Fibroblast Activation Protein α Antibody [A9L24] Datasheet

Biological Description

Specificity	Fibroblast Activation Protein α Antibody [A9L24] detects endogenous levels of total Fibroblast Activation Protein α protein.
Background	Fibroblast Activation Protein α (FAP), a type II transmembrane serine protease of the S9B prolyl oligopeptidase subfamily, shares close homology with dipeptidyl peptidase IV while exhibiting dual dipeptidyl peptidase and endopeptidase activities that cleave post-proline bonds in bioactive peptides and denatured collagens. FAP features a short cytoplasmic tail, a transmembrane domain, and a large extracellular region encompassing an α/β-hydrolase catalytic triad alongside an eight-bladed β-propeller domain essential for homodimerization and enzymatic activation. Active as a disulfide-linked homodimer on the surface of cancer-associated fibroblasts, FAP degrades extracellular matrix components like type I collagen and gelatin, facilitating tumor stroma remodeling and tumor cell migration through enhanced matrix metalloproteinase activity. FAP modulates intracellular signaling by cleaving substrates such as neuropeptide Y, peptide YY, substance P, and FGF-21, which influences fibroblast proliferation and immune evasion in the tumor microenvironment. FAP expression on reactive stromal fibroblasts activates Akt and ERK pathways, promoting endothelial sprout formation and vascularization in colorectal and osteosarcoma models. FAP emerges during wound healing, fibrosis, and inflammation where it coordinates epithelial-mesenchymal interactions and tissue repair via controlled proteolysis. FAP overexpression in over 90% of epithelial cancers correlates with aggressive disease progression, while its absence in most normal adult tissues underscores selective therapeutic targeting potential.

Specificity

Fibroblast Activation Protein α Antibody [A9L24] detects endogenous levels of total Fibroblast Activation Protein α protein.

Background

Fibroblast Activation Protein α (FAP), a type II transmembrane serine protease of the S9B prolyl oligopeptidase subfamily, shares close homology with dipeptidyl peptidase IV while exhibiting dual dipeptidyl peptidase and endopeptidase activities that cleave post-proline bonds in bioactive peptides and denatured collagens. FAP features a short cytoplasmic tail, a transmembrane domain, and a large extracellular region encompassing an α/β-hydrolase catalytic triad alongside an eight-bladed β-propeller domain essential for homodimerization and enzymatic activation. Active as a disulfide-linked homodimer on the surface of cancer-associated fibroblasts, FAP degrades extracellular matrix components like type I collagen and gelatin, facilitating tumor stroma remodeling and tumor cell migration through enhanced matrix metalloproteinase activity. FAP modulates intracellular signaling by cleaving substrates such as neuropeptide Y, peptide YY, substance P, and FGF-21, which influences fibroblast proliferation and immune evasion in the tumor microenvironment. FAP expression on reactive stromal fibroblasts activates Akt and ERK pathways, promoting endothelial sprout formation and vascularization in colorectal and osteosarcoma models. FAP emerges during wound healing, fibrosis, and inflammation where it coordinates epithelial-mesenchymal interactions and tissue repair via controlled proteolysis. FAP overexpression in over 90% of epithelial cancers correlates with aggressive disease progression, while its absence in most normal adult tissues underscores selective therapeutic targeting potential.

Usage Information

Application

WB, IHC

Dilution

WB	IHC
1:1000	1:250

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

88 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

References

https://pubmed.ncbi.nlm.nih.gov/22608558/
https://pubmed.ncbi.nlm.nih.gov/29207091/

Fibroblast Activation Protein α Antibody [A9L24]

Biological Description

Usage Information

References

Application Data