Recombinant Human Pulmonary Surfactant-Associated Protein C (SFTPC) Protein (His)

Name: Recombinant Human Pulmonary Surfactant-Associated Protein C (SFTPC) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09771P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Pulmonary Surfactant-Associated Protein C (SFTPC) Protein (His) is produced by our Mammalian cell expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P11686
Target Symbol	SFTPC
Synonyms	BRICD6; BRICHOS domain containing 6; PSP C; PSPC; PSPC_HUMAN; Pulmonary surfactant apoprotein 2; Pulmonary surfactant apoprotein PSP C; pulmonary surfactant apoprotein-2 SP-C; Pulmonary surfactant associated protein C; Pulmonary surfactant associated proteolipid SPL pVal; Pulmonary surfactant associated proteolipid SPL(Val); Pulmonary surfactant protein SP5; Pulmonary surfactant-associated protein C; Pulmonary surfactant-associated proteolipid SPL(Val); SFTP 2; SFTP2; SFTPC; SFTPC surfactant pulmonary associated protein C; SMDP2; SP 5; SP C; SP-C; SP5; SPC; Surfactant associated protein pulmonary 2; Surfactant protein c; Surfactant proteolipid SPL-pVal; Surfactant pulmonary associated protein C
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	N-6His
Target Protein Sequence	FGIPCCPVHLKRLLIVVVVVVLIVVVIVGALLMGL
Expression Range	24-58aa
Protein Length	Full Length of Mature Protein
Mol. Weight	7.7kDa
Research Area	Transport
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces.
Subcellular Location	Secreted, extracellular space, surface film.
Database References	HGNC: 10802 OMIM: 178620 KEGG: hsa:6440 STRING: 9606.ENSP00000316152 UniGene: PMID: 27884070 a novel mutation in SFTPC [c.435G->A, p.(Gln145)] that was associated with onset of symptoms in early infancy, progressive respiratory failure with need for prolonged support, and eventual lung transplant at 1 year of age (Review) PMID: 27362365 c.435G>C variant in the SFTPC gene associated with fatal neonatal respiratory distress syndrome. The c.435G>C mutation is deleterious not because of its amino acid substitution but because of its subsequent splicing defect and should be referred to as r.325_435del and p.Leu109_Gln145del. PMID: 28295039 an intricate link between caveolin-1 and Src kinase-mediated cell signaling and alveolar epithelial cell apoptosis due to loss of SP-C expression through p53 and uPA system-mediated cross-talk, is reported. PMID: 28385810 Rare mutations in surfactant-associated genes contribute to neonatal respiratory distress syndrome. The frequency of mutations in these genes in the Chinese population is unknown. We resequenced all exons of the surfactant protein-C (SFTPC) and we did not find any rare mutations in SFTPC PMID: 26547207 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-positive cytoplasmic vesicles . PMID: 26375473 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. PMID: 25782673 analysis of clinical patterns in patients with SFTPC mutations PMID: 25657025 support a chaperone function of the BRICHOS domain, possibly together with the linker region, during pro-SP-C biosynthesis in the endoplasmic reticulum PMID: 26041777 cleavage of BRICHOS in a loop region that is cleaved during proSP-C biosynthesis results in increased capacity to delay Abeta(42) fibril formation. PMID: 25891900 Structural modeling of transmembrane (BRICHOS) domains of SFTPC precursor and BRI2/ITM2B (integral membrane protein 2B) identifies conserved region structurally complementary to beta-sheet-/amyloid-prone regions in BRICHOS domain-containing proteins. PMID: 24099305 The A116D mutation leads to impaired processing of proSP-C in alveolar epithelial cells, alters cell viability and lipid composition, and also activates cells of the immune system. PMID: 22458263 (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. PMID: 21542803 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. PMID: 21165348 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. PMID: 21828032 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. PMID: 21707890 Our study indicates that missense single nucleotide polymorphisms and haplotypes of SFTPA1, SFTPA2 and SFTPD are associated with susceptibility to community-acquired pneumonia(CAP), and that several haplotypes also influence severity and outcome of CAP. PMID: 21310059 misfolded surfactant protein C has a role in endoplasmic reticulum stress in epithelial-mesenchymal transition of alveolar epithelial cells PMID: 21169555 sequencing of the five translated exons of the SFTPC gene1 from blood samples demonstrated the same heterozygous I73T substitution in both the child and the mother; neither of them had mutation of the SFTPB and ABCA3 genes. PMID: 21248320 JNK signaling has a role in mediating SP-C BRICHOS-induced cytokine release PMID: 20463293 children with SFTPC mutation associated lung diseases have HRCT pattern that were characterized by ground-glass opacities that were predominately diffuse but can be patchy in some cases and lung cysts with thin wall and different sizes. PMID: 20658481 Mutations in the gene encoding surfactant protein C (SFTPC) have been found in children and families with idiopathic pneumonias PMID: 20656946 I73T mutation of SFTPC protein leads to impaired processing of proSP-C in alveolar type II cells, alters their stress tolerance and surfactant lipid composition, and activates cells of the immune system. PMID: 21092132 Reduced SFTPC transcription contributes to the genetic risk for neonatal respiratory distress syndrome in developmentally susceptible infants. PMID: 20539253 two novel mutations were identified in highly conserved areas of the SFTPC gene, and show that heterozygotes for the mutations have normal lung function and are unaffected by COPD and interstitial lung disease. PMID: 19910179 Although neonatal presentation may be observed in some patients with mutations in the BRICHOS domain, surfactant protein C gene (SFTPC)-associated lung disease usually presents within the first months of life with cough, tachypnoea and failure to thrive. PMID: 20403820 The human SP-C promoter sequence will enhance gene expression specifically in alveolar type II epithelial cells in mouse lung. PMID: 20054353 Subclinical fibrotic changes may be present in family members of patients with SFTPC mutation-associated interstitial lung disease and suggest ABCA3 variants could affect disease pathogenesis. PMID: 20371530 SFTPC SNP rs4715 associates with the duration of preterm premature rupture of fetal membranes, and SP-C is expressed in gestational tissues. We propose that fetal SFTPC moderates inflammatory activation within the fetal extra-embryonic compartment PMID: 19735006 Data show that knockdown of MKS3 inhibited degradation of mutant SP-C. PMID: 19815549 review of synthesis and post-translational processing of surfactant protein C PMID: 11699575 mutations causally related to familial interstitial lung disease PMID: 11893657 Biosynthesis of surfactant protein C (SP-C). Sorting of SP-C proprotein involves homomeric association via a signal anchor domain PMID: 11907042 associated with usual interstitial pneumonitis and cellular nonspecific interstitial pneumonitis in one kindred PMID: 11991887 role of cathepsin H in processing in pneumocytes PMID: 12034564 surfactant protein C processing requires a type II transmembrane topology directed by juxtamembrane positively charged residues PMID: 12933801 surfactant protein C has a role in interstitial lung disease and lung development PMID: 14525980 An incompletely processed form of SP-C precursor found in association with childhood SP-B deficiency associates with surfactant phospholipids and is secreted into the airspaces with the large aggregate form of surfactant, but it lacks surface activity. PMID: 15049696 Observations suggest that individuals with this particular mutation in surfactant protein C gene might be at increased risk of interstitial lung disease of variety of types. PMID: 15133475 NMR solution structure and analysis of potential C-terminal dimerization site of a recombinant mutant of surfactant-associated protein C. PMID: 15153097 Missense mutation of the surfactant protein C gene is associated with interstitial lung disease in newborn. PMID: 15293602 proSP-C BRICHOS mutations induce a dynamic toxic gain-of-function, causing apoptotic cell death both by early ER accumulation leading to an exaggerated unfolded protein response and by enhanced deposition of cellular aggregates associated with proteasome PMID: 15778495 Infection of cells expressing mutant SP-C with respiratory syncytial virus resulted in significantly enhanced cytotoxicity associated with accumulation of the mutant proprotein, pronounced activation of the unfolded protein response, and cell death. PMID: 16449190 Erm is involved in SP-C regulation, which results from an interaction with TTF-1 PMID: 16613858 Recombinant SP-C forms improved movement of phospholipid molecules into the interface (during adsorption), or out from the interfacial film (during compression) PMID: 16631109 Brichos domain-containing C-terminal part of pro-surfactant protein C binds to an unfolded poly-val transmembrane segment PMID: 16709565 The influence of palmitoylation was studied for full length SP-Cs as well as truncated variants with the N-terminal residues 1-17 and 1-13, respectively. PMID: 17051367 an inverse SFTPC haplotype distribution was found between children with asthma and respiratory syncytial virus infection PMID: 17121584 These results suggest common cellular responses, including initiation of cell-death signaling pathways, to these lung disease-associated SP-C BRICHOS domain proteins. PMID: 17586700 finding of heterozygosity for ABCA3 mutations in severely affected infants with SFTPC I73T, and independent inheritance from disease-free parents supports that ABCA3 acts as a modifier gene for the phenotype associated with an SFTPC mutation. PMID: 17597647

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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