Recombinant Human Ribonuclease pancreatic(RNASE1)

Code CSB-YP019789HU
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Source Yeast
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Code CSB-EP019789HU
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Source E.coli
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Code CSB-EP019789HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP019789HU
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Source Baculovirus
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Code CSB-MP019789HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names RNASE1
Uniprot No. P07998
Alternative Names HP-RNase; Pancreatic ribonuclease; Rib 1; RIB-1; Rib1; Ribonuclease 1; Ribonuclease A; Ribonuclease a family 1; Ribonuclease pancreatic; Ribonuclease RNase A family 1; Ribonuclease RNase A family 1 pancreatic; RNAS1_HUMAN; RNase 1; RNase A; RNase UpI-1; Rnase1; RNAseA
Species Homo sapiens (Human)
Expression Region 29-156
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Data

Function Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.
Gene References into Functions
  1. Data suggest that ribonuclease inhibitor (RNH1) protects HeLa cells from ribonuclease 1 (RNase 1). PMID: 27806571
  2. Focusing on the increase in an N-glycosylated Asn residue of serum pancreatic ribonuclease 1, specifically Asn(88), affords a new diagnostic marker for pancreatic cancer PMID: 25336120
  3. Deletion of five residues in the hinge loop of pancreatic ribonuclease induces formation of a domain-swapped dimer that leads to the generation of linear aggregates of pancreatic RNase, revealed by the crystal packing. PMID: 24100329
  4. The reduced conformational flexibility of eosinophil cationic protein can be dynamically and functionally reproduced in the RNase A scaffold. PMID: 23135272
  5. The nuclear transport of PE5 is critical for its cytotoxicity. PMID: 20352290
  6. The role on the dimerization process of different residues of a domain-swapped dimer human pancreatic ribonuclease variant. PMID: 21767499
  7. In human pancreatic ribonuclease both glutamine 28 and arginine 39 are important for the cleavage of dsRNA. PMID: 21408145
  8. Vascular RNase1 and RNase5 are mainly produced by vascular endothelial cells and can serve, depending on the vascular bed, different functions in vascular homeostasis and endothelial cell responses. PMID: 21103661
  9. Studies illustrate of the making dimeric pancreatic RNase through removal by directed mutagenesis of most of the N-terminal alpha-helix to the remainder of the protein. PMID: 19156888
  10. Human endothelial cells selectively express large amounts of pancreatic-type ribonuclease (RNase 1) PMID: 12210760
  11. Results show that Glycine 38 is crucial for the full catalytic activity of the human enzyme on duplex RNA as its substitution with aspartate or alanine results in a drastic reduction in the dsRNA cleavage activity of HPR. PMID: 12237131
  12. Results reveal the dendritic cell-activating activity of pancreatic ribonuclease and suggest that it is a likely participant of inflammatory and immune responses--an endogenous multifunctional immune alarmin. PMID: 15528350
  13. Altogether the results suggest that the pressure-folding transition state of ribonuclease A looks like a collapsed globule with some secondary structure and a weakened hydrophobic core. This is the first direct comparison using a set of mutants. PMID: 16597833
  14. RNase-1 has ribonuclease H activity. PMID: 16738129
  15. Human pancreatic-ribonuclease interacts with importin alpha through different basic residues, including Lys1 and the arginine clusters 31-33 and 89-91. PMID: 16780873
  16. The results were confirmed at the level of mRNA and protein, and suggested that four genes (OPCML, RNASE1, YES1 and ACK1) could play a key role in the tumorigenesis and metastasis of gastric cancer. PMID: 17109515
  17. Structural and energetic aspects of the interaction between human RI (hRI) and human pancreatic ribonuclease (RNase 1), is reported. PMID: 17350650
  18. Coulombic forces mediate extracellular and intracellular equilibria in a dichotomous manner that both endangers cells and defends them from the potentially lethal enzymatic activity of ribonucleases. PMID: 17705507
  19. irrespective of differences in ethnic groups, RNASE1 might show markedly low heterogeneity in its genetic structure with regard to these SNPs PMID: 18219569
  20. Multiple side chain conformations observed for key surface residues are proposed to be crucial for membrane binding as well as translocation and efficient RNA hydrolysis. PMID: 18495155

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Subcellular Location Secreted
Protein Families Pancreatic ribonuclease family
Tissue Specificity Pancreas and other tissues and body fluids (indicating it may have other physiological functions besides its role in digestion).
Database Links

HGNC: 10044

OMIM: 180440

KEGG: hsa:6035

STRING: 9606.ENSP00000344193

UniGene: Hs.78224


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