Recombinant Human Mindin His-tag Protein, CF Summary
Product Specifications
Glu32-Val331, with a C-terminal 6-His tag
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.
11539-SP
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute lyophilized material at 250 μg/mL in sterile PBS. For liquid material, refer to CoA for concentration. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
Recombinant Human Mindin His-tag Protein (Catalog # 11539-SP) binds to fluorescein-conjugated E. coli Bioparticles. The ED50 for this effect is 0.200‑2.40 μg/mL.
Reconstitution Calculator
Background: Mindin
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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