Recombinant Human Upf0568 Protein C14Orf166 (RTRAF) Protein (GST)

Name: Recombinant Human Upf0568 Protein C14Orf166 (RTRAF) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08644P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Upf0568 Protein C14Orf166 (RTRAF) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9Y224
Target Symbol	RTRAF
Synonyms	C14orf166; CGI 99; CGI-99; CGI99; Chromosome 14 open reading frame 166; CLE; CLE7; CN166_HUMAN; Homeobox prox 1; LCRP369; RLL motif containing 1; RLLM1; UPF0568 protein C14orf166
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MFRRKLTALDYHNPAGFNCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLRDVNCPFKIQDRQEAIDWLLGLAVRLEYGDNAEKYKDLVPDNSKTADNATKNAEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKAIRILVQERLTQDAVAKANQTKEGLPVALDKHILGFDTGDAVLNEAAQILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLGKVGR
Expression Range	1-244aa
Protein Length	Full Length
Mol. Weight	55.1kDa
Research Area	Neuroscience
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	RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. Component of the tRNA-splicing ligase complex and is required for tRNA ligation. May be required for RNA transport.; (Microbial infection) In case of infection by influenza virus A (IVA), is involved in viral replication.
Subcellular Location	Nucleus. Cytoplasm, cytosol. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.; Nucleus. Cytoplasm.
Protein Families	RTRAF family
Database References	HGNC: 23169 OMIM: 610858 KEGG: hsa:51637 STRING: 9606.ENSP00000261700 UniGene: PMID: 26219895 C14orf166, a cellular protein required for viral replication, is incorporated into influenza virus particles. PMID: 26864902 C14orf166 promotes bladder cancer cell proliferation and can be a novel prognostic biomarker for patients with bladder cancer. PMID: 26905879 C14orf166 could be a novel prognostic biomarker of breast cancer, it also contributes to cell proliferation by regulating G1/S transition. PMID: 26883017 Overexpression of chromosome 14 open reading frame 166 correlates with disease progression in nasopharyngeal carcinoma. PMID: 25964093 Silencing of CLE causes reduction of influenza A virus polymerase activity, viral RNA transcription and replication, virus titer, and viral particle production. PMID: 21900157 spatial interactions of hnRNPH1, NF45, and C14orf166 with HCVc174 likely modulate HCV or cellular functions during acute and chronic HCV infection PMID: 21823664 A novel protein CGI-99 is isolated, which may be involved in the functional regulation of human ninein in the centrosome structure and may also be important in brain development and tumorigenesis. PMID: 15147888 c14orf166 was identified asa novel metastasis-associated protein, and the roles of radixin, moesin and c14orf166 in pancreatic cancer metastasis deserve further investigations. PMID: 19152423

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.