Complement C1q Binding Protein (C1QBP) Antibody

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273€ (100 µl)

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935106861
info@markelab.com
name
Complement C1q Binding Protein (C1QBP) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx132514
tested applications
WB, IHC, IF/ICC

Description

Complement C1q Binding Protein (C1QBP) Antibody is a Mouse Monoclonal antibody for the detection of Complement C1q Binding Protein (C1QBP).

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Primary Antibodies
Immunogen Target
Complement C1q Binding Protein (C1QBP)
Host
Mouse
Reactivity
Human
Recommended Dilution
Optimal dilutions/concentrations should be determined by the end user.
Clonality
Monoclonal
Conjugation
Unconjugated
Isotype
IgG
Clone ID
S614
Purification
Antigen-specific affinity chromatography followed by Protein A affinity chromatography.
Size 1
100 µl
Size 2
200 µl
Size 3
1 ml
Form
Liquid
Tested Applications
WB, IHC, IF/ICC
Buffer
PBS, pH 7.4, containing 0.02% NaN3, 50% glycerol.
Availability
Shipped within 5-10 working days.
Storage
Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
Background
Antibody anti-C1QBP
Status
RUO
Note
Concentration: 1 mg/ml -

Descripción

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Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular "heads" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A-and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. In infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B and Staphylococcus aureus protein A. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. Involved in replication of Rubella virus. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppresion of interleukin-12 production in monocyte-derived dendritic cells. Involved in regulation of antiviral response by inhibiting DDX58-and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection. Involved in HIV-1 replication, presumably by contributing to splicing of viral RNA.

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