Recombinant Human Cellular Nucleic Acid-Binding Protein (CNBP) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04442P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Cellular Nucleic Acid-Binding Protein (CNBP) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04442P
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Product Overview

Description Recombinant Human Cellular Nucleic Acid-Binding Protein (CNBP) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P62633
Target Symbol CNBP
Synonyms CCHC type zinc finger nucleic acid binding protein; Cellular nucleic acid binding protein; Cellular nucleic acid-binding protein; CNBP; CNBP_HUMAN; CNBP1; DM2; Erythroid differentiation related; PROMM; Proximal myotonic myopathy nucleic acid binding protein; RNF163; Sterol regulatory element binding protein; ZCCHC22; Zinc finger protein 273; Zinc finger protein 9 (a cellular retroviral nucleic acid binding protein); Zinc finger protein 9; ZNF9
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence SSNECFKCGRSGHWARECPTGGGRGRGMRSRGRGFQFVSSSLPDICYRCGESGHLAKDCDLQEDACYNCGRGGHIAKDCKEPKREREQCCYNCGKPGHLARDCDHADEQKCYSCGEFGHIQKDCTKVKCYRCGETGHVAINCSKTSEVNCYRCGESGHLARECTIEATA
Expression Range 2-170aa
Protein Length Full Length of Mature Protein of Isoform 2
Mol. Weight 34.6kDa
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.
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 Single-stranded DNA-binding protein that preferentially binds to the sterol regulatory element (SRE) sequence 5'-GTGCGGTG-3', and thereby mediates transcriptional repression. Has a role as transactivator of the Myc promoter. Binds single-stranded RNA in a sequence-specific manner.; Binds G-rich elements in target mRNA coding sequences. Prevents G-quadruplex structure formation in vitro, suggesting a role in supporting translation by resolving stable structures on mRNAs.; Binds to RNA.; Binds to RNA.; Binds to RNA.; Binds to RNA.; Binds to RNA.
Subcellular Location Nucleus. Cytoplasm. Endoplasmic reticulum.; [Isoform 1]: Cytoplasm.; [Isoform 2]: Cytoplasm.; [Isoform 4]: Cytoplasm.; [Isoform 5]: Cytoplasm.; [Isoform 6]: Cytoplasm.; [Isoform 8]: Cytoplasm.
Database References

HGNC: 13164

OMIM: 116955

KEGG: hsa:7555

STRING: 9606.ENSP00000410769

UniGene: PMID: 29199958

  • [CCTG]n repeat expansion, differently from the DM1 mutation, does not influence the methylation status of the CNBP gene and other molecular mechanisms are involved in the pathogenesis of Myotonic Dystrophy type 2.. PMID: 29291944
  • RNA sequence preferences of unconventional RNA-binding proteins, Nudt21 and CNBP, has been described. PMID: 27956239
  • A second point is that DM mutations, although located in noncoding regions, may reduce the expression of mutant alleles, raising questions whether loss-of-function may contribute to the phenotype, or possibly impose a safety limit on knockdown therapies that create or aggravate a DMPK or CNBP deficiency state PMID: 28376341
  • CNBP is supporting translation by resolving stable structures on mRNAs. PMID: 28329689
  • A G-rich motif in the lncRNA Braveheart interacts with Cnbp to specify the cardiovascular lineage. PMID: 27618485
  • The cnbp overexpression rescued the Treacher Collins Syndrome phenotype in a dose-dependent manner by a reactive oxygen species-cytoprotective action that prevented the redox-responsive genes' upregulation but did not normalize the synthesis of ribosomal RNAs. PMID: 27711076
  • High CNBP expression is associated with Medulloblastoma. PMID: 26460945
  • CNBP overexpression caused increase of cell death and suppression of cell metastasis through its induction of G-quadruplex formation in the promoter of hnRNP K resulting in hnRNP K down-regulation PMID: 24594223
  • Arginine methylation of CNBP in the RG motif does not change the subcellular localization but regulates its RNA binding activity. PMID: 24726729
  • CNBP are novel antigens for SLE patients and the recognition of CNBP might be differentiated dependent on the level of arginine methylation. PMID: 23642268
  • suggested a new possibility of CNBP as a potential anti-cancer target based on CNBP's biological function in c-myc transcription PMID: 23774591
  • CNBP associates with the poly(A) binding protein and accumulates in stress granules. PMID: 23285195
  • The co-segregation of Myotonic dystrophy type 2 with a recessive CLCN1 mutation provided the explanation for the unusual clinical findings for juvenile onset of myotonia in a 14-year-old female with Myotonic dystrophy type 2 and her affected mother PMID: 22407275
  • Myotonic dystrophy 2(autosomal dominant, multisystem disorder caused by a CCTG tetranucleotide repeat expansion located in intron 1 of the zinc finger protein 9 gene (ZNF9 gene) on chromosome 3q 21.3.) described in Israeli Jewish European ancestry. PMID: 22332444
  • CCTG repeat expansions in the CNBP gene are responsible for myotonic dystrophy type 2. PMID: 21204798
  • Study concludes that DM2 patients from the Netherlands, including a North-African family, harbor a common haplotype surrounding the ZNF9 gene. PMID: 21224892
  • These data suggest that Gis2 is functionally orthologous to ZNF9 and acts as a cap-independent translation factor. PMID: 21277287
  • ZNF9 expression in myotonic dystrophy type 2 patients is altered at multiple levels. PMID: 20971734
  • ZNF9 is abundantly expressed in human myofibres, where it is located in the sarcomeric I bands, and no modification of this pattern is observed in myotonic dystrophy type 2 muscles. PMID: 20102514
  • Data identify ZNF9 as a regulator of cap-independent translation and indicate that ZNF9 activity may contribute mechanistically to the myotonic dystrophy type 2 phenotype. PMID: 20174632
  • Six of seven of the Zn(2+) fingers from the CNBP protein can be used as substitutes for the Zn(2+) finger in the NH(2)-terminal position of HIV-1 nucleocapsid, and thus support virus replication PMID: 12857921
  • The proximal myotonic myopathy phenotype is associated with DM2-(CCTG)(n) expansion mutations. PMID: 15261229
  • In twenty-six individuals from a family with DM, the CCTG repeats in ZNF9 were found in normal range. PMID: 15476170
  • results show that a single nucleotide polymorphism located in the first intron of the ZNF9 gene is in linkage disequilibrium with the DM2 mutation PMID: 15652222
  • Results indicate that the (CCTG)n expansion in the ZNF9 intron does not appear to have a direct consequence on the expression of the gene itself. PMID: 16376058
  • the downstream molecular effects of a DM2 mutation are triggered by the accumulation of CCUG repeat tract alone and do not decrease ZNF9 expression at the mRNA or protein level PMID: 16624843
  • We present two first-degree relatives with an athletic clinical phenotype, pathological evidence of subsarcolemmal vacuolation, and molecular genetic confirmation of DM2(the molecular defect of the zinc finger protein 9 gene) PMID: 17068784
  • PCBP2 and ZNF9 stimulate translation of the ornithine decarboxylase internal ribosomal entry site . PMID: 17327219
  • These data contribute to the clinical and molecular correlation of ZNF9 gene short expansion in myotonic dystrophy. PMID: 18804219
  • Validated occurrence of an unusual TG 3' splice site in intron 3. PMID: 17672918

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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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