The ABL1/ABL2 AB-393/439 Antibody (PAC021441) is a polyclonal antibody specifically designed for research involving the ABL1 and ABL2 proteins. These proteins are members of the Abelson family of non-receptor tyrosine kinases, known for their role in various cellular processes including cell growth, differentiation, and response to DNA damage.Raised in rabbits, this antibody is highly reactive with human samples and has been validated for use in Western blot applications. It specifically binds to the ABL1 and ABL2 proteins, enabling their detection and analysis in a variety of cell types. This makes it an excellent tool for studies in cancer research, molecular biology, and signal transduction pathways.
The ABL1/ABL2 AB-393/439 Antibody is essential for understanding the functions and regulation of the ABL1 and ABL2 proteins, which are often dysregulated in cancer and other diseases. By studying these proteins, researchers can gain valuable insights into the underlying mechanisms of disease progression and potentially identify new targets for therapeutic intervention. This antibody is a valuable asset for any research laboratory looking to deepen their understanding of ABL1 and ABL2 biology.
Antibody Name:
ABL1/ABL2 (Ab-393/439) Antibody (PACO21441)
Antibody SKU:
PACO21441
Size:
100ul
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
ELISA:1:2000-1:10000, WB:1:500-1:1000
Species Reactivity:
Human, Mouse
Immunogen:
Peptide sequence around aa.391~395/437~441(D-T-Y-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 peptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific peptide.
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Western blot analysis of extract from MCF-7, 293, HepG2 cells using ABL1/2 (Ab-393/439) Antibody.
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.
Synonyms:
ABL; v-abl; c-ABL; p150; JTK7
UniProt Protein 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. 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]
