Analytical Data
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Gene name
CEMIP2
- Application
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Alternative Names
Cemip2; Kiaa1412
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Species
Human
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Source
E. coli
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Tag
N-terminal His and TRxA Tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UHN6
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Expression Region
104-250aa
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AA Sequence
SSKYAPDENCPDQNPRLRNWDPGQDSAKQVVIKEGDMLRLTSDATVHSIVIQDGGLLVFGDNKDGSRNITLRTHYILIQDGGALHIGAEKCRYKSKATITLYGKSDEGESMPTFGKKFIGVEAGGTLELHGARKASWTLLARTLNSS
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Molecular Weight
18.0 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
CEMIP2, or Cell Migration-Inducing and Hyaluronan-Binding Protein 2, is a member of the KIAA1199 gene family, which has garnered attention due to its role in various cellular processes, including cell migration, proliferation, and extracellular matrix remodeling. Research indicates that CEMIP2 is involved in the regulation of hyaluronic acid metabolism, a key component of the extracellular matrix, which contributes to tissue hydration and cell signaling. Elevated levels of CEMIP2 have been implicated in several pathological conditions, including cancer, where it appears to facilitate tumor progression and metastasis by promoting epithelial-mesenchymal transition (EMT) and enhancing cell migratory properties. Moreover, CEMIP2's interaction with inflammatory signaling pathways highlights its potential involvement in chronic inflammatory diseases. The study of CEMIP2 as a recombinant protein aims to elucidate its functional roles and molecular mechanisms. By producing CEMIP2 in vitro, researchers can investigate its biochemical properties and interactions with other cellular components, paving the way for therapeutic applications. Understanding CEMIP2's mechanisms could lead to novel strategies for targeting tumor metastasis and other diseases characterized by excessive cell migration and matrix remodeling. Thus, CEMIP2 represents a promising candidate for further research in fields ranging from oncology to regenerative medicine, highlighting the importance of this protein in both health and disease contexts.
