Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

CrkL (32H4) Mouse mAb #3182

Applications Reactivity Sensitivity MW (kDa) Isotype
W H R Hm Endogenous 39 Mouse IgG1

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  R=Rat  Hm=Hamster
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

CrkL (32H4) Mouse mAb detects endogenous levels of CrkL protein. It does not cross-react with related proteins.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to amino-terminal residues of human CrkL.

Western Blotting

Western Blotting

Western blot analysis of extracts from HT29 (lane 1), THP1 (lane 2), C6 (lane 3), SUP-M2 (lane 4) and Jurkat (lane 5) cells, using CrkL (32H4) Mouse mAb.

Background

CrkL, a 39 kDa adaptor protein, has a key regulatory role in hematopoietic cells. CrkL has one SH2 and two SH3 domains, with 60% homology to CrkII (1). The amino-terminal SH3 domain of CrkL binds proteins such as C3G, SOS, PI3K, c-Abl and BCR/Abl. The SH2 domain of CrkL can bind to tyrosine-phosphorylated proteins such as Cbl, HEF1, CAS and paxillin (2,3). CrkL is involved in various signaling cascades initiated by different cytokines and growth factors. The biological outcomes of the Crk-activated signal transduction include the modulation of cell adhesion, cell migration and immune cell responses (4). CrkL is a prominent substrate of the BCR/Abl oncoprotein in chronic myelogenous leukemia and binds to both BCR/Abl and c-Abl (5). CrkL is prominently and constitutively tyrosine phosphorylated in CML neutrophils and is not phosphorylated in normal neutrophils. Moreover, stimulation of normal neutrophils with cytokines and agonists does not induce tyrosine phosphorylation of this protein (6), indicating that it may be a useful target for therapeutic intervention or as a disease marker. Tyr207 in CrkL is the BCR/Abl phosphorylation site (7).

  1. Satter, M. and Salgia, R. (1998) Leukemia 12, 637-644.
  2. Feller, S. M. et al. (1998) J. Cell. Physiol. 177, 535-552.
  3. Kiyokawa, E. et al. (1997) Crit. Rev. Oncog. 8, 329-342.
  4. Feller, S. M. et al. (2001) Oncogene 20, 6348-6371.
  5. Grumbach, I. M. et al. (2001) Br. J. Haematol. 112, 327-336.
  6. Nicholas, G. L. et al. (1994) Blood 84, 2912-2918.
  7. de Jong, R. et al. (1997) Oncogene 14, 507-513.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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