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tartrate resistant acid phosphatase trap staining  (Servicebio Inc)

 
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    Servicebio Inc tartrate resistant acid phosphatase trap staining
    Tartrate Resistant Acid Phosphatase Trap Staining, supplied by Servicebio Inc, 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/product/tartrate+resistant+acid+phosphatase+trap+staining/acid+phosphatase+resistant+tartrate/pm42321186-529-30-3
    Average 86 stars, based on 1 article reviews
    tartrate resistant acid phosphatase trap staining - by Bioz Stars, 2026-10
    86/100 stars

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    Related Articles

    Staining:

    Article Title: Magnesium ion hydrogel enhances resistance to radiation-induced bone injury by modulating the bone immune microenvironment and promoting microvascularization
    Article Snippet: .. Each sample underwent HE, Masson staining and tartrate-resistant acid phosphatase (TRAP) staining according to the instructions provided by the manufacturer (Servicebio, China). ..

    Article Title: OX40L in endothelial cells promotes temporomandibular joint subchondral bone angiogenesis and osteoclastogenesis in mice
    Article Snippet: .. Additionally, sagittal sections were processed for tartrate-resistant acid phosphatase (TRAP) staining (Servicebio, China) to quantify osteoclast numbers in the subchondral bone. ..

    Article Title: OX40L in endothelial cells promotes temporomandibular joint subchondral bone angiogenesis and osteoclastogenesis in mice.
    Article Snippet: Sagittal sections of the condyle were subjected to Safranin O/Fast Green staining (Solarbio) and haematoxylin and eosin (HE) staining (Biosharp, China). .. Three randomly selected sections were blindly assessed by three independent observers (YZ, ZL, JL) using the Osteoarthritis Research Society International (OARSI) recommended histopathological grading system.16 Additionally, sagittal sections were processed for tartrate-resistant acid phosphatase (TRAP) staining (Servicebio, China) to quantify osteoclast numbers in the subchondral bone. ..

    Article Title: Mechanism of EC ‐ EXOs ‐Derived THBS3 Targeting CD47 to Regulate BMSCs Differentiation to Ameliorate Bone Loss
    Article Snippet: .. Paraffin sections of bone tissue were prepared for Haematoxylin–eosin (HE) staining (Servicebio, China), tartrate resistant acid phosphatase (TRAP) staining (Servicebio, China), and Osteocalcin (OCN) immunohistochemical staining (Servicebio, China) (Tables and ). .. Paraffin sections of bone tissue were prepared for Haematoxylin–eosin (HE) staining (Servicebio, China), tartrate resistant acid phosphatase (TRAP) staining (Servicebio, China), and Osteocalcin (OCN) immunohistochemical staining (Servicebio, China) (Tables and ).

    Article Title: Decoding the synergistic potential of herbal medicine and dietary supplements for treating postmenopausal osteoporosis.
    Article Snippet: Quinoa with saponins removed (lot number: 20181009) was obtained from Shanxi Province Huayang Pharmaceutical Co. Salidroside (CAS: 10338–51-9) and nuezhenide (CAS: 39011–92–2) were purchased from Chengdu Herbpurify Co., Ltd., with purity higher than 98 %. .. Ethylenediaminetetraacetic acid (EDTA) was purchased from Beijing Chemical Reagent Company, and hematoxylin and eosin (H&E) staining solutions were obtained from Beijing Solarbio Biotechnology Co. Tartrate-resistant acid phosphatase (TRAP) staining reagent was purchased from Servicebio Biotechnology Co. ..

    Article Title: Targeting the PARP10-BCAT2 axis disrupts branched-chain amino-acid metabolism to suppress bone metastasis in lung cancer.
    Article Snippet: .. We thank Wuhan Servicebio Technology Co., Ltd. (Wuhan, Hubei, China) for professional technical support in histological processing, including hematoxylin and eosin (H&E) staining of bone and visceral tissue sections, and tartrate-resistant acid phosphatase (TRAP) staining of bone specimens. .. We thank OE Biotech Co., Ltd. (Shanghai, China) for transcriptome sequencing, untargeted metabolomics sequencing, and bioinformatics data analysis support.

    Article Title: Moxibustion ameliorates abnormal subchondral bone remodeling by promoting ACSL1-mediated autophagy to degrade NLRP3 in osteoarthritis
    Article Snippet: .. In accordance with the kit’s operating instructions, dewaxing was followed by Safranin O-Fast Green staining (Sigma-Aldrich), hematoxylin and eosin (H&E) staining and tartrate-resistant acid phosphatase (TRAP) staining (Servicebio). ..

    Immunohistochemical staining:

    Article Title: Mechanism of EC ‐ EXOs ‐Derived THBS3 Targeting CD47 to Regulate BMSCs Differentiation to Ameliorate Bone Loss
    Article Snippet: .. Paraffin sections of bone tissue were prepared for Haematoxylin–eosin (HE) staining (Servicebio, China), tartrate resistant acid phosphatase (TRAP) staining (Servicebio, China), and Osteocalcin (OCN) immunohistochemical staining (Servicebio, China) (Tables and ). .. Paraffin sections of bone tissue were prepared for Haematoxylin–eosin (HE) staining (Servicebio, China), tartrate resistant acid phosphatase (TRAP) staining (Servicebio, China), and Osteocalcin (OCN) immunohistochemical staining (Servicebio, China) (Tables and ).

    H&E Stain:

    Article Title: Moxibustion ameliorates abnormal subchondral bone remodeling by promoting ACSL1-mediated autophagy to degrade NLRP3 in osteoarthritis
    Article Snippet: .. In accordance with the kit’s operating instructions, dewaxing was followed by Safranin O-Fast Green staining (Sigma-Aldrich), hematoxylin and eosin (H&E) staining and tartrate-resistant acid phosphatase (TRAP) staining (Servicebio). ..



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    Servicebio Inc tartrate resistant acid phosphatase trap staining
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    Comparative effects of BMP9 and BMP2 on osteogenic differentiation and osteoclastogenesis in vitro. (A) Real‐time PCR analysis of key osteogenic genes (Col1, Runx2, ALP, and OCN) in MC3T3‐E1 cells treated with 8 nM of BMP2 or BMP9 for 3, 5, and 7 days. All gene‐expression levels were normalized to GAPDH. (B) Western blot analysis of osteogenic marker proteins in cell lysates harvested after 7 days of treatment with BMP2 or BMP9. GAPDH was used as the loading control. Densitometric quantification of band intensities (integrated density) normalized to GAPDH is shown below the blots and presented as relative protein expression. (C) Western blot showing dose‐dependent p‐Smad1/5/9 in MC3T3‐E1 cells exposed to varying concentrations of BMP2 or BMP9. Phosphorylation was quantified by densitometry and expressed as fold change vs. control after normalization using [(p‐Smad1/5/9)/(total Smad1/5/9)] and further normalized to GAPDH, as shown in the graph below the blots. Asterisks indicate statistical significance for pairwise comparisons between BMP2 and BMP9 at the same concentration (****, p < 0.0001), unless otherwise indicated. (D) ALP activity and representative images of ALP staining in MC3T3‐E1 cultures after 7 days of induction with BMP2 or BMP9. (E) Alizarin Red S staining illustrating mineralized nodule formation after extended culture with BMP2 or BMP9. (F) Representative <t>TRAP‐stained</t> images of RAW 264.7‐derived osteoclasts following treatment with RANKL (3 nM), BMP2 (8 nM), or BMP9 (8 nM) for 5 days. TRAP‐positive multinucleated osteoclasts are indicated by arrows. Scale bar, 20 μm. (G) Quantification of TRAP‐positive multinucleated cells per well. Data are presented as the mean ± SD ( n = 3 independent experiments), and p ‐values were calculated using one‐way analysis of variance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001). BMP, bone morphogenetic protein; PCR, polymerase chain reaction; ALP, alkaline <t>phosphatase;</t> Col1, collagen type I; Runx2, runt‐related transcription factor 2; OCN, osteocalcin; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase.
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    TaKaRa tartrate resistant acid phosphatase trap
    Chemokine (C-X-C motif) ligand 5 (CXCL5) inhibits receptor activator of nuclear factor kappa-B ligand (RANKL)-induced osteoclast differentiation. a), c), and e) Immunofluorescence staining confirmed that CXCL5 (1 or 50 ng/ml) inhibits RANKL-induced differentiation of RAW264.7 cells into cathepsin K (CTSK)-positive osteoclast-like cells. b), d), and f) CXCL5 decreased the differentiation of RAW264.7 cells <t>into</t> <t>tartrate-resistant</t> acid <t>phosphatase</t> <t>(TRAP)-positive</t> osteoclast-like cells. Purple indicates TRAP expression, and cyan indicates nuclei. g) and h) Western blot analysis showed that CXCL5 (1 ng/ml) inhibited RANKL-induced differentiation of RAW264.7 cells by suppressing the transcription factor nuclear factor of activated T-cells cytoplasmic 1 (NFATc1), resulting in decreased CTSK expression at 72 hours of treatment. Data are presented as the mean (standard error of the mean (SEM)) and analyzed using one-way analysis of variance (ANOVA) followed by Tukey’s multiple comparison test. *p < 0.05, **p < 0.01, ***p < 0.001. DAPI, 4′,6-diamidino-2-phenylindole.
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    Image Search Results


    Comparative effects of BMP9 and BMP2 on osteogenic differentiation and osteoclastogenesis in vitro. (A) Real‐time PCR analysis of key osteogenic genes (Col1, Runx2, ALP, and OCN) in MC3T3‐E1 cells treated with 8 nM of BMP2 or BMP9 for 3, 5, and 7 days. All gene‐expression levels were normalized to GAPDH. (B) Western blot analysis of osteogenic marker proteins in cell lysates harvested after 7 days of treatment with BMP2 or BMP9. GAPDH was used as the loading control. Densitometric quantification of band intensities (integrated density) normalized to GAPDH is shown below the blots and presented as relative protein expression. (C) Western blot showing dose‐dependent p‐Smad1/5/9 in MC3T3‐E1 cells exposed to varying concentrations of BMP2 or BMP9. Phosphorylation was quantified by densitometry and expressed as fold change vs. control after normalization using [(p‐Smad1/5/9)/(total Smad1/5/9)] and further normalized to GAPDH, as shown in the graph below the blots. Asterisks indicate statistical significance for pairwise comparisons between BMP2 and BMP9 at the same concentration (****, p < 0.0001), unless otherwise indicated. (D) ALP activity and representative images of ALP staining in MC3T3‐E1 cultures after 7 days of induction with BMP2 or BMP9. (E) Alizarin Red S staining illustrating mineralized nodule formation after extended culture with BMP2 or BMP9. (F) Representative TRAP‐stained images of RAW 264.7‐derived osteoclasts following treatment with RANKL (3 nM), BMP2 (8 nM), or BMP9 (8 nM) for 5 days. TRAP‐positive multinucleated osteoclasts are indicated by arrows. Scale bar, 20 μm. (G) Quantification of TRAP‐positive multinucleated cells per well. Data are presented as the mean ± SD ( n = 3 independent experiments), and p ‐values were calculated using one‐way analysis of variance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001). BMP, bone morphogenetic protein; PCR, polymerase chain reaction; ALP, alkaline phosphatase; Col1, collagen type I; Runx2, runt‐related transcription factor 2; OCN, osteocalcin; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase.

    Journal: Clinical Implant Dentistry and Related Research

    Article Title: Bone Morphogenetic Protein ( BMP ) 9 Outperforms BMP2 in Osteogenesis and Osseointegration: In Vitro and In Vivo

    doi: 10.1111/cid.70135

    Figure Lengend Snippet: Comparative effects of BMP9 and BMP2 on osteogenic differentiation and osteoclastogenesis in vitro. (A) Real‐time PCR analysis of key osteogenic genes (Col1, Runx2, ALP, and OCN) in MC3T3‐E1 cells treated with 8 nM of BMP2 or BMP9 for 3, 5, and 7 days. All gene‐expression levels were normalized to GAPDH. (B) Western blot analysis of osteogenic marker proteins in cell lysates harvested after 7 days of treatment with BMP2 or BMP9. GAPDH was used as the loading control. Densitometric quantification of band intensities (integrated density) normalized to GAPDH is shown below the blots and presented as relative protein expression. (C) Western blot showing dose‐dependent p‐Smad1/5/9 in MC3T3‐E1 cells exposed to varying concentrations of BMP2 or BMP9. Phosphorylation was quantified by densitometry and expressed as fold change vs. control after normalization using [(p‐Smad1/5/9)/(total Smad1/5/9)] and further normalized to GAPDH, as shown in the graph below the blots. Asterisks indicate statistical significance for pairwise comparisons between BMP2 and BMP9 at the same concentration (****, p < 0.0001), unless otherwise indicated. (D) ALP activity and representative images of ALP staining in MC3T3‐E1 cultures after 7 days of induction with BMP2 or BMP9. (E) Alizarin Red S staining illustrating mineralized nodule formation after extended culture with BMP2 or BMP9. (F) Representative TRAP‐stained images of RAW 264.7‐derived osteoclasts following treatment with RANKL (3 nM), BMP2 (8 nM), or BMP9 (8 nM) for 5 days. TRAP‐positive multinucleated osteoclasts are indicated by arrows. Scale bar, 20 μm. (G) Quantification of TRAP‐positive multinucleated cells per well. Data are presented as the mean ± SD ( n = 3 independent experiments), and p ‐values were calculated using one‐way analysis of variance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001). BMP, bone morphogenetic protein; PCR, polymerase chain reaction; ALP, alkaline phosphatase; Col1, collagen type I; Runx2, runt‐related transcription factor 2; OCN, osteocalcin; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase.

    Article Snippet: Recombinant human RANKL (11682‐HNCH; Sino Biological, Beijing, China) and a tartrate‐resistant acid phosphatase (TRAP) staining kit (MK300; Takara Bio, Shiga, Japan) were used for the osteoclast differentiation assay.

    Techniques: In Vitro, Real-time Polymerase Chain Reaction, Gene Expression, Western Blot, Marker, Control, Expressing, Phospho-proteomics, Concentration Assay, Activity Assay, Staining, Derivative Assay, Polymerase Chain Reaction

    Chemokine (C-X-C motif) ligand 5 (CXCL5) inhibits receptor activator of nuclear factor kappa-B ligand (RANKL)-induced osteoclast differentiation. a), c), and e) Immunofluorescence staining confirmed that CXCL5 (1 or 50 ng/ml) inhibits RANKL-induced differentiation of RAW264.7 cells into cathepsin K (CTSK)-positive osteoclast-like cells. b), d), and f) CXCL5 decreased the differentiation of RAW264.7 cells into tartrate-resistant acid phosphatase (TRAP)-positive osteoclast-like cells. Purple indicates TRAP expression, and cyan indicates nuclei. g) and h) Western blot analysis showed that CXCL5 (1 ng/ml) inhibited RANKL-induced differentiation of RAW264.7 cells by suppressing the transcription factor nuclear factor of activated T-cells cytoplasmic 1 (NFATc1), resulting in decreased CTSK expression at 72 hours of treatment. Data are presented as the mean (standard error of the mean (SEM)) and analyzed using one-way analysis of variance (ANOVA) followed by Tukey’s multiple comparison test. *p < 0.05, **p < 0.01, ***p < 0.001. DAPI, 4′,6-diamidino-2-phenylindole.

    Journal: Bone & Joint Research

    Article Title: CXCL5 suppresses osteoclastogenesis and protects against lipoteichoic acid-induced bone loss by modulating PLCγ2 and c-Fos signalling in gram-positive periprosthetic joint infection

    doi: 10.1302/2046-3758.153.BJR-2025-0290.R1

    Figure Lengend Snippet: Chemokine (C-X-C motif) ligand 5 (CXCL5) inhibits receptor activator of nuclear factor kappa-B ligand (RANKL)-induced osteoclast differentiation. a), c), and e) Immunofluorescence staining confirmed that CXCL5 (1 or 50 ng/ml) inhibits RANKL-induced differentiation of RAW264.7 cells into cathepsin K (CTSK)-positive osteoclast-like cells. b), d), and f) CXCL5 decreased the differentiation of RAW264.7 cells into tartrate-resistant acid phosphatase (TRAP)-positive osteoclast-like cells. Purple indicates TRAP expression, and cyan indicates nuclei. g) and h) Western blot analysis showed that CXCL5 (1 ng/ml) inhibited RANKL-induced differentiation of RAW264.7 cells by suppressing the transcription factor nuclear factor of activated T-cells cytoplasmic 1 (NFATc1), resulting in decreased CTSK expression at 72 hours of treatment. Data are presented as the mean (standard error of the mean (SEM)) and analyzed using one-way analysis of variance (ANOVA) followed by Tukey’s multiple comparison test. *p < 0.05, **p < 0.01, ***p < 0.001. DAPI, 4′,6-diamidino-2-phenylindole.

    Article Snippet: Osteoclast formation was evaluated by immunostaining for cathepsin K (CTSK) (ab19027; Abcam, UK) and tartrate-resistant acid phosphatase (TRAP) (MK300; Takara Bio, Japan).

    Techniques: Immunofluorescence, Staining, Expressing, Western Blot, Comparison