Recombinant Rat Pulmonary surfactant-associated protein D(Sftpd)

Code CSB-YP021175RA
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP021175RA
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP021175RA-B
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP021175RA
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP021175RA
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity >85% (SDS-PAGE)
Target Names Sftpd
Uniprot No. P35248
Alternative Names Sftpd; Sftp4; Pulmonary surfactant-associated protein D; PSP-D; SP-D; CP4; Lung surfactant protein D
Species Rattus norvegicus (Rat)
Expression Region 20-374
Target Protein Sequence A EMKTLSQRSI TNTCTLVLCS PTENGLPGRD GRDGREGPRG EKGDPGLPGP MGLSGLPGPR GPVGPKGENG SAGEPGPKGE RGLVGPPGSP GISGPAGKEG PSGKQGNIGP QGKPGPKGEA GPKGEVGAPG MQGSAGAKGP AGPKGERGAP GEQGAPGNAG AAGPAGPAGP QGAPGSRGPP GLKGDRGAPG DRGIKGESGL PDSAALRQQM EALNGKLQRL EAAFSRYKKA ALFPDGQSVG DKIFRAANSE EPFEDAKEMC RQAGGQLASP RSATENAAVQ QLVTAHSKAA FLSMTDVGTE GKFTYPTGEA LVYSNWAPGE PNNNGGAENC VEIFTNGQWN DKACGEQRLV ICEF
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
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.
Gene References into Functions
  1. in acute lung injury, serum level increased from day 5, peaked on day 10, and then gradually decreased until day 28 PMID: 27541374
  2. SPA binds dipalmitoyl-phosphatidylcholine, the major surfactant lipid component, but not phosphatidylinositol; SPD exhibits the opposite preference. Data suggest flexibility in a key surface loop supports distinctive lipid binding of SPA; quadruple mutant SPA (E171D/P175E/R197N/K203D) that introduces SPD-like loop-stabilizing Ca2+ binding site in carbohydrate recognition domain exhibits ligand-binding preferences of SPD. PMID: 28719181
  3. In rat SP-D overexpressed mice, the lipopolysaccharide-induced levels of TNF-alpha and IL-10 in amniotic fluid and fetal serum and the expression of IL-10 in placenta and fetal membranes were significantly different from wild-type mice. PMID: 22892325
  4. Surfactant protein D modulated subpollen particle uptake in a cell type specific way (e.g. greater number of macrophages and epithelial cells, which participated in allergen particle uptake) and led to a decreased secretion of pro-inflammatory cytokines. PMID: 22296755
  5. Silica exposure causes dynamic changes of SP-D and CC16 protein expression in lung tissue and bronchoalveolar lavage fluid. PMID: 19080379
  6. An extended binding site for influenza A virus; calcium-dependent antiviral activity involves residues flanking the primary carbohydrate binding site as well as more remote residues displayed on the carbohydrate recognition domain surface. PMID: 20601494
  7. SP-D promotes attachment of allergen-containing subpollen particles to epithelial cells and may thus be involved in the inflammatory response to inhaled allergen. PMID: 20569420
  8. analysis of myeloperoxidase-dependent inactivation of surfactant protein D in vitro and in vivo PMID: 20228064
  9. Results suggest that SP-D-dependent processes regulating surfactant lipid homeostasis were disassociated from those mediating emphysema. PMID: 12163500
  10. Heterogeneous allele expression of SP-D mRNA in large intestine and other tissues. PMID: 12464693
  11. SP-A and SP-D are antimicrobial proteins that directly inhibit the proliferation of Gram-negative bacteria in a macrophage- and aggregation-independent manner by increasing the permeability of the microbial cell membrane PMID: 12750409
  12. SP-A and SP-D are antimicrobial proteins that directly inhibit the growth of Histoplasma capsulatum by increasing permeability of the organism PMID: 12857753
  13. SP-D interacts with chlamydial pathogens and enhance their phagocytosis into macrophages PMID: 15075250
  14. Degradation of pulmonary surfactant protein D by Pseudomonas aeruginosa elastase abrogates innate immune function PMID: 15123664
  15. SP-A and SP-D enhance mannose receptor-mediated phagocytosis of M. avium by macrophages PMID: 15187139
  16. results indicated SP-A & SP-D have distinct functions in lung homeostasis & the function of the neck domain & carbohydrate recognition domain of SP-D is dependent on its own NH2-terminal & collagenous domains that cannot be complemented by those of SP-A PMID: 16500946
  17. The ligand binding of homologous human, rat, and mouse trimeric trimeric neck plus carbohydrate recognition domain (neck+CRD) fusion proteins, each with identical N-terminal tags remote from the ligand-binding surface, was compared. PMID: 16514117
  18. VEGF increased expression of SP-D mRNA in preterm rat lung. PMID: 17267143
  19. Interactions with the side chain of inner core heptoses provide a potential mechanism for the recognition of diverse types of lipopolysaccharides by SP-D. PMID: 18092821
  20. These results show that antiviral activities of surfactant protein-D can be reproduced without the N-terminal and collagen domains and that cross-linking of these domains is essential for anti-influenza A virus activity. PMID: 18302538
  21. After OVA challenge alveolar epithelial cells Type II (AEII) show a significantly higher expression of SP-A and SP-D leading also to higher amounts of both SPs in BALF, and macrophages gather predominantly SP-A. PMID: 18802356
  22. S-nitrosylation of SP-D causes quaternary structural alterations and a swtich to its inflammatory signaling role. PMID: 19007302
  23. Multimerization of surfactant protein D, but not its collagen domain, is required for antiviral and opsonic activities related to influenza virus. PMID: 19017984

Show More

Hide All

Subcellular Location Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.
Protein Families SFTPD family
Database Links

KEGG: rno:25350

UniGene: Rn.11348

Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
Address
7505 Fannin St. Ste 610-312, Houston, TX 77054, USA
Join Us with

Subscribe newsletter

Leave a message

© 2007-2022 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1