Recombinant Mouse CLECSF6 Protein (Tagged)

Name: Recombinant Mouse CLECSF6 Protein (Tagged)
Brand: Beta LifeScience
SKU: BLA-1232P
Availability: InStock

Collections: Colony-stimulating factors and receptors (csfs), Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Host Species	Mouse
Accession	Q9QZ15
Synonym	C type (calcium dependent carbohydrate recognition domain) lectin superfamily member 6 C type lectin C type lectin DDB27 C type lectin superfamily 6 C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamily member 6 C-type lectin superfamily member 6 C-type lectin DDB27 C-type lectin domain family 4 member A C-type lectin domain family 4, member A C-type lectin domain family 4, member a2 C-type lectin superfamily member 6 CLC4A_HUMAN Clec4a Clec4a2 CLECSF6 DCIR Dcir1 DDB27 Dendritic cell immunoreceptor HDCGC13P Lectin like immunoreceptor Lectin, C-type, superfamily member 6 Lectin-like immunoreceptor LLIR
Description	Recombinant Mouse CLECSF6 Protein (Tagged) was expressed in E.coli. It is a Protein fragment
Source	E.coli
AA Sequence	QKYSQLLEEKKAAKNIMHNELNCTKSVSPMEDKVWSCCPKDWRLFGSHCY LVPTVSSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGILDTHAAYFIG LWDTGHRQWQWVDQTPYEESITFWHNGEPSSGNEKCATIIYRWKTGWGWN DISCSLKQKSVCQMKKINL
Molecular Weight	40 kDa including tags
Purity	>90% SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	May be involved in regulating immune reactivity. May play a role in modulating dendritic cells (DC) differentiation and/or maturation. May be involved in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation.; C-type lectin receptor that binds carbohydrates mannose and fucose but also weakly interacts with N-acetylglucosamine (GlcNAc) in a Ca(2+)-dependent manner. Involved in regulating immune reactivity. Once triggered by antigen, it is internalized by clathrin-dependent endocytosis and delivers its antigenic cargo into the antigen presentation pathway resulting in cross-priming of CD8(+) T cells. This cross-presentation and cross-priming are enhanced by TLR7 and TLR8 agonists with increased expansion of the CD8(+) T cells, high production of IFNG and TNF with reduced levels of IL4, IL5 and IL13. In plasmacytoid dendritic cells, inhibits TLR9-mediated IFNA and TNF production. May be involved via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation.
Subcellular Location	Cell membrane; Single-pass type II membrane protein; Extracellular side.
Database References	KEGG: mmu:26888 UniGene: Mm.47384
Tissue Specificity	Expressed in splenic antigen-presenting cells including B-cells, monocytes/macrophages, and dendritic cells (at protein level). Expressed in spleen and lymph node and slightly increased with dendritic cell maturation.

Gene Functions References

DCIR modulates immunity to M. tuberculosis through sustaining type I IFN signaling in DCs, which reduces IL-12-p70 production and Th1 expansion. As a consequence, DCIR-deficient mice control M. tuberculosis infection better than their WT counterparts but also develop more immunopathology in the lungs. PMID: 28069953
this study shows that upon injection of d-galactosamine and lipopolysaccharide, Dcir1-/- mice show decreased mortality rates and serum levels of alanine aminotransferase PMID: 28127756
Dcir1 enhances the pathogenesis of DSS colitis by altering neutrophil recruitment and their functions. PMID: 26497661
While DCIR1 was ubiquitously expressed on myeloid cells in various immune organs, significant expression of DCAR2 was detected only on subpopulations of conventional dendritic cells from bone marrow and skin-draining lymph nodes. PMID: 26431873
MCL-/- as well as DCIR-/- mice exhibited only a slightly increased severity of disease compared to wild-type mice indicating a limited role for MCL and DCIR in the regulation of intestinal immunity. PMID: 25068517
our findings show that DCIR plays an important role in maintaining bone homeostasis. PMID: 25926676
DCIR is a novel receptor for IVIg, mediating interaction of innate and adaptive immunity in tolerogenic responses. PMID: 24210883
This study indicates that DCIR is critically involved in Cerebral malaria induction PMID: 23918990
These results suggest that DCIR plays a protective role in limiting the Chikungunya virus-induced inflammatory response and subsequent tissue and joint damage. PMID: 23487448
These observations indicate that Dcir is a negative regulator of dendritic cell expansion and has a crucial role in maintaining the homeostasis of the immune system. PMID: 18204462

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.