{"product_id":"new-product-571754","title":"Phospho-Caspase-1 (S376) Polyclonal Antibody","description":"\u003cp\u003eCASP1 (caspase 1) encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. CASP1 was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. CASP1 has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing results in transcript variants encoding distinct isoforms.\u003c\/p\u003e\n\u003cp\u003eIntroducing the Phospho-Caspase-1 (S376) Polyclonal Antibody, a cutting-edge scientific tool meticulously designed to facilitate advanced research in the field of molecular biology. This antibody, derived from a polyclonal source, exhibits exceptional specificity and sensitivity, enabling precise detection and analysis of the phosphorylated form of Caspase-1 at serine 376 residue.\u003cbr\u003e\u003cbr\u003eCrafted with utmost precision and utilizing state-of-the-art technology, this antibody offers researchers an invaluable resource to unravel the intricate mechanisms underlying Caspase-1 activation and its subsequent involvement in various cellular processes. By targeting the phosphorylated form of Caspase-1, this antibody empowers investigators to delve deeper into the intricate signaling pathways and regulatory networks governing cellular responses.\u003cbr\u003e\u003cbr\u003eThe Phospho-Caspase-1 (S376) Polyclonal Antibody boasts an array of remarkable features that set it apart from conventional alternatives. Its exceptional specificity ensures minimal cross-reactivity, thereby guaranteeing accurate and reliable results. Furthermore, its high sensitivity enables the detection of even low levels of phosphorylated Caspase-1, facilitating the exploration of subtle molecular events.\u003cbr\u003e\u003cbr\u003eThis antibody has been rigorously validated through a series of stringent quality control measures, ensuring its consistent performance and reproducibility. Its compatibility with various experimental techniques, including Western blotting, immunohistochemistry, and immunofluorescence, further enhances its versatility and utility across diverse research applications.\u003cbr\u003e\u003cbr\u003eResearchers can confidently rely on the Phospho-Caspase-1 (S376) Polyclonal Antibody to unravel the intricate complexities of Caspase-1 phosphorylation, shedding light on its functional implications in cellular processes such as inflammation, apoptosis, and immune responses. By harnessing the power of this antibody, scientists can unlock novel insights into the fundamental mechanisms governing cellular homeostasis and disease pathogenesis.\u003cbr\u003e\u003cbr\u003eIn summary, the Phospho-Caspase-1 (S376) Polyclonal Antibody stands as an indispensable tool for researchers seeking to unravel the intricate intricacies of Caspase-1 phosphorylation. With its exceptional specificity, sensitivity, and compatibility with various experimental techniques, this antibody empowers scientists to delve deeper into the fascinating world of molecular biology, paving the way for groundbreaking discoveries and advancements in the field.\u003c\/p\u003e","brand":"BT Lab","offers":[{"title":"100ul \/ Rabbit \/ Primary antibody","offer_id":47543047979288,"sku":"BT-PHS00749","price":275.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0590\/5652\/1400\/products\/BT_Lab_7af526a9-853d-4c88-a0a0-f014fdc59a7f.png?v=1705642749","url":"https:\/\/danabiosci.com\/products\/new-product-571754","provider":"Dana Bioscience","version":"1.0","type":"link"}