Recombinant Human C1QBP Protein (aa 74-282, His Tag) | PKSH033350

Recombinant Human C1QBP Protein (aa 74-282, His Tag) | PKSH033350 | Gentaur US, UK & Europe Disrtribition

Synonyms: Complement Component 1 Q Subcomponent-Binding Protein Mitochondrial; ASF/SF2-Associated Protein p32; Glycoprotein gC1qBP; C1qBP; Hyaluronan-Binding Protein 1; Mitochondrial Matrix Protein p32; gC1q-R Protein; p33; C1QBP; GC1QBP; HABP1; SF2P32;gC1qR

Active Protein: N/A

Activity: Recombinant Human Hyaluronic Acid-binding Protein is produced by our E.coli expression system and the target gene encoding Leu74-Gln282 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Human Hyaluronic Acid-binding Protein is produced by our E.coli expression system and the target gene encoding Leu74-Gln282 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-6His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.

Purity: > 85 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.

Molecular Mass: 24.9 kDa

Formulation: Supplied as a 0.2 μm filtered solution of 20mM Tris, 20% Glycerol, 1mM DTT, pH 7.5.

Reconstitution: Not Applicable

Background: Complement Component 1Q Subcomponent-Binding Protein (C1QBP) is a nucleus protein that belongs to the MAM33 family. C1QBP is known to bind to the globular heads of C1q molecules and inhibit C1 activation. Mitochondrial C1QBP is a critical mediator of p14ARF-induced apoptosis. C1QBP functions as a chemotactic factor for immature dendritic cells, and migration is mediated through ligation of both C1QBP and cC1qR/CR. C1QBP overexpression successfully blocks mRNA accumulation from the adenovirus major late transcription unit (MLTU) and stimulates RNA polymerase II carboxy-terminal domain phosphorylation in virus-infected cells.

Research Area: Microbiology, immunology