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Validated All-in-One™ qPCR Primer for C1QBP(NM_001212.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
The human complement subcomponent C1q associates with C1r and C1s in order to yield the first component of the serum complement system. The protein encoded by this gene is known to bind to the globular heads of C1q molecules and inhibit C1 activation. This protein has also been identified as the p32 subunit of pre-mRNA splicing factor SF2, as well as a hyaluronic acid-binding protein. [provided by RefSeq].
Gene References into function
- This protein has also been identified as the p32 subunit of pre-mRNA splicing factor SF2, as well as a hyaluronic acid-binding protein
- The human complement subcomponent C1q associates with C1r and C1s in order to yield the first component of the serum complement system
- increase in expression over the rostral portion of the sperm head after capacitation; may play a role in human fertilization
- demonstrate that MT1-MMP via its cytoplasmic tail directly associates with a chaperone-like compartment-specific regulator gC1qR
- presence of homologous sequences of HABP1 cDNA, termed processed HABP1 pseudogene, in humans
- Maturation-dependent expression of this protein in monocyte-derived dendritic cells.
- gC1qR expressed on activated platelets may contribute directly to thrombosis, inflammation, and endovascular infections.
- binds with Hepacivirus core protein on CD8+ and CD4+ positive t-cells and inactivates lck and akt.
- Human p32 functions as a corepressor of CCAAT-binding factor-mediated transcription activation.
- data suggest that gC1qR may participate in tissue remodeling and inflammation by localizing TFPI-2 to the pericellular environment to modulate local protease activity and regulate High Molecular Weight Kininogen activation
- HABP1 expression in Schizosaccharomyces pombe induces growth inhibition, morphological abnormalities like elongation, multinucleation and aberrant cell septum formation, implicating its role in cell cycle progression and cytokinesis
- C1q functions as a chemotactic factor for immature dendritic cells, and migration is mediated through ligation of both gC1qR and cC1qR/CR.
- These studies suggest that HCV core protein can lead to enhanced p38- and gC1qR-dependent IL-8 expression.
- gC1qR down-regulates interleukin-12 production by signaling through 1-phosphatidylinositol 3-kinase. This is the first report to identify signaling pathways used by gC1qR-mediated immune suppression.
- p32 overexpression effectively blocks mRNA accumulation from the adenovirus major late transcription unit (MLTU) and stimulates RNA polymerase II carboxy-terminal domain phosphorylation in virus-infected cells.
- we speculate that the epitope of gC1qR is unmasked in the germ cell lineage; by reducing gC1qR by siRNA, an increase was observed in the number of apoptotic cells in ITO-II & TCam-2 cell lines showing an antiapoptotic property of gC1qR in the germ cells
- Data suggest that gC1qR serves as a molecular bridge between the complement and contact activation systems and is an important catalyst in inflammation.
- These data suggest a role for gC1qR in the initial stages of Bacillus cereus spore attachment and/or entry.
- P. falciparum-infected red blood cells use the 32-kDa human protein gC1qR/HABP1/p32 as a receptor to bind to human brain microvascular endothelial cells.
- Data demonstrated a direct and specific interaction between vasopressin V2 receptor and GC1q-Rthese two proteins via the arginine cluster of vasopressin V2 receptor.
- Differential isoform expression and interaction with the P32 regulatory protein controls the subcellular localization of the splicing factor U2AF26
- Mitochondrial p32/C1QBP is a critical mediator of p14ARF-induced apoptosis.
- Failure of p32 to interact with FOXC1 containing the disease-causing F112S mutation indicates that impaired protein interaction may be a disease mechanism for AR malformations.
- results establish p32, particularly its cell-surface-expressed form, as a new marker of tumor cells and tumor-associated macrophages/myeloid cells in hypoxic/metabolically deprived areas of tumors
- gC1qR is a physiological inhibitor of the RIG-I and MDA5-mediated antiviral signaling pathway
