Phospho-CrkL (Tyr207) (G4) rabbit mAb SureLight488 Conjugate
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CrkL (v-Crk sarcoma virus CT10 oncogene-like protein) is an adaptor protein composed of one Src Homology 2 (SH2) and two Src Homology 3 (SH3) domains separated by flexible linker sequences that act as building blocks to assemble multiprotein complexes (1). The Crk adaptor proteins (Crk and CrkL) constitute an integral part of a network of essential signal transduction pathways in humans and other organisms that act as major convergence points in tyrosine kinase signaling. CRKL is required for the normal development of multiple tissues that rely on fibroblast growth factor 8 (FGF8). Phosphorylation of Crk on Tyr 221 or CrkL on Tyr 207 causes intramolecular binding of the linker region to the SH2 domain, sequestering the SH2 and SH3N and preventing them from binding target proteins (2,3). Mounting evidence indicates that dysregulation of Crk proteins is associated with human diseases, including cancer and susceptibility to pathogen infections.
Applications | Flow Cytometry |
---|---|
Clone | CrklY207-G4 |
Format | SureLight 488 |
Validated Reactivity | Human, Mouse |
Cross Reactivity | Predicted to work with mouse, rat and other homologues. |
Clonality | Monoclonal |
Immunogen | A synthetic phospho0peptide corresponding to residues surrounding Tyr207 of human phospho Crkl |
Formulation | 1X PBS, 0.09% NaN3, 0.2% BSA |
Isotype | Rabbit IgGk |
Preparation | Protein A+G |
Recommended Usage | For flow cytometric staining, the suggested use of this reagent is 5 µL per million cells or 5 µL per 100 µL of staining volume. It is recommended that the reagent be titrated for optimal performance for each application. |
Storage | 2-8ºC |
Pseudonyms | Crk-like protein; CRKL; v-crk sarcoma virus CT10 oncogene homolog (avian)-like |
Uniprot ID | P46109 |
References | (1) ten Hoeve, J., C. Morris, N. Heisterkamp, and J. Groffen. 1993. Isolation and chromosomal localization of CRKL, a human Crk-like gene. Oncogene 82469-2474. (2) Rosen MK, Yamazaki T, Gish GD, Kay CM, Pawson T, Kay LE: Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein. Nature. 1995, 374: 477-479. (3) Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F: Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Nat Struct Mol Biol. 2007, 14: 503-510. |
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