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AB226226

Recombinant Human WDR77 protein (Tagged)

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Recombinant Human WDR77 protein (Tagged) is a Human Fragment protein, in the 1 to 312 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

MEP50, WD45, HKMT1069, Nbla10071, WDR77, Methylosome protein WDR77, Androgen receptor cofactor p44, Methylosome protein 50, WD repeat-containing protein 77, p44/Mep50, MEP-50

3 Images
Mass Spectrometry - Recombinant Human WDR77 protein (Tagged) (AB226226)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Human WDR77 protein (Tagged) (AB226226)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab226226 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) WDR77.

Mass Spectrometry - Recombinant Human WDR77 protein (Tagged) (AB226226)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Human WDR77 protein (Tagged) (AB226226)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab226226 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) WDR77.

SDS-PAGE - Recombinant Human WDR77 protein (Tagged) (AB226226)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human WDR77 protein (Tagged) (AB226226)

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

Q9BQA1

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MRKETPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGFCSAGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGDENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSL","proteinLength":"Fragment","predictedMolecularWeight":"49.6 kDa","actualMolecularWeight":null,"aminoAcidEnd":312,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9BQA1","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

WDR77 also known as MEP50 is a protein with a mass of about 37 kDa. It functions as a cofactor involved in methylation processes often forming part of protein complexes with PRMT5. WDR77 locates within the cell nucleus and is widely expressed in human tissues with higher levels observed in reproductive organs like the testis and prostate. The protein interacts with other proteins to affect transcription and RNA processing.
Biological function summary

WDR77 interacts with the protein arginine methyltransferase 5 (PRMT5) and contributes to the assembly and stabilization of methyltransferase complexes. This role is essential for its participation in the methylation of arginine residues on histones and other proteins which regulates gene expression. WDR77 influences cell proliferation and differentiation by modulating these processes especially in germ cells and prostate epithelial cells.

Pathways

WDR77 is an important player in the transcriptional repression pathway affecting histone modification. It connects intimately with important pathways like the PI3K/AKT signaling and cell cycle regulation. Through its interaction with PRMT5 WDR77 takes part in regulatory networks impacting gene silencing chromatin remodeling and the overall gene expression mechanism. The involvement of WDR77 in these pathways emphasizes its relationship with PRMT5 and other methylation-associated proteins.

WDR77 has links to prostate cancer and lung cancer. These associations may result from its role in cell cycle control and proliferation which becomes dysregulated in oncogenesis. WDR77's interaction with PRMT5 is critical in such conditions as changes in their activity can alter normal cell growth patterns. Research indicates that abnormal expression or function of WDR77 can lead to increased tumorigenesis in specific tissues emphasizing the protein's potential as a target for therapeutic interventions.

Specifications

Form

Liquid

General info

Function

Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones (PubMed : 11756452). This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed : 23071334).

Subcellular localisation

Nucleus

Product protocols

Target data

Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones (PubMed : 11756452). This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed : 23071334).
See full target information WDR77

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