Toll-like receptor 9 (TLR9) is a protein encoded by TLR9 gene in humans. It is also known as cluster of differentiation 289 (CD289) and is a member of TLR family.
Toll-like receptor 7 (TLR7) is a protein encoded by the TLR7 gene in humans and is a member of TLR family. TLRs controls host immune response against pathogens (e.g. viruses, bacteria and fungi) through recognition of pathogen-associated molecular patterns (PAMPs) which are specific to the microorganisms.
Pathogenic microorganisms utilize a variety of cell surface receptors to gain entry into host cells and to bypass the natural defense mechanisms. One of the most prominent receptors used in this fashion is the leukocyte adhesion receptor CD11b/c.
MCP1, also known as CCL2, is a small chemokine factor belonging to the CC chemokine family. It is predominantly produced by endothelial cells and macrophages, and specifically is a chemoattractant for monocytes and basophils. It is produced by a wide range of cell types in reaction to diverse inflammatory stimuli including tissue injury, infection, and inflammation.
Perforin, also known as the pore-forming protein, pfp, is a 70 kD cytolytic protein expressed in the cytoplasmic granules of cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells.
Perforin is a calcium-dependent pore forming cytolytic protein. Perforin is partially homologous to the terminal components of the membrane attack complex of complement and produces pores of up to 20nm in diameter on target membranes.
Myeloid differentiation primary response gene 88 (MYD88) encodes a cytosolic adapter protein that plays an essential role in innate and adaptive immune responses.
Scavenger Receptor Class B Membrane 1, also known as SR-BI plays an important role in lipid metabolism. Its main function is to mediate transfer of cholesterol between the cell surface and high density lipoprotein (HDL). HDL acts as an extracellular donor and acceptor of free and esterified Cholesterol. SR-BI also acts as a receptor for other ligands including lipoproteins, apoptotic cells and phospholipids.
Research antibodies have long been used to advance HIV/Aids research, however researchers at the California Institute of Technology have recently published a study [PMID: 22033520] developing a new antibody that may someday be used clinically to neutralize HIV. Beginning with a naturally occurring antibody (NIH45-46) purified from HIV positive patients, the researchers modified the antibody using a technique called structure-based rational design.
Antibody studies into the human immunodeficiency virus (HIV) centre around Gag, a highly complex polyprotein that has so far defied attempts to unravel its complex and varied modes of action. Now, a team from the NIST Center for Neutron Research have revealed a new model which has allowed the protein to be studied in far more clarity. The hope with antibody suppliers is that it will pave the way to understanding many more large, unfathomable proteins.
