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 About 5 results found for searched term "Lipoteichoic acid" (0.152 seconds)

Cat.No.  Name Target
M9917 Lipoteichoic acid Adjuvants
LTA
Lipoteichoic acid (LTA) is a complex component of cell walls of Gram-positive bacteria that are involved in a wide range of cell processes such as the stimulation of immune responses and cell signaling pathways, also used as adjuvant.
M25238 Pagibaximab Anti-infection
BSYX-A 110; Anti-S. Epidermidis LTA Recombinant Antibody
Pagibaximab is a chimeric IgG1 antibody recognizing the surface component lipoteichoic acid of S. aureus and S. epidermidis. Pagibaximab can be used to prevent staphylococcal sepsis.
M41070 HSGN-94 Antibiotic
HSGN-94 is a potent antimicrobial agent with lipoteichoic acid (LTA) biosynthesis inhibition.
M58535 Recombinant Human CD5L Protein (HEK293, C-6His) Cytokines and Growth Factors
CD5 Antigen-Like; CT-2
CD5 Antigen-Like (CD5L) is a soluble protein that belongs to group B of the scavenger receptor cysteine-rich (SRCR) superfamily. CD5L regulates mechanisms in inflammatory responses, such as infection or atherosclerosis. It binds to myelomonocytic and lymphoid cells and may play an important role in the regulation of the innate and adaptive immune systems. CD5L functions as a pattern recognition molecule by binding both lipoteichoic acid (LTA) on Gram positive and lipopolysaccharide (LPS) on Gram-negative bacteria and the SRCR domain one of CD5L retains both the LPS and LTA binding activities.
M58536 Recombinant Mouse CD5L Protein (HEK293, C-6His) Cytokines and Growth Factors
CD5 Antigen-Like; CT-2
CD5 Antigen-Like (CD5L) is a soluble protein that belongs to group B of the scavenger receptor cysteine-rich (SRCR) superfamily. CD5L regulates mechanisms in inflammatory responses, such as infection or atherosclerosis. It binds to myelomonocytic and lymphoid cells and may play an important role in the regulation of the innate and adaptive immune systems. CD5L functions as a pattern recognition molecule by binding both lipoteichoic acid (LTA) on Gram positive and lipopolysaccharide (LPS) on Gram-negative bacteria and the SRCR domain one of CD5L retains both the LPS and LTA binding activities.



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