Phospho-CrkL (Tyr207) (G4) rabbit mAb SureLight488 Conjugate

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2095
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.
More Information
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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