The Phospho-ABL1/ABL2 (Y393/439) Antibody (PAC03762) is a crucial tool for researchers studying the ABL1 and ABL2 proteins, which are tyrosine kinases that play essential roles in cell signaling and regulation. This polyclonal antibody, produced in rabbits, is highly specific for phosphorylation at tyrosine residues 393 and 439 on both ABL1 and ABL2 proteins in human samples.The antibody is validated for use in Western blot applications, enabling researchers to detect and analyze the phosphorylation status of ABL1 and ABL2 in various cell types. This makes it ideal for studies in cancer research, as dysregulation of ABL kinases has been implicated in the development and progression of various types of cancer.
Understanding the phosphorylation of ABL1 and ABL2 at specific tyrosine residues is crucial for unraveling the signaling pathways and molecular mechanisms that regulate cell growth, proliferation, and survival. By targeting these phosphorylation sites, researchers can gain valuable insights into the role of ABL kinases in both normal cellular function and disease processes, ultimately paving the way for the development of targeted therapies for cancer and other diseases.
Antibody Name:
Phospho-ABL1/ABL2 (Y393/439) Antibody
Antibody SKU:
PACO03762
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA, WB, IHC
Recommended Dilutions:
WB:1:500-1:2000, IHC:1:100-1:300
Species Reactivity:
Human, Mouse, Monkey
Immunogen:
synthesized peptide derived from human Abl1/2 around the phosphorylation site of Y393/439.
Form:
Liquid
Storage Buffer:
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Purification Method:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
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]