Recombinant Human Non-Secretory Ribonuclease (RNASE2) Protein (hFc)

Name: Recombinant Human Non-Secretory Ribonuclease (RNASE2) Protein (hFc)
Brand: Beta LifeScience
SKU: BLC-07496P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Non-Secretory Ribonuclease (RNASE2) Protein (hFc) is produced by our Mammalian cell expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P10153
Target Symbol	RNASE2
Synonyms	(Eosinophil-derived neurotoxin)(RNase UpI-2)(Ribonuclease 2)(RNase 2)(Ribonuclease US)
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-hFc
Target Protein Sequence	KPPQFTWAQWFETQHINMTSQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNISNCRYAQTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRII
Expression Range	28-161aa
Protein Length	Full Length of Mature Protein
Mol. Weight	44.4 kDa
Research Area	Immunology
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	This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities.
Subcellular Location	Lysosome. Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule.
Protein Families	Pancreatic ribonuclease family
Database References	HGNC: 10045 OMIM: 131410 KEGG: hsa:6036 STRING: 9606.ENSP00000303276 UniGene: Hs.728
Tissue Specificity	Liver, lung, spleen, leukocytes and body fluids.

Gene Functions References

In healthy children, 95th Percentile values ranged from 1519 mg/kg at 0 months to 54.4 mg/kg at 144 months for fecal calprotectin (fCP) and from 9.9 mg/kg at 0 months to 0.2 mg/kg at 144 months for fecal eosinophil-derived neurotoxin (fEDN). There was a significant association between age and fCP concentrations and age and fEDN concentrations and a significant association between fEDN and fCP. PMID: 28169973
EDN serum level could be considered a candidate molecule as a clinical biomarker for evaluating atopic dermatitis activity and a predictor of relapse PMID: 28866306
Serum EDN level may be a useful marker for monitoring persistent airflow limitation in adult patients with asthma who had positive results for house-dust-specific IgE antibodies. PMID: 26534742
increased in feces after the ingestion of enterocolitis-causative foods PMID: 24890227
RNASE2 gene expression was differentially expressed in rheumatoid arthritis patients considering a sequence polymorphism. PMID: 25221852
The antimicrobial protein, RNase 2 exhibits antiviral against respiratory syncytial virus. PMID: 9826755
findings show substantial amounts of EPX/EDN localise in an extra-granular, low equilibrium density compartment of eosinophils PMID: 23053729
A higher level of serum EDN was found specifically in patients with ALS, indicating that EDN may participate in the pathophysiology of Amyotrophic lateral sclerosis. PMID: 23533305
Eosinophil protein X in urine from asymptomatic neonates is a biomarker significantly associated with later development of allergic sensitization, nasal eosinophilia, and eczema during the first 6 years of life PMID: 21680952
atomic resolution structure PMID: 11876642
crystal structure of a post-translationally modified form of eosinophil-derived neurotoxin (EDN) with four extra residues on its N terminus ((-4)EDN) has been solved and refined at atomic resolution (1 A) PMID: 11916383
EDN and ECP are paralogs in human and Old World monkeys. PMID: 11959927
evidence for glycosylphosphatidylinositol (GPI)-anchored neurotoxin on granulocytes PMID: 12606041
data suggest that peripheral blood eosinophils from subjects with untreated asthma have increased inflammatory capacity, as reflected by greater intracellular concentrations of EDN PMID: 15356558
Results reveal the dendritic cell-activating activity of eosinophil-derived neurotoxin and suggest that it is a likely participant of inflammatory and immune responses--an endogenous multifunctional immune alarmin. PMID: 15528350
Results describe the crystal structure of placental ribonuclease inhibitor in complex with eosinophil-derived neurotoxin, and a mutational analysis based on this structure. PMID: 15755456
May possibly be associated with the development of tropical pulmonary eosinophilia. PMID: 16014847
Elevated glycosylated form of EDN in urine is associated with ovarian cancer PMID: 16428483
EGO is a novel ncRNA gene expressed during eosinophil development and is necessary for normal MBP and EDN transcript expression. PMID: 17351112
Data show that uEPX/c levels did not correlate with established markers of asthma severity and eosinophilic airway inflammation in atopic asthmatic children. PMID: 17641730
MAZ and Sp1 play important roles on the transcriptional activation of the human edn promoter through specific binding to a 34-nt segment present in representative primate eosinophil rnase promoters. PMID: 17927842
Urinary concentrations of eosinophil-derived neurotoxin in patients with atopic dermatitis show a significant positive correlation with disease severity. PMID: 17965582
EDN can activate myeloid DCs by triggering the Toll-like receptor (TLR)2-myeloid differentiation factor 88 signaling pathway PMID: 18195069
In three continental population groups (Asia, Europe, Africa), the angiogenin and RNase 2 genes appear to exhibit markedly less genetic heterogeneity with regard to T195C and A238G (ANG) and C425A (RNASE2) SNPs. PMID: 18636464
No variation in genes encoding eosinophil-derived neurotoxin for Atopic dermatitis pathogenesis in this German cohort. PMID: 19014520
the roles of the six discrete segments in transcription regulation were investigated and the -350/-329 region (ednR2) was shown to be involved in the regulation of edn expression PMID: 19115260
ECP and EDN disrupt skin integrity and cause inflammation PMID: 19717523

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.