mouth

Expression system: HEK293 Cells
Length: 1-344, Partial
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-529, Partial
Activity: Not Tested

Expression system: E. coli
Length: 38-208, Full Length of Mature Protein
Activity: Organoid Coculture、Cells

Lysosome membrane protein II (LIMPII),also known as SCARB2, is a type III multi-pass membrane glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes on all tissues and cell types so far examined. Earlier studies in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal lysosomal compartment. The protein deficiency in mice was reported to impair cell membrane transport processes and cause pelvic junction obstruction, deafness, and peripheral neuropathy. Further studies in human showed that this protein is identified as a receptor for EV71 (human enterovirus species A, Enterovirus 71) and CVA16 (coxsackievirus A16) which are most frequently associated with hand, foot and mouth disease (HFMD). Mutations in this gene caused an autosomal recessive progressive myoclonic epilepsy-4 (EPM4), also known as action myoclonus-renal failure syndrome (AMRF). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. In addition, LIMPII also has been shown to bind thrombospondin-1, may contribute to the pro-adhesive changes of activated platelets during coagulation, and inflammation.

Expression system: E. coli
Length: 44-556, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 22-706, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-394, Partial
Activity: Not Tested

Herpes simplex viruses (human herpesviruses types 1 and 2) commonly cause recurrent infection affecting the skin, mouth, lips, eyes, and genitals. Herpes simplex virus type 2 (HSV-2) infection is responsible for significant neurological morbidity, perhaps more than any other virus. Herpes simplex virus type 2–associated neurological disease may result from primary infection or reactivation of latent HSV-2. Common severe infections include encephalitis, meningitis, neonatal herpes, and, in immunocompromised patients, disseminated infection.

Scavenger Receptor Class B Member 2 (SCARB2) is a type III multi-pass membrane glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes on all tissues and cell types so far examined. Earlier studies in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal lysosomal compartment. The protein deficiency in mice was reported to impair cell membrane transport processes and cause pelvic junction obstruction, deafness, and peripheral neuropathy. Further studies in human showed that this protein is identified as a receptor for EV71 (human enterovirus species A, Enterovirus 71) and CVA16 (coxsackievirus A16) which are most frequently associated with hand, foot and mouth disease (HFMD). Mutations in this gene caused an autosomal recessive progressive myoclonic epilepsy-4 (EPM4), also known as action myoclonus-renal failure syndrome (AMRF). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. In addition, SCARB2 also has been shown to bind thrombospondin-1, may contribute to the pro-adhesive changes of activated platelets during coagulation, and inflammation.

ITGB6 is known to be one of the major receptor components involved in host tropism of foot-and-mouth disease (FMD) virus in cattle. A competitive PCR technique called ARMS PCR was adapted to identify a single-nucleotide polymorphism (SNP), G29A, db SNP Id: rs109075046, in the 5' untranslated region (5'UTR) of the bovine ITGB6 gene. ITGB6 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 75.4 kDa and the accession number is P18564-1.

BPIFB1, also known as LPLUNC1, belongs to the BPI LBP Plunc superfamily, plunc family. BPIFB1 may be involved in the innate immune response to bacterial exposure in the mouth, nasal cavities, and lungs. BPIFB1 is expressed in the upper respiratory tract and oral cavity, which may function in host defence. The expression of BPIF proteins is associated with CF lung disease in humans and mice. It is unclear if this elevation of protein production, which results from phenotypic alteration of the cells within the diseased epithelium, plays a role in the pathogenesis of the disease. BPIFB1 is an abundant, secreted product of goblet cells and minor mucosal glands of the respiratory tract and oral cavity and suggest that the protein functions in the complex milieu that protects the mucosal surfaces in these locations.

Expression system: HEK293 Cells
Length: 21-392, Extracellular Domain
Activity: Not Tested