Myeloid-Related Proteins 14 (MRP14) (Macrophage Marker) Antibody - With BSA and Azide
Mouse Monoclonal Antibody [Clone MRP14/840 ]
|Application ||IHC-P, IF, FC|
|Other Accession||6280 (S100A9 / Calgranulin B / MRP-14), 112405 (S100A9 / Calgranulin B / MRP-14)|
|Isotype||Mouse / IgM, kappa|
|Other Names||Protein S100-A9, Calgranulin-B, Calprotectin L1H subunit, Leukocyte L1 complex heavy chain, Migration inhibitory factor-related protein 14, MRP-14, p14, S100 calcium-binding protein A9, S100A9, CAGB, CFAG, MRP14|
|Storage||Store at 2 to 8°C.Antibody is stable for 24 months.|
|Precautions||Myeloid-Related Proteins 14 (MRP14) (Macrophage Marker) Antibody - With BSA and Azide is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||CAGB, CFAG, MRP14|
|Function||S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH- oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF- kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. Has transnitrosylase activity; in oxidatively-modified low- densitity lipoprotein (LDL(ox))-induced S-nitrosylation of GAPDH on 'Cys-247' proposed to transfer the NO moiety from NOS2/iNOS to GAPDH via its own S-nitrosylated Cys-3. The iNOS-S100A8/A9 transnitrosylase complex is proposed to also direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C- x-x-[DE] motif.|
|Cellular Location||Secreted. Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation or endothelial adhesion of monocytes, is secreted via a microtubule-mediated, alternative pathway|
|Tissue Location||Calprotectin (S100A8/9) is predominantly expressed in myeloid cells. Except for inflammatory conditions, the expression is restricted to a specific stage of myeloid differentiation since both proteins are expressed in circulating neutrophils and monocytes but are absent in normal tissue macrophages and lymphocytes. Under chronic inflammatory conditions, such as psoriasis and malignant disorders, also expressed in the epidermis. Found in high concentrations at local sites of inflammation or in the serum of patients with inflammatory diseases such as rheumatoid, cystic fibrosis, inflammatory bowel disease, Crohn's disease, giant cell arteritis, cystic fibrosis, Sjogren's syndrome, systemic lupus erythematosus, and progressive systemic sclerosis. Involved in the formation and deposition of amyloids in the aging prostate known as corpora amylacea inclusions. Strongly up-regulated in many tumors, including gastric, esophageal, colon, pancreatic, bladder, ovarian, thyroid, breast and skin cancers|
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Recognizes a protein of14kDa, identified as MRP-14 (also known as Calgranulin B or S100AA9). It comprises 60% of the cytoplasmic protein fraction of circulating polymorphonuclear granulocytes and is also found in monocytes, macrophages and ileal tissue eosinophils. Peripheral blood monocytes carry the antigen extra- and intracellularly, neutrophils only intracellularly. It is a potent chemotactic factor for neutrophils. Plasma concentrations are elevated in diseases associated with increased neutrophil activity, like inflammatory bowel disease. Granulocytes terminate their existence after transmigration through the intestinal wall. Therefore, it is also detectable in feces. Elevated levels have been observed in body fluids such as plasma, saliva, gingival crevicular fluid, stools, and synovial fluid during infection and inflammatory conditions. This MAb reacts with neutrophils, monocytes, and macrophages, and has been shown as an important marker for identifying macrophages in tissue sections.
Kong, J.P., et al. 2004. Loss of myeloid-related proteins 8 and myeloid- related proteins 14 expression in human esophageal squamous cell carcinoma correlates with poor differentiation. World J. Gastroenterol. 10: 1093-1097
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