Synthesized acetyl-peptide derived from human TAL1/2 around the acetylation site of K221.

This antibody detects endogenous levels of TAL1 only when phosphorylated at Human:K221+K222, Mouse:K221+K222, Rat:K221+K222,and dually phosphorylated at two sites. It can also detects endogenous levels of TAL2 only when phosphorylated at Human:K36+K37, Mouse:K36+K37, Rat:K36+K37,and dually phosphorylated at two sites.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):DkkLS

TAL1/TAL2

T-cell acute lymphocytic leukemia protein 1 homolog/T-cell acute lymphocytic leukemia protein 2

TAL1 ;
BHLHA17 ;
SCL ;
TCL5 ;
T-cell acute lymphocytic leukemia protein 1 ;
TAL-1 ;
Class A basic helix-loop-helix protein 17 ;
bHLHa17 ;
Stem cell protein ;
T-cell leukemia/lymphoma protein 5 ;
TAL2 ;
BHLHA19 ;
T-cell acute lymphocytic leukemia protein 2 ;
TAL-2 ;
Class A basic helix-loop-helix protein 19 ;
bHLHa19

alternative products:The splicing pattern is cell-lineage dependent,disease:A chromosomal aberration involving TAL1 may be a cause of some T-cell acute lymphoblastic leukemias (T-ALL). Translocation t(1;14)(p32;q11) with T-cell receptor alpha chain (TCRA) genes.,domain:The helix-loop-helix domain is necessary and sufficient for the interaction with DRG1.,function:Implicated in the genesis of hemopoietic malignancies. It may play an important role in hemopoietic differentiation. Serves as a positive regulator of erythroid differentiation.,PTM:Phosphorylated on serine residues. Phosphorylation of Ser-122 is strongly stimulated by hypoxia.,PTM:Ubiquitinated; subsequent to hypoxia-dependent phosphorylation of Ser-122, ubiquitination targets the protein for rapid degradation via the ubiquitin system. This process may be characteristic for microvascular endothelial cells, since it could not be observed in large vessel endothelial cells.,similarity:Contains 1 basic helix-loop-helix (bHLH) domain.,subunit:Efficient DNA binding requires dimerization with another bHLH protein. Forms heterodimers with TCF3. Binds to the LIM domain containing protein LMO2 and to DRG1. Can assemble in a complex with LDB1 and LMO2. Component of a TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3.,tissue specificity:Leukemic stem cell.,

Alternative products:The splicing pattern is cell-lineage dependent,Disease:A chromosomal aberration involving TAL1 may be a cause of some T-cell acute lymphoblastic leukemias (T-ALL). Translocation t(1;14)(p32;q11) with T-cell receptor alpha chain (TCRA) genes.,Domain:The helix-loop-helix domain is necessary and sufficient for the interaction with DRG1.,Function:Implicated in the genesis of hemopoietic malignancies. It may play an important role in hemopoietic differentiation. Serves as a positive regulator of erythroid differentiation.,PTM:Phosphorylated on serine residues. Phosphorylation of Ser-122 is strongly stimulated by hypoxia.,PTM:Ubiquitinated; subsequent to hypoxia-dependent phosphorylation of Ser-122, ubiquitination targets the protein for rapid degradation via the ubiquitin system. This process may be characteristic for microvascular endothelial cells, since it could not be observed in large vessel endothelial cells.,similarity:Contains 1 basic helix-loop-helix (bHLH) domain.,subunit:Efficient DNA binding requires dimerization with another bHLH protein. Forms heterodimers with TCF3. Binds to the LIM domain containing protein LMO2 and to DRG1. Can assemble in a complex with LDB1 and LMO2. Component of a TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3.,tissue specificity:Leukemic stem cell.,

Nucleus .

Leukemic stem cell.