| Code | CSB-RA591359A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
Integrin alpha-2, also known as CD49b or VLA-2 receptor alpha subunit, serves as a critical collagen receptor that mediates cell-extracellular matrix interactions essential for cell adhesion, migration, and signaling. This integrin subunit plays fundamental roles in platelet function, wound healing, and tissue homeostasis, while its dysregulation has been implicated in cancer progression and metastasis, making it a significant target for researchers investigating cell adhesion biology, tumor microenvironment dynamics, and platelet disorders.
This recombinant monoclonal antibody, clone 5G2, offers the reproducibility and consistency that demanding experimental workflows require. Produced using recombinant technology with a defined sequence, this rabbit IgG antibody eliminates the lot-to-lot variability that can compromise longitudinal studies or multi-site collaborations. The affinity-purified format ensures high specificity for your target while minimizing background interference.
Validation studies demonstrate robust performance across multiple applications. In western blot analysis, the antibody successfully detects integrin alpha-2 in diverse human cell lines including HEK293, HeLa, MCF-7, A431, and A549 lysates at dilutions of 1:500 to 1:2000. The observed band at approximately 150 kDa, slightly higher than the predicted 129 kDa molecular weight, reflects the extensive glycosylation characteristic of this cell surface receptor. For tissue-based studies, immunohistochemistry validation in paraffin-embedded human cervical cancer tissue confirms reliable detection at dilutions of 1:50 to 1:200, with optimized protocols using citrate buffer antigen retrieval.
Whether investigating integrin-mediated signaling pathways, characterizing tumor cell adhesion properties, or exploring platelet biology, this antibody provides a dependable tool for advancing your research into cell-matrix interactions and their pathological implications.
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