Recombinant Human Prosurfactant Protein B

Beta LifeScience SKU/CAT #: BLA-7342P

Recombinant Human Prosurfactant Protein B

Beta LifeScience SKU/CAT #: BLA-7342P
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Product Overview

Host Species Human
Accession P07988
Synonym 18 kDa pulmonary-surfactant protein 6 kDa protein PSP B PSPB PSPB_HUMAN Pulmonary surfactant apoprotein PSP-B Pulmonary surfactant-associated protein B Pulmonary surfactant-associated protein, 18-KD Pulmonary surfactant-associated proteolipid SPL(Phe) SFTB3 SFTP3 SFTPB SMDP1 SP B SP-B SPB surfactant protein B Surfactant, pulmonary-associated protein B surfactant-associated protein, pulmonary, 3
Description Recombinant Human Prosurfactant Protein B was expressed in Wheat germ. It is a Full length protein
Source Wheat germ
AA Sequence MAESHLLQWLLLLLPTLCGPGTAAWTTSSLACAQGPEFWCQSLEQALQCR ALGHCLQEVWGHVGADDLCQECEDIVHILNKMAKEAIFQDTMRKFLEQEC NVLPLKLLMPQCNQVLDDYFPLVIDYFQNQTDSNGICMHLGLCKSRQPEP EQEPGMSDPLPKPLRDPLPDPLLDKLVLPVLPGALQARPGPHTQDLSEQQ FPIPLPYCWLCRALIKRIQAMIPKGALAVAVAQVCRVVPLVAGGICQCLA ERYSVILLDTLLGRMLPQLVCRLVLRCSMDDSAGPRSPTGEWLPRDSECH LCMSVTTQAGNSSEQAIPQAMLQACVGSWLDREKCKQFVEQHTPQLLTLV PRGWDAHTTCQALGVCGTMSSPLQCIHSPDL
Molecular Weight 69 kDa including tags
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

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. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter.
Subcellular Location Secreted, extracellular space, surface film.
Database References
Associated Diseases Pulmonary surfactant metabolism dysfunction 1 (SMDP1); Respiratory distress syndrome in premature infants (RDS)

Gene Functions References

  1. rs7316 polymorphism associated with respiratory distress syndrome in Iranian premature newborns PMID: 28738720
  2. TGF beta markedly decreased expression of SP-A, SP-B, SP-C, fatty acid synthase, and the phospholipid transporter ABCA3. However, TGF beta increased protein levels of SP-D with little change in mRNA levels. PMID: 29621540
  3. Surfactant protein B suppresses lung cancer progression by inhibiting secretory phospholipase A2 activity and arachidonic acid production. PMID: 28743125
  4. Data show that the thermal transitions observed in N-terminal propeptide of proSP-B (SP-BN) may correspond to the unfolding of certain protein domains or subdomains and/or to oligomers dissociation whereas the overall protein shows resistance to temperature-induced unfolding up to ~ 86 degrees C. PMID: 27380171
  5. SP-A (+186A/G) and SP-B (1580C/T) polymorphisms are strongly associated with the risk of respiratory distress syndrome (RDS) in preterm infants. Notably, reduced serum SP-A levels were correlated with a high risk of RDS and may serve as novel biomarkers for RDS detection and monitoring. PMID: 28011976
  6. Differences were found regarding SPA and pro-SPB expression in the vast majority of subjects: in some lungs, SPA was more expressed whereas in others pro-SPB showed an higher degree of immunoreactivity. The expression of both surfactant proteins was not strictly correlated with gestational age. PMID: 27734990
  7. There is no significant association between the gene polymorphism of the R236C site in exon 7 of SP-B gene and the incidence ofneonatal respiratory distress syndrome (NRDS) in Han populations in that region. PMID: 27655533
  8. 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-B (SFTPB) and we did not find any rare mutations in SFTPB PMID: 26547207
  9. mice with SP-B-C allele are more susceptible to S. aureus pneumonia than mice with SP-B-T allele, and that CMC2.24 attenuates lung injury thus reducing mortality. PMID: 26863117
  10. In term newborns with pneumonia, SP-B increases with respect to total phospholipids, and disaturated-phosphatidylcholine and is turned over at a faster rate. PMID: 26107393
  11. SP-B -18C/A and 1580C/T polymorphisms are associated with bronchopulmonary dysplasia PMID: 26045806
  12. These results demonstrate for the first time that human SP-B C allele is more susceptible to bacterial pneumonia than SP-B T allele in vivo. PMID: 26620227
  13. Significant differences in frequency of occurrence of unfavorable genotypes CC rs1965708, AA rs1059046 of SFTPA2 gene and CC rs1130866 of SFTPB gene in influenza patients in comparison with individuals of the control group were not detected. PMID: 26950992
  14. Investigated the relationship between SP-A2 and SP-B gene polymorphisms and respiratory distress syndrome in preterm neonates. PMID: 26061924
  15. Given these fact SP-B deficiency may be considered as a further field for research on regenerative therapy i. e. stem cell administration in models of postnatal SP-B deficiency. PMID: 25565191
  16. Results support a critical role of SP-B for promoting pulmonary surface film formation. PMID: 25360829
  17. SFTPB variants are associated with chronic obstructive pulmonary disease susceptibility and lung function in the Chinese Han population. PMID: 25299874
  18. Surfactant protein B gene polymorphism is associated with severe influenza. PMID: 24337193
  19. data support the hypothesis that proSP-B glycosylation due to Ile131Thr variation may have a causal role in genetic susceptibility to acute respiratory distress PMID: 24002332
  20. It was concluded that the polymorphisms of SP-B intron 4 and C/A-18 could be associated with BPD in Chinese Han infants, and the del allele of intron 4 and A allele of C/A-18 might be used as markers of susceptibility in the disease. PMID: 23771654
  21. there was no evidence for any association between common polymorphisms in the SP-B and SP-D genes and COPD risk (all p>0.05). PMID: 24093802
  22. Glucocorticoids mediated surfactant protein B production, maturation, and release is amplified by caffeine. PMID: 24163141
  23. macrophages participate in the repression of SFTPB expression by LPS, and that macrophage-released cytokines (including TNF) regulate the transcription factor CEBPB PMID: 23590297
  24. D2S388-5 microsatellite polymorphism of surfactant protein B may be associated with susceptibility to COPD in Xinjiang Kazakhs. PMID: 23088317
  25. elevated expression in nasal mucosa in chronic rhinosinusitis with polyps PMID: 23406594
  26. Mutations in exon 4 of the surfactant protein B gene demonstrate an association between homozygous mutations with C/C genotype in SP-B gene and neonatal respiratory distress. PMID: 23330012
  27. caffeine is able to induce the expression of SP-transcription factors and affects the signaling pathways of glucocorticoids, amplifying their effects PMID: 23272120
  28. The results indicate that tryptophan oxidation causes substantial disruptions in helical structure and lipid interactions. PMID: 21128671
  29. review focuses on published association studies of surfactant proteins A and D genetic polymorphisms with respiratory, and non-respiratory diseases in adults, children, and newborns [review] PMID: 22201752
  30. The present study demonstrated that the AG genotype of AG 9306 polymorphism was a protective factor against the development of respiratory distress syndrome, other polymorphisms studied (G/C at 8714, C/T at 1580, A/C at -18) were not associated with RDS. PMID: 21180884
  31. In patients undergoing major vascular abdominal surgery, SP-B values increase progressively during mechanical ventilation stages compared to advanced glycation end-products (RAGE) kinetics. PMID: 21736957
  32. SP-B 1580C/T polymorphism contributes to the etiology of respiratory distress syndrome. PMID: 22289747
  33. Circulating levels of SP-B increase with greater smoking burden and independently associate with abdominal abdominal aortic plaque among current smokers. PMID: 21817103
  34. Genetic variations in the gene coding for surfactant protein B are associated with more severe lung injury as indicated by the association of specific single nucleotide polymorphism genotypes and haplotypes PMID: 21283003
  35. Surfactant protein B and RAGE increases in the plasma during cardiopulmonary bypass PMID: 20650982
  36. Surfactant protein B polymorphisms have a role in pulmonary function and COPD PMID: 20693256
  37. Disaturated-phosphatidylcholine and surfactant protein-B have a different turnover both in healthy and diseased lungs. PMID: 21429235
  38. Absence of this protein resulted in Congenital pulmonary alveolar proteinosis in two newborn children PMID: 20005435
  39. Surfactant protein-B 121ins2 heterozygosity is associated with reduced lung function and increased risk for COPD among smokers PMID: 19833825
  40. review of lipid-protein interactions of hydrophobic proteins SP-B and SP-C in lung surfactant assembly and dynamics PMID: 11699574
  41. Data suggest that SMAD3 interactions with the positive regulators NKX2.1 and HNF-3 underlie the molecular basis for TGF-beta-induced repression of surfactant protein B gene transcription. PMID: 12161428
  42. role of Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580 in disease PMID: 12356334
  43. suggest that polymorphisms in intron 4 of the surfactant protein B gene independently modify the course of neonatal respiratory distress syndrome PMID: 12424586
  44. An association between SP-B polymorphism and RDS was found in premature, first-born twins. In particular, the threonine allele was associated with an increased risk of RDS. PMID: 12483294
  45. dimeric SP-B(1-25) is more efficient in restoring lung function in neonatal RDS and ARDS than monomeric SP-B(1-25) surfactant. PMID: 12490037
  46. surfactant protein B expression is regulated by an enhancer region which binds to thyroid transcription factor-1, retinoic acid receptor, signal transducers and activators of transcription 3, nuclear receptor coactivators (SRC-1, ACTR, TIF2, and CBP/p300 PMID: 12573987
  47. Mutataions and Polymorphisms in SFTPB is associated with severe unexplained respiratory distress PMID: 12784301
  48. SP-B expression is regulated by PPARgamma in the lung PMID: 12829715
  49. Reduced SP-B expression due to elevated nitric oxide levels can contribute to lung injury. PMID: 12896877
  50. In human lungs, mature SP-B is involved in the structural organization of lamellar bodies and tubular myelin by the formation of core particles. PMID: 12972403

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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