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Commit: 611277b6de3cd1bb065350b6ef8d63df412b7185
XML generation date: 2024-07-11 16:01:09.590
Product last modified at: 2024-11-21T22:00:10.463Z
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PDP - Template Name: Antibody Sampler Kit
PDP - Template ID: *******4a3ef3a

Human Reactive Exosome Marker Antibody Sampler Kit #80610

    Product Information

    Product Description

    The Human Reactive Exosome Marker Antibody Sampler Kit provides an economical means of analyzing proteins that can be present on exosomes. The kit includes enough antibodies to perform two western blot experiments with each primary antibody.

    Specificity / Sensitivity

    Each antibody in the Human Reactive Exosome Marker Antibody Sampler Kit detects endogenous levels of its target protein.

    Source / Purification

    Monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues surrounding Val178 of human CD9, Ile181 of human CD81, Pro346 of human Alix, Ile368 of human flotillin-1, residues near the amino terminus of human TSG101 and human syntenin-1/MDA9, and a recombinant protein fragment of human CD63. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to human HSP70. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Exosomes are small (30-150 nm) membrane-bound vesicles that are secreted by various cell types under normal and pathological conditions (1,2). They originate from intracellular multivesicular endosomes upon fusion with the plasma membrane. Exosomes have emerged as an important mechanism of intercellular communication facilitating the transfer of membrane and cytosolic proteins, lipids, and RNA.

    A variety of methods have been described to isolate exosomes and understand their composition (3-7). Heterogeneity in exosome composition can be attributed to the cells of origin as well as the isolation methods. However, there are protein markers that appear with high frequency. Tetraspanins are a family of cell surface glycoproteins with four transmembrane domains often found in exosomes (8). Tetraspanins CD9, CD81, and CD63 appear in exosomes and have been the target of immune-affinity approaches of exosome isolation. Flotillin-1 is a lipid raft-associated integral membrane protein that is incorporated into exosomes (9). Exosomes also contain proteins involved in endosomal membrane trafficking, collectively known as the ESCRT (endosomal sorting complex required for transport) pathway. Alix regulates cellular processes, such as endocytic membrane trafficking and cell adhesion through interactions with ESCRT proteins including endophilins, and CIN85 (Cbl-interacting protein of 85 kDa), and plays a role in exosome biogenesis (10-12). Syntenin-1 (MDA9, SDCBP) is a member of the PDZ family of proteins that functions as a scaffold adaptor protein regulating numerous signal transduction pathways (13). Syntenin-1 interacts with Alix to regulate exosome biogenesis (12). Tumor susceptibility gene 101 (TSG101) is a fundamental component of the ESCRT complex I involved in regulating the trafficking of proteins throughout the endosomal compartment (14). TSG101 is involved in regulating diverse biological processes, such as cell proliferation, viral budding and release, and exosome biosynthesis (15,16). The heat shock protein HSP70 is a molecular chaperone involved in protein folding that can be induced upon environmental stress (17). HSP70 may also be secreted through exosomes (18).
    1. Raposo, G. and Stoorvogel, W. (2013) J Cell Biol 200, 373-83.
    2. van Niel, G. et al. (2018) Nat Rev Mol Cell Biol 19, 213-228.
    3. Jeppesen, D.K. et al. (2019) Cell 177, 428-445.e18.
    4. Kowal, J. et al. (2016) Proc Natl Acad Sci U S A 113, E968-77.
    5. Sidhom, K. et al. (2020) Int J Mol Sci 21, 6466. doi: 10.3390/ijms21186466.
    6. Patel, G.K. et al. (2019) Sci Rep 9, 5335.
    7. Tauro, B.J. et al. (2012) Methods 56, 293-304.
    8. Hemler, M.E. (2005) Nat Rev Mol Cell Biol 6, 801-11.
    9. de Gassart, A. et al. (2003) Blood 102, 4336-44.
    10. Katoh, K. et al. (2003) J Biol Chem 278, 39104-13.
    11. Chatellard-Causse, C. et al. (2002) J Biol Chem 277, 29108-15.
    12. Baietti, M.F. et al. (2012) Nat Cell Biol 14, 677-85.
    13. Pradhan, A.K. et al. (2020) Cancer Metastasis Rev 39, 769-781.
    14. Katzmann, D.J. et al. (2001) Cell 106, 145-55.
    15. Garrus, J.E. et al. (2001) Cell 107, 55-65.
    16. Zhong, Q. et al. (1998) Cancer Res 58, 2699-702.
    17. Nollen, E.A. and Morimoto, R.I. (2002) J Cell Sci 115, 2809-16.
    18. Zhan, R. et al. (2009) Biochem Biophys Res Commun 387, 229-33.
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