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Merck
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09-409

Sigma-Aldrich

Anti-SUMO-1 Antibody

Upstate®, from rabbit

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

polyclonal

species reactivity (predicted by homology)

all

manufacturer/tradename

Upstate®

technique(s)

western blot: suitable

isotype

IgG

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

General description

The small ubiquitin-related modifier SUMO-1 belongs to the growing family of ubiquitin-related proteins involved in post translational protein modification1. It is present in all eukaryotic kingdoms and is highly conserved from yeast to humans. SUMO-1 does not appear to target proteins for degradation but seems to be involved in the modulation of protein-protein interactions. An increasing number of SUMO-1 substrates are being described but three major substrates for SUMO-1 modification are RanGAP1 and PML proteins.

Specificity

Recognizes SUMO-1. This antibody shows no cross-reactivity with ubiquitin, multi-ubiquitin chains, SUMO2/3, UCRP, Nedd8, and FAT10.

Immunogen

Synthetic peptide corresponding to amino acid residues 11-101 of human SUMO-1.

Application

Anti-SUMO-1 Antibody detects level of SUMO-1 & has been published & validated for use in WB.

Linkage

Replaces: 04-453

Physical form

100 µL of purified by salt precipitation in PBS containing 0.01% sodium azide. Dilute to working strength with 50mM Tris-HCl buffer (pH 7.6) containing 1.5% sodium chloride and 1% normal goat serum (if a goat anti-rabbit IgG linker antibody is to be used).
Format: Purified

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Lorna Moll et al.
eLife, 7 (2018-11-08)
Although aging-regulating pathways were discovered a few decades ago, it is not entirely clear how their activities are orchestrated, to govern lifespan and proteostasis at the organismal level. Here, we utilized the nematode Caenorhabditis elegans to examine whether the alteration
C Kretz-Remy et al.
Biochemistry and cell biology = Biochimie et biologie cellulaire, 77(4), 299-309 (1999-11-05)
Regulation of protein functions can be achieved by posttranslational protein modifications. One of the most studied modifications has been conjugation to ubiquitin, which mainly targets substrate proteins for degradation by the 26 S proteasome. Recently, SUMO/sentrin, a ubiquitin-like protein has
P Bayer et al.
Journal of molecular biology, 280(2), 275-286 (1998-07-09)
The recently discovered small ubiquitin-related modifier SUMO-1 belongs to the growing family of ubiquitin-related proteins involved in postranslational protein modification. Unlike ubiquitin, SUMO-1 does not appear to target proteins for degradation but seems to be involved in the modulation of
S Müller et al.
Nature reviews. Molecular cell biology, 2(3), 202-210 (2001-03-27)
Covalent modification of cellular proteins by the ubiquitin-like modifier SUMO regulates various cellular processes, such as nuclear transport, signal transduction, stress response and cell-cycle progression. But, in contrast to ubiquitylation, sumoylation does not tag proteins for degradation, but seems to

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