SIGLEC8 Antibodies

Sialic acid-binding Ig-like lectin 8 (SIGLEC8)

Putative adhesion molecule that mediates sialic-acid dependent binding to red blood cells (PubMed:10856141, PubMed:10625619). Preferentially binds to alpha-2,3-linked sialic acid.

Also binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface (PubMed:10625619).

Gene Information

Human
Gene Name:	SIGLEC8
Uniprot:	Q9NYZ4
Entrez:	27181

Family

Belongs to:
immunoglobulin superfamily

Alternative Names

CD329 antigen; CDw329; MGC59785; SAF2; SAF2SAF-2; sialic acid binding Ig-like lectin 8; Sialoadhesin family member 2; Siglec8; Siglec-8; SIGLEC8L; SIGLEC8Lsialic acid-binding Ig-like lectin 8

Molecular Weight

Mass (kDA):
54.042 kDA

Genomic Context

Human
Location:	19q13.41
Sequence:	19; NC_000019.10 (51450997..51458454, complement)

Tissue Specificity

Expressed specifically on red blood cells namely basophil, mast cells and eosinophils.

Subcellular Localizations

Membrane; Single-pass type I membrane protein.

Diseases

• Inflammation
• Asthma
• Eosinophilia
• Tissue Adhesions
• Hypereosinophilic Syndrome
• Allergy
• Autoimmune Reaction
• Rhinorrhea
• Myeloid Leukemia, Chronic
• Immediate Hypersensitivity
• Churg-strauss Syndrome
• Eosinophilic Leukemia
• Mucocutaneous Lymph Node Syndrome

• Delayed Hypersensitivity
• Malignant Neoplasms
• Myeloid Leukemia
• Esophagitis
• Lupus Erythematosus, Systemic
• Chimera Disorder
• Tissue Damage

Interacting Proteins

• TFF1

Pathways

• Cell Death
• Transport
• Electron Transport
• Pathogenesis
• Smooth Muscle Contraction
• Programmed Cell Death
• Induction Of Apoptosis
• Anaphylaxis
• Glycosylation
• Hypersensitivity
• Muscle Contraction

• Chemotaxis
• Sensitization
• Mrna Splicing
• Mast Cell Degranulation
• Secretion

PTMs

• Cleavage
• Sulphation

• Biotinylation
• Reduction

• Glycosylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SIGLEC8

Best Uses Of The SIGLEC8 Marker

We will discuss in this article the benefits of Boster Bio's SIGLEC8 marker antibody. The antibodies are highly affine and have been validated by immunohistochemistry, Western Blotting, and ELISA. In addition to their high affinity, Boster antibodies are safe and effective. We also discuss applications of this antibody as a part of immunotherapy, research on cancer, and hematology.

Primary antibodies of high-affinity

High-affinity primary antibodies are produced by human immune cells against the SIGLEC8 marker. The sialic acid-binding and lectins make up a large class of immunoglobulin -like lectins known as Siglecs. The subfamily consists of approximately 50 to 99 siglecs, and shares significant sequence homology the CD33 marker. Most members of the subfamily share an ITIM-like DNA sequence.

Both mouse and human models are currently being developed for the development high-affinity primary antibodies using the SIGLECTA-1 or -B fragments. Both the mouse models used to identify mast cells in humans and eosinophils showed high-affinity affinity for SIGLEC8 markers. Both murine models also showed that antigens stimulated mast cells growth, which is a crucial aspect in the pathogenesis and progression of tumors.

Although sialyl-ligands to Siglec-8 are not well understood, studies in mice have shown ST3GalIII activates these proteins. These proteins then interact with Siglec-8 on eosinophils, leading to enhanced binding of the high-avidity glycan. The exact nature and function of the ligand have not been determined.

The sialic acid concentration in immune cells is extremely high, exceeding 100mM in B cells. However, Siglec binding points are often'masked" by interactions with other Glycan ligands. This makes high-affinity primary antibody that recognizes this antigen inherently sensitive. They are however not 100% selective. Because of this, they may be unsuitable for research on rheumatoid arthritis.

Although Siglecs serve a variety of functions, the majority are involved in innate immunity system signalling. Their primary function is to act in cell-to–cell adhesion. High-affinity primary antibody directed against the SIGLEC8 mark will recognize this antigen in a wide array of samples. If the immune system recognizes SIGLEC8 antibodies containing CD33 it is probable that these proteins will be recognized by the cells.

Applications in immunotherapy

In this study, the SIGLEC8 protein was measured in human serum using a sandwich ELISA with paired capture and detection antibodies and Streptavidin-horseradish peroxidase and Super AquaBlue. The standard curve, based on Siglec-8Ig, was used to calculate the values. The detection limit of the sSiglec-8 ELISA was 0.5 to 60.0 ng/mL.

Agonic anti-human FceRI Antibodies were used to activate human primaryMCs derived mainly from CD34+ peripheral cells. The cells blocked FceRI-dependent calcium flux from Siglec-8-expressing BMMCs. Furthermore, Siglec-8 transgenic mice exhibited comparable inhibition of FceRI-mediated secretion in vitro and in vivo models.

The findings suggest that Siglec-8 may be a valuable biomarker for cancer. As the expression of Siglec-8 on immune cells interacts with tumor cells, it could potentially be a therapeutic strategy in combination with endocrine therapies. The functional effects of Siglec-8 may also be studied in cell culture models. This study has revealed a novel mechanism for controlling immune responses in cancer models.

The activation of Siglec-8 in MCs is dependent on FceRI signaling molecules. It inhibits FceRI by recruiting SH2-containing proteinphosphatase. Moreover, it inhibits FceRI by attenuating intracellular signaling and degranulating MCs. The SIGLEC8 kinase trees provides additional information about the function of Siglec-8 protein within immune system function.

Siglec-8 was initially only found on eosinophils. It is now well-known that Siglec-8 can be found in mast cells as well as eosinophils. Using an anti-Siglec-8 antibody inhibits inflammation in eosinophils. Anti-Siglec-8 antigen-based therapy was proven to be effective in eliminating eosinophils.

Safety

There is much debate surrounding the safety and efficacy of the SIGLEC8 marker. Molecular markers are used to monitor protein activity. While the function of SIGLEC8 remains unknown, a growing body of evidence suggests that it is safe to use. Siglec-8 also expresses on mast cells and in eosinophils but is not expressed too much on neutrophils or basophils.

Mouse mAbs were created after the discovery of SIGLEC8. Allakos, Inc. licensed the 2E2 clone. They are currently developing a range SIGLEC-8-mAbs for clinical trials. While the safety of this mAb is yet to be confirmed, its potent eosinophil-depleting activity supports its potential use in cancer therapy.

Siglecs, single-pass cells surface receptors with immunoglobulin -like motifs, are called siglecs. They are also involved with inhibitory cell signaling. The Siglec family is particularly attractive therapeutically, according to molecular data. The family of molecules comprises four member-receptor-related siglecs, including SIGLEC8, SIGLEC1, SIGLEC2, and SIGLEC4.

Siglec-8 was not extensively studied but has been found to be high in many inflammatory diseases such as asthma, eosinophilic reflux disease, and other conditions. After treatment with prednisone, imatinib, Siglec-8 expression on blood eosinophils is stable. Eosinophils derived from airway tissue (bronchoalveolar levage) show similar levels of Siglec-8 on the surface as those in blood.

The SIGLEC8 gene is expressed on eosinophils and mast cells, and is a promising therapeutic target for allergic diseases. Animal and human studies of AK002 have shown that it inhibits the activity of mast cells and depletes blood eosinophils. The antibody does not cross-react with other recombinant Siglecs. This is important because it allows researchers to identify which mAbs can be used safely.

Cost

The cost of the SIGLEC8 marker varies depending on whether the company uses a proprietary version or an open-source gene. The latter is preferable to the first. The SIGLEC8 Gene is available for commercial purposes. The cost of a commercial copy varies depending on the source. Open-source versions can be as high as three hundred dollars while proprietary versions can run more than one hundred.

The cost of the SIGLEC8 marker varies widely from one laboratory to another, but the price will be a major factor for some researchers. If your lab requires the gene-editing of your research samples, you should consider purchasing a custom-built Siglec8 marker. This test is highly sensitive, and can be used in screening for genetic diseases in both humans and mice. It is also an excellent way to track changes within your cells.