CRP Protein (AA 17-224, N-Term)

Catalog No. ABIN2666544

This Recombinant CRP protein is expressed in Escherichia coli (E. coli).

Quick Overview for CRP Protein (AA 17-224, N-Term) (ABIN2666544)

Target: CRP (C-Reactive Protein (CRP))

Protein Type: Recombinant

Biological Activity: Active

Origin: Human

Source: Escherichia coli (E. coli)

Application: Biochemical Assay (BCA)

Purity: > 95 % , as determined by Coomassie stained SDS-PAGE.

Product Details

Protein Characteristics: AA 17-224, N-Term

Sterility: 0.22 μm filtered

Endotoxin Level:

Less than 0.1 EU per μg of protein as determined by the LAL method.

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

Biological activity: Human CRP, when immobilized at 2 μg/mL, is able to bind recombinant APCS in a dose-dependent manner with a median binding affinity (BD50) of 0.1 - 0.4 μg/mL.

Restrictions: For Research Use only

Handling

Format: Liquid

Reconstitution: For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20 °C to -70 °C. Stock solutions can also be prepared at 50 - 100 μg/mL in sterile buffer (PBS, HPBS, DPBS, or EBSS) containing carrier protein such as 0.2 - 1 % BSA or HSA and stored in working aliquots at -20 °C to -70 °C.

Buffer: 0.22 μm filtered protein solution is in 20 mM Tris, 150 mM NaCl, 2 mM CaCl2, and pH 7.5.

Handling Advice: Avoid repeated freeze/thaw cycles.

Storage: -20 °C

Storage Comment: Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for six months, or at -70°C for one year.

Target Details

Target: CRP (C-Reactive Protein (CRP))

Alternative Name: C-Reactive Protein

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.

Molecular Weight: The 209 amino acid recombinant protein has a predicted molecular mass of approximately 23 kDa. The protein migrates approximately at 26 kDa in DTT-reducing and non-reducing conditions by SDS-PAGE. The predicted N-terminal amino acid is Met.

Pathways: Carbohydrate Homeostasis