Fibroblast Activation Protein α Antibody [A9L24]

Catalog No.: F2214

Application: Reactivity: Human

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代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

使用情報

Dilution
WB1:1000 IHC1:250

Application
WB, IHC

Source
Rabbit Monoclonal Antibody

Reactivity
Human

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
^*なぜ予測分子量と実際の分子量が異なるのか？下記の原因により、実際の分子量が予測と異なる：タンパク質の翻訳後修飾（リン酸化/糖鎖付加），スプライシングバリアント，イソフォーム，相対的な電荷，ポリマー。

Datasheet & SDS

生物学的記述

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
[1] Kelly T, et al. Int Rev Cell Mol Biol. 2012;297:83-116. [2] Cao F, et al. Mol Med Rep. 2018 Feb;17(2):2593-2599.

PVDFメンブレン孔径参考表

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%