Analytical Data
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Gene name
PCGF5
- Application
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Alternative Names
MGC16202; OTTHUMP00000020085; PCGF 5; PCGF5; PCGF5_HUMAN; Polycomb group ring finger 5; Polycomb group RING finger protein 5; Ring finger protein (C3HC4 type) 159; RING finger protein 159; RNF159
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86SE9
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Expression Region
1-256 aa
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AA Sequence
MATQRKHLVK DFNPYITCYI CKGYLIKPTT VTECLHTFCK TCIVQHFEDS NDCPRCGNQV HETNPLEMLR LDNTLEEIIF KLVPGLREQE LERESEFWKK NKPQENGQDD TSKADKPKVD EEGDENEDDK DYHRSDPQIA ICLDCLRNNG QSGDNVVKGL MKKFIRCSTR VTVGTIKKFL SLKLKLPSSY ELDVLCNGEI MGKDHTMEFI YMTRWRLRGE NFRCLNCSAS QVCSQDGPLY QSYPMVLQYR PRIDFG
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Molecular Weight
29.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
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.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
PCGF5 (Polycomb group ring finger 5) is a member of the Polycomb group (PcG) proteins, which are crucial regulators of gene expression and chromatin dynamics. These proteins function primarily through the formation of multi-subunit complexes that modify histones, leading to transcriptional repression of target genes. Research into PCGF5 has gained interest due to its involvement in various biological processes, including development, stem cell maintenance, and cellular differentiation. Aberrations in the expression of PCGF5 have been linked to several diseases, notably cancer, where it may contribute to tumorigenesis and the aggressive nature of certain malignancies. Understanding the structure and function of recombinant PCGF5 is essential for elucidating its role in these pathways and could provide insights into potential therapeutic targets. The study of recombinant PCGF5 protein facilitates the exploration of its interaction with other cofactors and the identification of downstream targets, enhancing our comprehension of its function within the Polycomb repressive complexes (PRCs). Moreover, investigating PCGF5’s influence on gene silencing mechanisms could reveal novel strategies for modifying gene expression in therapeutic contexts, particularly in cancer treatment where reactivation of silenced tumor suppressor genes holds promise. Therefore, the biophysical characterization of recombinant PCGF5 and its complexes is an important step towards unraveling the complex regulatory networks orchestrated by PcG proteins and advancing our understanding of their implications in health and disease.
