Analytical Data
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Gene name
MYOC
- Application
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Alternative Names
MYOC；GLC1A；TIGR；Myocilin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99972
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Expression Region
33-504aa
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AA Sequence
RTAQLRKA NDQSGRCQYT FSVASPNESS CPEQSQAMSV IHNLQRDSST QRLDLEATKA RLSSLESLLH QLTLDQAARP QETQEGLQRE LGTLRRERDQ LETQTRELET AYSNLLRDKS VLEEEKKRLR QENENLARRL ESSSQEVARL RRGQCPQTRD TARAVPPGSR EVSTWNLDTL AFQELKSELT EVPASRILKE SPSGYLRSGE GDTGCGELVW VGEPLTLRTA ETITGKYGVW MRDPKPTYPY TQETTWRIDT VGTDVRQVFE YDLISQFMQG YPSKVHILPR PLESTGAVVY SGSLYFQGAE SRTVIRYELN TETVKAEKEI PGAGYHGQFP YSWGGYTDID LAVDEAGLWV IYSTDEAKGA IVLSKLNPEN LELEQTWETN IRKQSVANAF IICGTLYTVS SYTSADATVN FAYDTGTGIS KTLTIPFKNR YKYSSMIDYN PLEKKLFAWD NLNMVTYDIK LSKM
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
MYOC, or Myocilin, is a protein encoded by the MYOC gene and is primarily expressed in the trabecular meshwork of the eye, playing a crucial role in regulating intraocular pressure. Abnormalities in MYOC are associated with certain types of glaucoma, particularly primary open-angle glaucoma. Research into MYOC recombinant proteins has gained significant attention due to their potential implications in understanding the pathophysiology of glaucoma and developing novel therapeutic strategies. Recombinant MYOC proteins enable researchers to study its structure, function, and interactions in vitro, facilitating the exploration of how mutations in the MYOC gene contribute to increased ocular pressure and retinal damage. Furthermore, the production of recombinant MYOC proteins allows for the assessment of their stability and potential as biomarkers for glaucoma diagnosis. By elucidating the molecular mechanisms involved in MYOC-related glaucoma, researchers aim to identify targets for gene therapy and pharmacological interventions, contributing to improved management and treatment options for affected individuals. This line of research holds promise for advancing our knowledge of glaucoma pathology and enhancing patient outcomes through tailored therapeutic approaches.
