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Creative Biolabs offers anti-sumoylation antibodies prepared by our excellent High-Affi™ technology. The affinity purified antibodies are produced by immunizing animals with synthetic peptide corresponding to a sequence within SUMO-1 or SUMO-2/3. SUMO-1 antibody detects endogenous levels of recombinant SUMO-1 which is conjugated to RanGAP, PML, p53 and IκB-α as monomers. SUMO-2/-3 antibody detects poly-SUMO chains which are conjugated to topoisomerase II and APP.
Sumoylation is a post-translational modification with the process that SUMO (small ubiquitin-like modifier) proteins are modified on substrate proteins catalyzed by an enzymatic cascade analogous to that involved in ubiquitination. In contrast to ubiquitin, SUMO is not used to tag proteins for degradation but can regulate various protein function including protein-protein interactions and subcellular localization. Sumoylation is also involved in a variety of cellular processes, such as transcriptional regulation, nuclear-cytosolic transport, apoptosis, protein stability, response to stress, and progression through the cell cycle.
There are four SUMO isoforms identified in humans: SUMO-1, SUMO-2, SUMO-3, and SUMO-4. Among, SUMO-2 and SUMO-3 are highly similar to each other, but are distinct from SUMO-1. SUMO-2 and SUMO-3 occupy a greater percentage of protein modification than SUMO-1 does. Differ from SUMO-1, they can form polymeric chains. SUMO-4 shows similarity to SUMO-2/3 but differs in having a proline instead of the glutamine at position 90, and only using for modification of proteins under stress conditions.
Mature SUMO is produced when the last four amino acids of the C-terminus have been cleaved off to allow the formation of an isopeptide bond between the C-terminal glycine residue of SUMO and an acceptor lysine on the target protein. Generally, sumoylation is substoichiometric, and this modification is rapidly taken off by desumoylating enzymes. This dynamic and reversed process makes essential contributions to diseases, including cancers, neuronal dysfunction, diabetes, and cardiovascular diseases. Typically, sumoylation is highly expressed in cancer tissues, and interfering with sumoylation could be a valid anti-cancer strategy. Sumoylation also interacts closely with other post-translational modification. For example, in the pathology of Alzheimer’s disease (AD), the sumoylation of tau (τ) protein causes hyperphosphorylation at multiple AD-associated sites. Accordingly, the hyperphosphorylation of τ promotes its sumoylation as well; and in turn, inhibits the ubiquitination of tau proteins, finally resulting in the inhibition of τ degradation.
Fig. 1 The SUMO pathway. (Henley J. M. 2014)
Creative Biolabs has developed an extensive panel of antibodies against each of the SUMO proteins using High-Affi™ technology. The antibodies recognize three SUMO isoforms (SUMO-1, SUMO-2 and SUMO-3), which could be applied in detection and quantization of sumoylated proteins. Moreover, a bunch of stunning immunoassays has been generated with our sumoylation-specific antibodies.
In addition to the sumoylation-specific antibody, Creative Biolabs also provides a comprehensive list of PTM-specific antibody production services of your choice.
|Glycosylation||ISGylation||Tyrosine sulfation||Tyrosine nitration|
Fatty Acylation (N-Myristoylation,
Henley J M, Craig T J, and Wilkinson K A. (2014). “Neuronal sumoylation: Mechanisms, physiology, and roles in neuronal dysfunction”. Physiol Rev, 94(4): 1249-1285.
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