Human CLEC5A peptide

Name: Human CLEC5A peptide
SKU: DAG-P0277
Rating: 5 (1 reviews)

Synthetic Human CLEC5A peptide

COA

SDS

Datasheet

Summary

Specificity

Expressed in peripheral blood monocytes and in the monocyte/macrophage cell lines U-937 and Mono-Mac-6, but not in cell lines of other origins. Expression is down-regulated when monocytes differentiate into dendritic cells.

Nature

Synthetic

Tag/Conjugate

Unconjugated

SequenceSimilarities

Contains 1 C-type lectin domain.

Purity

70 - 90% by HPLC.

Format

Liquid

Preservative

None

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.

Entrez Gene ID

23601

Antigen Description

This gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of this family share a common protein fold and have diverse functions, such as cell adhesion, cell-cell signalling, glycoprotein turnover, and roles in inflammation and immune response. The encoded type II transmembrane protein interacts with dnax-activation protein 12 and may play a role in cell activation. Alternative splice variants have been described but their full-length sequence has not been determined. [provided by RefSeq, Jul 2008]

Function

carbohydrate binding; virus receptor activity;

Synonyms

CLEC5A; C-type lectin domain family 5, member A; MDL1; MDL-1; CLECSF5; C-type lectin domain family 5 member A; C-type lectin superfamily member 5; myeloid DAP12-associating lectin 1; myeloid DAP12-associating lectin-1; C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamily member 5;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Viral resistance of MOGS-CDG patients implies a broad-spectrum strategy against acute virus infections

ANTIVIRAL THERAPY

Authors: Chang, Jinhong; Block, Timothy M.; Guo, Ju-Tao

Abstract

Sadat et al. reported in the 24 April 2014 issue of the New England Journal of Medicine that patients genetically deficient in the gene encoding mannosyl-oligosaccharide glucosidase (MOGS), also known as endoplasmic reticulum (ER) glucosidase I, manifested a severe hypogammaglobulinaemia without clinical evidence of an infectious diathesis. This paradox phenomenon is, at least in part, because the impaired N-linked glycan processing of the patients compromises their ability to support efficient replication and cellular entry of viruses. This finding unambiguously validates ER glucosidases as valuable targets for antiviral agents against a broad-spectrum of enveloped viruses.

Dengue tropism for macrophages and dendritic cells: the host cell effect

JOURNAL OF GENERAL VIROLOGY

Authors: Flipse, Jacky; Torres, Silvia; Diosa-Toro, Mayra; van der Ende-Metselaar, Heidi; Herrera-Rodriguez, Jose; Urcuqui-Inchima, Silvio; Huckriede, Anke; Rodenhuis-Zybert, Izabela A.; Smit, Jolanda M.

Abstract

Dengue virus infects immune cells, including monocytes, macrophages and dendritic cells (DC). We compared virus infectivity in macrophages and DC, and found that the virus origin determined the cell tropism of progeny virus. The highest efficiency of re-infection was seen for macrophage-derived dengue virus. Furthermore, in the presence of enhancing antibodies, macrophage-derived virus gave greater enhancement of infection compared with immature DC derived virus. Taken together, our results highlight the importance of macrophages in dengue infection.