Analytical Data
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Gene name
EMILIN1
- Application
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Alternative Names
EMILIN1；EMI；EMILIN-1
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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
Q9Y6C2
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Expression Region
676-1016aa
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AA Sequence
DLGATKDRIISEINRLQQEATEHATESEERFRGLEEGQAQAGQCPSLEGRLGRLEGVCERLDTVAGGLQGLREGLSRHVAGLWAGLRETNTTSQMQAALLEKLVGGQAGLGRRLGALNSSLQLLEDRLHQLSLKDLTGPAGEAGPPGPPGLQGPPGPAGPPGSPGKDGQEGPIGPPGPQGEQGVEGAPAAPVPQVAFSAALSLPRSEPGTVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTGHRHEKVEAVLSRSNQGVARVDSGGYEPEGLENKPVAESQPSPGTLGVFSLILPLQAGDTVCVDLVMGQLAHSEEPLTIFSGALLYGDPELEHA
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Molecular Weight
39 kDa
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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
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Protein Description
EMILIN1, or Elastin Microfibril Interfacer 1, is a glycoprotein that plays a critical role in the extracellular matrix, primarily influencing the organization and elasticity of connective tissues. It is known to interact with elastin and other structural proteins, contributing to vascular stability and tissue integrity. Research has shown that EMILIN1 is involved in various biological processes, including angiogenesis, tissue remodeling, and inflammation. Abnormal expression of EMILIN1 has been linked to several pathological conditions, such as cardiovascular diseases, fibrotic disorders, and tumors. The characterization of recombinant EMILIN1 protein has gained interest in the scientific community for its potential therapeutic applications and as a biomarker for disease progression. Recombinant protein technology allows for the production of EMILIN1 in controlled environments, ensuring high purity and bioactivity, which can facilitate studies on its molecular functions, interactions, and regulatory mechanisms. By investigating the properties of recombinant EMILIN1, researchers aim to enhance our understanding of its role in health and disease, paving the way for novel strategies in disease treatment and prevention. This focus on EMILIN1 highlights the essential interplay between the extracellular matrix components and cellular behaviors, emphasizing the importance of this protein in maintaining cardiovascular health and potential implications in regenerative medicine. Therefore, the study of EMILIN1 not only provides insights into fundamental biological processes but also holds promise for developing innovative therapeutic approaches targeting various diseases linked to extracellular matrix dysfunction.
