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monoclonal mouse antibodies against human cd44  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc monoclonal mouse antibodies against human cd44
    Figure 5. Immunological detection of caspase-mediated cleavages of extracellular proteins in normal (pH 7.4) and acidic (pH 6.0) environments. For the detection of extracellular cleavages, MDA-MB-231 cells were used. Red arrows indicate bands representing cleaved fragments, while black arrows indicate full-length proteins present in total cell lysates. (A) Detected caspase-3 or -7 extracellular cleavages of the selected targets (NRP-1, <t>CD44,</t> CSPG4) in an acidic (pH 6.0) environment in either DPBS or MES buffer. (B) Detection of caspase extracellular cleavages in a normal (pH 7.4) environment using either DPBS or HEPES buffer. NRP-1, neuropilin-1; <t>CD44,</t> <t>CD44</t> antigen; CSPG4, chondroitin sulfate proteoglycan 4.
    Monoclonal Mouse Antibodies Against Human Cd44, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 425 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/monoclonal mouse antibodies against human cd44/product/Cell Signaling Technology Inc
    Average 96 stars, based on 425 article reviews
    monoclonal mouse antibodies against human cd44 - by Bioz Stars, 2026-02
    96/100 stars

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    1) Product Images from "Apoptotic Caspases-3 and -7 Cleave Extracellular Domains of Membrane-Bound Proteins from MDA-MB-231 Breast Cancer Cells."

    Article Title: Apoptotic Caspases-3 and -7 Cleave Extracellular Domains of Membrane-Bound Proteins from MDA-MB-231 Breast Cancer Cells.

    Journal: International journal of molecular sciences

    doi: 10.3390/ijms26083466

    Figure 5. Immunological detection of caspase-mediated cleavages of extracellular proteins in normal (pH 7.4) and acidic (pH 6.0) environments. For the detection of extracellular cleavages, MDA-MB-231 cells were used. Red arrows indicate bands representing cleaved fragments, while black arrows indicate full-length proteins present in total cell lysates. (A) Detected caspase-3 or -7 extracellular cleavages of the selected targets (NRP-1, CD44, CSPG4) in an acidic (pH 6.0) environment in either DPBS or MES buffer. (B) Detection of caspase extracellular cleavages in a normal (pH 7.4) environment using either DPBS or HEPES buffer. NRP-1, neuropilin-1; CD44, CD44 antigen; CSPG4, chondroitin sulfate proteoglycan 4.
    Figure Legend Snippet: Figure 5. Immunological detection of caspase-mediated cleavages of extracellular proteins in normal (pH 7.4) and acidic (pH 6.0) environments. For the detection of extracellular cleavages, MDA-MB-231 cells were used. Red arrows indicate bands representing cleaved fragments, while black arrows indicate full-length proteins present in total cell lysates. (A) Detected caspase-3 or -7 extracellular cleavages of the selected targets (NRP-1, CD44, CSPG4) in an acidic (pH 6.0) environment in either DPBS or MES buffer. (B) Detection of caspase extracellular cleavages in a normal (pH 7.4) environment using either DPBS or HEPES buffer. NRP-1, neuropilin-1; CD44, CD44 antigen; CSPG4, chondroitin sulfate proteoglycan 4.

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    Image Search Results


    Figure 5. Immunological detection of caspase-mediated cleavages of extracellular proteins in normal (pH 7.4) and acidic (pH 6.0) environments. For the detection of extracellular cleavages, MDA-MB-231 cells were used. Red arrows indicate bands representing cleaved fragments, while black arrows indicate full-length proteins present in total cell lysates. (A) Detected caspase-3 or -7 extracellular cleavages of the selected targets (NRP-1, CD44, CSPG4) in an acidic (pH 6.0) environment in either DPBS or MES buffer. (B) Detection of caspase extracellular cleavages in a normal (pH 7.4) environment using either DPBS or HEPES buffer. NRP-1, neuropilin-1; CD44, CD44 antigen; CSPG4, chondroitin sulfate proteoglycan 4.

    Journal: International journal of molecular sciences

    Article Title: Apoptotic Caspases-3 and -7 Cleave Extracellular Domains of Membrane-Bound Proteins from MDA-MB-231 Breast Cancer Cells.

    doi: 10.3390/ijms26083466

    Figure Lengend Snippet: Figure 5. Immunological detection of caspase-mediated cleavages of extracellular proteins in normal (pH 7.4) and acidic (pH 6.0) environments. For the detection of extracellular cleavages, MDA-MB-231 cells were used. Red arrows indicate bands representing cleaved fragments, while black arrows indicate full-length proteins present in total cell lysates. (A) Detected caspase-3 or -7 extracellular cleavages of the selected targets (NRP-1, CD44, CSPG4) in an acidic (pH 6.0) environment in either DPBS or MES buffer. (B) Detection of caspase extracellular cleavages in a normal (pH 7.4) environment using either DPBS or HEPES buffer. NRP-1, neuropilin-1; CD44, CD44 antigen; CSPG4, chondroitin sulfate proteoglycan 4.

    Article Snippet: Primary antibodies used for detection were polyclonal rabbit antibodies against cleaved caspase-3 (#9661, Cell Signaling, Danvers, MA, USA), polyclonal rabbit antibodies against cleaved caspase-7 (#9491, Cell Signaling, Danvers, MA, USA), polyclonal rabbit antibodies against β-actin (A2066, Sigma Aldrich, St. Louis, MO, USA), polyclonal sheep antibodies against human neuropilin-1 (#AF3870, R&D Systems, Minneapolis, MN, USA), monoclonal mouse antibodies against human CD44 (#3570, Cell Signaling, Danvers, MA, USA) and rabbit monoclonal antibodies against human CSPG4 (#43916, Cell Signaling, Danvers, MA, USA).

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