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Sialic acid-binding Immunoglobulin-like lectins (Siglecs) are cell-surface I-type lectins that act as immunomodulatory sialic acid-binding receptors. Siglecs belong to the Immunoglobulin (Ig) superfamily. They are expressed on various immune cells that include immune cells of both lymphoid and myeloid origin, namely neutrophils, eosinophils, monocytes, macrophages, NK cells, DCs, mast cells, and B and T cells.
All Siglecs are single-pass type 1 integral membrane proteins containing extracellular domains with one (or two, in the case of Siglec-12) unique and homologous N-terminal V-set Ig domain, followed by variable numbers of C2-set Ig domains, ranging from 16 in sialoadhesin to 1 in CD33. Based on sequence homologies,the Siglecs can be divided into two groups: one including all CD33-related Siglecs and the other consisting of Siglec-1 (Sialoadhesin), Siglec-2 (CD22), Siglec-4 (myelin-associated glycoprotein, MAG) and Siglec-15.
The Siglec-15 protein plays a critical role in cellular interactions, selectively binding to sialylated glycoproteins with affinity for sialic acid residues. Binding to TYROBP and HCST suggests involvement in complex signaling pathways. Siglec-15 Protein, Human (HEK293, mFc) is the recombinant human-derived Siglec-15 protein, expressed by HEK293 , with C-mFc labeled tag.
The Siglec-15 protein plays a critical role in cellular interactions, selectively binding to sialylated glycoproteins with affinity for sialic acid residues. Binding to TYROBP and HCST suggests involvement in complex signaling pathways. Siglec-15 Protein, Human (HEK293, Fc) is the recombinant human-derived Siglec-15 protein, expressed by HEK293 , with C-hFc labeled tag.
The Siglec-15 protein plays a critical role in cellular interactions, selectively binding to sialylated glycoproteins with affinity for sialic acid residues. Binding to TYROBP and HCST suggests involvement in complex signaling pathways. Siglec-15 Protein, Human (Biotinylated, HEK293, Fc-Avi) is the recombinant human-derived Siglec-15 protein, expressed by HEK293 , with C-Avi, C-hFc labeled tag.
The Siglec-2/CD22 protein mediates B cell interactions and may direct B cell localization within lymphoid tissues. It recognizes sialylated glycoproteins, especially α-2,6-linked sialic acid, and participates in cis-interactions at the cell surface. Siglec-2/CD22 Protein, Human (HEK293, His) is the recombinant human-derived Siglec-2/CD22 protein, expressed by HEK293 , with C-6*His labeled tag.
Siglec-10 Protein, identified as a putative adhesion molecule, mediates sialic-acid dependent cellular binding, preferring alpha-2,3- or alpha-2,6-linked sialic acid. Its sialic acid recognition site may undergo masking through cis interactions. In immune responses, Siglec-10 acts as an inhibitory receptor, inducing ligand-induced tyrosine phosphorylation, recruiting SH2 domain-containing phosphatases, and negatively regulating B-cell antigen receptor signaling via PTPN6/SHP-1. In collaboration with CD24, it selectively suppresses the immune response to DAMPs, regulates NK cell response, controls autoimmunity, and inhibits cross-presentation during adaptive immune responses by CD8-alpha(+) dendritic cells. Siglec-10 interacts with proteins including PTPN6/SHP-1, NCF1, CD24, HMGB1, RIGI, CBL, and PTPN11. Siglec-10 Protein, Human (Biotinylated, HEK293, Fc-Avi) is the recombinant human-derived Siglec-10 protein, expressed by HEK293 , with C-Avi, C-hFc labeled tag. The total length of Siglec-10 Protein, Human (Biotinylated, HEK293, Fc-Avi) is 530 a.a., with molecular weight of 100-130 kDa.
Siglec-10 protein is thought to be a putative adhesion molecule that mediates sialic acid-dependent cell binding, preferentially selecting α-2,3- or α-2,6-linked sialic acid. Its sialic acid recognition site may be masked by cis interactions. Siglec-10 Protein, Human (Biotinylated, R119A, HEK293, His-Avi) is the recombinant human-derived Siglec-10 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of Siglec-10 Protein, Human (Biotinylated, R119A, HEK293, His-Avi) is 530 a.a., with molecular weight of 68-80 kDa.
Siglec-10 protein is thought to be a putative adhesion molecule that mediates sialic acid-dependent cell binding, preferentially selecting α-2,3- or α-2,6-linked sialic acid. Its sialic acid recognition site may be masked by cis interactions. Siglec-10 Protein, Human (R119A, HEK293, His-Avi) is the recombinant human-derived Siglec-10 protein, expressed by HEK293 , with C-Avi, C-His labeled tag.
Sialic acid-binding Ig-like lectin 9; Siglec-9; CDw329; Protein FOAP-9; SIGLEC9
Human
HEK293
Siglec-9 Protein is a member of the Siglec cell surface immunoglobulin family.Siglec-9 is highly expressed on human neutrophils and monocytes and low on natural killer cells, and sub-populations of T and B lymphocytes.Siglec-9 induces human neutrophil apoptosis and autophagy-like cell death and also inhibits tumor activity.Siglec-9 Protein, Human (HEK293, His) is the recombinant human-derived Siglec-9 protein, expressed by HEK293 , with C-6*His labeled tag.
Siglec-5 Protein, a putative adhesion molecule, participates in sialic-acid dependent cellular binding, showing equal affinity for alpha-2,3-linked and alpha-2,6-linked sialic acid. Its sialic acid recognition site may be masked through cis interactions with sialic acids on the same cell surface. Siglec-5 Protein, Human (HEK293, His-Flag-Fc) is the recombinant human-derived Siglec-5 protein, expressed by HEK293 , with C-hFc, C-Flag, C-6*His labeled tag. The total length of Siglec-5 Protein, Human (HEK293, His-Flag-Fc) is 418 a.a., with molecular weight of 90-110 kDa.
Siglec-3/CD33 protein is a sialic acid-binding lectin that mediates cell-cell interactions and maintains immune cell quiescence. It prefers α-2,3- and α-2,6-linked glycans with sialic acid. Siglec-3/CD33 Protein, Human (HEK293, Fc-Myc) is the recombinant human-derived Siglec-3/CD33 protein, expressed by HEK293 , with C-Myc, C-Fc labeled tag. The total length of Siglec-3/CD33 Protein, Human (HEK293, Fc-Myc) is 242 a.a., with molecular weight of ~92 kDa.
MAG/Siglec-4a protein binds gangliosides, RTN4R, and RTN4RL2, mediating myelinating cell-neuron interactions. It maintains axon myelination, protects motoneurons, prevents axon degeneration, and inhibits neurite outgrowth. It exists as a monomer or homodimer, interacting with BSG isoform 2. MAG/Siglec-4a Protein, Rat (HEK293, His) is the recombinant rat-derived MAG/Siglec-4a protein, expressed by HEK293 , with C-10*His labeled tag. The total length of MAG/Siglec-4a Protein, Rat (HEK293, His) is 497 a.a., .
Siglec-10 protein is thought to be a putative adhesion molecule that mediates sialic acid-dependent cell binding, preferentially selecting α-2,3- or α-2,6-linked sialic acid. Its sialic acid recognition site may be masked by cis interactions. Siglec-10 Protein, Human (HEK293, Fc) is the recombinant human-derived Siglec-10 protein, expressed by HEK293 , with C-hFc labeled tag.
MAG/Siglec-4a is an adhesion molecule that binds to neuronal gangliosides, RTN4R, and RTN4RL2, promoting myelination interactions. Although not important for initial myelination, it may maintain axonal myelination and protect motor neurons, especially after injury, through interactions with RTN4R and RTN4RL2. MAG/Siglec-4a Protein, Human (HEK293, His) is the recombinant human-derived MAG/Siglec-4a protein, expressed by HEK293 , with C-6*His labeled tag.
Siglec-15 Protein, a Siglec family member and type-1 transmembrane protein, is constitutively expressed in osteoclasts, macrophages and dendritic cells. Siglec-15 plays a pivotal role in the development and differentiation of osteoclastogenesis, inhibiting antigen-specific T cell responses in vitro and in vivo. Siglec-15 Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived Siglec-15 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of Siglec-15 Protein, Cynomolgus (HEK293, His) is 244 a.a., with molecular weight of 30-40 kDa.
Siglec-15 Protein, a Siglec family member and type-1 transmembrane protein, is constitutively expressed in osteoclasts, macrophages and dendritic cells. Siglec-15 plays a pivotal role in the development and differentiation of osteoclastogenesis, inhibiting antigen-specific T cell responses in vitro and in vivo. Siglec-15 Protein, Mouse (HEK293, His) is the recombinant mouse-derived Siglec-15 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of Siglec-15 Protein, Mouse (HEK293, His) is 239 a.a., with molecular weight of 30-40 kDa.
Siglec-6 Protein, a putative adhesion molecule, facilitates sialic acid-dependent binding to cells, specifically binding to alpha-2,6-linked sialic acid. Its sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. Siglec-6 interacts with LEP. Siglec-6 Protein, Human (HEK293, Fc) is the recombinant human-derived Siglec-6 protein, expressed by HEK293 , with C-hFc labeled tag. The total length of Siglec-6 Protein, Human (HEK293, Fc) is 305 a.a., with molecular weight of 70-90 kDa.
Siglec-7 protein is a putative adhesion molecule that mediates sialic acid-dependent cell binding with preference for α-2,3- and α-2,6-linked sialic acids.It interacts with disialoganglioside and may be masked by cis interactions.Siglec-7 Protein, Human (HEK293, His) is the recombinant human-derived Siglec-7 protein, expressed by HEK293 , with C-6*His labeled tag.
Siglec-8 protein is a putative adhesion molecule that mediates sialic acid-dependent binding to erythrocytes, preferring α-2,3-linked sialic acid and interacting with α-2,6-linked sialic acid . Its sialic acid recognition site may be hidden through cis interactions with sialic acid on the surface of the same cell. Siglec-8 Protein, Human (HEK293, His) is the recombinant human-derived Siglec-8 protein, expressed by HEK293 , with C-6*His labeled tag.
The Siglec-15 protein plays a critical role in cellular interactions, selectively binding to sialylated glycoproteins with affinity for sialic acid residues. Binding to TYROBP and HCST suggests involvement in complex signaling pathways. Siglec-15 Protein, Human (HEK293, His) is the recombinant human-derived Siglec-15 protein, expressed by HEK293 , with C-6*His labeled tag.
Siglec-10 protein is thought to be a putative adhesion molecule that mediates sialic acid-dependent cell binding, preferentially selecting α-2,3- or α-2,6-linked sialic acid. Its sialic acid recognition site may be masked by cis interactions. Siglec-10 Protein, Human (HEK293, His) is the recombinant human-derived Siglec-10 protein, expressed by HEK293 , with C-His labeled tag.
