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SFTPC encodes the pulmonary-associated surfactant protein C (SPC), an extremely hydrophobic surfactant protein essential for lung function and homeostasis after birth. Additionally we are shipping Surfactant Protein C Kits (43) and Surfactant Protein C Proteins (2) and many more products for this protein.
Showing 10 out of 106 products:
Human Polyclonal Surfactant Protein C Primary Antibody for IHC (fro), IHC (p) - ABIN1108993
Diaz, Valdivia, Martinez, Palacios, Harris, Novales, Garrido, Valderrama, Shilling, Kirberg, Hebel, Fierro, Bravo, Siegel, Leon, Klapp, Venegas: Helicobacter pylori vacA s1a and s1b alleles from clinical isolates from different regions of Chile show a distinct geographic distribution. in World journal of gastroenterology : WJG 2006
Show all 7 references for ABIN1108993
Human Polyclonal Surfactant Protein C Primary Antibody for EIA, IF - ABIN954775
Wambach, Yang, Wegner, An, Hackett, Cole, Hamvas: Surfactant protein-C promoter variants associated with neonatal respiratory distress syndrome reduce transcription. in Pediatric research 2010
Show all 5 references for ABIN954775
Human Monoclonal Surfactant Protein C Primary Antibody for ELISA, WB - ABIN1098147
Zhong, Zhou, Ann, Minoo, Liu, Banfalvi, Krishnaveni, Dubourd, Demaio, Willis, Kim, duBois, Crandall, Beers, Borok: Role of endoplasmic reticulum stress in epithelial-mesenchymal transition of alveolar epithelial cells: effects of misfolded surfactant protein. in American journal of respiratory cell and molecular biology 2011
Show all 2 references for ABIN1098147
Human Polyclonal Surfactant Protein C Primary Antibody for IHC, WB - ABIN2776859
Garmany, Wambach, Heins, Watkins-Torry, Wegner, Bennet, An, Land, Saugstad, Henderson, Nogee, Cole, Hamvas: Population and disease-based prevalence of the common mutations associated with surfactant deficiency. in Pediatric research 2008
Human Monoclonal Surfactant Protein C Primary Antibody for ELISA, WB - ABIN520151
Wong, Keating, Lu, Duchesneau, Wang, Sacher, Hu, Waddell: Identification of a bone marrow-derived epithelial-like population capable of repopulating injured mouse airway epithelium. in The Journal of clinical investigation 2009
Data suggests that different SP-C mutations have unique consequences for interstitial lung diseases. Mutations here resulted in aberrant proSP-c products
In vivo deficiency of SP-C leads to inflammation, increased cytokine production by type II cells, and persistent inflammation after repetitive LPS (show TLR4 Antibodies) stimulation.
Transgenic restoration of SP-C reduces inflammation and improves viral clearance in the lungs of SP-C deficient mice.
The SPC H2B-GFP allele allowed the FACS-based enrichment and gene expression profiling of AT2 cells.
misfolded surfactant protein C has a role in endoplasmic reticulum stress in epithelial-mesenchymal transition of alveolar epithelial cells
Cytoprotective-selective activated protein C (show PROC Antibodies) attenuates Pseudomonas aeruginosa-induced lung injury in mice
The differential expression of mRNA by both airway level and lung region was determined for surfactant protein C.
To target type II alveolar epithelial cells with this model, we generated transgenic mice that express DTR (show HBEGF Antibodies) off of the type II cell-specific surfactant protein C (SPC) promoter.
Nedd4-2 (show NEDD4L Antibodies)-mediated ubiquitination regulates lumenal relocation of SP-C, leading to processing and, ultimately, secretion of SP-C.
pulmonary surfactant protein C binds with CD14 (show CD14 Antibodies) and lipopolysaccharide
In interstitial lung disease, abnormal proSP-C was seen in small and dense lamellar bodies in type II alveolar epithelial cells. A549 cells expressing proSP-C(L55F) had abnormal organelles. It partly colocalized in CD63 (show CD63 Antibodies)-positive cytoplasmic vesicles .
We sequenced SFTPC and analyzed morphology, ultrastructure and SP expression in lung tissue when available. We identified eight subjects who were heterozygous for SP-C mutations.
analysis of clinical patterns in patients with SFTPC mutations
support a chaperone function of the BRICHOS domain, possibly together with the linker region, during pro-SP-C biosynthesis in the endoplasmic reticulum
cleavage of BRICHOS in a loop region that is cleaved during proSP-C biosynthesis results in increased capacity to delay Abeta (show APP Antibodies)(42) fibril formation.
Structural modeling of transmembrane (BRICHOS) domains of SFTPC precursor and BRI2/ITM2B (integral membrane protein 2B (show ITM2B Antibodies)) identifies conserved region structurally complementary to beta-sheet-/amyloid-prone regions in BRICHOS domain-containing proteins.
(surfactant protein C), a specific functional marker of human type II alveolar epithelial cells, was detected in differentiated cells by RT-PCR (reverse transcription-PCR) analysis after day 15.
Several genetic abnormalities have been associated with familial pulmonary fibrosis. The present study examined the genes coding for surfactant protein-C, ATPbinding cassette protein A3 and telomerase, and found no abnormalities.
Mutation increases endoplasmic reticulum stress and induces apoptotic cell death compared with wild-type SP-C in alveolar type II cells, supporting the significance of this mutation in the pathogenesis of pulmonary fibrosis.
Data show that, in contrast to its wild-type counterpart, SP-C(I73T) is misdirected to the plasma membrane and subsequently internalized to the endocytic pathway via early endosomes, leading to the accumulation of abnormally processed proSP-C isoforms.
The hydrophobic surfactant proteins SP-B and SP-C induce formation of bicontinuous inverse cubic phases.
Data indicate that surfactant protein C (SP-C) structure does not seem altered by palmitoylation or the lipid environment.
Data suggest that transient exposure of surfactant to polymers like hyaluronan (HA) could be a promising strategy for the production of more efficient therapeutic surfactants SP-A (show SFTPA1 Antibodies), SP-B and SP-C preparations.
SP-B and SP-C proteins promote the formation of proteolipid channels in which lipid molecules are functionally involved.
Palmitoylation is key for the functional cooperation of SP-C with SP-B that enables cholesterol-containing surfactant films to reach very low tensions under compression.
Surfactant protein SP-B promoted film formation and reextension to lower surface tensions than SP-C.
finds evidence of an interaction between cholesterol-enriched phases and SP-C, and confirms that physiological concentrations of cholesterol do not have any detrimental effect on lung surfactant with a proper lipid and protein composition
study the effects of the interaction of SP-C with Dipalmitoleoylphosphatidylethanolamine on the adsorption and interfacial disintegration of phospholipid lamellar and non-lamellar phases and on the phase coexistence in insoluble DPoPE monomolecular films
This gene encodes the pulmonary-associated surfactant protein C (SPC), an extremely hydrophobic surfactant protein essential for lung function and homeostasis after birth. Pulmonary surfactant is a surface-active lipoprotein complex composed of 90% lipids and 10% proteins which include plasma proteins and apolipoproteins SPA, SPB, SPC and SPD. The surfactant is secreted by the alveolar cells of the lung and maintains the stability of pulmonary tissue by reducing the surface tension of fluids that coat the lung. Multiple mutations in this gene have been identified, which cause pulmonary surfactant metabolism dysfunction type 2, also called pulmonary alveolar proteinosis due to surfactant protein C deficiency, and are associated with interstitial lung disease in older infants, children, and adults. Alternatively spliced transcript variants encoding different protein isoforms have been identified.
surfactant protein C
, surfactant, pulmonary-associated protein C
, pulmonary surfactant-associated protein C
, pulmonary surfactant-associated proteolipid SPL(Val)
, BRICHOS domain containing 6
, pulmonary surfactant apoprotein-2 SP-C
, Surfactant pulmonary-associated protein C
, Surfactant, pulmonary-associated protein C
, surfactant associated protein C
, type I SP-C
, type II SP-C