Lysosomes are membrane-bound organelles essential to cell metabolism. They contain hydrolytic enzymes capable of digesting nearly all types of biomolecules including unused proteins, damaged organelles, and other unwanted materials in the cytoplasm from outside and inside the cell.

As a critical step in the autophagic pathway, an autophagosome containing cellular materials to be disposed fuses with a lysosome, and the contents of the autophagosome are degraded by the lysosome’s hydrolytic enzymes. This process is necessary for healthy cell function, and the failure of autophagy is responsible for a majority of cell damage accumulation and aging.

Lysosome marker antibodies detect proteins specific to the lysosome and can aid in the study of the structure and functions of lysosomes. Lysosome marker antibodies can also help elucidate the role or roles a protein may play in a number of tasks that are centered in or influenced by the lysosome.  Additionally, lysosome marker antibodies are useful as tools to track the fusion of the lysosome with the autophagosome just before degradation of the autolysosome contents. Quality Invitrogen lysosome marker antibodies are available for your research needs.

Lysosome marker antibody targets

  • ADRB2
  • BECN1
  • CD34
  • CD63
  • CD68
  • CXCR4
  • IGF2R
  • LAMP1
  • LAMP2
  • MPO
  • PDGFRB
  • RAB9A
  • SERPINB14
  • TLR3
  • TLR7

Featured product data

Immunohistochemistry detection of RAB9 on normal deparaffinized human tonsil tissue tissues. To expose target proteins, heat-induced antigen retrieval was performed using 10 mM sodium citrate (pH 6.0) buffer, microwaved for 8–15 minutes. Following antigen retrieval tissues were blocked in 3% BSA-PBS for 30 minutes at room temperature. Tissues were then probed at a dilution of 1:100 with a mouse monoclonal antibody recognizing RAB9 (Cat. No. MA3-067) or without primary antibody (negative control) overnight at 4°C in a humidified chamber. Tissues were washed extensively with PBST and endogenous peroxidase activity was quenched with a peroxidase suppressor. Detection was performed using a biotin-conjugated secondary antibody and SA-HRP, followed by colorimetric detection using DAB. Tissues were counterstained with hematoxylin and prepped for mounting.


Immunofluorescent analysis of RAB9 using a RAB9 antibody shows staining in HeLa cells. RAB9 (green), F-actin staining with Phalloidin (red), and nuclei with DAPI (blue) is shown. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (negative control) or with an antibody recognizing RAB9 (Cat. No. MA3-067) at a dilution of 1:200 overnight at 4°C, washed with PBS and incubated with a DyLight 488−conjugated secondary antibody (Cat. No. 35552 for GAR; Cat. No. 35503 for GAM). Images were taken at 60x magnification.


Western blot analysis of LAMP1. Analysis was performed by loading 20 µg of HeLa cell lysate and 5 µL of a protein ladder per well onto a 4–12% Bis-Tris polyacrylamide gel. Proteins were transferred to a nitrocellulose membrane and blocked with 5% BSA/TBST for at least 1 hour. The membrane was probed with an anti-LAMP1 polyclonal antibody (Cat. No. PA1-654A) at a dilution of 1:500 for one hour at room temperature, washed in TBS-0.1% Tween 20, and probed with a goat anti-rabbit IgG-Poly HRP secondary antibody (Cat. No. 32260) at a dilution of 1:100,000 for 1 hour. Chemiluminescent detection was performed using Thermo Scientific SuperSignal West Dura Extended Duration Substrate (Cat. No. 34075).


Annotated product references

Cat. No. MA3-067 was used in immunocytochemistry and western blot to study the interaction of the TIP47 lipid droplet-binding protein with HCV NS5A and the role of this interaction in the regulation of viral RNA replication. Vogt DA, Camus G, Herker E et al. (2013) Lipid droplet-binding protein TIP47 regulates hepatitis C Virus RNA replication through interaction with the viral NS5A protein. PLos Pathog 9:e1003302.

Cat. No. PA1-654A was used in immunocytochemistry to investigate the effect of retromer malfunction on amyloidogenic APP processing. Sullivan CP, Jay AG, Stack EC et al. (2011) Retromer disruption promotes amyloidogenic APP processing. 43:338−345.