The SDEA Antibody (PAC063047) is a polyclonal antibody designed for research involving SDEA, a protein associated with immune responses and inflammation regulation. This antibody is raised in rabbits and exhibits high reactivity with human samples, making it ideal for use in Western blot applications. By binding to the SDEA protein, this antibody enables detection and analysis in various cell types, making it a valuable tool for studies in immunology and cancer research.
SDEA, also known as a critical regulator of immune responses, plays a crucial role in maintaining immune homeostasis and regulating inflammatory processes. Its involvement in immune modulation positions it as a promising target for research on diseases such as cancer, autoimmune disorders, and chronic inflammatory conditions. By understanding the function of SDEA, researchers can develop potential therapies that manipulate immune responses in disease contexts.
Antibody Name:
sdeA Antibody (PACO63047)
Antibody SKU:
PACO63047
Size:
50ul
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
ELISA:1:2000-1:10000, WB:1:1000-1:5000
Species Reactivity:
Legionella pneumophila subsp
Immunogen:
Recombinant Legionella pneumophila subsp Ubiquitinating/deubiquitinating enzyme SdeA protein (19-268AA)
Western Blot. Positive WB detected in Recombinant protein. All lanes: sdeA antibody at 1:2000. Secondary. Goat polyclonal to rabbit IgG at 1/50000 dilution. Predicted band size: 32 kDa. Observed band size: 32 kDa.
Background:
Secreted effector that interferes with the host cell ubiquitin pathway and is required for intracellular bacterial replication. Catalyzes the ubiquitination of several mammalian Rab proteins (Rab33b, Rab1, Rab6a and Rab30) during L.pneumophila infection, without engaging the standard cellular enzyme cascade (E1 and E2). Transfers an ADP-ribose moiety from NAD to the 'Arg-42' residue of ubiquitin in a reaction that releases nicotinamide. The modified ubiquitin is subsequently transferred to the substrate protein through an unknown mechanism that results in the release of AMP. Cannot ubiquitinate the endosomal Rab5 or the cytoskeletal small GTPase Rac1. Also acts as a deubiquitinase (DUB), catalyzing the cleavage of three of the most abundant polyubiquitin chains ('Lys-11', 'Lys-48' and 'Lys-63') with a distinct preference for 'Lys-63' linkages; is thus able to efficiently remove 'Lys-63'-linked polyubiquitin chains from the phagosomal surface. Is also able to remove NEDD8 from neddylated proteins, but is unable to recognize SUMO. The DUB activity of SdeA is important for regulating the dynamics of ubiquitin association with the bacterial phagosome, but is dispensable for its role in intracellular bacterial replication.
