The Phospho-ABL1/ABL2 (Tyr393/439) Antibody (PAC024508) is a valuable tool for researchers studying the function of the ABL1 and ABL2 proteins in cell signaling pathways. These proteins are involved in diverse cellular processes, including cell growth, differentiation, and apoptosis. The antibody, generated in rabbits, specifically recognizes these phosphorylated forms of ABL1/ABL2 in human samples, allowing for precise detection and analysis in Western blot applications.ABL1 and ABL2 are non-receptor tyrosine kinases that play important roles in signaling cascades that regulate cell proliferation and survival. Phosphorylation of specific tyrosine residues, such as Tyr393 and Tyr439, is known to modulate their activity and downstream signaling effects.
By targeting these phosphorylated sites, researchers can gain insights into the mechanisms by which ABL1 and ABL2 contribute to normal cellular function and disease processes.Studies have shown that dysregulation of ABL1 and ABL2 is associated with various cancers, including leukemia, breast cancer, and lung cancer, highlighting the importance of understanding their signaling pathways. With its high specificity and sensitivity, the Phospho-ABL1/ABL2 (Tyr393/439) Antibody is a valuable tool for investigating the role of these kinases in cancer development and progression, as well as potential therapeutic targeting strategies.
Peptide sequence around phosphorylation site of tyrosine 393/439 (D-T-Y(p)-T-A) derived from Human ABL1/2.
Form:
Liquid
Storage Buffer:
Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Purification Method:
Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Western blot analysis of extracts from HL60 cells using ABL1/2(phospho-Tyr393/439) Antibody and the same antibody preincubated with blocking peptide.
Immunofluorescence staining of methanol-fixed Hela cells using ABL1/2(phospho-Tyr393/439) Antibody.
Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using ABL1/2(Phospho-Tyr393/439) Antibody(left) or the same antibody preincubated with blocking peptide(right).
Background:
Regulates cytoskeleton remodeling during cell differentiation, cell division and cell adhesion. Localizes to dynamic actin structures, and phosphorylates CRK and CRKL, DOK1, and other proteins controlling cytoskeleton dynamics. Regulates DNA repair potentially by activating the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks.
Wang, J.Y. et al. (2000) Oncogene 19, 5643-5650. Danial, N.N. et al. (2000) Oncogene 19, 2523-2531. Brasher, B.B. et al. (2000) J. Biol. Chem. 275, 35631-35637. Pluk, H. et al. (2002) Cell 108, 247-259.
Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1.
NCBI Summary:
This gene is a protooncogene that encodes a protein tyrosine kinase involved in a variety of cellular processes, including cell division, adhesion, differentiation, and response to stress. The activity of the protein is negatively regulated by its SH3 domain, whereby deletion of the region encoding this domain results in an oncogene. The ubiquitously expressed protein has DNA-binding activity that is regulated by CDC2-mediated phosphorylation, suggesting a cell cycle function. This gene has been found fused to a variety of translocation partner genes in various leukemias, most notably the t(9;22) translocation that results in a fusion with the 5' end of the breakpoint cluster region gene (BCR; MIM:151410). Alternative splicing of this gene results in two transcript variants, which contain alternative first exons that are spliced to the remaining common exons. [provided by RefSeq, Aug 2014]
