Recombinant Mouse MBL-1 Protein Summary
Product Specifications
Ser18-Ala239
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
2077-MB
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
2077-MB/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: MBL-1
Mannan binding lectin (MBL) belongs to the collectin family of innate immune defense proteins, which binds to an array of carbohydrate patterns on pathogen surfaces (1, 2). Collectin family members share common structural features: a cysteine rich amino-terminal domain, a collagen-like region, an alpha -helical coiled-coil neck domain and a carboxy terminal C-type (Ca++-dependent) lectin or carbohydrate recognition domain (CRD). MBL homotrimerizes to form a structural unit joined by N-terminal disulfide bridges. These homotrimers further associate into oligomeric structures of up to 6 units. Whereas two forms of MBL proteins (MBL-1, also known as S-MBP or MBL-A and MBL-2, also known as L-MBP or MBL-C) exist in rodents and other animals, only one functional MBL protein is present in humans. Mouse MBL-1 shares about 52% and 60% amino acid sequence identity with mouse MBL-2 and human MBL, respectively.
In mouse, MBL-1 and MBL-2 are the only collectins that can activate complement via the lectin complement pathway (1, 2). Serum oligomeric MBL associates with MBL-associated serine protease (MASP) proenzymes. The MBL-MASP proenzyme complex preferentially interacts with sugar patterns containing mannose, glucose, L-fucose, or N-acetyl-glucosamine present at a terminal nonreducing postion on the cell surface of various pathogens and certain tumor cells. This interaction induces pro-enzyme activation and the triggering of the complement cascade, resulting in opsonization and pathogen removal via humoral and cellular immune responses. MBL does not recognize self-components or glycoproteins from other higher animals due to the presence of terminal sialic acid or galactose that interrupts the repeating carbohydrate structures (3). A number of membrane receptors for MBL, including C1q phagocytic receptor (C1qRp), calreticulin (also known as C1qR), and CR1 (CD35), have been described. Interactions with these receptors may also be important in stimulating phagocytosis (1, 2).
Mouse MBL-1 and MBL-2 are produced primarily in the liver and are secreted into the blood stream. In addition, mouse MBL-1 is also expressed in lung, kidney and testis while MBL-2 is expressed in kidney, thymus and small intestine (1, 4, 5).
- Holmskov, U. et al. (2003) Annu. Rev. Immunol. 21:547.
- Fujita, R. et al. (2004) Immunol. Rev. 198:185.
- Saevarsdottir, S. et al. (2004) Scand. J. Immnunol. 60:23.
- Uemura, K. et al. (2002) J. Immunol. 169:6945.
- Wagner, S. et al. (2003) J. Immunol. 170:1462.
Citations for Recombinant Mouse MBL-1 Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Mice deficient in ficolin, a lectin complement pathway recognition molecule, are susceptible to Streptococcus pneumoniae infection.
Authors: Endo, Yuichi, Takahashi, Minoru, Iwaki, Daisuke, Ishida, Yumi, Nakazawa, Naomi, Kodama, Toshihis, Matsuzaka, Tomohiro, Kanno, Kazuko, Liu, Yu, Tsuchiya, Kohsuke, Kawamura, Ikuo, Ikawa, Masahito, Waguri, Satoshi, Wada, Ikuo, Matsushita, Misao, Schwaeble, Wilhelm, Fujita, Teizo
J Immunol, 2012-11-12;189(12):5860-6.
Species: Bacteria - Streptococcus pneumoniae
Sample Types: Whole Cells
Applications: Binding Assay -
Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity.
Authors: Nimmerjahn F, Anthony RM, Ravetch JV
Proc. Natl. Acad. Sci. U.S.A., 2007-05-07;104(20):8433-7.
Species: Human
Sample Types:
Applications: Surface Plasmon Resonance
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