Ultra-LEAF Purified anti-human CRP C-reactive protein Antibody anti-CRP - A16065C,BioLegend,696003

Host

Mouse

Reactivity

Human

Application

Neut -Quality tested

Platform ID

BAB110824923

BioLegend

Headquarters

8999 BioLegend Way San Diego, CA 92121 United States

Contact

Tel: 1-858-455-9588
Fax: +49 (4131) 7023913

Email:

Product Specifications
Scientific Background

Specifications

NameUltra-LEAF Purified anti-human CRP C-reactive protein Antibody anti-CRP - A16065C
Cat. No.696003
HostMouse
RRIDAB_2686982 (BioLegend Cat. No. 696003)AB_2686983 (BioLegend Cat. No. 696004)
IsotypeMouse IgG1, κ
ReactivityHuman
ApplicationNeut -Quality tested
ClonalityMonoclonal
Clone NumberA16065C
ConcentrationThe antibody is bottled at the concentration indicated on the vial, typically between 2 mg/mL and 3 mg/mL. Older lots may have also been bottled at 1 mg/mL. To obtain lot-specific concentration and expiration, please enter the lot number in ourCertificate of Analysisonline tool.
TargetCRP
ImmunogenRecombinant human CRP/PTX1
PurityThe Ultra-LEAF™ (Low Endotoxin, Azide-Free) antibody was purified by affinity chromatography.
Formulation0.2 µm filtered in phosphate-buffered solution, pH 7.2, containing no preservative.
StorageThe antibody solution should be stored undiluted between 2°C and 8°C. This Ultra-LEAF™ solution contains no preservative; handle under aseptic conditions.
Regulatory StatusResearch Use Only

Scientific Background

C-reactive protein (also known as CRP and Pentraxin 1 (PTX1)), is a member of pentraxin protein family. Similar to other pentraxins, CRP is a pattern recognition molecule that is able to recognize pathogens and promote their clearance. CRP tends to form a non-covalently linked pentamer with each subunit made up of two antiparallel β-sheets and a single short α-helix. It is characterized by the presence of a cleft that extends from the center of the subunit to its edge at the central pore of the pentamer structure. It has been demonstrated that CRP binds to the phosphocholine moieties expressed on the surface of dead or dying cells and some bacteria. This leads to the activation of the complement system and promotion of phagocytosis by macrophages to clear necrotic and apoptotic cells. CRP is secreted by hepatocytes and is a biomarker for inflammation. IL-6 has been shown to be an effective inducer of this protein. Besides binding to apoptotic cells, CRP also binds to a variety of molecules including C1q, bacterial polysaccharide, CD64, CD32, APCS, HDL, and fibronectin. In addition to participating in immune responses, CRP is also a prominent partaker in endothelial dysfunction and atherosclerosis. It was shown that CRP may exhibit direct proantherogenic effects by upregulating angiotensin type I receptor in smooth muscle cells and promoting their migration, proliferation, neointimal formation, and reactive oxygen species production. Mature human CRP shares 71% amino acid sequence homology with its mouse counterpart.

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