Cell Signaling Technology

Product Pathways - Phosphatases

OCRL1 Antibody #8797

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M R Mk Endogenous 103 Rabbit

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

Protocols

Specificity / Sensitivity

OCRL1 Antibody recognizes endogenous levels of total OCRL1 protein. This antibody also cross-reacts with a 51 KDa protein of unknown origin in some cell lines.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly88 of human OCRL1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from ACHN and COS-7 cells using OCRL1 Antibody.

Background

OCRL1 is an inositol 5-phosphatase that selectively dephosphorylates the 5 position of the inositol ring. Its substrates include phosphatidylinositol 4,5-bisphosphate, inositol 1,4,5-trisphosphate, and inositol 1,3,4,5-tetrakisphosphate (1). Research studies indicate that mutations in OCRL1 are linked to Oculocerebrorenal syndrome or Lowe syndrome, an X-linked disorder distinguished by mental retardation and congenital cataracts, as well as Dent's disease (2,3). OCRL1 interacts with several endocytic proteins, including clathrin, AP-2, and RabGTPases (4-7). OCRL1 is localized to the Golgi complex, endosomes, and late stage clathrin-coated pits (6,8). OCRL1 controls early endosome function (8), regulating membrane traffic from endosomes to the Golgi. It is also involved in cytokinesis (9) and cilia assembly (10).

  1. Astle, M.V. et al. (2006) IUBMB Life 58, 451-6.
  2. Attree, O. et al. (1992) Nature 358, 239-42.
  3. Hoopes, R.R. et al. (2005) Am J Hum Genet 76, 260-7.
  4. Erdmann, K.S. et al. (2007) Dev Cell 13, 377-90.
  5. Mao, Y. et al. (2009) EMBO J 28, 1831-42.
  6. Shin, H.W. et al. (2005) J Cell Biol 170, 607-18.
  7. Hyvola, N. et al. (2006) EMBO J 25, 3750-61.
  8. Choudhury, R. et al. (2005) Mol Biol Cell 16, 3467-79.
  9. Vicinanza, M. et al. (2011) EMBO J 30, 4970-85.
  10. Coon, B.G. et al. (2012) Hum Mol Genet 21, 1835-47.

Application References

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

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