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Key Documents

HPA001295

Sigma-Aldrich

Anti-FCN1 antibody produced in rabbit

enhanced validation

Ab2, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-Collagen/fibrinogen domain-containing protein 1 antibody produced in rabbit, Anti-Ficolin-α antibody produced in rabbit, Anti-Ficolin-1 precursor antibody produced in rabbit, Anti-Ficolin-A antibody produced in rabbit, Anti-M-Ficolin antibody produced in rabbit

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.43

Pricing and availability is not currently available.

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human

enhanced validation

recombinant expression
orthogonal RNAseq
Learn more about Antibody Enhanced Validation

technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:200-1:500

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Immunogen

Ficolin-1 precursor recombinant protein epitope signature tag (PrEST)

Application

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Biochem/physiol Actions

FCN1 (Ficolin-1) also called as M-ficolin belongs to the ficolin family of proteins. It is mainly expressed in the peripheral blood leukocytes and is suggested to function as a plasma protein with elastin-binding activity. It is a transmembrane C-type lectin that functions as a pattern-recognition receptor in innate immunity. It binds to monocyte transmembrane G protein-coupled receptor 43 (GPCR43) and forms a complex. Upon microbial invasion, this complex activates the NF-κB cascade in immune signaling. Acidosis at the site of infection induces the complex to interact with C-reactive protein (CRP) to form CRP-M-ficolin-GPCR43, which inhibits IL-8 production thus preventing immune overactivation. The protein binds to 9-O-acetylated 2-6-linked sialic acid derivatives. It also binds to various glycans containing sialic acid having a 2-3 linkage.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST76115

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Fibrinogen-related proteins in ixodid ticks.
Sterba, J., et al.
Parasites & vectors, 41, 127-127 (2011)
Michihito Katayama et al.
International immunology, 31(1), 23-32 (2018-09-01)
Previously, we reported that mRNA expression of ficolin-1 (FCN1), a component of the complement lectin pathway, is elevated in peripheral blood mononuclear cells of patients with vasculitis syndrome, and that FCN1-positive cells infiltrate into inflamed regions in patient specimens. In
Jan Sterba et al.
Parasites & vectors, 4, 127-127 (2011-07-07)
Fibrinogen-related proteins with lectin activity are believed to be part of the tick innate immune system. Several fibrinogen-related proteins have been described and characterised mainly on the basis of their cDNA sequences while direct biochemical evidence is missing. One of
Evelyne Gout et al.
The Journal of biological chemistry, 285(9), 6612-6622 (2009-12-25)
Ficolins are oligomeric innate immune recognition proteins consisting of a collagen-like region and a fibrinogen-like recognition domain that bind to pathogen- and apoptotic cell-associated molecular patterns. To investigate their carbohydrate binding specificities, serum-derived L-ficolin and recombinant H- and M-ficolins were
Jing Zhang et al.
Journal of immunology (Baltimore, Md. : 1950), 185(11), 6899-6910 (2010-11-03)
Although transmembrane C-type lectins (CLs) are known to initiate immune signaling, the participation and mechanism of action of soluble CLs have remained enigmatic. In this study, we found that M-ficolin, a conserved soluble CL of monocyte origin, overcomes its lack

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