na 2

Human Fc gamma RIIIB CD16b Protein is a receptor for the Fc region of immunoglobulins gamma. Low affinity receptor. Binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. May serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils. Fc gamma RIIIB CD16b (NA2) Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 23.7 kDa and the accession number is O75015-1.

Human Fc gamma RIIIB CD16b Protein is a receptor for the Fc region of immunoglobulins gamma. Low affinity receptor. Binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. May serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils. Fc gamma RIIIB CD16b (NA2) Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 23.7 kDa and the accession number is O75015-1.

Expression system: HEK293 Cells
Length: 36-469, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-469, Full Length
Activity: Enzyme activity

Expression system: E. coli
Length: 1-102, Partial
Activity: Not Tested

Expression system: E. coli
Length: 574-689, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-650, Full Length
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 499-582, Partial
Activity: Not Tested

SLC23A2 Protein-VLP, Human, Recombinant (His) is expressed in Mammalian cell. The accession number is Q9UGH3.

Human sialidase 2 (NEU2) is a cytoplasmic sialidase that degrades sialyl glycoconjugates, including glycoproteins and gangliosides, via hydrolysis of terminal sialic acids to produce asialo-type molecules. It belongs to a family of glycohydrolytic enzymes that remove sialic acid residues from glycoproteins and glycolipids. NEU2 expression as assessed by quantitative real-time PCR was found to be extremely low or undetectable in many human tissues and cells, with notable exceptions like the placenta and testis. The human cytosolic sialidase NEU2 is the only mammalian enzyme structurally characterized and represents a valuable model to study the specificity of novel NA inhibitory drugs. Diseases associated with NEU2 include Galactosialidosis and Discrete Subaortic Stenosis.

Clostridium perfringens C. perfringens (formerly known as C. welchii) is a Gram-positive, rod-shaped, anaerobic, spore-forming bacterium of the genus Clostridium. C. perfringens is ubiquitous in nature and can be found as a normal component of decaying vegetation, marine sediment, the intestinal tract of humans and other vertebrates, insects, and soil. C. perfringens is commonly encountered in infections as a benign component of the normal flora. In this case, its role in disease is minor. Infections due to C. perfringens show evidence of tissue necrosis, bacteremia, emphysematous cholecystitis, and gas gangrene, which is also known as clostridial myonecrosis. NA, also called sialidases, specifically catalyze the hydrolysis removal of terminal sialic acid residues from viral and cellular glycoconjugates. C. Perfringens neuraminidase catalyzes the hydrolysis of alpha-(2->3)-, alpha-(2->6)-, glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates, but has little activity against the α2-8 glycosidic linkages. The function of the neuraminidase is to release sialic acids for use as carbon and energy sources for the non-pathogenic bacterium, while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors

ATP1B2 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 27.7 kDa and the accession number is P14415.

Expression system: E. coli
Length: 132-357, Partial
Activity: Not Tested