About Products Protein Database Contact

SERPING1

Gene
Serping1
Protein
Plasma protease C1 inhibitor
Organism
Mus musculus
Length
504 amino acids
Function
Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. May inhibit chymotrypsin and kallikrein.
Similarity
Belongs to the serpin family.
Mass
55.585 kDa
Sequence
MASRLTPLTLLLLLLAGDRAFSDPEATSHSTQDPLEAQAKSRESFPERDDSWSPPEPTVLPSTWPTTSVAITITNDTMGKVANESFSQHSQPAAQLPTDSPGQPPLNSSSQPSTASDLPTQATTEPFCPEPLAQCSDSDRDSSEAKLSEALTDFSVKLYHAFSATKMAKTNMAFSPFSIASLLTQVLLGAGDSTKSNLESILSYPKDFACVHQALKGFSSKGVTSVSQIFHSPDLAIRDTYVNASQSLYGSSPRVLGPDSAANLELINTWVAENTNHKIRKLLDSLPSDTCLVLLNAVYLSAKWKITFEPKKMMAPFFYKNSMIKVPMMSSVKYPVAQFDDHTLKAKVGQLQLSHNLSFVIVVPVFPKHQLKDVEKALNPTVFKAIMKKLELSKFLPTYLTMPHIKVKSSQDMLSVMEKLEFFDFTYDLNLCGLTEDPDLQVSAMKHETVLELTESGVEAAAASAISFGRSLPIFEVQRPFLFLLWDQQHRFPVFMGRVYDPRG

Gene
Serping1
Protein
Plasma protease C1 inhibitor
Organism
Rattus norvegicus
Length
504 amino acids
Function
Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein (By similarity).
Similarity
Belongs to the serpin family.
Mass
55.611 kDa
Sequence
MASKLTPLTLLLLLLAGDRAFSDSEVTSHSSQDPLVVQEGSRDSVPERDGSRSPIEHTGQSSTWPTTSGSTKISNDTMDQVANESFIQHVQPAAQLPEDSPSQSPVNSSSPPSTASAPPTQAPTEPLCPEPLAWCSDSDRDSSEATLSEALTDFSVKLYHAFSATKKAETNMAFSPFSIASLLTQVLLGAGDSTKSNLEDILSYPKDFACVHQTLKAFSSKGVTSVSQIFHSPDLAIRDTYVNASLSLYGSSPRVLGPDGDANLKLINTWVAENTNHKINELLDSLPSDTRLVLLNAVYLSAKWKKTFEQKKMMASFLYKNSMIKVPMLSSKKYPLALFNDQTLKAKVGQLQLSHNLSFVIMVPQSPTHQLEDMEKALNPTVFKAILKKLELSKFQPTYVMMPRIKVKSSQDMLSIMEKLEFFDFTYDLNLCGLTEDPDLQVSSMKHETVLELTETGVEAAAASTISVARNLLIFEVQQPFLFLLWDQRHKFPVFMGRVYDPRA

Gene
SERPING1
Protein
Plasma protease C1 inhibitor
Organism
Homo sapiens
Length
500 amino acids
Function
Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein.
Similarity
Belongs to the serpin family.
Mass
55.154 kDa
Sequence
MASRLTLLTLLLLLLAGDRASSNPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTTEPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFVLWDQQHKFPVFMGRVYDPRA

Gene
SERPING1
Protein
Plasma protease C1 inhibitor
Organism
Oryctolagus cuniculus
Length
18 amino acids
Function
Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein.
Similarity
Belongs to the serpin family.
Mass
2.134 kDa
Fragment
single
Sequence
VARSLLIFEVQQPFLFLL