Mouse Abl2 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | Q4JIM5 |
Reactivity | Mouse |
Host | Rabbit |
Clonality | polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 128196 Da |
Other Names | Abelson tyrosine-protein kinase 2, Abelson murine leukemia viral oncogene homolog 2, Abelson-related gene protein, Tyrosine-protein kinase ARG, Abl2 {ECO:0000312|EMBL:AAY860391, ECO:0000312|MGI:MGI:87860} |
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Target/Specificity | This Mouse Abl2 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 1011-1044 amino acids from the C-terminal region of Mouse Abl2. |
Dilution | WB~~1:2000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Mouse Abl2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | Abl2 {ECO:0000312|EMBL:AAY86039.1, ECO:0000312|MGI:MGI:87860} |
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Function | Non-receptor tyrosine-protein kinase that plays an ABL1- overlapping role in 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 MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL or DOK1. Required for adhesion-dependent phosphorylation of ARHGAP35 which promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (PubMed:22810897). |
Cellular Location | Cytoplasm, cytoskeleton |
Tissue Location | Most abundant in adult mouse brain, especially in synapse-rich regions. |
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Background
Non-receptor tyrosine-protein kinase that plays an ABL1- overlapping role in 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 MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL or DOK1. Required for adhesion-dependent phosphorylation of ARHGAP35 which promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1.
References
Wang Y.,et al.Proc. Natl. Acad. Sci. U.S.A. 98:14865-14870(2001).
Tanis K.Q.,et al.Mol. Cell. Biol. 23:3884-3896(2003).
Koleske A.J.,et al.Neuron 21:1259-1272(1998).
Kain K.H.,et al.J. Biol. Chem. 276:16185-16192(2001).
Woodring P.J.,et al.J. Cell Sci. 116:2613-2626(2003).
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