| Application | Recommended Dilution |
|---|---|
| IHC | 1:20-1:200 |
| IF | 1:20-1:200 |
| FC | 1:20-1:200 |
HMGB1 (High Mobility Group Box 1) serves as a critical nuclear protein with dual functionality in chromatin architecture and inflammatory signaling. Within the nucleus, HMGB1 facilitates DNA bending and stabilizes nucleosome formation, while its extracellular release acts as a damage-associated molecular pattern (DAMP) that triggers innate immune responses. This positions HMGB1 at the intersection of epigenetics, cell stress, and inflammation research, making it a valuable target for studies spanning cancer biology, autoimmunity, and sepsis.
This recombinant monoclonal antibody (clone 1E7) offers the reproducibility that demanding experimental workflows require. Because recombinant production ensures a sequence-defined, consistent reagent across every lot, researchers can confidently compare results across extended studies without the variability inherent to traditional hybridoma-derived antibodies. The mouse IgG2a isotype and affinity-purified formulation further support clean, specific detection in human samples.
Validation data demonstrates reliable performance across multiple platforms. Immunohistochemistry staining of paraffin-embedded human salivary gland tissue at 1:100 dilution reveals clear target localization using standard citrate-based antigen retrieval. Immunofluorescence analysis in HeLa cells at 1:200 shows distinct nuclear signal when counter-stained with DAPI, consistent with HMGB1's expected subcellular distribution. Flow cytometry experiments using fixed and permeabilized HeLa cells confirm specific detection with clear separation from isotype control, supporting quantitative single-cell analyses.
The antibody's compatibility with ELISA, immunohistochemistry, immunofluorescence, and flow cytometry provides flexibility for researchers investigating HMGB1 across tissue sections, cultured cells, and protein-based assays. This versatility makes it well-suited for epigenetics and nuclear signaling studies where consistent, multi-platform detection of this important chromatin-associated protein is essential.
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