.

PPAP2B Antibody in Western Blot (WB) — Figure 4 LPP3 regulates glioblastoma cell migration . (A) The time line indicates when glioblastoma cell lines were plated, shRNA (retrovirus) mediated knockdown was conducted, medium was added, and the migration assay was performed as described in materials and methods. (B) Quantification of glioblastoma cell migration through the Boyden chamber. The data represent the mean +- s.e.m. n = 5-7, Y= P < 0.05 vs. control shRNA treated group. (C) Efficiency of knockdown of LPP3 was assessed by western blotting with the indicated antibodies. All experiments are representative of those obtained in at least three separate experiments with similar results.

PPAP2B Antibody in Western Blot (WB) — Figure 1 Expression of LPP3 in primary tumors . (A) Western blot was probed with an anti-LPP3-C-cyto antibody. Each lane contained 10 mug total protein prepared from primary human tumor tissues. LPP3 protein is indicated by two black arrows. (B) Tumor line cell extracts were analyzed by WB with the indicated antibodies. All blots shown are representative of those obtained from at least three separate experiments with similar results.

PPAP2B Antibody — Modulation of expression of target protein by cell treatment to demonstrate antibody specificity. Immunofluorescence analysis of PPAP2B using anti PPAP2B monoclonal antibody (Product # 39-1000) shows increased expression of PPAP2B in HeLa cells treated with EGF. {TM}

PPAP2B Antibody — Figure 5 LPP3 regulates glioblastoma tumor growth. (A) Stable clones of U87 and U118 were selected and efficiency of knockdown was determined by western blotting with the indicated antibodies. LPP3-knockdown decreased total β-catenin, CYCLIN-D1, and CD133 proteins, whereas it had no effect on LPP2 or GAPDH. (B) Conditioned media were collected and subjected to ELISA for VEGF, IL-8, and TIMP-2. LPP3-knockdown in U87 and U118 cells reduced the concentration of VEGF and IL-8, whereas TIMP-2 was unaffected. (C) In the xenograft assay, mice receiving cells that expressed control shRNA showed increased tumor growth (n = 12, ¥ P < 0.05) after 14 and 28 days. LPP3-knockdown reduced U87 and U118 tumor growth (n = 12, ¶ P < 0.05). (D) Representative images from the xenograft assay. Dotted circles indicate the location of tumor implants. {KD}

Product Details

39-1000

Applications

Tested Dilution

Publications

Western Blot (WB)

Assay-dependent

View 5 publications 5 publications

Immunohistochemistry (IHC)

-

View 1 publication 1 publication

Immunocytochemistry (ICC/IF)

2 µg/mL

View 1 publication 1 publication

Flow Cytometry (Flow)

-

View 1 publication 1 publication

ELISA (ELISA)

Assay-dependent

-

Immunoprecipitation (IP)

-

View 1 publication 1 publication

Product Specifications

Species Reactivity

Human

Published species

Human

Host/Isotype

Mouse / IgG1, kappa

Class

Monoclonal

Type

Antibody

Clone

ZV002

Immunogen

Recombinant protein derived from an internal region of human VCIP

Conjugate

Unconjugated

Form

Liquid

Concentration

0.5 mg/mL

Purification

Protein A

Storage buffer

PBS, pH 7.4

Contains

0.1% sodium azide

Storage conditions

-20°C

Shipping conditions

Ambient (domestic); Wet ice (international)

AB_2533397

Target Information

Human vascular endothelial growth factor produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38231 Dalton. The rHuVEGF is purified by proprietary chromatographic techniques.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

Product References

Lipid phosphate phosphatase 3 maintains NO-mediated flow-mediated dilatation in human adipose resistance arterioles.

The Journal of physiology

Chabowski DS,Hughes WE,Hockenberry JC,LoGiudice J,Beyer AM,Gutterman DD

39-1000 was used in Western Blot to suggest LPP3 is crucial in the disease-associated switch in the mediator of FMD.

Wed Feb 01 00:00:00 UTC 2023

Endothelial lipid phosphate phosphatase-3 deficiency that disrupts the endothelial barrier function is a modifier of cardiovascular development.

Cardiovascular research

Chatterjee I,Baruah J,Lurie EE,Wary KK

Published figure using PPAP2B monoclonal antibody (Product # 39-1000) in Western Blot

Fri Jul 01 00:00:00 UTC 2016

Mechanosensitive PPAP2B Regulates Endothelial Responses to Atherorelevant Hemodynamic Forces.

Circulation research

Wu C,Huang RT,Kuo CH,Kumar S,Kim CW,Lin YC,Chen YJ,Birukova A,Birukov KG,Dulin NO,Civelek M,Lusis AJ,Loyer X,Tedgui A,Dai G,Jo H,Fang Y

Published figure using PPAP2B monoclonal antibody (Product # 39-1000) in Western Blot

Fri Jul 31 00:00:00 UTC 2015

Lipid phosphate phosphatase-3 regulates tumor growth via β-catenin and CYCLIN-D1 signaling.

Molecular cancer

Chatterjee I,Humtsoe JO,Kohler EE,Sorio C,Wary KK

Published figure using PPAP2B monoclonal antibody (Product # 39-1000) in Western Blot

Wed May 11 00:00:00 UTC 2011

Lipid phosphate phosphatase-3 regulates tumor growth via β-catenin and CYCLIN-D1 signaling.

Molecular cancer

Chatterjee I,Humtsoe JO,Kohler EE,Sorio C,Wary KK

Published figure using PPAP2B monoclonal antibody (Product # 39-1000) in Western Blot

Wed May 11 00:00:00 UTC 2011

Lipid phosphate phosphatase-3 regulates tumor growth via β-catenin and CYCLIN-D1 signaling.

Molecular cancer

Chatterjee I,Humtsoe JO,Kohler EE,Sorio C,Wary KK

Published figure using PPAP2B monoclonal antibody (Product # 39-1000) in Western Blot

Wed May 11 00:00:00 UTC 2011

Lipid phosphate phosphatase 3 stabilization of beta-catenin induces endothelial cell migration and formation of branching point structures.

Molecular and cellular biology

Humtsoe JO,Liu M,Malik AB,Wary KK

Thu Apr 01 00:00:00 UTC 2010

Lipid phosphate phosphatase 3 stabilization of beta-catenin induces endothelial cell migration and formation of branching point structures.

Molecular and cellular biology

Humtsoe JO,Liu M,Malik AB,Wary KK

Thu Apr 01 00:00:00 UTC 2010

Lipid phosphate phosphatase 3 stabilization of beta-catenin induces endothelial cell migration and formation of branching point structures.

Molecular and cellular biology

Humtsoe JO,Liu M,Malik AB,Wary KK

Thu Apr 01 00:00:00 UTC 2010

Bioinformatics

Protein Aliases: EC 3.1.3.4; Lipid phosphate phosphohydrolase 3; MGC15306; PAP-2b; PAP2 beta; PAP2-b; PAP2-beta; Phosphatidate phosphohydrolase type 2b; Phosphatidic acid phosphatase 2b; phosphatidic acid phosphatase type 2B; Phospholipid phosphatase 3; type-2 phosphatidic acid phosphatase-beta; vascular endothelial growth factor and type I collagen inducible; Vascular endothelial growth factor and type I collagen-inducible protein; VCIP

Gene Aliases: Dri42; LPP3; PAP2B; PLPP3; PPAP2B; VCIP

UniProt ID: (Human) O14495

Entrez Gene ID: (Human) 8613

Function(s)

phosphoprotein phosphatase activity integrin binding protein binding phosphatidate phosphatase activity sphingosine-1-phosphate phosphatase activity lipid phosphatase activity phosphatase

Process(es)

blood vessel development gastrulation with mouth forming second negative regulation of protein phosphorylation protein dephosphorylation lipid metabolic process phospholipid metabolic process germ cell migration regulation of Wnt signaling pathway sphingolipid biosynthetic process homotypic cell-cell adhesion canonical Wnt signaling pathway involved in positive regulation of endothelial cell migration canonical Wnt signaling pathway involved in positive regulation of cell-cell adhesion canonical Wnt signaling pathway involved in positive regulation of wound healing phospholipid dephosphorylation positive regulation of peptidyl-tyrosine phosphorylation protein stabilization positive regulation of sequence-specific DNA binding transcription factor activity Bergmann glial cell differentiation regulation of sphingolipid mediated signaling pathway

Performance Guarantee

If an Invitrogen™ antibody doesn't perform as described on our website or datasheet,we'll replace the product at no cost to you, or provide you with a credit for a future purchase.*

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