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1401 12944 Ensembl ENSG00000132693 ENSMUSG00000037942 UniProt P02741 P14847 RefSeq (mRNA) NM_000567 NM_001329057 NM_001329058 NM_001382703 NM_007768 RefSeq (protein) NP_000558 NP_001315986 NP_001315987 NP_001369632 NP_031794 Location (UCSC) Chr 1: 159.71 – 159.71 Mb Chr 1: 172.53 – 172.66 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse C-reactive protein (CRP) is an annular (ring ...
Adjusting your daily protein intake can help you reach your weight and fitness goals, but health experts say these are six of the most common mistakes people make that can keep you from maximizing ...
In contrast, C-reactive protein (with a half-life of 6–8 hours) rises rapidly and can quickly return to within the normal range if treatment is employed. For example, in active systemic lupus erythematosus, one may find a raised ESR but normal C-reactive protein. [citation needed] They may also indicate liver failure. [11]
C-reactive protein, an acute phase protein produced by the liver; cAMP receptor protein (catabolite gene activator protein) Cysteine-rich protein, a class of small proteins; Carbon-fiber-reinforced polymers; Chinese restaurant process, in probability theory; Chronic relapsing polyneuropathy, an acquired disorder of the nervous system
Insulin-like growth factor 1, a polypeptide protein hormone which plays an important role in childhood growth and continues to have anabolic effects in adults Thrombopoietin , a glycoprotein hormone that regulates the production of platelets by the bone marrow
Ceruloplasmin is the major copper-carrying protein in the blood, and in addition plays a role in iron metabolism. It was first described in 1948. [ 8 ] Another protein, hephaestin , is noted for its homology to ceruloplasmin, and also participates in iron and probably copper metabolism.
Contrary to popular belief, haemoglobin is not a blood protein, as it is carried within red blood cells, rather than in the blood serum. Serum albumin accounts for 55% of blood proteins, [1] is a major contributor to maintaining the oncotic pressure of plasma and assists, as a carrier, in the transport of lipids and steroid hormones.
C1q can also be activated in other ways, for example by binding to pentraxins such as C-reactive protein [2] or directly to the surface of pathogens. [1] Such binding of C1q leads to conformational changes in the C1q molecule, which activates the associated C1r molecules. Active C1r cleaves the C1s molecules, activating them.