Recombinant Human Dna-Directed Rna Polymerase Iii Subunit Rpc1 (POLR3A) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00603P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Dna-Directed Rna Polymerase Iii Subunit Rpc1 (POLR3A) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00603P
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Product Overview

Description Recombinant Human Dna-Directed Rna Polymerase Iii Subunit Rpc1 (POLR3A) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O14802
Target Symbol POLR3A
Synonyms (RNA polymerase III subunit C1)(DNA-directed RNA polymerase III largest subunit)(DNA-directed RNA polymerase III subunit A)(RNA polymerase III 155 kDa subunit)(RPC155)(RNA polymerase III subunit C160)
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence FPEKVNKANINFLRKLVQNGPEVHPGANFIQQRHTQMKRFLKYGNREKMAQELKYGDIVERHLIDGDVVLFNRQPSLHKLSIMAHLARVKPHRTFRFNECVCTPYNADFDGDEMNLHLPQTEEAKAEALVLMGTKANLVTPRNGEPLIAAIQDFLTGAYLLTLKDTFFDRAKACQIIASILVGKDEKIKVRLPPPTILKPVTLWTGKQIFSVILRPSDDNPVRANLRTKGKQYCGKGEDLC
Expression Range 392-632aa
Protein Length Partial
Mol. Weight 31.4 kDa
Research Area Epigenetics And Nuclear Signaling
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway.
Subcellular Location Nucleus.
Protein Families RNA polymerase beta' chain family
Database References

HGNC: 30074

OMIM: 607694

KEGG: hsa:11128

STRING: 9606.ENSP00000361446

UniGene: PMID: 30450527

  • RNA polymerase III (Pol III) transcribes medium-sized non-coding RNAs (collectively termed Pol III genes), and data show that when Pol III genes are hypo-methylated, MYC amplifies their transcription, regardless of its recognition DNA motif. PMID: 28846112
  • the first transgenic mice with a leukodystrophy-causing Polr3a mutation do not recapitulate the childhood-onset hypomyelinating leukodystrophy observed in the majority of human patients with POLR3A mutations. PMID: 28407788
  • This is the first individual reported with two truncating POLR3A variants, suggesting that biallelic severe loss of function variants are associated with WRS. Sequencing of POLR3A and perhaps related genes such as POLR3B in additional patients with clinical findings of WRS is needed to prove this gene-disease association. PMID: 27612211
  • Findings suggest that AP-1 factors are regulators of RNA polymerase III (Pol III)-driven 5S rRNA and U6 snRNA expression with a potential role in cell proliferation. PMID: 28488757
  • For some of its complex functions, variation in RNAP III activity levels lead to nonuniform changes in tRNA pools that can shift the translation profiles of key codon-biased mRNAs with resultant phenotypes or disease states. (Review) PMID: 27068803
  • Mutations in POLR3A are a frequent cause of sporadic and recessive spastic ataxia. PMID: 28459997
  • RNA polymerase III (RNAPIII) is specialized for transcription of short, abundant nonprotein-coding RNA transcripts. PMID: 27911719
  • Our transcriptome-wide investigations revealed an overall decrease in the levels of Pol III-transcribed tRNAs and an imbalance in the levels of regulatory ncRNAs such as small nuclear and nucleolar RNAs (snRNAs and snoRNAs). PMID: 27506977
  • Multicenter retrospective study to collect neuroradiologic, clinical, and molecular data of patients with mutations in POLR3A and POLR3B without the classic MRI phenotype: diffuse hypomyelination is not an obligatory feature of POLR3-related disorders; two distinct patterns, selective involvement of the corticospinal tracts and cerebellar atrophy, are added to the MRI presentation of POLR3-related disorders PMID: 27029625
  • Mutations in POLR3A or POLR3B are rare in patients with unclassified hypomyelination. PMID: 26011300
  • Mutations in POLR3A are associated with a more severe clinical course of 4H leukodystrophy. PMID: 25339210
  • MRI in patients with POLR3B mutations revealed smaller cerebellar structures, especially vermis, than those in POLR3A mutations. MRI also showed milder hypomyelination in patients with POLR3B mutations than those with POLR3A mutations PMID: 23643445
  • Investigated POLR3A and POLR3B mutations in patients with genetically unexplained hypomyelinating leukodystrophies with features of Pol III-related leukodystrophies. Recessive mutations in POLR3A or POLR3B were uncovered in all 14 patients. PMID: 23355746
  • Studies indicate that aatients with anti-RNAP have an increased risk of malignancy within a 5-year timeframe before or after onset of systemic sclerosis (SSc) skin changes. PMID: 22189167
  • Mutations in POLR3A and POLR3B encoding RNA Polymerase III subunits cause an autosomal-recessive hypomyelinating leukoencephalopathy PMID: 22036171
  • Mutations of POLR3A encoding a catalytic subunit of RNA polymerase Pol III cause a recessive hypomyelinating leukodystrophy. PMID: 21855841
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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