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Kremen-1 hFc Chimera, Human

KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. KRM1 selectively binds to the mature viral particle above the canyon of the viral protein 1 (VP1) subunit and contacts across two adjacent asymmetry units. The key residues for receptor binding are conserved among most KRM1-dependent enteroviruses, suggesting a uniform mechanism for receptor binding.
￥4100
Z05553-100

产品简介
Species Human
Protein Construction
Kremen-1 (Arg21-Thr392)_x000D_
Accession # Q96MU8-1		 hFc
N-term C-term
Purity > 95% as determined by Bis­Tris PAGE 
> 95% as determined by HPLC
Endotoxin Level Less than 1EU per μg by the LAL method.
Expression System HEK293
Theoretical Molecular Weight 67.6 kDa
Apparent Molecular Weight Due to glycosylation, the protein migrates to 80-110 kDa based on Bis-Tris PAGE result.
Formulation Lyophilized from 0.22μm filtered solution in PBS (pH 7.4).
Reconstitution Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
Storage & Stability Upon receiving, the product remains stable up to 6 months at -20 °C or below. Upon reconstitution, the product should be stable for 3 months at -80 °C. Avoid repeated freeze-thaw cycles.
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图例
Kremen-1 HFc Chimera, Human

The purity of Kremen-1 hFc Chimera, Human is greater than 95% as determined by SEC-HPLC. »

Kremen-1 HFc Chimera, Human

Kremen-1 hFc Chimera, Human on Bis-Tris PAGE under reduced condition. The purity is greater than 95%. »

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技术背景
Target Background KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. KRM1 selectively binds to the mature viral particle above the canyon of the viral protein 1 (VP1) subunit and contacts across two adjacent asymmetry units. The key residues for receptor binding are conserved among most KRM1-dependent enteroviruses, suggesting a uniform mechanism for receptor binding.
Synonyms Kremen protein 1; KREMEN; KRM1; KREMEN1
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For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.