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Mouse Anti-FAP Recombinant Antibody (1E5) (CBMAB-A2832-LY)

The product is antibody recognizes FAP. The antibody 1E5 immunoassay techniques such as: WB, ELISA.
See all FAP antibodies
Published Data
Fig.1 Western blot analysis of tenascin C (TNC), fibroblast activation protein (FAP), prolyl 4-hydroxylase (P4H) and a-SMA.
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Summary

Host Animal
Mouse
Specificity
Human
Clone
1E5
Antibody Isotype
IgG2a, κ
Application
WB, ELISA

Basic Information

Immunogen
FAP (AAH26250, 525 a.a. ~ 624 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Fibroblast Activation Protein Alpha
Introduction
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]
Entrez Gene ID
2191
UniProt ID
Q12884
Alternative Names
DKFZp686G13158; DPPIV; FAPA
Research Area
Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769, PubMed:16480718, PubMed:16410248, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721).

Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219, PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711).

Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16651416, PubMed:16410248, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288).

Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817).

The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.
Biological Process
Angiogenesis Source: UniProtKB-KW
Cell adhesion Source: UniProtKB-KW
Endothelial cell migration Source: UniProtKB
Melanocyte apoptotic process Source: UniProtKB
Melanocyte proliferation Source: UniProtKB
Negative regulation of cell proliferation involved in contact inhibition Source: UniProtKB
Negative regulation of extracellular matrix disassembly Source: UniProtKB
Negative regulation of extracellular matrix organization Source: UniProtKB
Positive regulation of execution phase of apoptosis Source: UniProtKB
Proteolysis Source: UniProtKB
Proteolysis involved in cellular protein catabolic process Source: UniProtKB
Regulation of cell cycle Source: UniProtKB
Regulation of collagen catabolic process Source: UniProtKB
Regulation of fibrinolysis Source: BHF-UCL
Cellular Location
Prolyl endopeptidase FAP: Cell membrane; Lamellipodium membrane; Invadopodium membrane; Ruffle membrane; Cell surface; Membrane. Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin.
Antiplasmin-cleaving enzyme FAP, soluble form: Secreted. Found in blood plasma and serum.
Isoform 2: Cytoplasm
Topology
Cytoplasmic: 1-4
Helical: 5-25
Extracellular: 26-760
PTM
N-glycosylated.
The N-terminus may be blocked.

Yuan, Z., Hu, H., Zhu, Y., Zhang, W., Fang, Q., Qiao, T., ... & Wang, X. (2021). Colorectal cancer cell intrinsic fibroblast activation protein alpha binds to Enolase1 and activates NF-κB pathway to promote metastasis. Cell death & disease, 12(6), 1-15.

Labiano, S., Roh, V., Godfroid, C., Hiou-Feige, A., Romero, J., Sum, E., ... & Romero, P. (2021). CD40 Agonist Targeted to Fibroblast Activation Protein α Synergizes with Radiotherapy in Murine HPV-Positive Head and Neck TumorsSynergistic Antitumor Effect of Radiotherapy and FAP-CD40 in HNSCC. Clinical Cancer Research, 27(14), 4054-4065.

Juillerat-Jeanneret, L., Tafelmeyer, P., & Golshayan, D. (2021). Regulation of fibroblast activation protein-α expression: focus on intracellular protein interactions. Journal of Medicinal Chemistry, 64(19), 14028-14045.

Bughda, R., Dimou, P., D’Souza, R. R., & Klampatsa, A. (2021). Fibroblast activation protein (FAP)-targeted CAR-T cells: Launching an attack on tumor stroma. ImmunoTargets and Therapy, 10, 313.

Fitzgerald, A. A., & Weiner, L. M. (2020). The role of fibroblast activation protein in health and malignancy. Cancer and Metastasis Reviews, 39(3), 783-803.

Hintz, H. M., Gallant, J. P., Vander Griend, D. J., Coleman, I. M., Nelson, P. S., & LeBeau, A. M. (2020). Imaging Fibroblast Activation Protein Alpha Improves Diagnosis of Metastatic Prostate Cancer with Positron Emission TomographyImaging FAP in Prostate Cancer. Clinical Cancer Research, 26(18), 4882-4891.

Roy, J., Hettiarachchi, S. U., Kaake, M., Mukkamala, R., & Low, P. S. (2020). Design and validation of fibroblast activation protein alpha targeted imaging and therapeutic agents. Theranostics, 10(13), 5778-5789.

Solano-Iturri, J. D., Beitia, M., Errarte, P., Calvete-Candenas, J., Etxezarraga, M. C., Loizate, A., ... & Larrinaga, G. (2020). Altered expression of fibroblast activation protein-α (FAP) in colorectal adenoma-carcinoma sequence and in lymph node and liver metastases. Aging (Albany NY), 12(11), 10337.

Windisch, P., Röhrich, M., Regnery, S., Tonndorf-Martini, E., Held, T., Lang, K., ... & Adeberg, S. (2020). Fibroblast activation protein (FAP) specific PET for advanced target volume delineation in glioblastoma. Radiotherapy and Oncology, 150, 159-163.

Solano-Iturri, J. D., Errarte, P., Etxezarraga, M. C., Echevarria, E., Angulo, J., López, J. I., & Larrinaga, G. (2020). Altered tissue and plasma levels of fibroblast activation protein-α (FAP) in renal tumours. Cancers, 12(11), 3393.

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For research use only. Not intended for any clinical use.

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