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AB241371

Anti-UBR7 antibody

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(2 Publications)

Rabbit Polyclonal UBR7 antibody. Suitable for IP, WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human UBR7 aa 1-50.

View Alternative Names

C14orf130, UBR7, Putative E3 ubiquitin-protein ligase UBR7, N-recognin-7, RING-type E3 ubiquitin transferase UBR7

2 Images
Immunoprecipitation - Anti-UBR7 antibody (AB241371)
  • IP

Supplier Data

Immunoprecipitation - Anti-UBR7 antibody (AB241371)

UBR7 was immunoprecipitated from HEK-293T (human epithelial cell line from embryonic kidney transformed with large T antigen) whole cell lysate (1 mg for IP; 20% of IP loaded) using ab241371 at 6μg/mg lysate. Western blot was performed on the immunoprecipitate using ab241371 at 0.1 μg/ml.

Lane 1 : ab241371 IP in HEK-293T whole cell lysate.
Lane 2 : Control IgG.

Detection : Chemiluminescence with an exposure time of 30 seconds.

All lanes:

Immunoprecipitation - Anti-UBR7 antibody (ab241371)

Predicted band size: 48 kDa

false

Western blot - Anti-UBR7 antibody (AB241371)
  • WB

Supplier Data

Western blot - Anti-UBR7 antibody (AB241371)

All lanes:

Western blot - Anti-UBR7 antibody (ab241371) at 0.1 µg/mL

Lane 1:

HEK-293T (human epithelial cell line from embryonic kidney transformed with large T antigen) whole cell lysate at 50 µg

Lane 2:

HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell lysate at 50 µg

Lane 3:

Jurkat (human T cell leukemia cell line from peripheral blood) whole cell lysate at 50 µg

Predicted band size: 48 kDa

true

Exposure time: 30s

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, IP

applications

Immunogen

Synthetic Peptide within Human UBR7 aa 1-50. The exact immunogen used to generate this antibody is proprietary information.

Q8N806

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IP" : {"fullname" : "Immunoprecipitation", "shortname":"IP"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IP-species-checked": "testedAndGuaranteed", "IP-species-dilution-info": "2-10 µg/mg of lysate", "IP-species-notes": "<p></p>", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/2000 - 1/10000", "WB-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 - 8 Preservative: 0.09% Sodium azide Constituents: Tris citrate/phosphate
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

UBR7 also known as E3 ubiquitin-protein ligase UBR7 is a protein encoded by the UBR7 gene. The molecular mass of UBR7 is approximately 82 kDa. This protein is expressed in various human tissues with notable higher levels in the liver kidney and heart. Mechanically UBR7 functions as an E3 ubiquitin ligase which means it plays a role in attaching ubiquitin molecules to specific substrates marking them for degradation by the proteasome.
Biological function summary

UBR7 acts within cellular protein quality control by ensuring misfolded or damaged proteins are ubiquitinated for degradation. It is part of a larger ubiquitin-proteasome system which tightly controls protein turnover and homeostasis within the cell. This system helps maintain cell functions by regulating the abundance of key proteins involved in various cellular processes such as signal transduction and cell cycle control.

Pathways

The ubiquitin-proteasome system where UBR7 plays a significant role intersects with the cell cycle regulation and DNA damage response pathways. UBR7 interacts with proteins like p53 a well-known tumor suppressor playing a regulatory role in its stability and activity. Additionally it is involved in pathways concerning apoptosis contributing to programmed cell death when abnormal cells are detected.

Aberrations in UBR7 activity have been linked to cancer particularly related to disruptions in the regulation of p53. The dysregulation can lead to uncontrolled cell growth and tumor development. UBR7 also associates with neurodegenerative disorders where the accumulation of misfolded proteins due to impaired ubiquitination contributes to neuronal damage. Here its connection with proteins such as Tau is significant as abnormal ubiquitination patterns have been observed in cases of Alzheimer's disease.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
See full target information UBR7

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

eLife 11: PubMed36066346

2022

A specific role for importin-5 and NASP in the import and nuclear hand-off of monomeric H3.

Applications

Unspecified application

Species

Unspecified reactive species

Alonso Javier Pardal,Andrew James Bowman

Cell death discovery 7:392 PubMed34907164

2021

CRISPR/Cas9 genome-wide screening identifies LUC7L2 that promotes radioresistance via autophagy in nasopharyngeal carcinoma cells.

Applications

Unspecified application

Species

Unspecified reactive species

Lin Shen,Chao Li,Fang Chen,Liangfang Shen,Zhanzhan Li,Na Li
View all publications

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