Human Elongin B protein (Recombinant) (No-Tag) (STJP019617)

SPECIFICATIONS
HostE.coli
ImmunogenHuman
STJP019617
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General Information

Short DescriptionRecombinant-Human Elongin B-No-Tag protein was developed from e.coli and has a target region of No-Tag. For use in research applications.
ApplicationsSDS-PAGE
HostE.coli
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

Concentration1 mg/mL
FormulationLiquid in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 0.1mM PMSF, 20% Glycerol
Storage InstructionFor short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles.

Target Information

Gene SymbolELOB
Gene ID6923
Uniprot IDELOB_HUMAN
Accession NumberNP_009039
ImmunogenHuman
Immunogen Region1-118aa
Immunogen SequenceMDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVQ

Additional Info

Function 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). 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. Core component of multiple cullin-2 and cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes), which mediate the ubiquitination of target proteins. 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. Component the von Hippel-Lindau ubiquitination complex CBC(VHL). 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. The ECS(ASB9) complex mediates ubiquitination and degradation of CKB. As part of a multisubunit ubiquitin ligase complex, polyubiquitinates monoubiquitinated POLR2A. ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase. As part of the ECS(RAB40C) complex, mediates ANKRD28 ubiquitination and degradation, thereby inhibiting protein phosphatase 6 (PP6) complex activity and focal adhesion assembly during cell migration. (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. The complex can also ubiquitinate APOBEC3H to some extent.
Protein Name Elongin-B
Elob
Elongin 18 Kda Subunit
Rna Polymerase Ii Transcription Factor Siii Subunit B
Siii P18
Transcription Elongation Factor B Polypeptide 2
Database Links Reactome: R-HSA-112382
Reactome: R-HSA-1234176
Reactome: R-HSA-167152
Reactome: R-HSA-167200
Reactome: R-HSA-167238
Reactome: R-HSA-167243
Reactome: R-HSA-167246
Reactome: R-HSA-167287
Reactome: R-HSA-167290
Reactome: R-HSA-180585
Reactome: R-HSA-674695
Reactome: R-HSA-6796648
Reactome: R-HSA-75955
Reactome: R-HSA-8951664
Reactome: R-HSA-9010553
Reactome: R-HSA-9705462
Reactome: R-HSA-983168
Reactome: R-HSA-9833109
Cellular Localisation Nucleus
Alternative Protein Names Elongin-B protein
Elob protein
Elongin 18 Kda Subunit protein
Rna Polymerase Ii Transcription Factor Siii Subunit B protein
Siii P18 protein
Transcription Elongation Factor B Polypeptide 2 protein
ELOB protein
TCEB2 protein

Information sourced from Uniprot.org

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