3.4.21.45: complement factor I
This is an abbreviated version!
For detailed information about complement factor I, go to the full flat file.
Word Map on EC 3.4.21.45
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3.4.21.45
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hemolytic
-
convertase
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macular
-
properdin
-
uremic
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cell-bound
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c3d
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fluid-phase
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glomerulonephritis
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complement-mediated
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opsonization
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medicine
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i-mediated
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eculizumab
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alpha\'-chain
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c4-binding
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c4bp
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microangiopathic
-
opsonin
- 3.4.21.45
-
hemolytic
-
convertase
-
macular
- properdin
-
uremic
-
cell-bound
- c3d
-
fluid-phase
- glomerulonephritis
-
complement-mediated
-
opsonization
- medicine
-
i-mediated
- eculizumab
-
alpha\'-chain
-
c4-binding
- c4bp
-
microangiopathic
-
opsonin
Reaction
Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage =
Synonyms
C3b inactivator, C3b/C4b inactivator, C3bINA, CFI, complement C3b inactivator, complement C3b/C4b inactivator, complement C4b inactivator, complement C4bi, complement compoment C3b inactivator, complement factor I, complement inhibitor factor I, complement regulator factor I, conglutinogen-activating factor C, factor I, factor I-like activity, fI, GcIf-1, GcIf-2, GcIf-3, GcIf-4, IF, plasma protease factor I, serine protease Factor I
ECTree
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Molecular Weight
Molecular Weight on EC 3.4.21.45 - complement factor I
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27590
calculated for non-glycosylated light chain, estimated basing upon results of the N-linked glycan analysis
30270
estimated for light chain of a partially deglycosylated factor I bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site
35290
calculated for non-glycosylated heavy chain, estimated basing upon results of the N-linked glycan analysis
3569
approximate reduction of molecular weight for the heavy chain after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases
35900
native light chain, estimated basing upon results from the N-linked glycan analysis
37960
estimated for heavy chain of a partially deglycosylated factor I bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site
38000
41530
native heavy chain, estimated basing upon results from the N-linked glycan analysis
50000
5632
approximate reduction of molecular weight for the light chain after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases
62880
total calculated molecular weight for non-glycosylated factor I, estimated basing upon results of the N-linked glycan analysis
68230
estimated for total protein bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site
77430
deduced for total protein of the native factor I basing upon results from the N-linked glycan analysis
88000
892
Man3GlcNAc2 core, deduced molecular weight of N-linked glycan structure
90000
9201
approximate reduction of molecular weight for total molecule of factor I after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases
additional information
mutant protein reveals a slightly different migration pattern during electrophoresis under reducing conditions, due to proximity of the mutation to a cysteine residue
38000
-
1 * 38000 + 1 * 50000, non-catalytic 50000 Da subunit is disulfide-linked to the 38000 Da catalytic subunit
38000
-
1 * 50000 + 1 * 38000, SDS-PAGE, the enzyme is proteolytically processed into the heavy and the light chain that remain covalently linked by a disulfide bond, domains structure overview
50000
-
Western blotting, truncated Q336x mutant under non-reducing conditions and heavy chain of CFI under reducing conditions
50000
-
1 * 38000 + 1 * 50000, non-catalytic 50000 Da subunit is disulfide-linked to the 38000 Da catalytic subunit
50000
-
1 * 50000 + 1 * 38000, SDS-PAGE, the enzyme is proteolytically processed into the heavy and the light chain that remain covalently linked by a disulfide bond, domains structure overview
88000
reduced form, RRKR-linker peptide not cleaved, corresponds to pro-complemement factor I
88000
reduced form, RRKR-linker peptide not cleaved, corresponds to pro-complement factor I
88000
SDS-PAGE, nonreducing conditions, detection of murine complement factor I by using a crossreactive polyclonal goat antibody against human complement factor I
88000
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Western blotting, wild-type and the Q232K, C237Y and S250L mutants under non-reducing conditions