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AB196396

Recombinant Human PRDM14 protein (GST tag N-Terminus)

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(1 Publication)

Recombinant Human PRDM14 protein (GST tag N-Terminus) is a Human Fragment protein, in the 2 to 412 aa range, expressed in Escherichia coli, with >70%, suitable for SDS-PAGE.

View Alternative Names

PR domain zinc finger protein 14, PR domain-containing protein 14, PRDM14

1 Images
SDS-PAGE - Recombinant Human PRDM14 protein (GST tag N-Terminus) (AB196396)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human PRDM14 protein (GST tag N-Terminus) (AB196396)

4-20% SDS-PAGE with Coomassie staining : 2 μg ab196396.

Key facts

Purity

>70% SDS-PAGE

Expression system

Escherichia coli

Tags

GST tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9GZV8

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.04% Sorbitan monolaurate, ethoxylated, 0.02% Potassium chloride

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>" } } }

Sequence info

[{"sequence":"MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDLEVLFQ^GPLGSALPRPSEAVPQDKVCYPPESSPQNLAAYYTPFPSYGHYRNSLATVEEDFQPFRQLEAAASAAPAMPPFPFRMAPPLLSPGLGLQREPLYDLPWYSKLPPWYPIPHVPREVPPFLSSSHEYAGASSEDLGHQIIGGDNESGPCCGPDTLIPPPPADASLLPEGLRTSQLLPCSPSKQSEDGPKPSNQEGKSPARFQFTEEDLHFVLYGVTPSLEHPASLHHAISGLLVPPDSSGSDSLPQTLDKDSLQLPEGLCLMQTVFGEVPHFGVFCSSFIAKGVRFGPFQGKVVNASEVKTYGDNSVMWEIFEDGHLSHFIDGKGGTGNWMSYVNCARFPKEQNLVAVQCQGHIFYESCKEIHQNQELLVWYGDCYEKFLDIPVSLQVTEPGKQPSGPSEESAEGYRCERCGKVFTYK","proteinLength":"Fragment","predictedMolecularWeight":"72 kDa","actualMolecularWeight":null,"aminoAcidEnd":412,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9GZV8","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

PRDM14 also known as PR domain zinc finger protein 14 acts as a transcription factor with a mass of approximately 64 kDa. It contains an N-terminal PR (PRDI-BF1 and RIZ) domain and zinc-finger motifs within its structure which participate in DNA binding. The protein expresses highly in embryonic stem cells and primordial germ cells showing a strong presence in pluripotent cell states.
Biological function summary

PRDM14 plays a vital role in the maintenance of pluripotency and regulation of gene expression during early embryonic development. It forms part of a regulatory network that includes other factors like OCT4 and SOX2 promoting stem cell self-renewal and inhibiting differentiation. This protein directly influences the expression of genes related to germ cell formation.

Pathways

PRDM14 interacts with several key signaling pathways notably the stem cell pluripotency pathway and the Wnt signaling pathway. It collaborates closely with proteins such as NANOG and TET proteins modulating gene expression patterns essential for pluripotent stem cell identity. Through these pathways PRDM14 ensures proper cell fate decisions during development.

PRDM14’s dysfunctions associate with certain cancers and reproductive health issues. Aberrant expression or mutation of PRDM14 appear in germ cell tumors as its regulatory functions become disrupted. Additionally PRDM14 may link to infertility disorders due to its role in germ cell development. Alterations in its activity can disrupt interactions with proteins like PRDM1 impacting normal cell proliferation and differentiation.

Specifications

Form

Liquid

General info

Function

Transcription factor that has both positive and negative roles on transcription. Required for the maintenance of embryonic stem cell identity and the reacquisition of pluripotency in somatic cells. May play an essential role in germ cell development at 2 levels : the reacquisition of potential pluripotency, including SOX2 up-regulation, and successful epigenetic reprogramming, characterized by EHMT1 repression. Its association with CBFA2T2 is required for the functions in pluripotency and germ cell formation (By similarity). Directly up-regulates the expression of pluripotency gene POU5F1 through its proximal enhancer. Binds to the DNA consensus sequence 5'-GGTC[TC]CTAA-3'.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily.

Subcellular localisation

Nucleus

Product protocols

Target data

Transcription factor that has both positive and negative roles on transcription. Required for the maintenance of embryonic stem cell identity and the reacquisition of pluripotency in somatic cells. May play an essential role in germ cell development at 2 levels : the reacquisition of potential pluripotency, including SOX2 up-regulation, and successful epigenetic reprogramming, characterized by EHMT1 repression. Its association with CBFA2T2 is required for the functions in pluripotency and germ cell formation (By similarity). Directly up-regulates the expression of pluripotency gene POU5F1 through its proximal enhancer. Binds to the DNA consensus sequence 5'-GGTC[TC]CTAA-3'.
See full target information PR domain zinc finger protein 14

Publications (1)

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

Cancer science 109:373-383 PubMed29178343

2017

PRDM14 directly interacts with heat shock proteins HSP90α and glucose-regulated protein 78.

Applications

Unspecified application

Species

Unspecified reactive species

Chiharu Moriya,Hiroaki Taniguchi,Satoru Nagatoishi,Hisayoshi Igarashi,Kouhei Tsumoto,Kohzoh Imai
View all publications

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