CLEC7A blocking peptide

Name: CLEC7A blocking peptide
SKU: CDBP5170
Rating: 5 (1 reviews)

Synthetic CLEC7A blocking peptide for IB

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COA

SDS

Datasheet

Nature

Synthetic

Tag/Conjugate

Unconjugated

Format

Liquid

Concentration

200 μg/mL

Preservative

None

Storage

-20°C

Gene ID

8915

UniProt ID

O95999

Antigen Description

This gene was identified by its translocation in a case of mucosa-associated lymphoid tissue (MALT) lymphoma. The protein encoded by this gene contains a caspase recruitment domain (CARD), and has been shown to induce apoptosis and to activate NF-kappaB. This protein is reported to interact with other CARD domain containing proteins including CARD9, 10, 11 and 14, which are thought to function as upstream regulators in NF-kappaB signaling. This protein is found to form a complex with MALT1, a protein encoded by another gene known to be translocated in MALT lymphoma. MALT1 and this protein are thought to synergize in the activation of NF-kappaB, and the deregulation of either of them may contribute to the same pathogenetic process that leads to the malignancy. [provided by RefSeq, Jul 2008]

Function

NF-kappaB binding; enzyme binding; contributes_to kinase activator activity; kinase binding; protease binding; protein C-terminus binding; protein binding; protein kinase B binding; protein kinase binding; protein self-association; transcription coactivator activity; transcription factor binding; ubiquitin binding; ubiquitin protein ligase binding

Synonyms

BCL10; B-cell CLL/lymphoma 10; CLAP; mE10; CIPER; c-E10; CARMEN; B-cell lymphoma/leukemia 10; hCLAP; cCARMEN; cellular-E10; cellular homolog of vCARMEN; CARD-containing proapoptotic protein; CARD containing molecule enhancing NF-kB; CARD-containing apoptotic signaling protein; caspase-recruiting domain-containing protein; CARD-containing molecule enhancing NF-kappa-B; mammalian CARD-containing adapter molecule E10; CED-3/ICH-1 prodomain homologous E10-like regulator

Citations

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Customer Reviews

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beta-Glucans in food modify colonic microflora by inducing antimicrobial protein, calprotectin, in a Dectin-1-induced-IL-17F-dependent manner

MUCOSAL IMMUNOLOGY

Authors: Kamiya, T.; Tang, C.; Kadoki, M.; Oshima, K.; Hattori, M.; Saijo, S.; Adachi, Y.; Ohno, N.; Iwakura, Y.

Abstract

Dectin-1 (gene symbol: Clec7a) is a receptor for beta-glucans that play an important role for the host defense against fungi. Recently, we showed that Clec7a(-/-) mice are resistant against dextran sodium sulfate (DSS)-induced colitis because of regulatory T-cell population expansion in the colon. The regulatory T-cell expansion is caused by expansion of commensal Lactobacillus murinus whose growth is suppressed by an antimicrobial protein, calprotectin S100A8/A9. In this report, we showed that S100A8 was mainly produced by mouse colonic epithelial cells. S100A8 was not induced directly by Dectin-1 but by Dectin-1-induced cytokines, especially interleukin-17F (IL-17F), that were produced by several types of innate immune cells including CD11c(+)/CD11b(+) myeloid cells in colonic lamina propria. S100A8/A9 heterodimer preferentially suppressed the growth of L. murinus that was increased in both Clec7a(-/-) and II17f(-/-) mice. Furthermore, similar expansion of L. murinus and DSS-colitis resistance were observed in mice fed with beta-glucanfree food. These observations suggest that food-derived b-glucans control the specific commensal microbiota via the Dectin-1-IL-17F-calprotectin axis to maintain the intestinal homeostasis.

Polymorphisms of the immune-modulating receptor dectin-1 in pigs: their functional influence and distribution in pig populations

IMMUNOGENETICS

Authors: Shinkai, Hiroki; Toki, Daisuke; Okumura, Naohiko; Takenouchi, Takato; Kitani, Hiroshi; Uenishi, Hirohide

Abstract

Dectin-1, a C-type lectin receptor that recognizes fungal beta-glucans, is involved in antifungal immunity and the regulation of intestinal immune homeostasis. Dectin-1 is involved in both synthesis and maturation of interleukin-1 beta, a key pro-inflammatory cytokine in immunity. Here, we assessed the genetic diversity in the gene encoding dectin-1 (CLEC7A) within various pig populations and examined the influence of these polymorphisms on the two different signaling pathways after ligand recognition. An amino-acid polymorphism located in the carbohydrate-recognition domain, leucine to serine at position 138 (L138S), which occurred exclusively in Japanese wild boars at low frequency, significantly increased NF-kappa B induction but not caspase-8 activity after stimulation with zymosan. In contrast, other amino-acid polymorphisms present at comparatively high frequency in commercial pig populations had little influence on ligand recognition. These results suggest that functionally neutral polymorphisms in dectin-1 are widespread in pig populations.