Anti-EYA4, NT (Eyes Absent Homolog 4)

EYA4 is thought to play a role in transcription regulation during organogenesis through its intrinsic protein phosphatase activity. It may be involved in development of the eye and for continued function of the mature organ of Corti. The haloacid dehalogenase domain at the C terminus of Eya4 contains the tyrosine-phosphatase activity (that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph)), and the N-terminal half carries the threonine-phosphatase activity. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. EYA4 promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. Mutations of the threonine-phosphatase, but not the tyrosine-phosphatase, abolished the ability of Eya4 to enhance the innate immune response, suggesting that EYA proteins regulate the innate immune response by modulating the phosphorylation state of signal transducers for intracellular pathogens. Mutations in EYA4 are associated with postlingual, progressive, autosomal dominant hearing loss at the deafness, autosomal dominant nonsyndromic sensorineural 10 locus. Defects in this gene are also associated with dilated cardiomyopathy 1J. Four transcript variants encoding distinct isoforms have been identified. Applications: Suitable for use in ELISA and Immunohistochemistry. Other applications not tested. Recommended Dilution: ELISA: 1:128,000, Immunohistochemistry (Formalin fixed paraffin embedded): 3.75ug/ml, Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.