Herpes 1 IgM ELISA Kit (DEIA346)

Regulatory status: For research use only, not for use in diagnostic procedures.

Write a review

Size
96T
Sample
serum, plasma
Species Reactivity
Human
Intended Use
The Herpes1 IgM Antibody ELISA Test Kit has been designed for the the detection and the quantitative determination of specific IgM antibodies against Herpes 1 in serum and plasma.
Contents of Kit
1. Microwell plate: 1 x 96 wells
2. Calibrator A (Negative Control): 1 x 2 mL
3. Calibrator B (Cut-Off Standard): 1 x 2 mL
4. Calibrator C (Weak Positive Control): 1 x 2 mL
5. Calibrator D (Positive Control): 1 x 2 mL
6. Enzyme Conjugate: 1 x 5 mL
7. Substrate: 1 x 15 mL
8. Stop Solution: 1 x 15 mL
9. Sample Diluent: 1 x 60 mL
10. Washing Buffer: 1 x 60 mL
Storage
For more detailed information, please download the following document on our website.
Sensitivity
1.10 U/mL

Citations


Have you cited DEIA346 in a publication? Let us know and earn a reward for your research.

Customer Reviews


Write a review, share your experiences with others and get rewarded !
Product Name Cat. No. Applications Host Species Datasheet Price Add to Basket
Product Name Cat. No. Applications Host Species Datasheet Price Add to Basket

References


Effect of SUMO-SIM Interaction on the ICP0-Mediated Degradation of PML Isoform II and Its Associated Proteins in Herpes Simplex Virus 1 Infection

JOURNAL OF VIROLOGY

Authors: Fada, Behdokht Jan; Kaadi, Elie; Samrat, Subodh Kumar; Zheng, Yi; Gu, Haidong

ND10 nuclear bodies, as part of the intrinsic defenses, impose repression on incoming DNA. Infected cell protein 0 (ICP0), an E3 ubiquitin ligase of herpes simplex virus 1 (HSV-1), can derepress viral genes by degrading ND10 organizers to disrupt ND10. These events are part of the initial tug of war between HSV-1 and host, which determines the ultimate outcome of infection. Previously, we reported that ICPO differentially recognizes promyelocytic leukemia (PML) isoforms. ICP0 depends on a SUMO-interaction motif located at residues 362 to 364 (SIM362-364) to trigger the degradation of PML isoforms II, IV, and VI, while using a bipartite sequence flanking the RING domain to degrade PML I. In this study, we investigated how the SUMO-SIM interaction regulates the degradation of PML II and PML II-associated proteins in ND10. We found that (i) the same regulatory mechanism for PML II degradation was detected in cells permissive or nonpermissive to the ICP0-null virus; (ii) the loss of a single SIM362-364 motif was restored by the presence of four consecutive SIMs from RNF4, but was not rescued by only two of the RNF4 SIMs; (iii) the loss of three C-terminal SIMs of ICP0 was fully restored by four RNF4 SIMs and also partially rescued by two RNF4 SIMs; and (iv) a PML II mutant lacking both lysine SUMOylation and SIM was not recognized by ICP0 for degradation, but was localized to ND10 and mitigated the degradation of other ND10 components, leading to delayed viral production. Taken together, SUMO regulates ICP0 substrate recognition via multiple fine-tuned mechanisms in HSV-1 infection. IMPORTANCE HSV-1 ICP0 is a multifunctional immediate early protein key to effective replication in the HSV-1 lytic cycle and reactivation in the latent cycle. ICP0 transactivates gene expression by orchestrating an overall mitigation in host intrinsic/innate restrictions. How ICP0 coordinates its multiple active domains and its diverse protein-protein interactions is a key question in understanding the HSV-1 life cycle and pathogenesis. The present study focuses on delineating the regulatory effects of the SUMO-SIM interaction on ICP0 E3 ubiquitin ligase activity regarding PML II degradation. For the first time, we discovered the importance of multivalency in the PML II-ICP0 interaction network and report the involvement of different regulatory mechanisms in PML II recognition by ICP0 in HSV-1 infection.

Vision-aware target recognition toward autonomous robot by Kinect sensors

SIGNAL PROCESSING-IMAGE COMMUNICATION

Authors: Chang, Qiuxiang; Xiong, Zhenkai

Target recognition is a key module in modern human-computer interaction (HCI) and computer vision systems It is pervasively used in many domains like autonomous vehicles and robot, remote operation, and video surveillance. However, due to the complicated environment and object occlusion, target recognition is still a challenging task. In this paper, we propose a novel target recognition algorithm toward autonomous robot by leveraging the Kinect sensors. More specifically, we utilize the Kinect sensors to capture scenario image in real-time. Subsequently, we present an improved HSV-based image segmentation algorithm to decompose the captured image, where morphological operation is employed for foreground target extraction. Afterward, we leverage Spatial Pyramid (SP)-based scheme for visual feature extraction. Then, we adopt a new distance metric for target matching. Comprehensive experimental results have shown the effectiveness of our proposed method.

Online Inquiry

Name:
Phone: *
E-mail Address: *
Technology Interest:
Type of Organization:
Service & Products Interested: *
Project Description:
Verification code
Click image to refresh the verification code.

Online Inquiry

  Interested in larger quantities ? request a quote!
  Protocol may be improved. Please feel free to contact us to obtain the latest version.!

Ordering Information

Payment methods we support:
Invoice / Purchase Order
Credit card

OUR PROMISE TO YOU Guaranteed product quality expert customer support

Inquiry Basket