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HPA009085

Sigma-Aldrich

Anti-SIGLEC5 antibody produced in rabbit

enhanced validation

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

Synonym(s):

Anti-GLT-1, Anti-SLC1A2

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About This Item

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

biological source

rabbit

Quality Level

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: 1:20-1:50

immunogen sequence

KARRKQAAGRPEKMDDEDPIMGTITSGSRKKPWPDSAGDQASPPGDAPPLEEQKELHYASLSFSEMKSREPKDQEAPSTTEYSEIKTSK

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SIGLEC5(8778)

General description

SIGLEC5 (sialic acid binding Ig like lectin 5) is a surface receptor, which binds to carbohydrates, and is expressed on neutrophils, monocytes, and B-cells of human myeloid and lymphoid cell lineage. It belongs to the Siglec protein family. It is commonly known as CD170.

Immunogen

Sialic acid-binding Ig-like lectin 5 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

SIGLEC5 (sialic acid binding Ig like lectin 5) is involved in immunosppressiveness by interacting in a hemophilic manner. It interacts with acute phase protein a1-acid glycoprotein, group B streptococcal cell-wall-anchored β protein and the sialylated lipopolysaccharide of Neisseria meningitides. This protein recruits the phosphatases SHP-1 and SHP-2 to its intracellular ITIMs (immunoreceptor tyrosine-based inhibitory motif), which prevents the activation of kinase-dependent activation cascades. Unmasking of this protein is essential for the proinflammatory effect of S. pneumoniae desialylation of the leukocyte cell surface. Interaction of Group B Streptococcus (GBS) β protein with SIGLEC5 results in suppression of human leukocytes phagocytosis function, oxidative burst, and extracellular trap production. This leads to increased bacterial survival.

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 APREST71740

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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Therése Nordström et al.
The Journal of biological chemistry, 286(39), 33981-33991 (2011-07-29)
Sialic acid-binding immunoglobulin-like lectins (Siglecs) are receptors believed to be important for regulation of cellular activation and inflammation. Several pathogenic microbes bind specific Siglecs via sialic acid-containing structures at the microbial surface, interactions that may result in modulation of host
Yung-Chi Chang et al.
mBio, 3(1), doi:10-doi:10 (2012-01-05)
Cell surface expression of sialic acid has been reported to decrease during immune cell activation, but the significance and regulation of this phenomenon are still being investigated. The major human bacterial pathogen Streptococcus pneumoniae causes pneumonia, sepsis and meningitis, often
Aaron F Carlin et al.
The Journal of experimental medicine, 206(8), 1691-1699 (2009-07-15)
Group B Streptococcus (GBS) is a leading cause of invasive bacterial infections in human newborns. A key GBS virulence factor is its capsular polysaccharide (CPS), displaying terminal sialic acid (Sia) residues which block deposition and activation of complement on the
Adam W Barb et al.
Protein expression and purification, 88(2), 183-189 (2013-01-17)
Sialic-acid-binding immunoglobulin-like lectin (Siglec5) is a carbohydrate-binding surface receptor expressed on neutrophils, monocytes and B cells in human lymphoid and myeloid cell lineages. Existing structural and functional data fail to define the clear ligand specificity of Siglec5, though like other

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