Where does SUMO cleave?

A: SUMO Protease 1 is a highly specific enzyme œ it recognizes the entire SUMO structure and consistently cleaves at the junction to deliver a protein with designed N-terminus. A variety of protein fusions have been investigated and the enzyme never cleaves within the protein of interest.

How does SUMO protease work?

How does SUMO protease work? SUMO protease, also known as Ulp, is a recombinant fragment of ULP1 (Ubl-specific protease 1) from Saccharomyces cerevisiae. It is highly specific for the SUMO protein fusion, recognizing the tertiary structure of SUMO rather than an amino acid sequence.

What is the molecular weight of his tag?

0.2–1.6 kDa
His-tags. Molecular Weight: 0.2–1.6 kDa.

Why does His-tag bind nickel?

When a protein having a His-tag is brought into contact with a carrier on which a metal ion such as nickel is immobilized under the condition of pH 8 or higher, the histidine residue chelates the metal ion and binds to the carrier.

What is the biological function of Rad18?

Rad18 is involved in the regulation of melanoma cell proliferation. The Rad6-Rad18 enzyme plays an essential role in promoting replication through DNA lesions by translesion synthesis in mammalian cells.

How do you increase protein solubility?

It is widely accepted that the solubility and stability of proteins can be increased by the use of additives in buffers (e.g., ionic compounds, salts, detergents, osmolytes, etc).

How does Halo tag work?

A covalent bond is formed between the HaloTag protein and HaloTag ligand when these two moieties come in contact, resulting in rapid and irreversible binding.

Why is histidine tag used?

This tag is most commonly used in the production of recombinant proteins since the string of histidine residues binds to several types of immobilized ions (such as nickel, cobalt and copper) under specific buffer conditions to allow for the simple detection and purification of His-tagged proteins.