SUMO-1 (human), (recombinant) (His-tag)



BML-UW9195-0500	500 µg	248.00 USD
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Product Details

Alternative Name:	Sentrin-1, Small ubiquitin-related modifier 1

MW:	~12kDa

Source:	Produced in E. coli. Human SUMO-1 is fused to a His-tag.

UniProt ID:	P63165

Formulation:	Liquid. In HEPES, pH 8.0, containing 50mM NaCl, 1mM DTT.

Purity:	≥95% (SDS-PAGE)

Application Notes:	In the presence of HeLa Fraction II or a combination of SUMO E1 and E2 (Prod. No. BML-UW9330 and BML-UW9320 respectively), with ATP, Mg²⁺, and DTT, mature SUMO-1 may be conjugated to soluble proteins. Typical in vitro concentration for non-rate limiting conjugate formation is 200μM to 1mM, depending upon conditions. Uses: 1. SUMO-1 modification of specific proteins in vitro. 2. Demonstrate novel proteins are potential targets for SUMOylation under in vitro conditions. 3. Generate substrates for deSUMOylating enzymes.

Shipping:	Dry Ice

Long Term Storage:	-80°C

Handling:	Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.

Scientific Background:	SUMO (small ubiquitin-related modifier) is a member of a family of ubiquitin-like proteins involved in the regulation of the cellular functions of a wide variety of proteins. Four members of the SUMO family have been described in vertebrates, SUMO-1 and the close homologues SUMO-2 and SUMO-3, with some 50% homology between SUMO-1 and SUMO-2/3. Although a fourth SUMO (SUMO-4) has been reported, there remains considerable debate as to whether this is a real and expressed gene product. The mechanism for SUMO conjugation is analogous to that of the ubiquitin system, relying upon utilisation of E1, E2 and (potentially) E3 cascade enzymes to covalently link the carboxy-terminal of SUMO proteins to specific lysine residues on target proteins via isopeptide bonds. Unlike ubiquitinylation, which leads, inter alia, to a degradative pathway, SUMO modification of target proteins is involved in nuclear protein targeting, formation of sub-nuclear complexes, regulation of transcriptional activities, and control of protein stability. A short sequence containing the consensus Ψ-K-X-D/E (where lysine is the modified amino acid, Ψ is a large hydrophobic residue and X is any amino acid residue) is thought to be necessary for protein SUMOylation to occur, however, SUMOylation has also been observed in cases where the consensus site is not conserved. Conjugation of mature SUMO proteins to specific lysine residues on target proteins via isopeptide bonds, is involved in a range of processes including nuclear protein targeting, formation of sub-nuclear complexes, regulation of transcriptional activities, and control of protein stability.

Regulatory Status:	RUO - Research Use Only

SUMO-1 (human), (recombinant) (His-tag) Western blot

SUMOylation assays for RANGAP1 target protein using SUMO-1, 2 and 3. SUMOylated proteins were detected by Western blotting using the appropriate BIOMOL SUMO antibodies. Results demonstrate the formation of SUMOylated target proteins of the expected size in all ATP containing reactions (+). The absence of such conjugates in negative control reactions (–) demonstrates that their formation is ATP dependent (required for E1 activation) and hence derived from the SUMO cascade.

SUMO-1 (human), (recombinant) (His-tag) SDS-PAGE

SDS-PAGE Analysis of SUMO-1 protein. Lane 1: MW markers (top to bottom) 66, 45, 36, 29, 24, 20 and 16. Lane 2: 10μg SUMO-1. Protein runs at ~20kDa.

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Product Literature References

DEK oncoprotein participates in heterochromatin replication via SUMO-dependent nuclear bodies: A. Pierzynska-Mach, et al.; J. Cell Sci. (2023), Abstract;

Resolving the zinc binding capacity of honey bee vitellogenin and locating its putative binding sites: V. Leipart, et al.; Insect Mol. Biol. 31, 810 (2022), Abstract;

An electrophoretic mobility shift assay identifies a mechanistically unique inhibitor of protein sumoylation: Y.S. Kim, et al.; Chem. Biol. 20, 604 (2013), Abstract; Full Text

Chemotherapeutic sensitivity of testicular germ cell tumors under hypoxic conditions is negatively regulated by SENP1-controlled sumoylation of OCT4: Y.C. Wu, et al.; Cancer Res. 72, 4963 (2012), Abstract; Full Text

A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activate heat shock transcription factors and is associated with susceptibility to type 1 diabetes mellitus: K.M. Bohren, et al.; J. Biol. Chem. 279, 27233 (2004), Abstract;

Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9: M.H. Tatham, et al.; J. Biol. Chem. 276, 35368 (2001), Abstract; Full Text

SUMO, ubiquitin's mysterious cousin: S. Miller, et al.; Nat. Rev. Mol. Cell Biol. 2, 202 (2001), (Review), Abstract;

SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting: M.S. Rodriguez, et al.; J. Biol. Chem. 276, 12654 (2001), Abstract;

SUMO-1 modification activates the transcriptional response of p53: M.S. Rodriguez, et al.; EMBO J. 18, 6455 (1999), Abstract; Full Text

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