TIA-1 Antibody recognizes endogenous levels of total TIA-1 protein. A band of unknown origin is detected at 100 kDa.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human TIA-1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
原厂资料:
Specificity / Sensitivity
TIA-1 Antibody recognizes endogenous levels of total TIA-1 protein. A band of unknown origin is detected at 100 kDa.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human TIA-1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
T-cell intracellular antibody 1 (TIA-1) is a member of the RNA-recognition motif (RRM) family of RNA-binding proteins that was originally found to induce DNA fragmentation in digitonin-permeabilized thymocytes (1). TIA-1 protein has about 80% identity to the related TIAR protein, both of which possess three amino-terminal RRM domains and a glutamine-rich carboxyl terminus (1,2). Alternative splicing is responsible for generating at least two isoforms of TIA-1 and TIAR (3,4). Several research studies indicate that TIA-1 and TIAR play a role in apoptosis, cellular stress, and inflammation. Importantly, TIA-1 and TIAR translocate from the nucleus to stress granules in response to a variety of environmental stresses (5-8). Stress granules function as sites of translational repression in response to potentially damaging conditions. mRNA transcripts targeted by TIA-1 and TIAR include TNF-α, COX-2, cytochrome c, GADD45α, and HIF-1α (8-13).