Skip to Content
Merck
All Photos(1)

Key Documents

U5379

Sigma-Aldrich

Anti-Ubiquitin antibody produced in rabbit

whole antiserum, lyophilized powder

Synonym(s):

Anti-Ubiquitin antibody

Sign Into View Organizational & Contract Pricing


About This Item

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

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

whole antiserum

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

mol wt

antigen 8.6 kDa

species reactivity

prokaryotes, eukaryotes

technique(s)

immunohistochemistry (frozen sections): suitable
western blot: 1:100 using ubiquitin purified from bovine red blood cells

UniProt accession no.

storage temp.

2-8°C

target post-translational modification

unmodified

Gene Information

General description

Ubiquitin (UBB) gene is mapped to human chromosome 17p11.2.
Ubiquitin is a highly conserved, 8.6kDa, eukaryotic cellular protein containing 76 amino acid residues. Ubiquitin is absent in prokaryotes.

Specificity

By immunoblotting, the antibody recognizes 1-3 protein bands using bovine red blood cell ubiquitin.

Immunogen

bovine red blood cell ubiquitin.

Application

Anti-Ubiquitin antibody produced in rabbit is used in:
  • immunostaining in neuropathology
  • immunohistochemistry
  • western blotting

Biochem/physiol Actions

Ubiquitin is involved in the selective degradation of many short-lived proteins by 26S proteasome. Proteins are targeted for degradation by covalent ligation to ubiquitin. This ubiquitin-mediated degradation of regulatory proteins plays crucial roles in the regulation of various processes, such as cell-cycle progression, signal transduction, transcriptional regulation, receptor down-regulation, stress response, protein trafficking and endocytosis. Ubiquitin protein also aids in immune response, metabolism, development, normal protein turnover, protein quality control by degrading misfolded and damaged proteins and apoptosis. Variation in the ubiquitin-mediated processes results in carcinogenesis.

Target description

Ubiquitin, present in both prokaryotes and eukaryotes, is a highly conserved 8.6 kDa protein. It is involved in the selective degradation of many short-lived proteins by the proteasome, an ATP-dependent protease. Proteins are targeted for degradation by covalent ligation to ubiquitin. This ubiquitin-mediated degradation of regulatory proteins plays important roles in the control of numerous processes, including cell-cycle progression, signal transduction, transcriptional regulation, receptor down-regulation, and endocytosis. It has also been implicated in immune response, metabolism, development, protein quality control, and apoptosis.

Physical form

Lyophilized from 0.01 M phosphate buffer, containing 1% lactose.

Reconstitution

Reconstitute the contents of the vial with 10 mL of Tris buffered saline. Since the antisera is preservative free, it is recommended that it be reconstituted in the presence of a preservative or aliquoted and frozen. Avoid repeated freeze/thaw cycles.

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

11 - Combustible Solids

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Rebecca L Welchman et al.
Nature reviews. Molecular cell biology, 6(8), 599-609 (2005-08-03)
Protein ubiquitylation is a recognized signal for protein degradation. However, it is increasingly realized that ubiquitin conjugation to proteins can be used for many other purposes. Furthermore, there are many ubiquitin-like proteins that control the activities of proteins. The central
J M Henderson et al.
Brain : a journal of neurology, 123 ( Pt 7), 1410-1421 (2000-06-27)
Whilst many reports mention neurofibrillary tangle pathology in the thalamus in progressive supranuclear palsy, there has been little detailed regional analysis of the distribution and density of thalamic pathology in this disease or in other parkinsonian syndromes. The caudal intralaminar
Andrew Kertesz et al.
Brain : a journal of neurology, 128(Pt 9), 1996-2005 (2005-07-22)
This is a clinicopathologic study of a prospective, clinic-based cohort of patients with frontotemporal dementia (FTD)/Pick complex, who were followed to autopsy. A total of 60 patients with the clinical syndromes of the behavioural variant of FTD (FTD-bv) (n =
A Hershko et al.
Annual review of biochemistry, 67, 425-479 (1998-10-06)
The selective degradation of many short-lived proteins in eukaryotic cells is carried out by the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent ligation to ubiquitin, a highly conserved small protein. Ubiquitin-mediated degradation of regulatory proteins
Mónika Lippai et al.
BioMed research international, 2014, 832704-832704 (2014-07-12)
The ubiquitin-proteasome system and autophagy were long viewed as independent, parallel degradation systems with no point of intersection. By now we know that these degradation pathways share certain substrates and regulatory molecules and show coordinated and compensatory function. Two ubiquitin-like

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service