Rabbit Anti-Human RNASE3 (internal) Polyclonal antibody

Name: Rabbit Anti-Human RNASE3 (internal) Polyclonal antibody
SKU: DPABH-13763
Rating: 5 (1 reviews)

Rabbit Anti-Human RNASE3 (internal) Polyclonal antibody for WB, IHC

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COA

SDS

Datasheet

Key features and details

Target: RNASE3
Host: Rabbit
Application: WB, IHC
Species Reactivity: Human

Summary

Specifications

Antibody Isotype

IgG

Species Reactivity

Human

Immunogen

Fusion protein corresponding to a region derived from internal residues of human ribonuclease, RNase A family, 3

Conjugate

Unconjugated

Applications

Application Notes

WB: 1:200-1:1000
IHC: 1:25-1:100

General Notes

This product (Catalog No. DPABH-13763) is a rabbit-derived IgG polyclonal antibody raised against human RNASE3. It has been affinity purified by protein A. Eosinophil cationic protein (UniProt P12724; also known as ECP, Ribonuclease 3, RNase 3) is encoded by the RNASE3 (also known as ECP, RNS3) gene (Gene ID 6037) in human. The major basic protein (MBP), eosinophil cationic protein (ECP), eosinophil derived neurotoxin (EDN) and eosinophil peroxidase (EPO), are eosinophil effector molecules implicated in host defense, immunoregulatory responses, and in allergic and inflammatory reactions. These highly cationic proteins are stored preformed within the eosinophil secondary granules and released in intact membrane-bound granules during cell lysis or through a complex system of vesiculotubular structures during "piecemeal necrosis". While eosinophil count and eosinophil surface expression of the activation marker CD69 are significantly correlated with serum concentrations of MBP, EDN and EPO, studies show that they are not correlated with ECP level. On the other hand, eosinophilic disease patients with normal eosinophil count show significantly increased concentrations of MBP, ECP, EDN, and EPO compared to normal donors. The measurement of MBP, ECP, EDN, and EPO levels thus provides a better predictor than eosinophil count alone in disease diagnosis. ECP is produced with a signal peptide sequence (a.a. 1-27), the removal of which yields the mature (a.a. 28-160) protein.
DPABH-13763 is suitable for use in Western blot (WB) (1:200–1:1,000), IHC (1:25–1:100) applications.
DPABH-13763 is supplied as a liquid formulation in pH7.4 PBS, 0.05% sodium azide, 40% Glycerol. For long-term storage, keep at −20 °C. For short-term use, store at 2–8 °C. Avoid repeated freeze–thaw cycles to maintain antibody integrity and performance.

Target

Alternative Names

RNASE3; ribonuclease, RNase A family, 3; ECP; RNS3; eosinophil cationic protein; RNase 3; ribonuclease 3; cytotoxic ribonuclease

Entrez Gene ID

6037

UniProt ID

P12724

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Human Antimicrobial RNases Inhibit Intracellular Bacterial Growth and Induce Autophagy in Mycobacteria-lnfected Macrophages

FRONTIERS IN IMMUNOLOGY

Authors: Lu, Lu; Arranz-Trullen, Javier; Prats-Ejarque, Guillem; Pulido, David; Bhakta, Sanjib; Boix, Ester

Abstract

The development of novel treatment against tuberculosis is a priority global health challenge. Antimicrobial proteins and peptides offer a multifaceted mechanism suitable to fight bacterial resistance. Within the RNaseA superfamily there is a group of highly cationic proteins secreted by innate immune cells with anti-infective and immune-regulatory properties. In this work, we have tested the human canonical members of the RNase family using a spot-culture growth inhibition assay based mycobacteria-infected macrophage model for evaluating their anti-tubercular properties. Out of the seven tested recombinant human RNases, we have identified two members, RNase3 and RNase6, which were highly effective against Mycobacterium aurum extra- and intracellularly and induced an autophagy process. We observed the proteins internalization within macrophages and their capacity to eradicate the intracellular mycobacterial infection at a low micro-molar range. Contribution of the enzymatic activity was discarded by site-directed mutagenesis at the RNase catalytic site. The protein induction of autophagy was analyzed by RT-qPCR, western blot, immunofluorescence, and electron microscopy. Specific blockage of auto-phagosome formation and maturation reduced the protein's ability to eradicate the infection. In addition, we found that the M. aurum infection of human THP1 macrophages modulates the expression of endogenous RNase3 and RNase6, suggesting a function in vivo. Overall, our data anticipate a biological role for human antimicrobial RNases in host response to mycobacterial infections and set the basis for the design of novel anti-tubercular drugs.

Isolation and Characterization of S-RNase-homologous Genes Expressed in Styles in 'Hyuganatsu' (Citrus tamurana hort. ex Tanaka)

HORTICULTURE JOURNAL

Authors: Honsho, Chitose; Umegatani, Shingo; Furukawa, Dai; Ishimura, Shuji; Tetsumura, Takuya

Abstract

In this study, S-RNase-homologous genes expressed in styles were isolated from a gametophytic selfincompatible citrus cultivar, 'Hyuganatsu'. Sweet orange and clementine genome databases were searched to identify 13 ribonuclease T2 (T2 RNase) genes. Further blast searches using citrus EST databases were conducted with these 13 sequences as queries to obtain five additional EST sequences. Known T2 RNase genes, including the S-RNases of Rosaceae, Solanaceae, and Plantaginaceae were retrieved from the public database. All data collected from the databases were combined to make a dataset for phylogenetic analysis. From the phylogenetic tree, 10 citrus sequences were found to be monophyletic to the Glade of S-RNases. Degenerate primers were designed from these genes to identify similar sequences in cDNA derived from 'Hyuganatsu' styles. RT-PCR and 3' and 5' RACE resulted in the isolation of three S-RNase-like sequences; these sequences were further characterized. Pistil-specific gene expression was confirmed for all sequences by RT-PCR; Citrus tamurana RNasel (CtRNS1) and RNase3 (CtRNS3) had basic pI values (> 8) and molecular weights of approximately 25 kDa, consistent with S-RNase features of other families. The distribution of CtRNS1, CtRNS2, and CtRNS3 was investigated using 10 citrus cultivars. CtRNS1 and CtRNS2 did not correspond to any S-haplotypes in the 10 cultivars, while CtRNS3 matched the citrus' S-1-haplotype.