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Key Documents

HPA010682

Sigma-Aldrich

Anti-SIGLEC9 antibody produced in rabbit

enhanced validation

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

Synonym(s):

Anti-Protein FOAP-9, Anti-Sialic acid-binding Ig-like lectin 9 precursor, Anti-Siglec-9

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About This Item

MDL number:
UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

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
Learn more about Antibody Enhanced Validation

technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:50-1:200

immunogen sequence

QNLTMTVFQGDGTVSTVLGNGSSLSLPEGQSLRLVCAVDAVDSNPPARLSLSWRGLTLCPSQPSNPGVLELPWVHLRDEAEFTCRAQNPLGSQQVYLNVSLQSKATSGVTQ

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SIGLEC9(27180)

General description

SIGLEC9 (sialic acid binding Ig-like lectin 9) gene encodes a member of the Siglec (sialic acid-binding Ig-like lectin) family that belongs to the immunoglobulin superfamily (IgSF). Siglecs are type-I transmembrane proteins that are expressed mainly on immune cells. The gene SIGLEC9 consists of seven exons interspaced by six introns and is mapped to human chromosome 19q13.4. The encoded protein spans a length of 463-amino-acids. Siglec-9 has been found to be expressed abundantly in bone marrow, placenta, spleen, and fetal liver. The Siglec family is characterized by the presence of one N-terminal V-set domain and a variable number of downstream C2 set domains. The members of this family are involved in mediating protein–carbohydrate interactions via specific interactions with sialic acid-containing glycoproteins and glycolipids.

Immunogen

Sialic acid-binding Ig-like lectin 9 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

Siglec-9 is a lectin that binds to sialic acids via the N-terminal V-set Ig domain. It contains tyrosine-based inhibitory motifs in its cytoplasmic tail. It inhibits unwanted neutrophil reactivity and controls innate immune response by recognizing host sialic acids as ′self′. It binds preferentially to α-2,3- or α-2,6-linked sialic acid. It facilitates the transduction of apoptotic and nonapoptotic death signals into neutrophils.

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 APREST71902

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

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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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Aaron F Carlin et al.
Blood, 113(14), 3333-3336 (2009-02-07)
Human neutrophil Siglec-9 is a lectin that recognizes sialic acids (Sias) via an amino-terminal V-set Ig domain and possesses tyrosine-based inhibitory motifs in its cytoplasmic tail. We hypothesized that Siglec-9 recognizes host Sias as "self," including in cis interactions with
G Foussias et al.
Genomics, 67(2), 171-178 (2000-07-25)
Using the positional cloning approach, we have identified siglec-9 (HGMW-approved symbol SIGLEC9) a novel member of the sialic acid-binding Ig-like lectin (Siglec) family, which belongs to the immunoglobulin superfamily (IgSF). We characterized the genomic structure of this gene and determined
J Q Zhang et al.
The Journal of biological chemistry, 275(29), 22121-22126 (2000-05-10)
Here we characterize the properties and expression pattern of Siglec-9 (sialic acid-binding Ig-like lectin-9), a new member of the Siglec subgroup of the immunoglobulin superfamily. A full-length cDNA encoding Siglec-9 was isolated from a dibutyryl cAMP-treated HL-60 cell cDNA library.
Stephan von Gunten et al.
Blood, 106(4), 1423-1431 (2005-04-14)
We report about new apoptotic and non-apoptotic death pathways in neutrophils that are initiated via the surface molecule sialic acid-binding immunoglobulin-like lectin (Siglec)-9. In normal neutrophils, Siglec-9 ligation induced apoptosis. Inflammatory neutrophils obtained from patients with acute septic shock or

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