Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

14-3-3 Family Antibody Sampler Kit #9769

Kit Includes Quantity Applications Reactivity MW (kDa) Isotype
14-3-3 β/α Antibody #9636 40 µl W H M R Mk 28 Rabbit
14-3-3 γ (D15B7) Rabbit mAb #5522 40 µl W H M R Mk Pg (C) (X) (Z) 27 Rabbit IgG
14-3-3 ζ/δ (D7H5) Rabbit mAb #7413 40 µl W H M R Mk Pg (C) 28 Rabbit IgG
14-3-3 ε Antibody #9635 40 µl W H M R Mk 28 Rabbit
14-3-3 τ Antibody #9638 40 µl W IHC-P H M R Mk 28 Rabbit
Anti-rabbit IgG, HRP-linked Antibody #7074 100 µl Goat
14-3-3 η (D23B7) Rabbit mAb #5521 40 µl W H M R Mk B Pg 27 Rabbit

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  C=Chicken  X=Xenopus  Z=Zebrafish  B=Bovine  Pg=Pig
Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Specificity / Sensitivity

Each antibody in the 14-3-3 Family Antibody Sampler Kit detects endogenous levels of its respective target.

Western Blotting

Western Blotting

Western blot analysis of whole cell extracts from various cell lines using 14-3-3 η (D23B7) Rabbit mAb #5521.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using 14-3-3 γ (D15B7) Rabbit mAb #5522.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using 14-3-3 ζ/δ (D7H5) Rabbit mAb #7413.


Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, NIH/3T3, PC12, and COS cells using 14-3-3 ε Antibody #9635.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, NIH/3T3, and C6 cells using 14-3-3 β/α Antibody #9636.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, NIH/3T3, and C6 cells using 14-3-3 τ Antibody #9638.


Description

The 14-3-3 Family Antibody Sampler Kit provides an economical means to investigate the expression of various 14-3-3 isoforms within the cell. The kit contains enough primary and secondary antibodies to perform four Western blot experiments.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to the sequences of human 14-3-3 ß/α, 14-3-3 ε and 14-3-3 τ proteins. Antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg80 of human 14-3-3 ζ/δ protein, Leu37 of human 14-3-3 η protein and Ile79 of human 14-3-3 γ protein.

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).

  1. Petersen, T.E. et al. (1990) J Biol Chem 265, 6104-11.
  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.

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

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