IL-13R alpha 1(Phospho Tyr405) Polyclonal Antibody

The protein encoded by this gene is a subunit of the interleukin 13 receptor. This subunit forms a receptor complex with IL4 receptor alpha, a subunit shared by IL13 and IL4 receptors. This subunit serves as a primary IL13-binding subunit of the IL13 receptor, and may also be a component of IL4 receptors. This protein has been shown to bind tyrosine kinase TYK2, and thus may mediate the signaling processes that lead to the activation of JAK1, STAT3 and STAT6 induced by IL13 and IL4.

The IL-13R alpha 1(Phospho Tyr405) Polyclonal Antibody is a highly specific and sensitive tool designed for the detection and quantification of IL-13R alpha 1 protein phosphorylated at Tyr405 residue. This antibody is produced using advanced polyclonal antibody technology, ensuring high affinity and specificity towards the target protein.

IL-13R alpha 1 is a crucial receptor involved in the signaling pathway of interleukin-13 (IL-13), a cytokine that plays a significant role in various physiological and pathological processes. Phosphorylation of Tyr405 residue in IL-13R alpha 1 has been shown to modulate its activity and downstream signaling events.

The IL-13R alpha 1(Phospho Tyr405) Polyclonal Antibody has been rigorously validated for its performance in various applications, including Western blotting, immunohistochemistry, and immunofluorescence. It exhibits exceptional sensitivity and specificity, enabling accurate and reliable detection of phosphorylated IL-13R alpha 1 protein in complex biological samples.

This antibody is supplied as a purified and lyophilized form, ensuring long-term stability and ease of storage. It is compatible with a wide range of experimental conditions and can be used in both research and clinical settings.

In summary, the IL-13R alpha 1(Phospho Tyr405) Polyclonal Antibody is a valuable tool for researchers and clinicians studying the IL-13 signaling pathway. Its high specificity, sensitivity, and versatility make it an essential component in the investigation of IL-13R alpha 1 phosphorylation and its functional implications.