SAB1403805
Monoclonal Anti-FAP antibody produced in mouse
clone 2F2, purified immunoglobulin, buffered aqueous solution
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Product Name
Monoclonal Anti-FAP antibody produced in mouse, clone 2F2, purified immunoglobulin, buffered aqueous solution
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
2F2, monoclonal
form
buffered aqueous solution
mol wt
antigen ~37.11 kDa
species reactivity
human
technique(s)
indirect ELISA: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... FAP(2191)
Related Categories
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Biochem/physiol Actions
Fibroblast activation protein (FAP) is expressed in several pathogenic sites including cancer, fibrosis, arthritis, wounding, or inflammation. FAP has in vitro dipeptidyl peptidase activity and collagenolytic activity. It cleaves N-terminal dipeptides from polypeptides and can degrade gelatin and type I collagen.
General description
Fibroblast activation protein (FAP) is a type II transmembrane serine protease and a cell surface antigen. It is encoded by the gene mapped to human chromosome 2q24.2. FAP is present as a homodimeric integral protein with dipeptidyl peptidase IV like fold. The encoded protein has an α/β-hydrolase domain and an eight-bladed β-propeller domain. It is not expressed in normal tissues. FAP is only expressed by activated fibroblasts in response to pathologic situations.
The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. It is selectively expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. This protein is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. (provided by RefSeq)
Immunogen
FAP (AAH26250, 525 a.a. ~ 624 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Sequence
PPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWS
Sequence
PPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWS
Physical form
Solution in phosphate buffered saline, pH 7.4
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Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Striking similarities in genetic aberrations between a rectal tumor and its lung recurrence
Rahma O E, et al.
World Journal of Gastrointestinal Oncology, 5(11), 198-198 (2013)
Fibroblast activation protein, a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts.
Park J E, et al.
The Journal of Biological Chemistry, 274(51), 36505-36512 (1999)
Thomas Kelly et al.
International review of cell and molecular biology, 297, 83-116 (2012-05-23)
Fibroblast activation protein-α (FAP) is a serine protease that can provide target specificity to therapeutic agents because in adults its expression is restricted to pathologic sites, including cancer, fibrosis, arthritis, wounding, or inflammation. It is not expressed in most normal
Kathleen Aertgeerts et al.
The Journal of biological chemistry, 280(20), 19441-19444 (2005-04-06)
Fibroblast activation protein alpha (FAPalpha) is highly expressed in epithelial cancers and has been implicated in extracellular matrix remodeling, tumor growth, and metastasis. We present the first high resolution structure for the apoenzyme as well as kinetic data toward small
Youfei Li et al.
The International journal of developmental biology, 58(5), 349-353 (2014-10-31)
Preeclampsia is a severe pregnancy complication in part due to insufficient implantation. This study aimed at elucidating the mechanism of action of dipeptidyl peptidase IV (DPPIV) in preeclampsia. Small activating RNAs (saRNA) were used to upregulate DPPIV expression in human
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