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商品編號


AG-40T-0387-R500



品牌


Adipogen



公司


Adipogen



公司分類


Proteins



Size

500 ?l

商品信息


More Information



Product Details



Product Type

Protein



Properties



Source/Host

Synthetic



Sequence

Human SUMO-interacting Motif (SIM) peptide conjugated to agarose.



Crossreactivity

Multi-species



Label/Conjugates

Agarose



Formulation

Liquid. In 50mM HEPES, pH 7.5, 250mM NaCl.



Other Product Data


Use:
This affinity resin is derived from a PIAS sequence and can be used for the enrichment, isolation, and identification of SUMOylated proteins. Equilibrate resin by washing with 5-10ml desired start buffer. Binding and elution of material is dependent on individual experimental conditions.

Storage:
The agarose can be re-used for at least 5-10 applications if properly maintained. After use, clean resin with 5ml 50mM Tris pH 9.0|1M KCl. Remove cleaning solution by washing resin with 5ml storage buffer.



Declaration

Manufactured by Boston Biochem



Shipping and Handling



Shipping

BLUE ICE



Short Term Storage

+4°C



Long Term Storage

+4°C



Handling Advice

Do not freeze.



Use/St
ABI
lity

Stable for at least 3 months after receipt when stored at +4°C.



Documents



MSD
S

No



Product Specification Sheet



Datasheet


Download PDF





Small ubiquitin-like modifiers (SUMOs) are a family of small, related proteins that are enzymatically attached to target proteins by a process termed SUMOylation. This post-translational modification regulates many cellular processes including DNA transcription and repair, cell cycle progression, protein intracellular trafficking, and nuclear receptor activities. SUMO binding and/or interaction with proteins is mediated by short amino acid consensus sequences termed SUMO-interacting motifs (SIMs). To date, all SIMs appear to contain a hydrophobic core sequence that is either preceded or succeeded by an acidic region composed of either glutamate or aspartate residues or phosphorylated serine or threonine residues. The hydrophobic core of SIMs has been shown to interact with the α?helix and β2-strand surfaces on SUMO proteins while the negatively charged residues surrounding the hydrophobic core appear to influence binding affinities and dictate binding preferences for the various SUMO isoforms. SIMs have been identified in numerous types of proteins including SUMO ligases (E3), transcription factors, and transcriptional repressors.