Recombinant Proteins

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LBP
CEA
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SLAMF1 Human

SLAMF1 Human Recombinant

SLAMF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (21-237 a.a) and having a molecular mass of 26.7kDa.
SLAMF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28378
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

SLAMF1 Human, Sf9

SLAMF1 Human Recombinant, Sf9

SLAMF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 226 amino acids (21-237a.a.) and having a molecular mass of 25.3kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
SLAMF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT28446
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

SLAMF6 Human

SLAMF6 Human Recombinant

SLAMF6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (22-226 a.a.) and having a molecular mass of 25.5kDa. SLAMF6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28527
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

SLAMF6 Human, sf9

SLAMF6 Human Recombinant, sf9

SLAMF6 Human Recombinant produced in Insect cells is a single, glycosylated polypeptide chain containing 214 amino acids (22-226) and having a molecular mass of 24.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
SLAMF6 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28645
Source
Baculovirus sf9 cells.
Appearance
Sterile Filtered clear solution.

SLAMF7 Human

SLAMF7 Human Recombinant

SLAMF7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 212 amino acids (23-226a.a.) and having a molecular mass of 23.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). SLAMF7 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28722
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear solution.
Definition and Classification

The Signaling Lymphocytic Activation Molecule (SLAM) family is a group of cell surface receptors belonging to the immunoglobulin superfamily. These receptors are primarily involved in the regulation of immune responses. The SLAM family consists of nine members: SLAMF1 (CD150), SLAMF2 (CD48), SLAMF3 (CD229), SLAMF4 (CD244), SLAMF5 (CD84), SLAMF6 (CD352), SLAMF7 (CD319), SLAMF8 (CD353), and SLAMF9 .

Biological Properties

Key Biological Properties: SLAM family receptors are type I transmembrane glycoproteins characterized by an amino-terminal IgV variable domain and a membrane-adjacent IgC2 constant domain. They also contain immunoreceptor tyrosine-based switch motifs (ITSMs) in their cytoplasmic domains .

Expression Patterns and Tissue Distribution: SLAM receptors are expressed on a wide range of immune cells, including B and T cells, natural killer (NK) cells, dendritic cells, macrophages, eosinophils, neutrophils, and platelets. The expression patterns vary among different SLAM family members .

Biological Functions

Primary Biological Functions: SLAM family receptors play crucial roles in immune cell communication and activation. They enhance T cell proliferation by stimulating the production of cytokines such as IL-4 and IFN-gamma. SLAM receptors also facilitate cell-to-cell adhesion during antigen presentation .

Role in Immune Responses and Pathogen Recognition: SLAM receptors can interact directly with microbes, promoting phagocytic cell migration to infection sites. For example, SLAMF1 is known to enhance phagocytosis by localizing to phagosomes and inducing signaling cascades that result in the fusion of phagosomes and lysosomes .

Modes of Action

Mechanisms with Other Molecules and Cells: SLAM receptors typically engage in homophilic interactions, meaning they bind to identical receptors on adjacent cells. This binding triggers downstream signaling cascades involving SLAM-associated proteins (SAPs) and other adaptor molecules .

Binding Partners and Downstream Signaling Cascades: SLAM receptors recruit SAPs, which in turn recruit Src family kinases like Fyn. This leads to the phosphorylation of ITSMs and the activation of downstream signaling pathways that promote immune cell activation and cytokine production .

Regulatory Mechanisms

Transcriptional Regulation: The expression of SLAM family receptors is regulated at the transcriptional level by various cytokines and transcription factors. For instance, the differentiation of monocytes into macrophages can upregulate SLAMF7 expression .

Post-Translational Modifications: SLAM receptors undergo post-translational modifications such as phosphorylation, which is crucial for their signaling functions. Phosphorylation of ITSMs is necessary for the binding of SAPs and the subsequent activation of downstream signaling pathways .

Applications

Biomedical Research: SLAM family receptors are valuable tools in immunological research due to their roles in immune cell activation and communication. They are studied in the context of various diseases, including immunodeficiencies and autoimmune disorders .

Diagnostic Tools and Therapeutic Strategies: SLAM receptors are potential targets for diagnostic and therapeutic applications. For example, monoclonal antibodies targeting SLAMF7 are being developed for the treatment of multiple myeloma .

Role in the Life Cycle

Development to Aging and Disease: SLAM family receptors are involved in various stages of the immune response throughout the life cycle. They play roles in the development of immune cells, their activation during infections, and the regulation of immune responses in aging and disease .

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