Analytical Data
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Gene name
RNF146
- Application
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Alternative Names
Dactylidin; dJ351K20.1 ; DKFZP434O1427; E3 ubiquitin-protein ligase rnf146; RING finger protein 146; RN146_HUMAN; RNF 146; Rnf146; RP3 351K20.1
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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
Q9NTX7
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Expression Region
1-359 aa
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AA Sequence
MMAGCGEIDH SINMLPTNRK ANESCSNTAP SLTVPECAIC LQTCVHPVSL PCKHVFCYLC VKGASWLGKR CALCRQEIPE DFLDKPTLLS PEELKAASRG NGEYAWYYEG RNGWWQYDER TSRELEDAFS KGKKNTEMLI AGFLYVADLE NMVQYRRNEH GRRRKIKRDI IDIPKKGVAG LRLDCDANTV NLARESSADG ADSVSAQSGA SVQPLVSSVR PLTSVDGQLT SPATPSPDAS TSLEDSFAHL QLSGDNTAER SHRGEGEEDH ESPSSGRVPA PDTSIEETES DASSDSEDVS AVVAQHSLTQ QRLLVSNANQ TVPDRSDRSG TDRSVAGGGT VSVSVRSRRP DGQCTVTEV
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Molecular Weight
38.9 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
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Protein Description
RNF146, also known as Ring Finger Protein 146, is an E3 ubiquitin ligase that plays a pivotal role in various cellular processes, including the regulation of protein degradation, cell cycle progression, and signal transduction. Its involvement in ubiquitination pathways has garnered significant attention, particularly in the context of cancer and neurodegenerative diseases, where dysregulation of protein homeostasis is a common feature. RNF146 is known to mediate the ubiquitination of several key substrates, thereby affecting their stability and function. Recent studies have suggested that RNF146 may be implicated in the modulation of cellular stress responses, particularly under conditions of oxidative stress, further emphasizing its potential as a therapeutic target. The generation of recombinant RNF146 protein facilitates detailed investigations into its biochemical properties, interactions with substrates, and functional implications in various signaling pathways. Understanding the molecular mechanisms of RNF146 could provide insights into its role in disease pathology and may pave the way for the development of novel strategies for intervention in diseases characterized by protein misfolding and aggregation. As such, research on RNF146 is poised to contribute significantly to the fields of molecular biology and therapeutic development.
