Polyclonal Antibodies: FAP, phospho-PIX
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Anti-murine Fibroblast Activation Protein (FAP) Polyclonal Antisera
Fibroblast activation protein is a type II integral membrane glycoprotein. Human FAP is selectively expressed by tumor stromal fibroblasts in epithelial carcinomas but not by epithelial carcinoma cells, normal fibroblasts or other normal tissues. FAP overexpression enhances tumorigenic potential and tumor growth rates in an animal model (see publication reference below).
Dr. Cheng and colleagues of Fox Chase Cancer Center have developed rabbit polyclonal antisera against recombinant murine FAP-ECD protein. These antisera can detect murine FAP in vitro and in vivo and have been used to detect FAP on paraffin embedded xenografts
|Applications:||WB, IHC (shown in the picture), FACS, and IF|
|Immunogen:||Recombinant Murine FAP-ECD protein. Murine FAP cDNA was re-engineered by PCR to eliminate the intracellular and transmembrane domains for production of an ECD-secreted protein|
|Citation:||Cheng JD, Dunbrack RL, et al. "Promotion of tumor growth by murine fibroblast activation protein, a serine protease, in an animal model," Cancer Res 2002 Aug;62(16):4767-72 [PMID: 12183436]|
The p21-activated kinases (PAKs) are important effector proteins of the small GTPases Cdc42 and Rac1 that control cytoskeletal rearrangements and cell proliferation. PIX (Pak interactive exchange factor, also known as Cool-1), which is widely expressed and enriched in Cdc42- and Rac1- driven focal complexes, is required for PAK recruitment to these sites. PIX interacts with PAK through binding of an unconventional proline-rich sequence in PAK to the SH3 domain of PIX.
|Immunogen:||Phosphopeptide surrounding PIX serine 340 [acetyl-CLSASPRMS(PO3)GFI-CONH2]|
|Citation:||Rennefahrt UE, Deacon SW, et al. "Specificity profiling of Pak kinases allows identification of novel phosphorylation sites," J Biol Chem 2007 May;282(21):15667-78 [PMID: 17392278]|