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SAB2900181

Sigma-Aldrich

Anti-FAP (AB1) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

170-kDa melanoma membrane-bound gelatinase, FAP, FAP alpha, FAPA, Seprase, fibroblast activation protein, fibroblast activation protein alpha

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

human

Technique(s)

immunohistochemistry: 10-20 μg/mL

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... FAP(2191)

Description générale

FAP gene is localized on human chromosome 2q24.2.
Fibroblast activation protein (FAP) is a type II transmembrane serine protease and a cell surface antigen. It is present as a homodimeric integral protein with dipeptidyl peptidase IV like fold. FAP has an α/β-hydrolase domain and an eight-bladed β-propeller domain. It is not expressed in normal tissues. The protein is only expressed by activated fibroblasts in response to pathologic situations.

Immunogène

Synthetic 18 amino acid peptide from extracellular domain of human FAP. Percent identity with other species by BLAST analysis: Human, Gorilla, Gibbon (100%); Monkey (94%); Bovine (89%); Marmoset (83%).

Application

Anti-FAP (AB1) antibody produced in rabbit has been used in immunohistochemistry.

Actions biochimiques/physiologiques

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.

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Forme physique

Solution in phosphate-buffered saline containing less than 0.1% sodium azide.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Les clients ont également consulté

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L Wagner et al.
Clinical and experimental immunology, 184(3), 265-283 (2015-12-17)
Dipeptidyl peptidase (DPP) 4 (CD26, DPP4) is a multi-functional protein involved in T cell activation by co-stimulation via its association with adenosine deaminase (ADA), caveolin-1, CARMA-1, CD45, mannose-6-phosphate/insulin growth factor-II receptor (M6P/IGFII-R) and C-X-C motif receptor 4 (CXC-R4). The proline-specific
Xuguang Yang et al.
Cancer research, 76(14), 4124-4135 (2016-05-25)
Cancer-associated fibroblasts (CAF) are components of the tumor microenvironment whose contributions to malignant progression are not fully understood. Here, we show that the fibroblast activation protein (FAP) triggers induction of a CAF subset with an inflammatory phenotype directed by STAT3
Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha
Kathleen Aertgeerts
The Journal of Biological Chemistry, 280 (2005)
FAP Promotes Immunosuppression by Cancer-Associated Fibroblasts in the Tumor Microenvironment via STAT3?CCL2 Signaling
Xuguang Yang
Cancer Research (2016)
Fibroblast Activation Protein, a Dual Specificity Serine Protease Expressed in Reactive Human Tumor Stromal Fibroblasts*
John E Park
The Journal of Biological Chemistry (1999)

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