Anti-TIA-1 / T-Cell Intracellular Antigen-1, clone TIA1/1352R

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. The T cell intracellular antigen 1 (TIA 1) is a 17 kDa cytoplasmic granule associated protein also designated as GMP 17, for granule membrane protein of 17 kDa. The GMP 17/TIA 1 molecule is expressed in cells possessing cytolytic potential and could be involved in the signaling cascade of Fas (CD95) mediated apoptosis. Within hematopoietic cell lines, the TIA1/1352R monoclonal antibody reacts with about 90% of CD16+, 50 60% of CD8+, and less than 10% of CD4+ normal peripheral blood lymphocytes. It reacts with almost all monocytes and granulocytes. This antibody also reacts with CD4+ activated T cell clones, activated NK cell clones, and Con activated thymocytes, but not with B lymphocytes or B cell lines. TIA1 antibody labels cytotoxic T cells and natural killer cells (NK cells). It is also expressed in T-cell lymphoma, large granular lymphocyte (LGL) leukemia and hairy cell leukemia. TIA1 expression in T-cell malignancies may help in differentiating LGL leukemia (high expression) from T-cell lymphocytosis and other T-cell diseases (low expression). TIA1 may also be used to label tumor-infiltrating lymphocytes in the study of immune response to malignancies. Protein function: RNA-binding protein involved in the regulation of alternative pre-RNA splicing and mRNA translation by binding to uridine-rich (U- rich) RNA sequences (PubMed:8576255, PubMed:11106748, PubMed:12486009, PubMed:17488725). Binds to U-rich sequences immediately downstream from a 5' splice sites in a uridine-rich small nuclear ribonucleoprotein (U snRNP)-dependent fashion, thereby modulating alternative pre-RNA splicing (PubMed:11106748, PubMed:8576255). Preferably binds to the U- rich IAS1 sequence in a U1 snRNP-dependent manner, this binding is optimal if a 5' splice site is adjacent to IAS1. Activates the use of heterologous 5' splice sites, the activation depends on the intron sequence downstream from the 5' splice site, with a preference for a downstream U-rich sequence (PubMed:11106748). By interacting with SNRPC/U1-C, promotes recruitment and binding of spliceosomal U1 snRNP to 5' splice sites followed by U-rich sequences, thereby facilitating atypical 5' splice site recognition by U1 snRNP (PubMed:11106748, PubMed:12486009, PubMed:17488725). Activates splicing of alternative exons with weak 5' splice sites followed by a U-rich stretch on its own pre-mRNA and on TIAR mRNA. Acts as a modulator of alternative splicing for the apoptotic FAS receptor, thereby promoting apoptosis (PubMed:11106748, PubMed:1934064, PubMed:17488725). Binds to the 5' splice site region of FAS intron 5 to promote accumulation of transcripts that include exon 6 at the expense of transcripts in which exon 6 is skipped, thereby leading to the transcription of a membrane-bound apoptotic FAS receptor, which promotes apoptosis (PubMed:11106748, PubMed:1934064, PubMed:17488725). Binds to a conserved AU-rich cis element in COL2A1 intron 2 and modulates alternative splicing of COL2A1 exon 2 (PubMed:17580305). Also binds to the equivalent AT-rich element in COL2A1 genomic DNA, and may thereby be involved in the regulation of transcription (PubMed:17580305). Binds specifically to a polypyrimidine-rich controlling element (PCE) located between the weak 5' splice site and the intronic splicing silencer of CFTR mRNA to promote exon 9 inclusion, thereby antagonizing PTB1 and its role in exon skipping of CFTR exon 9 (PubMed:14966131). Involved in the repression of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs), including target ARE-bearing mRNAs encoding TNF and PTGS2. Also participates in the cellular response to environmental stress, by acting downstream of the stress-induced phosphorylation of EIF2S1/EIF2A to promote the recruitment of untranslated mRNAs to cytoplasmic stress granules (SGs), leading to stress-induced translational arrest (PubMed:10613902). Formation and recruitment to SGs is regulated by Zn(2+). Possesses nucleolytic activity against cytotoxic lymphocyte target cells (PubMed:1934064). [The UniProt Consortium]