Recombinant Proteins

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SIGLEC9 Human

Sialic Acid Binding Ig Like Lectin 9 Human Recombinant

SIGLEC9 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 573 amino acids (18-348a.a.) and having a molecular mass of 63.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).
SIGLEC9 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26081
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

SIGLEC10 Human

Sialic Acid Binding Ig Like Lectin 10 Human Recombinant

SIGLEC10 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 678 amino acids (17-455 a.a.) and having a molecular mass of 75.6kDa. SIGLEC10 is expressed with a 239 hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26180
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

SIGLEC5 Human

Sialic Acid Binding Ig Like Lectin 5 Human Recombinant

SIGLEC5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 667 amino acids (17-441a.a.) and having a molecular mass of 74.2kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). SIGLEC5 is expressed with a 239 amino acid hIgG-His Tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26265
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

SIGLEC6 Human

Sialic Acid Binding Ig Like Lectin 6 Human Recombinant

SIGLEC6 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 563 amino acids (27-347a.a.) and having a molecular mass of 62.6kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). SIGLEC6 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26355
Source

Sf9, Baculovirus cells.

Appearance
Sterile filtered colorless solution.

SIGLEC7 Human

Sialic Acid Binding Ig Like Lectin 7 Human Recombinant

SIGLEC7 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 577 amino acids (19-353a.a.) and having a molecular mass of 64.2kDa. SIGLEC7 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26459
Source

Sf9, Baculovirus cells.

Appearance
Sterile filtered colorless solution.
Definition and Classification

SIGLECs (Sialic acid-binding immunoglobulin-like lectins) are a family of cell surface proteins that bind sialic acid. They are primarily found on the surface of immune cells and are a subset of the I-type lectins . There are 14 different mammalian SIGLECs, each providing an array of functions based on cell surface receptor-ligand interactions . SIGLECs are classified into two groups: the highly conserved group (including Sialoadhesins, CD22, MAG, and SIGLEC-15) and the CD33-related SIGLECs .

Biological Properties

SIGLECs are predominantly expressed on immune cells such as macrophages, B cells, T cells, dendritic cells, and natural killer cells . They are type I transmembrane proteins with an N-terminal V-type immunoglobulin domain that acts as the binding receptor for sialic acid . The expression patterns and tissue distribution of SIGLECs vary, with some being specific to certain cell types and tissues .

Biological Functions

The primary function of SIGLECs is to bind glycans containing sialic acids, which can be used in cell adhesion, cell signaling, and other processes . SIGLECs play crucial roles in immune responses by recognizing and binding to sialic acids on pathogens, thereby modulating immune cell activation, proliferation, and apoptosis . They are involved in pathogen recognition and help in distinguishing self from non-self .

Modes of Action

SIGLECs mediate their effects through interactions with other molecules and cells. They recognize sialic acids on the surface of cells and pathogens, leading to various downstream signaling cascades . These interactions can result in either inhibitory or activating signals, depending on the specific SIGLEC and its binding partners . For example, some SIGLECs contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs) that down-regulate signaling pathways, while others interact with adapter proteins like DAP12 to activate immune responses .

Regulatory Mechanisms

The expression and activity of SIGLECs are tightly regulated through various mechanisms. Transcriptional regulation involves specific transcription factors that control SIGLEC gene expression . Post-translational modifications, such as phosphorylation, also play a critical role in modulating SIGLEC activity and signaling . Additionally, the interaction with sialic acid ligands can influence the stability and localization of SIGLECs on the cell surface .

Applications

SIGLECs have significant applications in biomedical research, diagnostic tools, and therapeutic strategies. They are being explored as potential biomarkers for various diseases, including cancer and infectious diseases . Therapeutically, targeting SIGLECs with synthetic ligands or monoclonal antibodies holds promise for modulating immune responses in conditions like cancer and autoimmune diseases . SIGLECs are also being investigated for their role in enhancing the efficacy of immunotherapies .

Role in the Life Cycle

Throughout the life cycle, SIGLECs play essential roles from development to aging and disease. During development, SIGLECs are involved in the regulation of immune cell differentiation and maturation . In aging, changes in SIGLEC expression and function can impact immune system efficiency and contribute to age-related diseases . In disease contexts, SIGLECs are implicated in various pathological processes, including chronic inflammation, neurodegeneration, and cancer .

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