Recombinant Human Mindin His-tag Protein, CF Summary
Details of Functionality |
Measured by its ability to bind fluorescein-conjugated E. coli Bioparticles. The ED 50 for this effect is 0.200-2.40 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived human Mindin protein Glu32-Val331, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Glu 32 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
34 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 |
38-44 kDa, under reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution. |
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute lyophilized material at 250 μg/mL in sterile PBS. For liquid material, refer to CoA for concentration. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Mindin His-tag Protein, CF
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). The mature human protein shares 88% aa sequence identity with the mouse orthologs (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.
- Lucarelli, G. et al. (2013) J. Urol. 190:2271.
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