Analytical Data
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Gene name
EPYC
- Application
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Alternative Names
EPYC；DSPG3；PGLB；SLRR3B；Epiphycan
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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
Q99645
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Expression Region
1-322aa
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AA Sequence
MKTLAGLVLG LVIFDAAVTA PTLESINYDS ETYDATLEDL DNLYNYENIP VDKVEIEIAT VMPSGNREL LTPPPQPEKA QEEEEEEEST PRLIDGSSPQ EPEFTGVLGP HTNEDFPTCL LCTCISTTV YCDDHELDAI PPLPKNTAYF YSRFNRIKKI NKNDFASLSD LKRIDLTSNL ISEIDEDAF RKLPQLRELV LRDNKIRQLP ELPTTLTFID ISNNRLGRKG IKQEAFKDMY DLHHLYLTD NNLDHIPLPL PENLRALHLQ NNNILEMHED TFCNVKNLTY IRKALEDIRL DGNPINLSK TPQAYMCLPR LPVGSLV
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Molecular Weight
36 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
Related Products
Protein Description
The study of EPYC (Extracellular Matrix Protein with a Y-like Structure) recombinant proteins has gained significant attention in recent years due to their crucial role in tissue structure and wound healing. EPYC is a member of the small leucine-rich proteoglycan family, playing a vital role in cellular interactions and extracellular matrix organization. This protein is implicated in various biological processes, including development, inflammation, and fibrosis, making it a potential target for therapeutic interventions. Researchers are particularly interested in producing recombinant EPYC to better understand its function and to explore its applications in regenerative medicine and tissue engineering. By utilizing advanced recombinant DNA techniques, scientists aim to produce large quantities of pure EPYC protein, which can be used for structural studies, functional assays, and as a biomaterial in novel drug delivery systems. Additionally, elucidating the structure-function relationships of EPYC may lead to insights into its involvement in disease states, thus opening up new avenues for diagnostic and treatment strategies. Overall, the research on EPYC recombinant proteins is poised to enhance our understanding of extracellular matrix dynamics and its implications in health and disease, presenting exciting opportunities for biotechnological advancements.
