BT Lab
SKU:BT-AP02319
CUL-4B Polyclonal Antibody
CUL-4B Polyclonal Antibody
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CUL4B is a member of the cullin family. The cullin 4B forms a complex that functions as an E3 ubiquitin ligase and catalyzes the polyubiquitination of specific protein substrates in the cell. The protein interacts with a ring finger protein, and is required for the proteolysis of several regulators of DNA replication including chromatin licensing and DNA replication factor 1 and cyclin E. Multiple transcript variants encoding different isoforms have been found for this gene.
The CUL-4B Polyclonal Antibody is a highly specific and reliable tool designed for the detection and analysis of CUL-4B protein expression in various biological samples. This antibody has been meticulously developed using advanced immunization techniques and exhibits exceptional sensitivity and specificity.
CUL-4B, also known as Cullin-4B, is a crucial component of the Cullin-RING E3 ubiquitin ligase complex. It plays a pivotal role in regulating protein degradation and turnover by targeting specific substrates for ubiquitination and subsequent proteasomal degradation. Dysregulation of CUL-4B has been implicated in various pathological conditions, including cancer, neurodevelopmental disorders, and intellectual disabilities.
The CUL-4B Polyclonal Antibody has been extensively validated for its performance in various applications, including Western blotting, immunohistochemistry, and immunofluorescence. It exhibits excellent reactivity across a wide range of species, including human, mouse, and rat, making it a versatile tool for diverse research needs.
This antibody is manufactured using high-quality materials and undergoes rigorous quality control measures to ensure batch-to-batch consistency and reproducibility. It is supplied as a liquid formulation in a convenient size, allowing for easy handling and storage.
In summary, the CUL-4B Polyclonal Antibody is a reliable and specific tool for the detection and analysis of CUL-4B protein expression. Its exceptional performance and versatility make it an invaluable asset for researchers studying the intricate mechanisms of protein degradation and its implications in various diseases.
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