Product Name: ARGBP2 Antibody
Species Reactivity: Human
Tested Applications: Flow, IF, IHC-P, WB
Applications: For IF starting dilution is: 1:10~50For WB starting dilution is: 1:1000For IHC-P starting dilution is: 1:10~50For FACS starting dilution is: 1:10~50
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 124 kDa
Immunogen: This ARGBP2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 175-204 amino acids from the N-terminal region of human ARGBP2.
Host Species: Rabbit
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Physical State: Liquid
CAS NO.: 181223-80-3
Product: DEL-22379
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: 2 mg/ml
Storage Conditions: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: Sorbin and SH3 domain-containing protein 2, Arg/Abl-interacting protein 2, ArgBP2, Sorbin, SORBS2, ARGBP2, KIAA0777
Accession NO.: O94875
Protein Ino:
Official Symbol: SORBS2
Geneid: 8470
Background: Arg and c-Abl represent the mammalian members of the Abelson family of non-receptor protein-tyrosine kinases. They interact with the Arg/Abl binding proteins via the SH3 domains present in the carboxy end of the latter group of proteins. ARGBP2 is the sorbin and SH3 domain containing 2 protein. It has three C-terminal SH3 domains and an N-terminal sorbin homology(SoHo) domain that interacts with lipid raft proteins. The subcellular localization of this protein in epithelial and cardiac muscle cells suggests that it functions as an adapter protein to assemble signaling complexes in stress fibers, and that it is a potential link between Abl family kinases and the actin cytoskeleton.
PubMed ID:http://aac.asm.org/content/53/4/1331.abstract
