HPA010682
Anti-SIGLEC9 antibody produced in rabbit
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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All Photos(5)
About This Item
Recommended Products
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.
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:
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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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
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
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
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.
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