• Official Full Name
  • lysozyme
  • Background
  • The acronym ANCA (Antineutrophil Cytoplasmic Autoantibodies) is defined by an accumulation of autoantibodies with specificity against different granulocytic, monocytic and probably endothelial cytoplasmic antigens. PR3 and MPO are well defined as reliable serological markers for a definite group of primary systemic vasculitides (PSV), which were also named ANCA associated vasculitides (AAV). The occurrence of AAV is clearly higher than supposed. The incidence is 1.5 per 1000 and in the group of older persons nearly 5 per 1000. The clinical appearance of the AAV is characterized through manifestations in lung, kidney and respiratory tract. In the last years, newer investigations discovered and characterised a couple of new pANCA antigens: Elastase, Cathepsin G, Lysozyme and Lactoferrin. Up to now, ANCA screening has been done with immunofluorescence techniques, but often there have been difficulties in the evaluation and in clinical findings. Therefore, the results have to be scrutinised with counter examinations on other cells or in other test systems like ELISA. Moreover it was not possible to differentiate the single cANCA and pANCA antigens.
    1. Proteinase 3
    The major antigen for the cANCA reactivity is the neutral serine protease 3 (synonyms: p29, AGP7, Wegener autoantigen), which belongs to the Trypsin/Chymotrypsin family. In 1988 several groups showed that the antigen is a protein with a molecular weight of 29 kDa. PR3 was already described in 1973 by Ohlsson and Olsson under the name neutrophile collagenase. In the meantime it seams certain, that autoantibodies against PR3 are highly specific as serological marker for the diagnosis of Wegener's granulomatosis (specificity: initial phase 50%, generalization phase >90%).Moreover there is a correlation between the concentration of the autoantibodies and the disease activity.
    2. Myeloperoxidase
    Myeloperoxidase is the major antigen in nearly 60% of the pANCA findings. The occurrence of autoantibodies against MPO is classified as relevant marker for the rapid progressive nephritis. Moreover these antibodies occur in 70-90% in all patients with serious kidney injury. Over and about they have also been detected at the Churg-Strauss-Syndrom (CSS), Microscopic Polyangiitis (MPA) and other vasculitis diseases. The concentration of the autoantibodies correlates well with the disease activity of MPA. MPA is also characterised by clinical manifestations of lung, kidney and respiratory tract, but these manifestations are, in contrast to WG, not granulomatous. However, these antibodies have, in contrast to the high specificity of PR3 anti-bodies for WG, a minor specificity of 60% in the diagnosis of MPA. The absence of autoantibodies against MPO and PR3, by simultaneous detection of ANA can be used as a tool for differential diagnosis between AAV and SLE induced vasculitis.
    3. BPI
    Bactericidal permeability-increasing protein, BPI is a membrane-located protein that is classed as an ANCA-Antigen of polymorph-nuclear granulocytes and monocytes that bind endotoxin. Its autoantibodies are now classified as cANCA. Due to BPIs high affinity to lipopolysaccharides its antimicrobial effect against Gram-negative bacteria is significant. BPI is cleaved and thus inactivated by using Elastase or other serine protease. Autoantibodies against BPI are above all detected in chronically infectious intestinal diseases such as Morbus Crohn or colitis ulcerosa. In contrast to anti-MPO and anti-PR3 autoantibodies, those against BPI seem not to have any association with vasculitis.
    4. Elastase
    Elastase is a serine protease with a sequence homology of 54% to that of proteinase 3. It occurs mainly in polymorph-nuclear neutrophil granulocytes (PMN), in macrophages and endothelial cells. The dismantling of proteoglycans by neutrophiles is mainly due to Elastase's proteolytic activity. Furthermore, Elastase participates decisively in tissue destruction connected with emphysemas and rheumatoid arthritis. Autoantibodies against this antigen are generally associated with inflammatory rheumatic disorders, e.g. rheumatoid arthritis and vasculitis.
    5. Cathepsin G
    The cathepsins belong to a group of intracellular proteases mainly found in lysosomes, especially of the spleen, the liver and the kidney. Cathepsin G is a serine protease and a further pANCA antigen. It participates to a great part in the destruction of osteoid tissue as of its hydrolytic properties. The autoantibodies against Cathepsin G occur mainly in collagenosis and other related inflammatory rheumatic diseases, e.g. SLE, Sj?gren′s syndrome and Felty's syndrome.
    6. Lysozyme
    Lysozyme is a glycosidase, which decomposes the glycosidic bond between C-1 of MNAc and C-4 of GlcNAc. Lysozyme is localised in the azurophilic as well as in the specific granules of neutrophils and in extracellular liquid compartments like tears and salivary, where it spreads out his antimicrobial activities against invading bacteria. LZ belongs also to the pANCA and autoantibodies against Lysozyme occur in higher frequency in rheumatoid vasculitis and inflammatory bowel disease like colitis ulcerosa.
    7. Lactoferrin
    Lactoferrin (LF) is an iron-binding protein, which occurs in high concentrations in secretions at mucosa surfaces, in tears and in milk. LF also resides in the specific granules of polymorphnuclear neutrophil leukocytes (PMN) and becomes exocytosed upon PMN activation. During active inflammatory disease, raised serum levels of LF can be measured. The physiological antimicrobial effect of Lactoferrin depends on its iron-binding capacity, because most of the bacteria require iron for their own physiological pathways. LF inhibits myelopoiesis, prevents complement activation and prevents the formation of hydroxyl radicals. It is quite possible that LF has several important roles, like secretory IgA, as a non-specific antiphlogistic defence factor at mucosal surfaces. LF belongs to the pANCA, depending on the redistribution from the granules toward the nuclei, upon ethanol fixation. Autoantibodies against Lactoferrin occur in higher frequency in patients with rheumatoid vasculitis (RV), colitis ulcerosa (CU) and primary sclerosing cholangitis (PSC).
  • Synonyms
  • LYZ; lysozyme; lysozyme (renal amyloidosis); lysozyme C; renal amyloidosis; 1,4-beta-N-acetylmuramidase C; LZM
Source (Host):E. coliSpecies:Lophura Leucomelanos
Product nameRecombinant Lophura Leucomelanos LYZ Protein (1-129 aa), His-SUMO-tagged
Source (Host):Wheat GermSpecies:Human
Product nameRecombinant Human LYZ Protein, GST-tagged
Source (Host):RiceSpecies:Human
Product nameRecombinant Human Lysozyme
Source (Host):Chicken eggsSpecies:Chicken
Product nameLysozyme From Chicken Eggs (Food Grade)
Source (Host):HEK293Species:Human
Product nameRecombinant Human LYZ, MYC/DDK-tagged, 13C & 15N Labeled
Source (Host):Mammalian CellsSpecies:Human
Product nameRecombinant Human LYZ
Source (Host):E. coliSpecies:Human
Product nameRecombinant Human LYZ protein, His-tagged
Source (Host):Mammalian CellsSpecies:Rhesus Macaque
Product nameRecombinant Rhesus monkey LYZ Protein, His-tagged
Source (Host):E. coliSpecies:Chicken
Product nameRecombinant Chicken LYZ protein, His-tagged
Source (Host):Mammalian CellsSpecies:Chicken
Product nameRecombinant Chicken LYZ
Source (Host):Mammalian CellsSpecies:Zebrafish
Product nameRecombinant Zebrafish LYZ
Source (Host):LYZ(Human)Species:Human
Product nameRecombinant Human Lysozyme
Source (Host):Species:Human
Product nameNative Human Lysozyme
Source (Host):Species:Human
Product nameNative Human LYZ
Source (Host):Species:Human
Product nameNative Human LYZ
Source (Host):Human bloodSpecies:Human
Product nameNative Human Lysozyme(salivary)
Source (Host):Species:Chicken
Product nameNative Chicken lysozyme
Source (Host):Species:Human
Product nameRecombinant Human LYZ 293 Cell Lysate

Involved Pathway

LYZ involved in several pathways and played different roles in them. We selected most pathways LYZ participated on our site, such as Salivary secretion, which may be useful for your reference. Also, other proteins which involved in the same pathway with LYZ were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name
Pathway Related Protein
Salivary secretion

Protein Function

LYZ has several biochemical functions, for example, identical protein binding, lysozyme activity. Some of the functions are cooperated with other proteins, some of the functions could acted by LYZ itself. We selected most functions LYZ had, and list some proteins which have the same functions with LYZ. You can find most of the proteins on our site.
Related Protein
Function identical protein binding
Related Protein TNPO3; USP4; ATL1; DVL2; TRP53; DYRK1A; RIPK1; CLDN8; VAMP2; MRAP2
Function lysozyme activity
Related Protein SPACA5; LYG2; LYZ2; LYZL6; LYZ1; LYZL2; LYZ; LYZL1; SPACA3; LYZL4

Interacting Protein

LYZ has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with LYZ here. Most of them are supplied by our site. Hope this information will be useful for your research of LYZ.
IKBKB; USP1; NME2; VHL; KHK; CNBP; NFKBIB; TRIP6; LRRK1; PARP11; WRAP73; USP25; gpmI; midostaurin; ssrna_ac

LYZ Related Articles

Zhang, CJ; Wang, YZ; et al. Silica-based surface molecular imprinting for recognition and separation of lysozymes. ANALYTICAL METHODS 6:8584-8591(2014).
Omer, M; Park, SY; et al. Preparation of QP4VP-b-LCP liquid crystal block copolymer and its application as a biosensor. ANALYTICAL AND BIOANALYTICAL CHEMISTRY 406:5369-5378(2014).