SUMO-Qapture-T kit

The only commercially available kit for isolation and enrichment of SUMOylated proteins.



BML-UW1000A-0001	1 Kit	319.00 USD

Replaces Prod. #: BML-UW1000

Capture and isolation of SUMO-protein conjugates from specific cell/tissue lysates of interest with subsequent detection and analysis by Western blotting.
Identification of SUMO-modified protein substrates by proteomic analysis methods following release of free SUMOylated proteins in denatured form.
Selective purification/pull down of SUMOylated proteins from in vitro SUMOylation assays.

Figure 1: Western blot analysis of SUMO-Qapture enrichment of lysate- derived SUMO-1 modified proteins. Lane 1: MWM, Lane 2: Unbound lysate, Lane 3: Elution, Lane 4: Wash 1, Lane 5: Wash 2, Lane 6: Starting material.

Figure 1: Western blot analysis of SUMO-Qapture enrichment of lysate- derived SUMO-2/3 modified proteins. Lane 1: MWM, Lane 2: Unbound lysate, Lane 3: Elution, Lane 4: Wash 1, Lane 5: Wash 2, Lane 6: Starting material.

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Product Specification

Application:	For the isolation and enrichment of SUMOylated proteins.

Quantity:	Sufficient for 10 binding assays.

Use/Stability:	SUMO-Qapture-T matrix should be stored at 4ºC upon receipt. All other components should be stored at –80ºC to ensure stability and activity.

Handling:	Avoid freeze/thaw cycles.

Short Term Storage:	-80°C

Long Term Storage:	-80°C

Kit/Set Contains:	SUMO-Qapture-T matrix (Prod. No. BML-UW0980) 200 µL settled resin provided, 50% suspension Control SUMOylated-protein lysate (Prod. No. BML-UW0130A) 200 µg (100µL), 2mg/mL in 50mM TRIS-Cl, pH 7.5, 150mM sodium chloride, 200mM iodoacetamide SUMO-1, sheep polyclonal antibody (Prod. No. BML-PW0505) 10µL SUMO-2/3, sheep polyclonal antibody (Prod. No. BML-PW0510) 10µL

Miscellaneous/General:	The SUMO-Qapture kit is an efficient tool for the selective isolation of SUMOylated proteins. The kit facilitates the affinity purification of SUMOylated proteins from cell extracts and tissue lysates using a high-binding SIM-containing affinity matrix. Captured proteins are eluted under denaturing conditions followed by analysis by Western blotting, using the SUMO antibodies provided or antibodies to specific proteins of interest, or potential substrate identification by proteomic methods. SUMO-conjugate-containing samples are prepared in native form in the presence of protease inhibitors to prevent loss through the action of deSUMOylating enzymes. Optimization of binding permits complete isolation of the full range of SUMO-protein conjugates from a specific lysate. The kit is also supplied with a high quality SUMOylated protein solution for use as a positive control in SUMO-Qapture assays.

Background / Technical Information:	NOTE: BML-UW1000A SUMO-Qapture-T kit replaces BML-UW1000 SUMO-Qapture-T kit with the following changes: 1. Kit component BML-UW09080 SUMO-Qapture-T matrix has changed from 1 mg of peptide/1ml of packed resin to 2 mg of peptide/1ml of packed resin. 2. Kit component BML-UW0985 Control SUMOylated-protein lysate is replaced by BML-UW0130A Control SUMOylated-protein lysate, HeLa S100 fraction in Tris/NaCl containing iodoacetamide. 3. The SUMO antibody solutions are unchanged but have new Product Numbers: BML-PW0505 SUMO-1, sheep polyclonal antibody, and BML-PW0510 SUMO-2/3, sheep polyclonal antibody. 4. BML-UW0990 0.5mL Screw capped tube pack has been eliminated. Please read the manual instructions carefully!

General Literature References

PARP-1 transcriptional activity is regulated by sumoylation upon heat shock: N. Martin, et al.; EMBO J. 28, 3534 (2009), Abstract;

System-wide changes to SUMO modifications in response to heat shock: F. Golebiowski, et al.; Sci. Signal. 2, ra24 (2009), Abstract;

Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae: H. Windecker & H.D. Ulrich; J. Mol. Biol. 376, 221 (2008), Abstract;

In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy: I. Matic, et al.; Mol. Cell Proteomics 7, 132 (2008), Abstract;

In vivo modeling of polysumoylation uncovers targeting of Topoisomerase II to the nucleolus via optimal level of SUMO modification: Y. Takahashi & A. Strunnikov; Chromosoma 117, 189 (2008), Abstract;

RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation: M.H. Tatham, et al.; Nat. Cell Biol. 10, 538 (2008), Abstract;

The fast-growing business of SUMO chains: H.D. Ulrich; Mol. Cell. 32, 301 (2008), Abstract;

The Ulp2 SUMO protease is required for cell division following termination of the DNA damage checkpoint: D.C. Schwartz, et al.; Mol. Cell Biol. 27, 6948 (2007), Abstract;

Specification of SUMO1- and SUMO2-interacting motifs: C.M. Hecker, et al.; J. Biol. Chem. 281, 16117 (2006), Abstract;

SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae: C.H. Cheng, et al.; Genes Dev. 20, 2067 (2006), 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;

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

Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3: H. Saitoh & J. Hinchey; J. Biol. Chem. 275, 6252 (2000), Abstract;