Any process that modulates the frequency or rate of macrophage activation.

Interacting selectively with the insulin receptor.

Catalysis of the formation of the N6-(L-isoglutamyl)-L-lysine isopeptide, resulting in cross-linking polypeptide chains; the gamma-carboxamide groups of peptidyl-glutamine residues act as acyl donors, and the 6-amino-groups of peptidyl-lysine residues act as acceptors, to give intra- and intermolecular N6-(5-glutamyl)lysine cross-links.

insulin-like growth factor receptor binding

insulin-like growth factor receptor ligand

Interacting selectively with the insulin-like growth factor receptor.

Catalysis of the cleavage of Arg-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg bond in complement component C5 alpha-chain to yield C5a and C5b.

A protein complex whose composition varies amongst species; in rice it probably exists in a homo-tetramer to homo-hexamer form and in Gram negative bacteria as a dimer. Functions in the hydrolysis of alpha-(1,6)-D-glucosidic branch linkages.

Catalysis of the selective cleavage of Arg-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg bond in complement component C5 alpha-chain to form C5a and C5b.

Vinculin-containing myofibril attachment site which connects the Z-discs to the sarcolemma.

Catalysis of the selective cleavage of Lys(or Arg)-Ile bond in complement subcomponent C1s to form the active form of C1s (EC:3.4.21.42).

Catalysis of the cleavage of component C4 to C4a and C4b (Arg-Ala bond), and component C2 to C2a and C2b (Lys-Lys or Arg-Lys bond).

A ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in a polypeptide chain.

Catalysis of the cleavage of component factor B (Arg-Lys) when in complex with C3b or with cobra venom factor (CVF).

The modification of an amino acid to an active form, for incorporation into a peptide, protein or other macromolecule.

Catalysis of the inactivation of complement subcomponents C3b, iC3b and C4b by proteolytic cleavage.