LAMP2A Antibody / Chaperone-Mediated Autophagy Receptor Antibody [clone DIE-12] (RQ5402)

LAMP2A Antibody Human Liver Cancer IHC. Immunohistochemical staining of FFPE human liver cancer tissue using LAMP2A antibody demonstrated predominantly cytoplasmic staining consistent with the lysosomal localization of LAMP2A. Heat-induced epitope retrieval was performed by boiling tissue sections in pH6, 10 mM citrate buffer for 10-20 minutes followed by cooling prior to staining. The observed staining pattern is consistent with expression of the chaperone-mediated autophagy receptor in malignant hepatic cells. This LAMP2A Antibody, also called a Chaperone-Mediated Autophagy Receptor Antibody, is useful for investigating lysosomal biology, chaperone-mediated autophagy, and protein quality control in cancer tissues.

LAMP2A Antibody Human Choriocarcinoma Cell WB. Western blot testing of human JAR choriocarcinoma cell lysate using LAMP2A antibody detected a prominent band at approximately 100-110 kDa. Although the predicted core protein is smaller, LAMP2A is extensively N-linked glycosylated, producing an apparent molecular weight that commonly ranges from approximately 45-110 kDa depending on cell type and glycosylation status. The strong high-molecular-weight band observed is consistent with the mature glycosylated form of LAMP2A. This LAMP2A Antibody, also called a Chaperone-Mediated Autophagy Receptor Antibody, is suitable for studies of chaperone-mediated autophagy, lysosomal biology, and protein quality control.

LAMP2A Antibody Human Small Cell Lung Cancer IHC. Immunohistochemical staining of FFPE human small cell lung cancer tissue using LAMP2A antibody demonstrated predominantly cytoplasmic staining in tumor cells, consistent with the lysosomal localization of LAMP2A. Heat-induced epitope retrieval was performed by boiling tissue sections in pH6, 10 mM citrate buffer for 10-20 minutes followed by cooling prior to staining. The staining pattern is consistent with expression of the chaperone-mediated autophagy receptor in malignant pulmonary tissue. This LAMP2A Antibody, also called a Chaperone-Mediated Autophagy Receptor Antibody, is useful for investigating lysosomal function, chaperone-mediated autophagy, and cancer cell stress responses.

LAMP2A Antibody Human Pituitary Tumor IHC. Immunohistochemical staining of FFPE human pituitary tumor tissue using LAMP2A antibody demonstrated predominantly cytoplasmic staining in neoplastic cells, consistent with the lysosomal localization of LAMP2A. Heat-induced epitope retrieval was performed by boiling tissue sections in pH6, 10 mM citrate buffer for 10-20 minutes followed by cooling prior to staining. The widespread cytoplasmic immunoreactivity is consistent with expression of the chaperone-mediated autophagy receptor in pituitary tumor tissue. This LAMP2A Antibody, also called a Chaperone-Mediated Autophagy Receptor Antibody, is useful for investigating lysosomal biology, chaperone-mediated autophagy, and neuroendocrine tumor biology.

LAMP2A Antibody Human and Rat WB. Western blot testing of human HeLa (lane 1) and rat spleen (lane 2) lysates using LAMP2A antibody detected a prominent band at approximately 110 kDa in both samples. Although the predicted core protein is smaller, LAMP2A undergoes extensive N-linked glycosylation, resulting in an apparent molecular weight that commonly ranges from approximately 45-110 kDa depending on the degree of glycosylation and cell type. The observed bands are consistent with the mature glycosylated form of LAMP2A. This LAMP2A Antibody, also called a Chaperone-Mediated Autophagy Receptor Antibody, is suitable for studies of chaperone-mediated autophagy, lysosomal biology, and cellular protein homeostasis.

LAMP2A Antibody Mouse and Rat Liver WB. Western blot testing of mouse liver (lane 1) and rat liver (lane 2) tissue lysates using LAMP2A antibody detected a prominent band at approximately 100-110 kDa in both samples. Although the predicted core protein is smaller, LAMP2A undergoes extensive N-linked glycosylation, resulting in an apparent molecular weight that commonly ranges from approximately 45-110 kDa depending on glycosylation status and tissue type. The observed bands are consistent with the mature glycosylated form of LAMP2A. This LAMP2A Antibody, also called a Chaperone-Mediated Autophagy Receptor Antibody, is suitable for studies of chaperone-mediated autophagy, lysosomal biology, and protein homeostasis.