Recombinant Human DC-SIGN Protein (Fc Tag)

Name: Recombinant Human DC-SIGN Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-1558
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	Fc
Host Species	Human
Accession	NP_066978.1
Synonym	CD209, CDSIGN, CLEC4L, DC-SIGN, DC-SIGN1, MGC129965
Background	Dendritic cell (DC)-specific intercellular adhesion molecule 3 (ICAM-3) grabbing nonintegrin (DC-SIGN), also known as CD29, is a type II transmembrane protein on DCs with a C-type lectin extracellular domain, is capable of binding ICAM-3 on resting T cells in the secondary lymphoid organs, providing the initial contact between these cells during the establishment of cell-mediated immunity. It is not only a pattern recognition receptor but implicated in immunoregulation of DCs. It has important role in mediating DC adhesion, migration, inflammation, activating primary T cell, triggering immune response and participating in immune escape of pathogens and tumors. DC-SIGN also mediates capture and internalization of viral, bacterial, and fungal pathogens by dendritic cells, such as HIV-1, Ebola virus, cytomegalovirus, Dengue virus, and hepatitis C virus. DC-SIGN is unique in that it regulates adhesion processes, such as DC trafficking and T-cell synapse formation, as well as antigen capture. Moreover, even though several C-type lectins have been shown to bind HIV-1, DC-SIGN does not only capture HIV-1 but also protects it in early endosomes allowing HIV-1 transport by DC to lymphoid tissues, where it enhances trans infection of T cells.Immune CheckpointImmunotherapyCancer ImmunotherapyTargeted Therapy
Description	A DNA sequence encoding the N-terminally truncated extracellular domain (Lys 62-Ala 404) of human DC-SIGN (NP_066978.1) was expressed with the fused Fc region of human IgG1 at the N-terminus.
Source	HEK293
Predicted N Terminal	Glu 20
AA Sequence	Lys 62-Ala 404
Molecular Weight	The recombinant human Fc/DC-SIGN chimera is a disulfide-linked homodimeric protein. The reduced monomer consists of 580 a.a. and has a calculated molecular mass of 65.8 kDa. As a result of glycosylation, the apparent molecular mass of rh Fc/DC-SIGN is approximately 75 kDa in SDS-PAGE under reducing conditions.
Purity	>97% 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.

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.