Recombinant Human Myocilin His-tag Protein, CF

Immobilized Recombinant Human Myocilin supporst the adhesion of AGS human Gastric Adenocarcinoma cells. The ED50 for this effect is 0.3-3 μg/mL.

2 μg/lane of Recombinant Human Myocilin His-tag (Catalog# 3446-MY) was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 28-35 kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Myocilin His-tag Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of AGS human Gastric Adenocarcinoma cells. The ED₅₀ for this effect is 0.3-3 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human Myocilin protein
  Leu215-Met504, with a C-terminal 6-His tag
• N-terminal Sequence: Leu215
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, 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:
  • Bioactivity
• 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: 28-35 kDa, 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 °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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 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 Human Myocilin His-tag Protein, CF

• GLC1A
• GLC1Amyocilin
• GPOA
• JOAG
• JOAG1
• MYOC
• Myocilin
• myocilin, trabecular meshwork inducible glucocorticoid response
• TIGR
• TIGRmutated trabecular meshwork-induced glucocorticoid response protein
• Trabecular meshwork-induced glucocorticoid response protein

Background

Myocilin is a secreted glycoprotein that belongs to the family of olfactomedin-related proteins (1). Mature human Myocilin is synthesized as a 472 amino acid (aa) precursor that can be cleaved into a 194 aa N-terminal fragment containing leucine zipper motifs within two coil–coil domains and a 335 aa C-terminal fragment containing an olfactomedin (OLF) domain (2). The human OLF-domain shares 87% aa sequence identity with the OLF-domain in mouse and rat. The Myocilin gene is expressed in the human eye compartments. When it is secreted, it can be detected in the cornea, trabecular meshwork, aqueous humor, iris, ciliary body, choroid sclera, retina and the axons of optic nerve ganglion cells (3). Mutations of the MYOC gene are associated with primary open angle glaucoma (POAG), which is a complex disorder with a major heritable component (4). Myocilin interacts with itself to form dimers or multimers (2, 5-8), flotilin-1, optimedin, fibronectin, and fibrilin-1 as well as hevin and SPARC (2, 8-10). Myocilin stimulates cell migration that involves the activation of intergrin focal adhesion kinase (FAK)-serin/threonine kinase (AKT) signaling pathway (11). Myocilin binds specifically to the Heparin II domain of fibronectin (12).

1. Zeng, L.C. et al. (2005) FEBS Lett. 579:5443.
2. Resch, Z.T. and Fautsch M.P. (2009) Exp Eye Res. 88:704.
3. Karali, A. et al. (2000) Invest. Ophthalmol. Vis. Sci. 41:729.
4. Ikezoe, T. et al. (2003) Int J Mol Med. 12:259.
5. Aroca-Aguilar, J.D. et al. (2013) PLoS One 8:e54385.
6. Tamm, E.R. (2002) Prog Retin Eye Res 21:395.
7. Fautsch, M.P. et al. (2006) Exp Eye Res 82:1046.
8. Aroca-Aguilar, J.D. et al. (2011) Invest Ophthalmol Vis Sci 52:179.
9. Wentz-Hunter, K. et al. (2002) Invest Ophthalmol Vis Sci 43:176.
10. Ueda, J. et al. (2000) J Histochem Cytochem 48:1321.
11. Kwon, H.S. and Tomarev, S.I. (2011) J Cell Physiol 226:3392.
12. Filla, M.S. et al. (2002) Invest Ophthalmol Visual Sci. 43:151.