Recombinant human ABL2 protein (ab51259)
Key features and details
- Expression system: Baculovirus infected Sf9 cells
- Active: Yes
- Tags: His tag N-Terminus
- Suitable for: Functional Studies
Description
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Product name
Recombinant human ABL2 protein -
Expression system
Baculovirus infected Sf9 cells -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Amino acids
38 to 1167 -
Tags
His tag N-Terminus
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Associated products
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Substrate reagent
Specifications
Our Abpromise guarantee covers the use of ab51259 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Functional Studies
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Form
Liquid -
Additional notes
ab204848 (c Abl peptide) can be utilized as a substrate for assessing Kinase activity
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.00
Preservative: 1.02% Imidazole
Constituents: 0.00174% PMSF, 0.82% Sodium phosphate, 0.00308% DTT, 25% Glycerol (glycerin, glycerine), 1.74% Sodium chlorideThis product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
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Alternative names
- Abelson murine leukemia viral oncogene homolog 2
- Abelson related gene protein
- Abelson tyrosine-protein kinase 2
see all -
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 and receptor endocytosis. 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, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 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. ABL2 acts also as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 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. -
Tissue specificity
Widely expressed. -
Sequence similarities
Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.
Contains 1 protein kinase domain.
Contains 1 SH2 domain.
Contains 1 SH3 domain. -
Domain
Contains two distinct classes of F-actin-binding domains. Although both can bind F-actin, the 2 are required to bundle actin filaments. -
Post-translational
modificationsPhosphorylated at Tyr-261 by ABL1 in response to oxidative stress. Phosphorylated by PDGFRB.
Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation. -
Cellular localization
Cytoplasm, cytoskeleton. - Information by UniProt
Images
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The specific activity of ABL2 (ab51259) was determined to be 1050 nmol/min/mg as per activity assay protocol
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SDS PAGE analysis of ab51259
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Sample Purity Data.
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab51259 has not yet been referenced specifically in any publications.