Keratins are a large family of proteins that form the intermediate filament cytoskeleton of epithelial cells,which are classified into two major sequence types. Type I keratins are a group of acidic intermediate filament proteins,including K9–K23,and the hair keratins Ha1–Ha8. Type II keratins are the basic or neutral courterparts to the acidic type I keratins,including K1–K8,and the hair keratins,Hb1–Hb6. KRT7,also named as cytokeratin 7,is one member of type II basic cytokeratin. It is specifically expressed in the simple epithelia lining the cavities of the internal organs and in the gland ducts and blood vessels,and their neoplasms. KRT7 is marker of epithelial tissues,but not present in carcinomas of stratified squamous cell origin.This antibody is specifically against KRT7.
Protein disulfide-isomerase, also known as Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55 and P4HB, is a peripheral membrane protein which belongs to the protein disulfide isomerase family. P4HB is highly abundant. In some cell types, it seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. P4HB localizes near CD4-enriched regions on lymphoid cell surfaces. It is identified by mass spectrometry in melanosome fractions from stage I to stage IV. P4HB reduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell. P4HB catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, it seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. P4HB may therefore cause structural modifications of exofacial proteins. Inside the cell, it seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, P4HB functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, it facilitates aggregation (anti-chaperone activity). P4HB may be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. It also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.
Extracellular glycoprotein lacritin (Lacritin) is a secreted protein which consists of 119 amino acids after cleavage of the N-terminal signal peptide and displays several predicted alpha helices, mostly in the C-terminal half. Lacritin is highly expressed in the lacrimal gland, localizes primarily to secretory granules and secretory fluid. Lacritin modulates lacrimal acinar cell secretion, promotes ductal cell proliferation, and stimulates signaling through tyrosine phosphorylation and release of calcium. Lacritin is thus a multifunctional prosecretory mitogen with cell survival activity. Natural or bacterial cleavage of lacritin releases a C-terminal fragment that is bactericidal. Lacritin cell targeting is dependent on the cell surface heparan sulfate proteoglycan syndecan-1 (SDC1). Binding utilizes an enzyme-regulated 'off-on' switch in which active epithelial heparanase (HPSE) cleaves off heparan sulfate to expose a binding site in the N-terminal region of syndecan-1's core protein.
β-Lactamase-like Protein 2 (LACTB2) is a number of the metallo-beta-lactamase superfamily.LACTB2 also belongs to the Glyoxalase II family. LACTB2 is 288 amino acids long with 8 zinc-binding domains. The LACTB2 gene is expressed at high levels and annotates structural defects or features in 4 cDNA clones. LACTB2 proteins are expected to have hydrolase activity and metal ion-binding functions. LACTB2 protein is found to localize in mitochondrion. Other functions of LACTB2 is yet unknown.
Lactotransferrin is a member of the transferrin family that transfer iron to the cells and control the level of free iron in the blood and external secretions. Lactotransferrin is a secreted protein and contains two transferrin-like domains. Lactotransferrin can be cleaved into the following four chains: Kaliocin-1; Lactoferroxin-A; Lactoferroxin-B; and Lactoferroxin-C. Lactoferroxin A; Lactoferroxin B; and Lactoferroxin C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors; while Lactoferroxin B and Lactoferroxin C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors. LTF has antimicrobial activity (bacteriocide; fungicide) and is part of the innate defense; mainly at mucoses.
Human Lymphocyte activation gene 3 protein( LAG3) is a member of immunoglobulin (Ig) superfamily. LAG3 contains 4 extracellular Ig-like domains. The LAG3 gene contains 8 exons. LAG3 is involved in lymphocyte activation and can bind to HLA class-II antigens. It is selectively expressed in activated T and NK cells. LAG3 has a negative regulatory function in T cells and acts as as a new marker of T cell induced B cell activation. As a soluble molecule, LAG3 activates antigen-presenting cells through MHC class II signaling. It can lead to increased antigen-specific T-cell responses in vivo. LAG-3 has higher affinity to MHC class II than CD4.
Human Lymphocyte activation gene 3 protein( LAG3) is a member of immunoglobulin (Ig) superfamily. LAG3 contains 4 extracellular Ig-like domains. The LAG3 gene contains 8 exons. LAG3 is involved in lymphocyte activation and can bind to HLA class-II antigens. It is selectively expressed in activated T and NK cells. LAG3 has a negative regulatory function in T cells and acts as as a new marker of T cell induced B cell activation. As a soluble molecule; LAG3 activates antigen-presenting cells through MHC class II signaling. It can lead to increased antigen-specific T-cell responses in vivo. LAG-3 has higher affinity to MHC class II than CD4.
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