Analytical Data
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Gene name
OMD
- Application
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Alternative Names
OMD；SLRR2C；Osteomodulin
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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
Q99983
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Expression Region
21-421aa
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AA Sequence
QYETYQWDED YDQEPDDDYQ TGFPFRQNVD YGVPFHQYTL GCVSECFCPT NFPSSMYCDN RKLKTIPNIP MHIQQLYLQF NEIEAVTANS FINATHLKEI NLSHNKIKSQ KIDYGVFAKL PNLLQLHLEH NNLEEFPFPL PKSLERLLLG YNEISKLQTN AMDGLVNLTM LDLCYNYLHD SLLKDKIFAK MEKLMQLNLC SNRLESMPPG LPSSLMYLSL ENNSISSIPE KYFDKLPKLH TLRMSHNKLQ DIPYNIFNLP NIVELSVGHN KLKQAFYIPR NLEHLYLQNN EIEKMNLTVM CPSIDPLHYH HLTYIRVDQN KLKEPISSYI FFCFPHIHTI YYGEQRSTNG QTIQLKTQVF RRFPDDDDES EDHDDPDNAH ESPEQEGAEG HFDLHYYENQ E
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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
OMD, or Osteoglycin, is a small leucine-rich proteoglycan that plays a significant role in bone and cartilage development. Research into OMD has gained traction due to its involvement not only in skeletal health but also in various pathologies, including osteoporosis and osteoarthritis. OMD is known to interact with collagen and collagen-associated proteins, influencing the extracellular matrix's organization and integrity. Understanding the structure and function of OMD at the molecular level is crucial, as it may provide insights into therapeutic targets for musculoskeletal diseases. Additionally, recent studies have suggested that OMD may have implications in regulating inflammation and cellular signaling pathways, highlighting its potential as a biomarker for certain conditions. This growing interest in OMD has led to the exploration of recombinant protein technology to produce OMD in a laboratory setting, enabling more detailed studies on its properties, mechanisms of action, and potential applications in regenerative medicine and tissue engineering. Researchers are utilizing various expression systems, such as yeast and mammalian cells, to create functional OMD proteins that can be characterized and tested for their biological activities, paving the way for innovative strategies in treating bone and cartilage disorders.
