+1 877 302 8632
+1 888 205 9894 (Toll-free)

Protein Exosome Marker

Written/Edited by Dr. Stefan Pellenz, PhD

Exosomes are small (50-120nm) endosome derived extracellular microvesicles (EMV). They can contain a vast array of different proteins depending on their host cell which, and their components are further modulated by cellular state (e.g. stress or activation, or inhibition of specific signaling pathways).

What are Exosomes?

exosome biogenesis and protein markers

Exosome biogenesis (A) and protein exosome markers (B).

Exosomes were first observed in the early 1980s in the culture media of reticulocytes. They are produced in inward budding multivesicular bodies (MVBs). The resulting intra-luminal vesicles (ILV) are then released through exocytosis into the extracellular space. Based on early observations of this phenomena, the term “exosomes” was coined for such vesicles. Exosomes share similar topology to the plasma membrane and are released by virtually all cell types and have been confirmed in all bodily fluids (see Fig. A).

Get our exosome marker poster!

By clicking on the link below, you can download a copy of our Exosome poster as a PNG file.

Download a Copy
CD63 antibody  (AA 120-175) CD63 antibody  (AA 120-175) CD63 antibody (AA 120-175) (ABIN1440014)
  • Polyclonal CD63 antibody
  • For IF and Western Blotting
  • 5 PubMed References
  • In stock, fast delivery
CD24 antibody  (APC) CD24 antibody  (APC) CD24 antibody (APC) (ABIN2749227)
  • Monoclonal Antibody (SN3)
  • Conjugated to APC
  • 6 PubMed References
CD9 antibody CD9 antibody CD9 antibody (ABIN969030)
  • Monoclonal Antibody (5G6) to CD9
  • 2 PubMed References
  • In stock, fast delivery
CD81 antibody CD81 antibody CD81 antibody (ABIN2855163)
  • Polyclonal antibody to CD81
  • For ICC, FACS, IF, WB, IHC
  • 2 PubMed References
  • In stock, fast delivery

How are Exosomes Identified?

Exosomes can contain a vast array of different proteins depending on their host cell which, and their components are further modulated by cellular state (e.g. stress or activation, or inhibition of specific signaling pathways). Tetraspanins like CD9, CD63 and CD81 are the most common canonical exosome marker proteins, present on the vesicle surface. Surface localization of tetraspanin antigens makes them good candidate targets for immunolabeling and purification of exosomes from biological samples. Components of the endosomal sorting complex required for transport (ESCRT) like TSG101 and Alix, cytoskeletal proteins, integrins and annexins are also enriched on exosomes; these molecules play a pivotal role in exosome targeting and cell adhesion (see Fig. B).

Exosome Targets

How are Exosomes Studied?

The exosome secretome is vast and diverse, containing many different markers (see However, the presence of canonical surface markers like those listed abovepermit purification and in-depth study of exosome secretion and content from different sample types.

antibodies-online offers a range of kits for exosome purification and quantification from human biological fluids (plasma, serum, urine, saliva) or cell-culture media. We also offer kits intended for extraction and purification of RNA and DNA from exosomes. In addition to pre-generated assay kits, antibodies-online supplies you with a comprehensive selection of antibodies directed against known exosome proteins (see table).

Exosome Marker Antibodies

Protein Gene GeneID Uniprot Ref exocarta Top 100 proteins TS EF LP TA CS AG MT AP HS EN RG CA II VI ND
14-3-3 protein epsilon YWHAE 7531 P62258 - 22 X
14-3-3 protein zeta/delta YWHAZ 7534 P63104 - 15 X
78 kDa glucose-regulated protein HSPA5 3309 P11021 (1) 35 X
Actin, cytoplasmic 1 ACTB 60 P60709 - 5 X
ADAM10 ADAM10 102 O14672 (2) - X X X X
Alix PDCD6IP 10015 Q8WUM4 (3) 2 X
Alpha-Enolase ENO1 2023 P06733 (4) 9 X
Alpha-Synclein SNCA 6622 P37840 (32) - X X
Aminopeptidase N ANPEP 290 P15144 - - X X
Beta-amyloid APP 351 P05067 (5) - X
Annexin A5 ANXA5 308 P08758 (6) 20 X X
Annexin A2 ANXA2 302 P07355 (7) 6 X
AP-1 JUN 3725 P05412 - - X X
ATP citrate lyase ACLY 47 P53396 - 72 X
ATPase ATP1A1 476 P05023 - 39 X
Basigin BSG 682 P35613 (8) - X X
Caveolin-1 CAV1 857 Q03135 (9), (10) - X X
CD9 CD9 928 P21926 (11) 1 X
CD11a ITGAL 3683 P20701 (12) - X X
CD11b ITGAX 3687 P11215 (12) - X X
CD11c ITGAM 3684 P20702 (12) - X X
CD29 ITGB1 3688 P05556 (12) 34 X X
CD37 CD37 951 P11049 (11) - X
CD44 CD44 960 P16070 (13) - X X
CD49f ITGA6 3655 P23229 (12) 89 X X
CD63 CD63 967 P08962 (10), (11) 7 X X
CD81 CD81 975 P60033 (14) 24 X X
CD82 CD82 3732 P27701 (11) - X
CD142 TF 2152 P13726 (15) - X X
CD146 MCAM 4162 P43121 (15) - X X
CD163 CD163 9332 Q86VB7 (15) - X X X
Clathrin heavy chain 1 CLTC 1213 Q00610 - 23 X
Claudin-1 CLDN1 9076 O95832 (8) - X
Cofilin-1 CFL1 1072 P23528 - 25 X
- - (16) - X
- - (16) - X
EF-1-alpha-1 EEF1A1 1915 P68104 (4) 14 X
EF2 EEF2 1938 P13639 - 17 X
EGFR EGFR 1956 P00533 (15) - X
Ep-CAM EPCAM 4072 P16422 (17), (18) - X X
Fatty acid synthase FASN 2194 P49327 (3) 21 X X
Flotillin-1 FLOT1 10211 O75955 (18), (19) 41 X X
Flotillin-2 FLOT2 2319 Q14254 (19) - X
Fructose-bisphosphate aldolase A ALDOA 226 P04075 - 18 X
Glyceraldehyde-3-phosphate dehydrogenase GAPDH 2597 P04406 - 4 X
HCV core protein - - (20) - X
Heat shock protein HSP 90-alpha HSP90AA1 3320 P07900 (1) 10 X X
Heat shock protein HSP 90-beta HSP90AB1 3326 P08238 (1) 19 X
Heparanase HPSE 10855 Q9Y251 (21) - X X
- - (20) - X
- - (20) - X
HLA-DRA HLA-DRA 3122 P01903 (22) - X X X
HLA-G 3135 P17693 (23) - X X X
Hsc70 HSPA8 3312 P11142 (1) 3 X
- - (16) - X
Tax - - (20) - X
Huntingtin HTT 3064 P42858 (5) - X X
ICAM-1 ICAM1 3383 P05362 (24) - X
Leucine-rich receptor kinase 2 LRRK2 120892 Q5S007 (5) - X
L-lactate dehydrogenase A chain LDHA 3939 P00338 - 13 X
Lysosome-associated membrane glycoprotein 1 LAMP1 3916 P11279 (25) - X X
Lysosome-associated membrane glycoprotein 2 LAMP2 3920 P13473 (23) 88 X X
MHCI - - (26) - X X
- - (26) - X X
MUC1 MUC1 4582 P15941 (15) - X X
N-cadherin CDH2 1000 P19022 (15) - X X
Phosphoglycerate kinase 1 PGK1 5230 P00558 (4) 16 X
Placental Alkaline Phosphatase ALPP 250 P05187 (15) - X X
Prion proteins - - (5) - X
Prostate-specific antigen KLK3 354 P07288 (27) - X X
Pyruvate kinase PKM PKM 5315 P14618 (28) 12 X X
Rab-14 RAB14 51552 P61106 - 75 X
Rab-5a RAB5A 5868 P20339 - 80 X
Rab-5b RAB5B 5869 P61020 - 86 X
Rab-5c RAB5C 5878 P51148 - 64 X
Rab-7 RAB7A 7879 P51149 - 61 X
Rap 1B RAP1B 5908 P61224 - 33 X
Syndecan-1 SDC1 6382 P18827 (29) - X
Syndecan-4 SDC4 6385 P31431 (29) - X
Syntenin-1 SDCBP 6386 O00560 (30) 8 X
Tumor-Associated Glycoprotein TAG-72 - - (15) - X
Tetraspanin-8 Tspan8 7103 P19075 (15) - X X
Tsg101 TSG101 7251 Q99816 (31) 11 X
Vacuolar-sorting protein 35 VPS35 55737 Q96QK1 (5) - X X

Get our exosome marker poster!

By clicking on the link below, you can download a copy of our Exosome poster as a PNG file.

Download a Copy

Why are Exosomes important?

Secretion of exosomes occurs constitutively though the rate of exosome secretion, and composition of exosomes may be augmented by a variety of intrinsic or extrinsic factors (e.g. cell stress, signaling cascades). Despite their ubiquitous nature, exosomes are considered unconventional secretory pathway components.

Because exomes are secreted from nearly every cell type, their composition mirrors their host diversity, and depends heavily upon the type of cell from which they originate.

Since the molecular composition of exosomes is reflective of physiological or pathophysiological changes in their cell or tissue of origin, studying exosome composition offers a significant potential to develop new biomarkers for disease diagnosis (see Table).

SARS-CoV-2: Exploitation of Exosome Transport

It has been suggested that SARS-CoV-2 may exploit the exosome transport based on studies showing that SARS-CoV is released from infected cell by exocyotosis. SARS-CoV-2 Nsp3, Nsp4, and Nsp6 also induce the formation of double-membrane vesicles (DMVs), suggesting a connection a role of exosomes in virus propagation. This might also enable the virus to evade immune detection and explain apparent reinfection of convalescent COVID-19 patients. 33, 34, 35

Exosomes are also a widely-implicated in cell-cell communication. Exosome components may be transferred directly to neighboring cells, or may be shuttled across a number of different cells before reaching their end destination via a method known as transcytosis. Exosomes can, therefore, be used to transmit signals across large distances where simple diffusion may be insufficient. Their role in cell-cell communication suggests that exosomes may have a deeper role in many physiological processes; this hypothesis is supported by the observation that exosome signaling plays a direct role in development & patterning, immune response, neuronal communication, and tissue repair.

Because of their small size (nano-scale) and simple structure, exosomes may sometimes cross the blood-brain barrier. Various futurists have suggested that exosome delivery systems may offer an innovative new technology to target the central nervous system and treating various cerebral/neuropathic diseases without necessitating invasive surgery. The use of exosomes to transfer genetic information, or to deliver therapeutic agents is a currently underexplored field that holds vast medicinal potential.

In some pathologies, exosomes also act as vectors; tumor cell-derived exosomes play an active role in tumor angiogenesis and metastasis. Exosomes shed from stimulated blood cells and the vascular endothelium are involved in neurological disorders such as multiple sclerosis, transient ischemic attacks, and antiphospholipid syndrome. Exosomes may also carry damaged cellular material targeted for destruction, in doing so they may facilitate the spreading of toxic forms of aggregated proteins such as α-synuclein, β-amyloid, and prion proteins and contribute to the progression of neurodegenerative diseases. Some research also suggests that exosome transport has been exploited by viral pathogens to travel between host cells and evade immune detection.


  1. Lancaster, Febbraio: "Exosome-dependent trafficking of HSP70: a novel secretory pathway for cellular stress proteins." in: The Journal of biological chemistry, Vol. 280, Issue 24, pp. 23349-55, (2005) (PubMed).
  2. Lin, Li, Huang, Liu, Chen, Chen, Xu, Huang, Wang: "Exosomes: novel biomarkers for clinical diagnosis." in: TheScientificWorldJournal, Vol. 2015, pp. 657086, (2016) (PubMed).
  3. Duijvesz, Burnum-Johnson, Gritsenko, Hoogland, Vredenbregt-van den Berg, Willemsen, Luider, Paša-Tolić, Jenster: "Proteomic profiling of exosomes leads to the identification of novel biomarkers for prostate cancer." in: PloS one, Vol. 8, Issue 12, pp. e82589, (2014) (PubMed).
  4. Yu, Harris, Levine: "The regulation of exosome secretion: a novel function of the p53 protein." in: Cancer research, Vol. 66, Issue 9, pp. 4795-801, (2006) (PubMed).
  5. Kalani, Tyagi: "Exosomes in neurological disease, neuroprotection, repair and therapeutics: problems and perspectives." in: Neural regeneration research, Vol. 10, Issue 10, pp. 1565-7, (2015) (PubMed).
  6. Li, Aliotta, Asara, Tucker, Quesenberry, Lally, Ramratnam: "Quantitative proteomic analysis of exosomes from HIV-1-infected lymphocytic cells." in: Proteomics, Vol. 12, Issue 13, pp. 2203-11, (2012) (PubMed).
  7. Valapala, Vishwanatha: "Lipid raft endocytosis and exosomal transport facilitate extracellular trafficking of annexin A2." in: The Journal of biological chemistry, Vol. 286, Issue 35, pp. 30911-30925, (2011) (PubMed).
  8. Li, Sherman-Baust, Tsai-Turton, Bristow, Roden, Morin: "Claudin-containing exosomes in the peripheral circulation of women with ovarian cancer." in: BMC cancer, Vol. 9, pp. 244, (2009) (PubMed).
  9. Svensson, Christianson, Wittrup, Bourseau-Guilmain, Lindqvist, Svensson, Mörgelin, Belting: "Exosome uptake depends on ERK1/2-heat shock protein 27 signaling and lipid Raft-mediated endocytosis negatively regulated by caveolin-1." in: The Journal of biological chemistry, Vol. 288, Issue 24, pp. 17713-24, (2013) (PubMed).
  10. Logozzi, De Milito, Lugini, Borghi, Calabrò, Spada, Perdicchio, Marino, Federici, Iessi, Brambilla, Venturi, Lozupone, Santinami, Huber, Maio, Rivoltini, Fais: "High levels of exosomes expressing CD63 and caveolin-1 in plasma of melanoma patients." in: PloS one, Vol. 4, Issue 4, pp. e5219, (2009) (PubMed).
  11. Andreu, Yáñez-Mó: "Tetraspanins in extracellular vesicle formation and function." in: Frontiers in immunology, Vol. 5, pp. 442, (2014) (PubMed).
  12. Hoshino, Costa-Silva, Shen, Rodrigues, Hashimoto, Tesic Mark, Molina, Kohsaka, Di Giannatale, Ceder, Singh, Williams, Soplop, Uryu, Pharmer, King, Bojmar, Davies, Ararso, Zhang, Zhang, Hernandez et al.: "Tumour exosome integrins determine organotropic metastasis. ..." in: Nature, Vol. 527, Issue 7578, pp. 329-35, (2015) (PubMed).
  13. Marhaba, Klingbeil, Nuebel, Nazarenko, Buechler, Zoeller: "CD44 and EpCAM: cancer-initiating cell markers." in: Current molecular medicine, Vol. 8, Issue 8, pp. 784-804, (2009) (PubMed).
  14. Welker, Reichert, Susser, Sarrazin, Martinez, Herrmann, Zeuzem, Piiper, Kronenberger: "Soluble serum CD81 is elevated in patients with chronic hepatitis C and correlates with alanine aminotransferase serum activity." in: PloS one, Vol. 7, Issue 2, pp. e30796, (2012) (PubMed).
  15. Jakobsen, Paulsen, Bæk, Varming, Sorensen, Jørgensen: "Exosomal proteins as potential diagnostic markers in advanced non-small cell lung carcinoma." in: Journal of extracellular vesicles, Vol. 4, pp. 26659, (2015) (PubMed).
  16. Meckes, Raab-Traub: "Microvesicles and viral infection." in: Journal of virology, Vol. 85, Issue 24, pp. 12844-54, (2012) (PubMed).
  17. Zhou, Mohamadi, Poudineh, Kermanshah, Ahmed, Safaei, Stojcic, Nam, Sargent, Kelley: "Interrogating Circulating Microsomes and Exosomes Using Metal Nanoparticles." in: Small (Weinheim an der Bergstrasse, Germany), Vol. 12, Issue 6, pp. 727-32, (2016) (PubMed).
  18. Jakobsen, Paulsen, Bæk, Varming, Sorensen, Jørgensen: "Exosomal proteins as potential diagnostic markers in advanced non-small cell lung carcinoma." in: Journal of extracellular vesicles, Vol. 4, pp. 26659, (2015) (PubMed).
  19. Otto, Nichols: "The roles of flotillin microdomains--endocytosis and beyond." in: Journal of cell science, Vol. 124, Issue Pt 23, pp. 3933-40, (2012) (PubMed).
  20. Chahar, Bao, Casola: "Exosomes and Their Role in the Life Cycle and Pathogenesis of RNA Viruses." in: Viruses, Vol. 7, Issue 6, pp. 3204-25, (2016) (PubMed).
  21. Thompson, Purushothaman, Ramani, Vlodavsky, Sanderson: "Heparanase regulates secretion, composition, and function of tumor cell-derived exosomes." in: The Journal of biological chemistry, Vol. 288, Issue 14, pp. 10093-10099, (2013) (PubMed).
  22. Arita, Baba, Shibata, Niiro, Shimoda, Isobe, Kusaba, Nakano, Harada: "B cell activation regulates exosomal HLA production." in: European journal of immunology, Vol. 38, Issue 5, pp. 1423-34, (2008) (PubMed).
  23. Carosella, Rouas-Freiss, Tronik-Le Roux, Moreau, LeMaoult: "HLA-G: An Immune Checkpoint Molecule." in: Advances in immunology, Vol. 127, pp. 33-144, (2015) (PubMed).
  24. Segura, Nicco, Lombard, Veron, Raposo, Batteux, Amigorena, Thery: "ICAM-1 on exosomes from mature dendritic cells is critical for efficient naive T-cell priming." in: Blood, Vol. 106, Issue 1, pp. 216-23, (2005) (PubMed).
  25. Chivet, Javalet, Laulagnier, Blot, Hemming, Sadoul: "Exosomes secreted by cortical neurons upon glutamatergic synapse activation specifically interact with neurons." in: Journal of extracellular vesicles, Vol. 3, pp. 24722, (2014) (PubMed).
  26. Nakayama: "Antigen Presentation by MHC-Dressed Cells." in: Frontiers in immunology, Vol. 5, pp. 672, (2015) (PubMed).
  27. Saini: "PSA and beyond: alternative prostate cancer biomarkers." in: Cellular oncology (Dordrecht), Vol. 39, Issue 2, pp. 97-106, (2016) (PubMed).
  28. Shinohara, Taniguchi, Kumazaki, Yamada, Ito, Otsuki, Uno, Hayakawa, Minami, Naoe, Akao: "Anti-cancer fatty-acid derivative induces autophagic cell death through modulation of PKM isoform expression profile mediated by bcr-abl in chronic myeloid leukemia." in: Cancer letters, Vol. 360, Issue 1, pp. 28-38, (2015) (PubMed).
  29. Baietti, Zhang, Mortier, Melchior, Degeest, Geeraerts, Ivarsson, Depoortere, Coomans, Vermeiren, Zimmermann, David: "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes." in: Nature cell biology, Vol. 14, Issue 7, pp. 677-85, (2012) (PubMed).
  30. Ghossoub, Lembo, Rubio, Gaillard, Bouchet, Vitale, Slavík, Machala, Zimmermann: "Syntenin-ALIX exosome biogenesis and budding into multivesicular bodies are controlled by ARF6 and PLD2." in: Nature communications, Vol. 5, pp. 3477, (2014) (PubMed).
  31. Lee, El Andaloussi, Wood: "Exosomes and microvesicles: extracellular vesicles for genetic information transfer and gene therapy." in: Human molecular genetics, Vol. 21, Issue R1, pp. R125-34, (2013) (PubMed).
  32. Shi, Liu, Cook, Bullock, Zhao, Ginghina, Li, Aro, Dator, He, Hipp, Zabetian, Peskind, Hu, Quinn, Galasko, Banks, Zhang: "Plasma exosomal α-synuclein is likely CNS-derived and increased in Parkinson's disease." in: Acta neuropathologica, Vol. 128, Issue 5, pp. 639-650, (2015) (PubMed).
  33. Qian, Travanty, Oko, Edeen, Berglund, Wang, Ito, Holmes, Mason: "Innate immune response of human alveolar type II cells infected with severe acute respiratory syndrome-coronavirus." in: American journal of respiratory cell and molecular biology, Vol. 48, Issue 6, pp. 742-8, (2013) (PubMed).
  34. Elrashdy, Aljaddawi, Redwan, Uversky: "On the potential role of exosomes in the COVID-19 reinfection/reactivation opportunity." in: Journal of biomolecular structure & dynamics, Vol. 39, Issue 15, pp. 5831-5842, (2021) (PubMed).
  35. Farkash, Wilson, Jentzen: "Ultrastructural Evidence for Direct Renal Infection with SARS-CoV-2." in: Journal of the American Society of Nephrology : JASN, Vol. 31, Issue 8, pp. 1683-1687, (2020) (PubMed).
Stefan Pellenz
Dr. Stefan Pellenz, PhD
Product Manager at

Goal-oriented, time line driven scientist, proficiently trained in different academic institutions in Germany, France and the USA. Experienced in the life sciences e-commerce environment with a focus on product development and customer relation management.

Go to author page
You are here: