Recombinant Mouse Dectin-1 Protein (His Tag)

Name: Recombinant Mouse Dectin-1 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1590
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Mouse
Accession	NP_064392.2
Synonym	beta-GR, BGR, Clecsf12
Background	Dectin-1 was recently identified as the most important receptor for beta-glucan. It is a type II transmembrane protein which binds beta-1,3 and beta-1,6 glucans, and is expressed on most cells of the innate immune system and has been implicated in phagocytosis as well as killing of fungi by macrophages, neutrophils and dendritic cells. Recognition of beta-glucan by dectin-1 triggers effective immune response, including phagocytosis and proinflammatory factor production, to eliminate infecting fungi, which especially benefits immunocompromised patients against opportunistic fungal infection. In addition, dectin-1 is involved in the adaptive immune response as well as autoimmune diseases and immune tolerance. Dectin-1 can recognize and respond to live fungal pathogens and is being increasingly appreciated as having a key role in the innate responses to these pathogens. In addition to its exogenous ligands, Dectin-1 can recognize an unidentified endogenous ligand on T cells and may act as a co-stimulatory molecule. Recent studies have highlighted the importance of Dectin-1 in anti-fungal immunity, in both mice and humans, and have suggested a possible involvement of this receptor in the control of mycobacterial infections.
Description	A DNA sequence encoding the extracellular domain (Phe 69-Leu 244) of mouse CLEC7A (NP_064392.2) was fused with a His tag at the N-terminus.
Source	HEK293
Predicted N Terminal	His
AA Sequence	Phe 69-Leu 244
Molecular Weight	The secreted recombinant mouse CLEC7A consists of 193 a.a. and has a calculated molecular mass of 22.5 kDa. As a result of glycosylation, the apparent molecular mass of the recombinant protein is approximately 30-37 kDa in SDS-PAGE under reducing conditions.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Both PKD1 and PKD2 are required for channel activity. Involved in renal tubulogenesis. Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Acts as a regulator of cilium length, together with PKD2. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate interactions.
Subcellular Location	Cell membrane; Multi-pass membrane protein. Cell projection, cilium. Endoplasmic reticulum. Golgi apparatus.
Protein Families	Polycystin family
Database References	HGNC: 9008 OMIM: 173900 KEGG: hsa:5310 STRING: 9606.ENSP00000262304 UniGene: Hs.75813
Associated Diseases	Polycystic kidney disease 1 (PKD1)

Gene Functions References

Two novel mutations, c.6953_6977del and c.10937T>G (p.Val3646Gly) of the PKD1 gene are associated with the polycystic kidney disease. PMID: 29896735
this study reports the 3.6-angstrom cryo-electron microscopy structure of truncated human PKD1-PKD2 complex assembled in a 1:3 ratio. PMID: 30093605
VEGF/PKD-1 signaling axis increases angiogenic and arteriogenic gene expression. These studies suggest that the axis may regulate arteriolar differentiation through changing microvascular endothelial cells gene expression. PMID: 29380239
The novel frameshift mutations reported by this study are p. Q1997X, P. D73X and p. V336X. PMID: 29590654
newly identified sites for known mutations will facilitate the early diagnosis and prediction of prognosis in patients with ADPKD PMID: 29529603
PKD1 cytoplasmic C-terminal tail domain has a crucial role in renal prognosis in autosomal dominant polycystic disease. PMID: 28983800
PKD 1 mutation is associated with Autosomal dominant polycystic kidney disease. PMID: 28825164
Our results show that we have successfully generated a patient-specific iPS cell line with a mutation in PKD1 for study of renal disease pathophysiology. PMID: 29034881
These data reveal a novel function for PKD1 as a regulator of focal adhesion dynamics and by identifying PIP5Klgamma as a novel PKD1 substrate provide mechanistic insight into this process. PMID: 27775029
the PKD1/PKD2 mutation status differed by ethnicity, and the PKD1/PKD2 genotype may affect the clinical phenotype of autosomal dominant polycystic kidney disease PMID: 27782177
The novel pathogenic variants c.3607C> T and c.11354G> C in PKD1 is very interesting since they may represent Italian clusters. PMID: 27499327
SNX3-retromer complex regulates the surface expression and function of PC1 and PC2 PMID: 28620080
Study identified a novel heterozygous frameshift mutation in PKD1 gene segregating between affected and unaffected individuals suggesting an involvement in polycystic kidney disease (PKD). PMID: 28870863
we report for the first time that PKD1 was tightly regulated by androgen at the transcriptional level in prostate cancer cells and was a novel androgen-repressed gene. Further analysis identified FRS2 as a novel mediator of androgen-induced PKD1 repression. PMID: 28077787
novel frameshift mutation c.3903delC, p.A1302Pfs identified to be responsible for renal disease PMID: 28827396
Hyperactivation of the ERK pathway may be caused by down-regulation of PC-1 and PC-2 in lymphatic malformations, contributing to increased proliferation of lymphatic endothelial cells. PMID: 28552828
A novel mutation of the PKD1 gene has been identified with autosomal dominant polycystic kidney disease in an affected Chinese family. PMID: 28604956
Annualized median liver growth rates were 1.68, 1.5 and 1.24% for PKD1-T, PKD1-NT and PKD2 mutations, respectively (P = 0.49), and remained unaffected by the ADPKD genotype when adjusted for age, gender and baseline HtLV. PMID: 26932689
this study shows that diet-induced obesity links to estrogen receptor-positive breast cancer progression via LPA/PKD-1-CD36 signaling-mediated microvascular remodeling PMID: 28186980
Isolated polycystic liver disease genes define effectors of polycystin-1 function PMID: 28375157
mechanical load upregulates expression of Runx2 gene via potentiation of PC1-JAK2/STAT3 signaling axis, culminating to possibly control osteoblastic differentiation and ultimately bone formation. PMID: 27699453
Gly972Arg of PC-1 polymorphisms are associated with polycystic ovary syndrome. PMID: 27785750
cortactin binds to E-cadherin, and that a posttranslational modification of cortactin, RhoA-induced phosphorylation by protein kinase D1 (PKD1; also known as PRKD1) at S298, impairs adherens junction assembly and supports their dissolution. PMID: 27179075
Ten novel mutations in PKD1 gene were identified in 15 Chinese families with polycystic kidney disease. PMID: 28578020
The novel PKD1 c.8791+1_8791+5delGTGCG mutation has created a new splice site. PMID: 27984604
Data show that in 82 (87.2%) of the patients, pathogenic mutations were detected in PKD1 (79.0%-92.5%), whereas in 12 (12.8%) patients pathogenic mutations were detected in PKD2 (7.5%-21.0%). PMID: 27835667
our study reveals possible mechanisms of CFB upregulation in autosomal dominant polycystic kidney disease, and a novel role of PC1-C terminal tail in ADPKD-associated inflammation. PMID: 26984954
PKD1 mutation is associated with familial testicular germ cell tumor and autosomal dominant polycystic kidney disease. PMID: 27577987
we have quantified the contribution of genic and PKD1 allelic effects and sex to the Autosomal dominant polycystic kidney disease phenotype. Intrafamilial correlation analysis showed that other factors shared by families influence height-adjusted total kidney volume, with these additional genetic/environmental factors significantly affecting the Autosomal dominant polycystic kidney disease phenotype PMID: 26823553
The epithelial cell membrane protein E-cadherin physically binds to PKD1 which leads to a subcellular redistribution of PKD1. PMID: 26991955
PKD1 and PKD2 are susceptibility genes for familial intracranial aneurysms in a Japanese population. PMID: 27567292
These results suggest that the Ser at the 4166 site in PC1 is crucial in the PC1 mediated MEK/ERK/myc signaling pathway, which might be the key pathophysiological cause of Aortic dissection. PMID: 28076932
Novel PKD1 mutations in Chinese autosomal dominant polycystic kidney disease patients PMID: 26632257
The pathogenic mutation in PKD1 linked pedigree was c.8522G>A (p.E2771K) in exon 23. This C to T transition occurs at the CpG dinucleotides which is the known hotspot point for mutations. PMID: 26950445
Germline mutations in PKD1 gene is associated with autosomal-dominant polycystic kidney disease. PMID: 23300259
Host cortactin, PKD1 and actin are recruited by Trypanosoma cruzi extracellular amastigotes based on experiments in fixed and live cells by time lapse confocal microscopy. PMID: 26096820
PCs expression and p53 activation as a regulator of cell proliferation were further evaluated in vivo and in 69 advanced human carotid atherosclerotic plaques. PMID: 26286632
These results suggest that, at least in some patients, the severity of the cystic disease is inversely correlated with the level of polycystin 1 function. PMID: 26139440
Overexpression of PKD1 in a prostate cancer cell line model resulted in decreased cell proliferation and epithelial mesenchymal transition. PMID: 26764245
and MMP9 expression in PKD1 constitutively-active MD-MB-231 cells and MCF-7 knockdown cells were decreased and increased respectively PMID: 26775353
A substantial number of PKD1 missense or synonymous mutations characterize pre-mRNA splicing. One missense and 2 synonymous mutations induce significant defects in pre-mRNA splicing. PMID: 25757501
PKD1 gene variation plays a disease modifying role in patients diagnosed with ADPKD. PMID: 25880449
A short segment of chromosome 16 encodes the tumor suppressor gene tuberin as well as the protein polycystin 1 which are responsible for tuberous sclerosis complex type 2 and autosomal-dominant polycystic kidney disease type 1, respectively. PMID: 25355409
Case Report: polycystic kidney disease with steatocystoma multiplex. PKD1 mutations disrupt keratin 17 polymerization. PMID: 25111597
mutations within PKD1 and PKD2 can be linked to most of the cases of Japanese ADPKD, and the renal function decline was faster in patients with PKD1 mutations than in those with PKD2 mutations PMID: 24611717
PKD1 knockdown was found to be an efficient strategy to overcome resistance caused by LMP1 expression. Therefore, PKD1 could be a molecular target for therapeutic intervention in EBV-associated B cell lymphoma treatment. PMID: 24707946
Report novel nonsense mutation in exon 15 of PKD1 in polycystic liver disease. PMID: 25741140
Four novel PKD1 variants were identified in this study in autosomal-dominant polycystic kidney disease using long-range PCR followed by nested PCR PMID: 25531466
Data indicate that serine/threonine-protein kinase D1 (PKD1) stimulates estrogen receptor alpha (ERalpha) expression in breast cancer MCF-7 cells. PMID: 25287328
Both polycystins were detected on the spindle and mid-body of mitotic cells, while fibrocystin was on centrosome throughout cell cycle. PMID: 25367197

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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.

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