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RIZ1 Protein, Human, Recombinant (GST)

Catalog No. TMPY-01265
Synonyms: PR domain containing 2, with ZNF domain, MTB-ZF, RIZ1, HUMHOXY1, RIZ2, RIZ, KMT8

PR domain containing 2, with ZNF domain (PRDM2), also known as zinc finger protein RIZ, is a member of histone methyltransferase (HMT) class enzymes that methylate lysine residues of histones or proteins. HMTs contain a conserved catalytic core termed the SET domain, which shares sequence homology with an independently described sequence motif, the PR domain. PRDM2 contains 8 C2H2-type zinc fingers and a distinct SET domain, and is highly expressed in retinoblastoma cell lines and in brain tumors, as well as in a number of other cell lines and in brain, heart, skeletal muscle, liver and spleen. PRDM2 is an S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3, and is identified as a tumor suppressor. It is reported that intact PR( SET) sequence is required for tumor suppression functions, mutations in the PR domain caused activity reduction in human cancers. Also, S-adenosylhomocysteine or methyl donor deficiency inhibits RIZ1 and other H3 lysine 9 methylation activities. PRDM2 may also function as a DNA-binding transcription factor. It binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and acts as a transcriptional activator. Besides, PRDM2 (RIZ) can bind to the retinoblastoma protein (RB) and also Interacts with GATA3.

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RIZ1 Protein, Human, Recombinant (GST)
Pack Size Availability Price/USD Quantity
100 μg 5 days $ 600.00
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Biological Description
Technical Params
Product Properties
References and Literature
Description PR domain containing 2, with ZNF domain (PRDM2), also known as zinc finger protein RIZ, is a member of histone methyltransferase (HMT) class enzymes that methylate lysine residues of histones or proteins. HMTs contain a conserved catalytic core termed the SET domain, which shares sequence homology with an independently described sequence motif, the PR domain. PRDM2 contains 8 C2H2-type zinc fingers and a distinct SET domain, and is highly expressed in retinoblastoma cell lines and in brain tumors, as well as in a number of other cell lines and in brain, heart, skeletal muscle, liver and spleen. PRDM2 is an S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3, and is identified as a tumor suppressor. It is reported that intact PR( SET) sequence is required for tumor suppression functions, mutations in the PR domain caused activity reduction in human cancers. Also, S-adenosylhomocysteine or methyl donor deficiency inhibits RIZ1 and other H3 lysine 9 methylation activities. PRDM2 may also function as a DNA-binding transcription factor. It binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and acts as a transcriptional activator. Besides, PRDM2 (RIZ) can bind to the retinoblastoma protein (RB) and also Interacts with GATA3.
Species Human
Expression System E. coli
Tag GST
Accession Number Q13029-1
Synonyms PR domain containing 2, with ZNF domain, MTB-ZF, RIZ1, HUMHOXY1, RIZ2, RIZ, KMT8
Construction A DNA sequence encoding the N-terminal segment of human PRDM2 (NP_036363.2) (Met 1-Ala 200), containing the SET domian, was fused with the GST tag at the N-terminus.
Protein Purity > 86 % as determined by SDS-PAGE
Molecular Weight Approxiamtely 49.6 kDa
Endotoxin Please contact us for more information.
Formulation Lyophilized from sterile 20mM Tris, 150mM NaCl, 0. 5mM DTT, 0. 5mM GSH, pH 8.0. Pleasecon tact usfor any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage

Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Shipping

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

Research Background PR domain containing 2, with ZNF domain (PRDM2), also known as zinc finger protein RIZ, is a member of histone methyltransferase (HMT) class enzymes that methylate lysine residues of histones or proteins. HMTs contain a conserved catalytic core termed the SET domain, which shares sequence homology with an independently described sequence motif, the PR domain. PRDM2 contains 8 C2H2-type zinc fingers and a distinct SET domain, and is highly expressed in retinoblastoma cell lines and in brain tumors, as well as in a number of other cell lines and in brain, heart, skeletal muscle, liver and spleen. PRDM2 is an S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3, and is identified as a tumor suppressor. It is reported that intact PR( SET) sequence is required for tumor suppression functions, mutations in the PR domain caused activity reduction in human cancers. Also, S-adenosylhomocysteine or methyl donor deficiency inhibits RIZ1 and other H3 lysine 9 methylation activities. PRDM2 may also function as a DNA-binding transcription factor. It binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and acts as a transcriptional activator. Besides, PRDM2 (RIZ) can bind to the retinoblastoma protein (RB) and also Interacts with GATA3.

References and Literature

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Keywords

RIZ1 Protein, Human, Recombinant (GST) KMT-8 RIZ 1 PR domain containing 2, with ZNF domain MTB-ZF RIZ1 KMT 8 HUMHOXY1 HUMHOXY 1 RIZ-1 RIZ2 RIZ 2 HUMHOXY-1 RIZ-2 RIZ KMT8 recombinant recombinant-proteins proteins protein

 

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