Biochemical characterization of the murine S100A9 (MRP14) protein suggests that it is functionally equivalent to its human counterpart despite its low degree of sequence homology

European Journal of Biochemistry

Volumn 267, Issue 2, 2000, Pages 560-565

  Nacken, Wolfgang ^a   Sopalla, Claudia ^b   Pröpper, Christian ^b   Sorg, Clemens ^b   Kerkhoff, Claus ^b  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b NONE

Author keywords

Mouse; MRP14; Myeloid; S100 protein; S100A8 and S100A9

Indexed keywords

ANIMAL CELL; ARTICLE; CELL CULTURE; CELL DIFFERENTIATION; IMMUNOPRECIPITATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN LOCALIZATION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

ANIMALS; ANTIGENS, DIFFERENTIATION; BLOTTING, WESTERN; CALCIUM-BINDING PROTEINS; CALGRANULIN A; CALGRANULIN B; CELL LINE; CYTOSOL; GRANULOCYTE COLONY-STIMULATING FACTOR; GRANULOCYTES; HUMANS; L-LACTATE DEHYDROGENASE; LEUKOCYTES; MICE; PRECIPITIN TESTS; PROTEIN ISOFORMS; RECOMBINANT FUSION PROTEINS; S100 PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBCELLULAR FRACTIONS;

ANIMALIA; MAMMALIA; MURINAE;

EID: 0033958652     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01040.x     Document Type: Article

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