Human Recombinant MYOC protein, His Tag (V2LY-0526-LY5679)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant MYOC protein, His Tag consist of Amino Acid: 1-504 and predicts a molecular mass of 54.7 kDa.
Molecule Mass
54.7 kDa
Verified
HPLC
Sequence
Amino Acid: 1-504
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥95% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile ACN, TFA
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Myocilin
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.
Biological Process
Bone development Source: UniProtKB
Clustering of voltage-gated sodium channels Source: UniProtKB
ERBB2-ERBB3 signaling pathway Source: UniProtKB
Myelination in peripheral nervous system Source: UniProtKB
Negative regulation of cell-matrix adhesion Source: UniProtKB
Negative regulation of Rho protein signal transduction Source: UniProtKB
Negative regulation of stress fiber assembly Source: UniProtKB
Neuron projection development Source: UniProtKB
Non-canonical Wnt signaling pathway via JNK cascade Source: UniProtKB
Osteoblast differentiation Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of focal adhesion assembly Source: UniProtKB
Positive regulation of mitochondrial depolarization Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
Positive regulation of protein kinase B signaling Source: UniProtKB
Positive regulation of stress fiber assembly Source: UniProtKB
Positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
Regulation of MAPK cascade Source: UniProtKB
Signal transduction Source: GO_Central
Skeletal muscle hypertrophy Source: UniProtKB
Cellular Location
Secreted
extracellular space
extracellular matrix
extracellular exosome
Golgi apparatus
Endoplasmic reticulum
Rough endoplasmic reticulum
Mitochondrion
Mitochondrion intermembrane space
Mitochondrion inner membrane
Mitochondrion outer membrane
Other locations
Cytoplasmic vesicle
Cell projection
cilium
Note: Located preferentially in the ciliary rootlet and basal body of the connecting cilium of photoreceptor cells, and in the rough endoplasmic reticulum (PubMed:9169133). It is only imported to mitochondria in the trabecular meshwork (PubMed:17516541). Localizes to the Golgi apparatus in Schlemm's canal endothelial cells (PubMed:11053284). Appears in the extracellular space of trabecular meshwork cells by an unconventional mechanism, likely associated with exosome-like vesicles (PubMed:15944158). Localizes in trabecular meshwork extracellular matrix (PubMed:15944158).
Myocilin, C-terminal fragment:
Secreted
Myocilin, N-terminal fragment:
Endoplasmic reticulum
Note: Remains retained in the endoplasmic reticulum.
Involvement in disease
Glaucoma 1, open angle, A (GLC1A):
A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place.
PTM
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.

Saccuzzo, E. G., Youngblood, H. A., & Lieberman, R. L. (2023). Myocilin misfolding and glaucoma: A 20-year update. Progress in Retinal and Eye Research, 101188.

Zhou, B., Lin, X., Li, Z., Yao, Y., Yang, J., & Zhu, Y. (2022). Structure‒function‒pathogenicity analysis of C-terminal myocilin missense variants based on experiments and 3D models. Frontiers in Genetics, 13, 1019208.

Nakahara, E., & Hulleman, J. D. (2022). A simple secretion assay for assessing new and existing myocilin variants. Current eye research, 47(6), 918-922.

Sharma, R., & Grover, A. (2021). Myocilin-associated glaucoma: a historical perspective and recent research progress. Molecular Vision, 27, 480.

Atienzar-Aroca, R., Aroca-Aguilar, J. D., Alexandre-Moreno, S., Ferre-Fernández, J. J., Bonet-Fernández, J. M., Cabañero-Varela, M. J., & Escribano, J. (2021). Knockout of myoc Provides Evidence for the Role of Myocilin in Zebrafish Sex Determination Associated with Wnt Signalling Downregulation. Biology, 10(2), 98.

Judge, S. M., Deyhle, M. R., Neyroud, D., Nosacka, R. L., D'Lugos, A. C., Cameron, M. E., ... & Judge, A. R. (2020). MEF2c-dependent downregulation of myocilin mediates cancer-induced muscle wasting and associates with cachexia in patients with cancer. Cancer research, 80(9), 1861-1874.

O’Gorman, L., Cree, A. J., Ward, D., Griffiths, H. L., Sood, R., Denniston, A. K., ... & Gibson, J. (2019). Comprehensive sequencing of the myocilin gene in a selected cohort of severe primary open-angle glaucoma patients. Scientific reports, 9(1), 3100.

Alward, W. L., Van Der Heide, C., Khanna, C. L., Roos, B. R., Sivaprasad, S., Kam, J., ... & NEIGHBORHOOD Consortium. (2019). Myocilin mutations in patients with normal-tension glaucoma. JAMA ophthalmology, 137(5), 559-563.

Wang, H., Li, M., Zhang, Z., Xue, H., Chen, X., & Ji, Y. (2019). Physiological function of myocilin and its role in the pathogenesis of glaucoma in the trabecular meshwork. International journal of molecular medicine, 43(2), 671-681.

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For research use only. Not intended for any clinical use.

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