Fibroblast Activation Protein α Antibody [A9L24]

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IHC1:250

Application
WB, IHC

Reactivity
Human

Source
Rabbit Monoclonal Antibody

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

Predicted MW Observed MW
88 kDa 80-100 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

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

Clone
A9L24

Synonym(s)
Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, SIMP, Seprase, FAP

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.

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.

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

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%