| Applications: | Immunodepletion/Immunocompetition |
| Note: | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description : | Myocilin Blocking Peptide is synthetically produced from the sequence and is suitable for use in western blot applications. |
| Formulation: | Liquid form at 2.5mg/ml concentration in PBS. Up to 5% DMSO can be added. Orders with >1mg can be supplied in lyophilized powder form, or in buffer of choice. |
| Storage Instruction: | Store at-20°C for long term storage. Avoid freeze-thaw cycles. |
| Gene Symbol: | MYOC |
| Gene ID: | 4653 |
| Uniprot ID: | MYOC_HUMAN |
| Immunogen: | Synthetic peptide corresponding to unique amino acid sequence on Myocilin protein. |
| Tissue Specificity | Detected in aqueous humor. Detected in the eye (at protein level). Widely expressed. Highly expressed in various types of muscle, ciliary body, papillary sphincter, skeletal muscle, heart, and bone marrow-derived mesenchymal stem cells. Expressed predominantly in the retina. In normal eyes, found in the inner uveal meshwork region and the anterior portion of the meshwork. In contrast, in many glaucomatous eyes, it is found in more regions of the meshwork and seems to be expressed at higher levels than in normal eyes, regardless of the type or clinical severity of glaucoma. The myocilin 35 kDa fragment is detected in aqueous humor and to a lesser extent in iris and ciliary body. |
| Post Translational Modifications | Different isoforms may arise by post-translational modifications. Glycosylated. Palmitoylated. Undergoes a calcium-dependent proteolytic cleavage at Arg-226 by CAPN2 in the endoplasmic reticulum. The result is the production of two fragments, one of 35 kDa containing the C-terminal olfactomedin-like domain, and another of 20 kDa containing the N-terminal leucine zipper-like domain. |
| Function | Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork. |
| Peptide Name | Myocilin Myocilin 55 Kda Subunit Trabecular Meshwork-Induced Glucocorticoid Response Protein Cleaved Into - Myocilin - N-Terminal Fragment Myocilin 20 Kda N-Terminal Fragment - Myocilin - C-Terminal Fragment Myocilin 35 Kda N-Terminal Fragment |
| Cellular Localisation | Secreted Golgi Apparatus Cytoplasmic Vesicle Extracellular Space Extracellular Matrix Extracellular Exosome Mitochondrion Mitochondrion Intermembrane Space Mitochondrion Inner Membrane Mitochondrion Outer Membrane Rough Endoplasmic Reticulum Cell Projection Cilium Located Preferentially In The Ciliary Rootlet And Basal Body Of The Connecting Cilium Of Photoreceptor Cells And In The Rough Endoplasmic Reticulum It Is Only Imported To Mitochondria In The Trabecular Meshwork Localizes To The Golgi Apparatus In Schlemm's Canal Endothelial Cells Appears In The Extracellular Space Of Trabecular Meshwork Cells By An Unconventional Mechanism Likely Associated With Exosome-Like Vesicles Localizes In Trabecular Meshwork Extracellular Matrix Myocilin C-Terminal Fragment: Secreted N-Terminal Fragment: Endoplasmic Reticulum Remains Retained In The Endoplasmic Reticulum |
| Alternative Peptide Names | Myocilin protein Myocilin 55 Kda Subunit protein Trabecular Meshwork-Induced Glucocorticoid Response Protein Cleaved Into - Myocilin - N-Terminal Fragment protein Myocilin 20 Kda N-Terminal Fragment - Myocilin - C-Terminal Fragment protein Myocilin 35 Kda N-Terminal Fragment protein MYOC protein GLC1A protein TIGR protein |
Information sourced from Uniprot.org