| Code | CSB-RA111920A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| IHC | 1:50-1:200 |
LAMP2, or lysosome-associated membrane glycoprotein 2, serves as a critical component of the lysosomal membrane where it plays essential roles in autophagy, lysosomal stability, and cellular homeostasis. This heavily glycosylated protein has garnered significant research attention due to its involvement in cardiovascular biology and its utility as a reliable marker for lysosomal compartments. Mutations in LAMP2 are associated with Danon disease, a condition characterized by cardiomyopathy and skeletal muscle weakness, making this target particularly relevant for researchers investigating cardiac pathophysiology and autophagy-related disorders.
This recombinant monoclonal antibody, clone 23G11, offers the reproducibility and consistency that demanding research protocols require. Because the antibody sequence is defined and produced recombinantly in rabbit host cells, researchers can expect uniform performance across experiments and between lot numbers, eliminating the variability often encountered with traditional hybridoma-derived antibodies. The affinity-chromatography purification ensures high purity, while the liquid formulation with glycerol-based buffer supports long-term stability when stored properly at -20°C or -80°C.
Validation in immunohistochemistry demonstrates reliable detection of LAMP2 in human placenta tissue using a standard paraffin-embedded workflow with citrate buffer antigen retrieval. At a 1:100 dilution, the antibody produced clear staining using HRP-polymer detection and DAB visualization on an automated Leica Bond system, confirming its suitability for routine histological applications. The recommended working range of 1:50 to 1:200 provides flexibility for optimization across different tissue types and detection systems.
This antibody supports researchers studying lysosomal biology, autophagy mechanisms, and cardiovascular disease pathways where LAMP2 function is implicated.
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