STAT1, also known as STAT1a, is a transcription factor and member of the STAT protein family with roles in innate and adaptive immunity.{53705} It is composed of an N-terminal domain that is essential to protein-protein interactions and dimerization, a DNA binding domain that facilitates nuclear import and export, as well as DNA binding, a linker domain, tail segment, and a transactivation domain that facilitates transcription of target genes.{53706} STAT1B is an isoform of STAT1 that is formed by alternative splicing and lacks the 38-amino acid transactivation domain.{53707} Upon phosphorylation by JAKs, STAT1 dimerizes and is translocated to the nucleus to activate transcription of IFN-y-inducible genes.{53708} Because the C-terminal transactivation domain is required for STAT1 interaction with the transcriptional coactivator CREB-binding protein (CBP)/p300 and gene transcription, STAT1B is considered a dominant-negative regulator of STAT1 and overexpression of STAT1B inhibits IFN-y-induced gene expression in RAW 264.7 cells. STAT1B phosphorylation is increased and IFN-y-induced JAK1, JAK2, and STAT1 activation is decreased in RAW 264.6 cells infected with L. major and L. mexicana parasites, as well as M. avium bacteria.{53708,53709} STAT1B protein levels are reduced in patient-derived esophageal squamous cell carcinoma (ESCC) tumor samples and are positively correlated with lymph node metastasis, invasion, and shorter overall survival.{53707} Cayman’s STAT1B (human, recombinant) protein consists of 950 amino acids and has a calculated molecular weight of 111 kDa.
100 ug
Cayman Chemical
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