Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

14-3-3 β/α Antibody #9636

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk Endogenous 28 Rabbit

Applications Key:  W=Western Blotting
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

14-3-3 β/α Antibody detects endogenous levels of total 14-3-3 β/α protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence of human 14-3-3 β/α. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, NIH/3T3, and C6 cells using 14-3-3 β/α Antibody.

Background

Plasminogen is a zymogen that produced mainly by liver and circulates in blood (1, 2). Its structure has a 77 aa N-terminal activation peptide, followed by 5 kringle domains and a serin-proteinase domain. Plasminogen system play important role in dissolving the fibrin of blood clots and promoting cell migration by proteolytic degradation of extracellular matrix proteins and activation of MMPs(2,3). Plasminogen is activated through two steps, binding to the cell surface through interaction with its receptors and subsequent releasing of active serine proteinase from zymogen cleavage by acitvator t-PA (Tissue specific plasminogen activator) or u-PA (Urokinase plasminogen activator) (2,3). There are many plasminogen receptor identified on the cell surface, such as S100A10, enolase and PLG-R(KT) (4-6), etc. These receptors all has lysine residues at their C-terminal to interact with the kringle domain of plasminogen, leading to plasminogen localization on cell surface. Once on cell surface, the receptors also interact with t-PA/u-PA, presenting surface bound plasminogen for cleavage into active plasmin (2,3,7). Plasminogen system play importance role in biological process such as tumor migration and invasion, wound healing, macrophage recruitment, and srem cell mobilization (8-14).

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  2. Plow, E.F. et al. (1995) FASEB J 9, 939-45.
  3. Miles, L.A. et al. (2005) Front Biosci 10, 1754-62.
  4. Kwon, M. et al. (2005) Front Biosci 10, 300-25.
  5. Redlitz, A. et al. (1995) Eur J Biochem 227, 407-15.
  6. Lighvani, S. et al. (2011) Blood 118, 5622-30.
  7. Ceruti, P. et al. (2013) Exp Hematol Oncol 2, 12.
  8. Ranson, M. et al. (1998) Br J Cancer 77, 1586-97.
  9. Phipps, K.D. et al. (2011) Cancer Res 71, 6676-83.
  10. Creemers, E. et al. (2000) Am J Pathol 156, 1865-73.
  11. Romer, J. et al. (1996) Nat Med 2, 287-92.
  12. Gong, Y. et al. (2008) J Clin Invest 118, 3012-24.
  13. O'Connell, P.A. et al. (2010) Blood 116, 1136-46.
  14. Gong, Y. and Hoover-Plow, J. (2012) J Biomed Biotechnol 2012, 437920.

Application References

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Companion Products

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

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