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SAB1403805

Sigma-Aldrich

Monoclonal Anti-FAP antibody produced in mouse

clone 2F2, purified immunoglobulin, buffered aqueous solution

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

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

Gene Information

human ... FAP(2191)

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

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.

Physical form

Solution in phosphate buffered saline, pH 7.4

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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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
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
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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