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S8070

Sigma-Aldrich

Anti-SUMO-1 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-GMP1, Anti-PIC1, Anti-SMT3C, Anti-SMT3H3, Anti-Sentrin-1, Anti-Small Ubiquitin-related Modifiier-1, Anti-UBL1

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 14 kDa (unconjugated SUMO-1)
antigen 41 kDa (SUMO-1-GST)

species reactivity

human

technique(s)

immunoprecipitation (IP): 10-20 μg using a nuclear extract of HeLa cells
indirect immunofluorescence: 4-8 μg/mL using human HeLa cells
microarray: suitable
western blot: 0.5-1 μg/mL using nuclear extract of HeLa cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

cow ... SUMO1(614967)
human ... SUMO1(7341)
mouse ... Sumo1(22218)
rat ... Sumo1(301442)

Related Categories

General description

The SUMO-1 (small ubiquitin-like modifier 1) gene is mapped to human chromosome 2q33.1 and is highly conserved. The protein structure includes an α-helix core surrounded by four-stranded β-sheets.

Immunogen

synthetic peptide corresponding to amino acid 1-16 located at the N-terminus of human SUMO-1, conjugated to KLH. The sequence is identical in many species including mouse, rat, dog, bovine, and highly conserved (single amino acid substitution) in chicken and Xenopus SUMO-1. It is not found in human SUMO-2 and SUMO-3.

Application

Anti-SUMO-1 antibody produced in rabbit has been used in immunoblotting assay.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biochem/physiol Actions

SUMO (small ubiquitin-like modifier) proteins are associated with a number of cellular processes. SUMOylation mediated by SUMO1 is involved in nuclear transport mechanism, apoptosis, regulation of cyclin-dependent kinase 6 and protein stability. SUMO1 regulates tumor suppressor p53 protein, a transcription factor that is termed as the “guardian of the genome” plays a key role in the cell cycle events. Unlike ubiquitination which directs proteins for degradation, SUMOylation aims to alter the stability, localization and the function of the target protein.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Variants of transient receptor potential melastatin member 4 in childhood atrioventricular block.
Syam N, et al.
Journal of the American Heart Association, 5(5), e001625-e001625 (2016)
Small ubiquitin-related modifier 1 is involved in hepatocellular carcinoma progression via mediating p65 nuclear translocation.
Liu J, et al.
Oncotarget, 7(16), 22206-22206 (2016)
SUMOylation of Myc-family proteins.
Sabo A, et al.
PLoS ONE, 9(3), e91072-e91072 (2014)
Blocking CRMP2 SUMOylation reverses neuropathic pain.
A Moutal et al.
Molecular psychiatry, 23(11), 2119-2121 (2017-05-24)
A Central Cysteine Residue Is Essential for the Thermal Stability and Function of SUMO-1 Protein and SUMO-1 Peptide?Protein Conjugates.
Drobecq H, et al.
Bioconjugate Chemistry, 27(6), 1540-1546 (2016)

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