Recombinant Human Surfactant protein D/SP-D is a Human Full Length protein, in the 21 to 375 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
COLEC7, PSPD, SFTP4, SFTPD, Pulmonary surfactant-associated protein D, PSP-D, SP-D, Collectin-7, Lung surfactant protein D
Recombinant Human Surfactant protein D/SP-D is a Human Full Length protein, in the 21 to 375 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
pH: 7.2
Constituents: 99% Phosphate Buffer, 0.88% Sodium chloride
The purity of ab152069 is greater than 95%, as determined by SEC-HPLC and reducing SDS-PAGE.
Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
Belongs to the SFTPD family.
The N-terminus is blocked.
Previously labelled as Surfactant protein D.
Surfactant protein D (SP-D) also known as protein D functions as an important component of the innate immune system. It weighs around 43 kDa and is primarily expressed in pulmonary alveoli where lung cells synthesize it. SP-D belongs to the collectin family and has a C-type lectin domain that allows binding to carbohydrate structures on microbial surfaces. This ability enables SP-D to interact directly with various pathogens and infected cells targeting them for clearance. Researchers often study SP-D with 'anti-surfactant' antibodies using methods like the ELISA protocol including versions like ELISA Sp and ELISA Denise.
SP-D contributes to host defense by enhancing the uptake and elimination of pathogens by immune cells such as macrophages. Part of a larger protein complex SP-D can opsonize bacteria and viruses facilitating phagocytosis. Its role extends to modulating inflammation by affecting the production of pro-inflammatory cytokines. By maintaining homeostasis in surfactant composition it indirectly supports lung function and protects against lung injury. SP-D’s function involves communication and transmission of signals within the immune system making it integral to pulmonary immune processes.
Surfactant protein D is involved in the regulation of the complement and coagulation cascades as well as the pathogen recognition pathway. It is closely related to other collectins such as surfactant protein A (SP-A) which share similar mechanisms in the immune response. SP-D's interaction within these pathways highlights its role in identifying and neutralizing pathogens. Through its connections with related proteins SP-D plays an important part in modulating immune responses ensuring effective pathogen elimination without excessive inflammation.
SP-D has been linked with respiratory diseases such as chronic obstructive pulmonary disease (COPD) and pulmonary fibrosis. These conditions may involve impaired SP-D function or expression levels potentially due to genetic factors or environmental influences. SP-D also interacts with proteins like SP-A in these diseases participating in lung immune responses. Disrupted regulation of SP-D can contribute to chronic inflammatory states in the lungs exacerbating disease progression and leading to compromised lung function. Understanding SP-D's role in these contexts offers potential therapeutic insights for targeting pathological inflammation.
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