S100 protein polyclonal

Manufactured by Agilent Technologies

Sourced in Spain, Germany, United States

The S100 Protein (Polyclonal) is a laboratory equipment product offered by Agilent Technologies. It is a polyclonal antibody specifically targeting the S100 protein, which is a family of calcium-binding proteins involved in various cellular processes. The core function of this product is to provide researchers with a tool for the detection and analysis of S100 proteins in research samples.

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Lab products found in correlation

Dako autostainer plus, by Agilent Technologies (1 mentions) Dm5000b, by Leica (1 mentions) Benchmark xt system, by Roche (1 mentions) Anti nut antibody clone c52b1, by Cell Signaling Technology (1 mentions) Synaptophysin clone sy38, by Agilent Technologies (1 mentions) Cd56 clone mrq 42, by Cell Marque (1 mentions) Ck7 ov tl, by BioGenex (1 mentions)

3 protocols using s100 protein polyclonal

Histological and Immunohistochemical Analysis of Cartilage Samples

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In 9 cases we had enough pathologic tissue to perform a histological study. The remaining tissue was fixed in 10% buffered neutral formalin and paraffin embedded following standard procedure. Routine sections were stained with hematoxylin and eosin and Masson’s Trichrome and Safranin O. Selected sections were immunostained for Type II Collagen (clone 2B1.5, Master Diagnostica, Granada, Spain) and for S100 Protein (Polyclonal, DAKO, Barcelona, Spain) using a FLEX-Ready-to-Use immunohistochemical system (Envision, Glostrup, Denmark) and an automated immunostainer (DAKO Autostainer Plus, Dako). Appropriate controls were included.
Morphometric studies were performed to quantify cellularity in all histologic samples. The number of chondrocytes per surface unit was quantified in cartilage histologic sections stained with hematoxylin-eosin, using the image analysis software Leica QWin. For each sample a 1 mm² section was analyzed, from a representative cartilage area, using sequential images taken with a digital camera DC300 paired to an optical microscope Leica DM5000B at 20× magnification.

Guillén-García P., Rodríguez-Iñigo E., Guillén-Vicente I., Guillén-Vicente M., Fernández-Jaén T., Concejero V., Val D., Maestro A., Abelow S, & López-Alcorocho J.M. (2015). Viability of Pathologic Cartilage Fragments as a Source for Autologous Chondrocyte Cultures. Cartilage, 7(2), 149-156.

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Immunohistochemical Analysis of NUT Carcinoma

Cited 2 times

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The three NC cases were retrieved from the consultation files of three of the authors (A.A., I.F. and C.F.). They have been diagnosed in the years 2010, 2015 and 2017. Immunohistochemistry (IHC) was performed on 3-μm sections cut from paraffin blocks using a fully automated system (“Benchmark XT System”, Ventana Medical Systems Inc, 1910 Innovation Park Drive, Tucson, Arizona, USA) and the following antibodies: pankeratin (clone AE1/AE3, 1:40, Zytomed, Berlin, Germany), CK7 (OV-TL, 1:1000, Biogenex), p63 (SSI6, 1: 100, DCS), S100 protein (polyclonal, 1:2500, Dako), CD56 (clone MRQ-42, 1:100, CELL MARQUE), chromogranin A (clone LK2H10, 1:500, Beckman-Coulter GmbH), synaptophysin (clone SY38, 1:50, Dako), SMARCB1 (MRQ-27, 1:50, Zytomed), and anti-NUT antibody (clone C52B1, 1:45, Cell Signaling). Interpretation of results of the NUT IHC was based on published data showing distinctive granular (punctate or dusty) nuclear immunoreactivity present in > 50% of neoplastic cell nuclei.^{18 (link)} Epstein Barr virus (EBV) in-situ hybridization (EBER 1/2 probes, ZytoVision, Bremerhaven, Germany) was performed according to the manufacturer guidelines. Positive and negative controls were used throughout. Normal testicular tissue was used as a positive control for the NUT IHC.^{5 (link),6 (link)}

Agaimy A., Fonseca I., Martins C., Thway K., Barrette R., Harrington K.J., Hartmann A., French C.A, & Fisher C. (2018). NUT Carcinoma of the Salivary Glands. Clinicopathologic and Molecular Analysis of Three Cases and a Survey of NUT Expression in Salivary Gland Carcinomas. The American journal of surgical pathology, 42(7), 877-884.

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Retrospective GIST Tumor Analysis

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Fifty-eight patients with surgically resected GISTs, who were treated at the University Medical Center Hamburg-Eppendorf over a period of ten years were chosen retrospectively. All resected GISTs were diagnosed by immunohistochemical analyses (CD117, CH34, DOG1) and mutation analysis (KIT/PDGFRA) and interpreted as well as staged by two independent pathologists on a routine basis. Tissues were fixed in 4% buffered formalin and embedded in paraffin. Haematoxylin-eosin stained sections were cut from selected primary tumor blocks with representative tumor regions. Tissue cylinders with a diameter of 600 µm were punched out of the original donor block and arrayed on a new paraffin block using a semi-automated tissue arrayer. Subsequently, five µm sections of the complete TMA were constructed using the Paraffin Sectioning Aid System (Instrumentics, Hackensack, NJ, USA).
The patients were recruited after histological classification of the tumors including CD117 (c-kit; rabbit polyclonal) (Dako, Glostrup, Denmark), CD34 (mouse IgG1) (Novocastra Laboratories Ltd, Newcastle, United Kingdom), desmin (clone DE-R-11) (Dako), muscle actin (mouse IgG1; clone HHF35) (Enzo Diagnostics Inc., NY, USA), and S-100 protein (polyclonal) (Dako). The proliferative index was determined with Ki-67 (MIB1; IgG1) (Dako) and was categorized as mitotic count of < 5/50 high-power fields (HPF) and ≥ 5/50 HPF.

Karstens K.F., Bellon E., Polonski A., Wolters-Eisfeld G., Melling N., Reeh M., Izbicki J.R, & Tachezy M. (2020). Expression and serum levels of the neural cell adhesion molecule L1-like protein (CHL1) in gastrointestinal stroma tumors (GIST) and its prognostic power. Oncotarget, 11(13), 1131-1140.

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