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AB226831

Anti-Elongin-C antibody

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(3 Publications)

Rabbit Polyclonal Elongin-C antibody. Suitable for WB and reacts with Human, Dog, Cat samples. Cited in 3 publications. Immunogen corresponding to Synthetic Peptide within Human ELOC.

View Alternative Names

TCEB1, ELOC, Elongin-C, EloC, Elongin 15 kDa subunit, RNA polymerase II transcription factor SIII subunit C, SIII p15, Transcription elongation factor B polypeptide 1

3 Images
Western blot - Anti-Elongin-C antibody (AB226831)
  • WB

Supplier Data

Western blot - Anti-Elongin-C antibody (AB226831)

All lanes:

Western blot - Anti-Elongin-C antibody (ab226831) at 1/1000 dilution

All lanes:

PC-3 (human prostate adenocarcinoma cell line) cell lysate at 30 µg

Predicted band size: 12 kDa

true

Western blot - Anti-Elongin-C antibody (AB226831)
  • WB

Supplier Data

Western blot - Anti-Elongin-C antibody (AB226831)

Samples were separated by 15% SDS-PAGE.

All lanes:

Western blot - Anti-Elongin-C antibody (ab226831) at 1/1000 dilution

Lane 1:

MDCK whole cell extracts at 30 µg

Lane 2:

PG-4 whole cell extracts at 30 µg

Secondary

All lanes:

HRP-conjugated anti-rabbit IgG antibody

false

Western blot - Anti-Elongin-C antibody (AB226831)
  • WB

Supplier Data

Western blot - Anti-Elongin-C antibody (AB226831)

Samples were separated by 15% SDS-PAGE.

All lanes:

Western blot - Anti-Elongin-C antibody (ab226831) at 1/2000 dilution

Lane 1:

Jurkat whole cell extracts at 30 µg

Lane 2:

Raji whole cell extracts at 30 µg

Lane 3:

NCI-H929 whole cell extracts at 30 µg

Secondary

All lanes:

HRP-conjugated anti-rabbit IgG antibody

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Cat, Human, Dog

Applications

WB

applications

Immunogen

Synthetic Peptide within Human ELOC. The exact immunogen used to generate this antibody is proprietary information.

Q15369

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification
Storage buffer
pH: 7 Preservative: 0.025% Proclin 300 Constituents: PBS, 20% Glycerol (glycerin, glycerine)
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
-20°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.

Elongin C also known as Elongin BC is a small protein with a mass of approximately 11 kDa. This protein is part of the Elongin complex which includes Elongin B and Elongin A. It is widely expressed in various tissues facilitating its role in transcriptional regulation. Elongin C works mechanically by forming a complex with Elongin B to elongate RNA polymerase II transcription and it acts as an adaptor in various cellular processes.
Biological function summary

Elongin C participates in stabilizing the association of Elongin A with RNA polymerase II. It is an essential component of the transcription elongation complex influencing the transcriptional activity of genes. By forming a complex with Elongin B it propels the transcription process forward particularly in response to signals that regulate transcription elongation. Elongin C also connects with the cullin-RING E3 ubiquitin ligase (CRL) complex contributing to protein degradation pathways.

Pathways

Elongin C plays a significant role in the ubiquitin-proteasome system which targets proteins for degradation. It functions alongside Elongin A and Elongin B in this pathway where these components coordinate to control protein levels in the cell. Elongin C associates with the VHL (Von Hippel-Lindau) tumor suppressor protein in the pathway responsible for hypoxia-inducible factor (HIF) degradation therefore influencing cellular responses to oxygen availability.

Alterations in Elongin C are implicated in cancer and von Hippel-Lindau disease. The disruption of its function can affect the stability and degradation of HIF leading to aberrant cellular proliferation and tumor progression. Elongin C through interaction with VHL highlights its importance in managing proper cell growth and differentiation underpinning its potential role in developing therapeutic targets for cancer treatment.

Product protocols

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

Target data

SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (PubMed : 7821821). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity).. Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins (PubMed : 10205047, PubMed : 12004076, PubMed : 12050673, PubMed : 15590694, PubMed : 21199876, PubMed : 26138980, PubMed : 29775578, PubMed : 29779948, PubMed : 30166453, PubMed : 33268465, PubMed : 38326650). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes (PubMed : 10205047, PubMed : 12004076, PubMed : 12050673, PubMed : 15590694). Component the von Hippel-Lindau ubiquitination complex CBC(VHL) (PubMed : 10205047, PubMed : 12004076, PubMed : 12050673, PubMed : 15590694). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed : 26138980, PubMed : 29775578, PubMed : 29779948). The ECS(ASB9) complex mediates ubiquitination and degradation of CKB (PubMed : 33268465). As part of a multisubunit ubiquitin ligase complex, polyubiquitinates monoubiquitinated POLR2A (PubMed : 19920177). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity).. (Microbial infection) Following infection by HIV-1 virus, component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, which catalyzes ubiquitination and degradation of APOBEC3F and APOBEC3G (PubMed : 18562529, PubMed : 20532212, PubMed : 22190037, PubMed : 24225024, PubMed : 24402281, PubMed : 36754086). The complex can also ubiquitinate APOBEC3H to some extent (PubMed : 37640699).
See full target information ELOC

Publications (3)

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

Gene 932:148908 PubMed39218414

2024

MRPL13 is a metastatic and prognostic marker of breast cancer: A silico analysis accompanied with experimental validation.

Applications

Unspecified application

Species

Unspecified reactive species

Pei Dai,Yan'an Chen,Xiao Zhang,Long Liu,Zhenbo Cheng

iScience 27:109802 PubMed38746666

2024

Discovery of SOCS7 as a versatile E3 ligase for protein-based degraders.

Applications

Unspecified application

Species

Unspecified reactive species

Anaïs Cornebois,Marie Sorbara,Margot Cristol,Emmanuelle Vigne,Pierre Cordelier,Klervi Desrumeaux,Nicolas Bery

International journal of molecular medicine 46:675-684 PubMed32626954

2020

Paeonol exerts anti‑tumor activity against colorectal cancer cells by inducing G0/G1 phase arrest and cell apoptosis via inhibiting the Wnt/β‑catenin signaling pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Li-Hua Liu,Ren-Jie Shi,Zhi-Cheng Chen
View all publications

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