Measured by its ability to bind fluorescein-conjugated E. coli Bioparticles. Sankala, M. et al. (2002) J. Biol. Chem. 277:33378. The ED50 for this effect is 0.3-1.2 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Mindin protein
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
35 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
38-47 kDa, reducing conditions
Publications
Read Publication using 8500-SP in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE with silver staining
Reconstitution Instructions
Reconstitute at 250 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Mindin Protein, CF
Differentially expressed in cancerous and non-cancerous lung cells 1
DIL1
DIL-1
DIL1FLJ34460
DKFZp686G21139
FLJ16313
FLJ22401
Mindin
M-SPONDIN
RG-1
SPON2
Spondin 2
spondin 2, extracellular matrix protein
spondin-2
Background
Mindin, also known as Spondin-2 and DIL-1, is a member of the Mindin F-Spondin family of evolutionarily conserved, secreted extracellular matrix proteins. It is composed of an N-terminal F-spondin domain, which mediates integrin binding, and a C-terminal thrombospondin type I repeat, which binds to bacterial lipopolysaccharide (1). Mouse Mindin is synthesized as a 330 amino acid (aa) precursor protein with a molecule weight of approximately 36 kDa (2). The mature mouse protein shares 88% and 99% aa sequence identity with the human and rat orthologs, respectively (2). Mindin is expressed in a variety of tissues in mice with the highest expression levels being detected in lung, spleen, heart, and lymph nodes (2).
Mindin is essential for initiating innate and adaptive immune responses. It has been shown to be a pattern recognition receptor for bacterial pathogens and function as an opsonin for macrophage phagocytosis of bacteria (1, 2). Mindin also binds directly to influenza virus particles and is necessary for macrophage-dependent clearance of influenza viruses from the nasal cavity (3). In addition, Mindin serves as a ligand for leukocyte integrins (1). It is critical for T cell priming and recruitment of macrophages and neutrophils to sites of inflammation (4, 5). Mindin also regulates trafficking of eosinophils and granulocytes into the airspace and plays a role in the development of allergic airways disease (6, 7). Outside the immune system, Mindin has been shown to promote adhesion and outgrowth of hippocampal embryonic neurons, and to be an important mediator of brain ischemic injury and cardiac hypertrophy (8-11). Furthermore, it has been suggested that Mindin can serve as a marker for prostate and ovarian cancer, as well as diabetic nephropathy (12-14).
Li, Y. et al. (2009) EMBO J. 28:286.
He, Y.W. et al. (2004) Nat. Immunol. 5:88.
Jia, W. et al. (2008) J. Immunol. 180:6255.
Li, H. et al. (2006) EMBO J. 25:4097.
Jia, W. et al. (2005) Blood 106:3854.
Li, Z. et al. (2009) J. Leukoc. Biol. 85:124.
Tighe, R.M. et al. (2011) J. Allergy Ther. 2011 (Suppl. 1). pii: 001.
Feinstein, Y. et al. (1999) Development 126:3637.
Yan, L. et al. (2011) Cardiovasc. Res. 92:85.
Bian, Z.Y. et al. (2012) J. Mol. Med. (Berl.) 90:895.
Wang, L. et al. (2013) Exp. Neurol. 247:506.
Simon, I. et al. (2007) Gynecol. Oncol. 106:112.
Murakoshi, M. et al. (2011) Exp. Diabetes Res. 2011:486305.
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