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Recombinant Mouse Anti-LAMP2 Antibody (CBHb367) (CBMAB-Hb634-LY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBHb367
Antibody Isotype
IgG2b
Application
FC, Immuno assays

Basic Information

Immunogen
Lamp-2 protein
Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
0.1% BSA
Preservative
0.02% sodium azide
Concentration
0.1 mg/ml
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
LAMP2
Entrez Gene ID
3920
UniProt ID
P13473
Alternative Names
Lysosome-associated membrane glycoprotein 2, Lysosome-associated membrane protein 2, CD107 antigen-like family member B, LGP-96
Function
Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live (PubMed:8662539, PubMed:11082038, PubMed:18644871, PubMed:24880125, PubMed:27628032).
Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them for lysosomal degradation (PubMed:8662539, PubMed:11082038, PubMed:18644871, PubMed:24880125).
Plays a role in lysosomal protein degradation in response to starvation (By similarity).
Required for the fusion of autophagosomes with lysosomes during autophagy (PubMed:27628032).
Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes (PubMed:27628032).
Required for normal degradation of the contents of autophagosomes (PubMed:27628032).
Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits (PubMed:20518820).
Is not required for efficient MHCII-mediated presentation of endogenous antigens (PubMed:20518820).
Isoform LAMP-2C
Modulates chaperone-mediated autophagy. Decreases presentation of endogenous antigens by MHCII. Does not play a role in the presentation of exogenous and membrane-derived antigens by MHCII.
(Microbial infection) Supports the FURIN-mediated cleavage of mumps virus fusion protein F by interacting with both FURIN and the unprocessed form but not the processed form of the viral protein F.
Biological Process
Autophagosome maturationISS:UniProtKB
Cellular response to starvationISS:UniProtKB
Chaperone-mediated autophagyManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Establishment of protein localization to organelleManual Assertion Based On ExperimentIBA:GO_Central
Lysosomal protein catabolic processManual Assertion Based On ExperimentIMP:UniProtKB
Muscle cell cellular homeostasisIEA:Ensembl
Negative regulation of protein-containing complex assemblyIDA:ParkinsonsUK-UCL
Protein importManual Assertion Based On ExperimentTAS:ParkinsonsUK-UCL
Protein stabilizationISS:CAFA
Protein targetingISS:UniProtKB
Protein targeting to lysosome involved in chaperone-mediated autophagyManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of protein stabilityManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Cellular Location
Cell membrane
Endosome membrane
Lysosome membrane
Cytoplasmic vesicle, autophagosome membrane
This protein shuttles between lysosomes, endosomes, and the plasma membrane.
Involvement in disease
Danon disease (DAND):
DAND is a lysosomal glycogen storage disease characterized by the clinical triad of cardiomyopathy, vacuolar myopathy and mental retardation. It is often associated with an accumulation of glycogen in muscle and lysosomes.
Topology
Lumenal: 29-375
Helical: 376-399
Cytoplasmic: 400-410
PTM
O- and N-glycosylated; some of the 16 N-linked glycans are polylactosaminoglycans.
More Infomation

Yam, J. C., Zhang, X. J., Zhang, Y., Yip, B. H., Tang, F., Wong, E. S., ... & Pang, C. P. (2023). Effect of low-concentration atropine eyedrops vs placebo on myopia incidence in children: the LAMP2 randomized clinical trial. JAMA, 329(6), 472-481.

Liu, D., Xing, R., Zhang, Q., Tian, X., Qi, Y., Song, H., ... & Han, Y. (2023). The CREG1-FBXO27-LAMP2 axis alleviates diabetic cardiomyopathy by promoting autophagy in cardiomyocytes. Experimental & Molecular Medicine, 55(9), 2025-2038.

Rodrigues, P. M., Sousa, L. G., Perrod, C., Maceiras, A. R., Ferreirinha, P., Pombinho, R., ... & Alves, N. L. (2023). LAMP2 regulates autophagy in the thymic epithelium and thymic stroma-dependent CD4 T cell development. Autophagy, 19(2), 426-439.

Alcalai, R., Arad, M., Wakimoto, H., Yadin, D., Gorham, J., Wang, L., ... & Seidman, C. E. (2021). LAMP2 cardiomyopathy: consequences of impaired autophagy in the heart. Journal of the American Heart Association, 10(17), e018829.

Huang, P. S., Lin, Y. H., Chi, H. C., Tseng, Y. H., Chen, C. Y., Lin, T. K., ... & Lin, K. H. (2020). Dysregulated FAM215A stimulates LAMP2 expression to confer drug-resistant and malignant in human liver cancer. Cells, 9(4), 961.

Ye, G., Wu, H., Huang, J., Wang, W., Ge, K., Li, G., ... & Huang, Q. (2020). LAMP2: a major update of the database linking antimicrobial peptides. Database, 2020, baaa061.

Cui, L., Zhao, L. P., Ye, J. Y., Yang, L., Huang, Y., Jiang, X. P., ... & Huang, Y. (2020). The lysosomal membrane protein Lamp2 alleviates lysosomal cell death by promoting autophagic flux in ischemic cardiomyocytes. Frontiers in Cell and Developmental Biology, 8, 31.

Notomi, S., Ishihara, K., Efstathiou, N. E., Lee, J. J., Hisatomi, T., Tachibana, T., ... & Vavvas, D. G. (2019). Genetic LAMP2 deficiency accelerates the age-associated formation of basal laminar deposits in the retina. Proceedings of the National Academy of Sciences, 116(47), 23724-23734.

Dubois, A., Furstoss, N., Calleja, A., Zerhouni, M., Cluzeau, T., Savy, C., ... & Robert, G. (2019). RETRACTED ARTICLE: LAMP2 expression dictates azacytidine response and prognosis in MDS/AML. Leukemia, 33(6), 1501-1513.

Klaver, A. C., Coffey, M. P., Aasly, J. O., & Loeffler, D. A. (2018). CSF lamp2 concentrations are decreased in female Parkinson’s disease patients with LRRK2 mutations. Brain Research, 1683, 12-16.

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For research use only. Not intended for any clinical use.

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