Anti-Phospho-Abl1/2 (Y393/439) antibody

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Anti-Phospho-Abl1/2 (Y393/439) antibody

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Product name Anti-Phospho-Abl1/2 (Y393/439) antibody
Short Description Rabbit polyclonal against Phospho-Abl1/2 (Y393/439)
Description Rabbit polyclonal to Phospho-Abl1/2 (Y393/439).
Applications ELISA, IF, IHC-p, WB
Dilution range WB 1:500-1:2000
IHC 1:100-1:300
IF 1:200-1:1000
ELISA 1:5000
Specificity Phospho-Abl1/2 (Y393/439) polyclonal antibody detects endogenous levels of Abl1/2 protein only when phosphorylated at Y393/439.
Protein Name Tyrosine-Protein Kinase Abl1
Abelson Murine Leukemia Viral Oncogene Homolog 1
Abelson Tyrosine-Protein Kinase 1
Proto-Oncogene C-Abl
Immunogen Synthesized peptide derived from human Abl1/2 around the phosphorylation site of Y393/439.
Immunogen Region 380-460 aa
Storage Instruction Store at-20°C, and avoid repeat freeze-thaw cycles.
Host Rabbit
Clonality Polyclonal
Reactivity Human, Mouse
Conjugation Unconjugated
Concentration 1 mg/ml
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Isotype IgG
Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Gene ID 25
Gene Symbol ABL1
Molecular Weight 123 kDa
Database Links HGNC:76
Alternative Names Anti-Tyrosine-Protein Kinase Abl1 antibody
Anti-Abelson Murine Leukemia Viral Oncogene Homolog 1 antibody
Anti-Abelson Tyrosine-Protein Kinase 1 antibody
Anti-Proto-Oncogene C-Abl antibody
Anti-P150 antibody
Anti-ABL1 ABL JTK7 antibody
Function 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. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717'. 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. Regulates T-cell differentiation in a TBX21-dependent manner. Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity.
Post-translational Modifications Acetylated at Lys-711 by EP300 which promotes the cytoplasmic translocation.; Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity. Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity. DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation. Phosphorylation at Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division. Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1. Phosphorylation on Thr-735 is required for binding 14-3-3 proteins for cytoplasmic translocation. Phosphorylated by PRKDC.; Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation.
Cellular Localization Cytoplasm
Shuttles Between The Nucleus And Cytoplasm Depending On Environmental Signals
Sequestered Into The Cytoplasm Through Interaction With 14-3-3 Proteins
Localizes To Mitochondria In Response To Oxidative Stress (By Similarity)
Isoform Ib: Nucleus Membrane
The Myristoylated C-Abl Protein Is Reported To Be Nuclear
Tissue Specificity Widely expressed.
Swiss-Prot Key ABL1_HUMAN
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