Recombinant Human CLEC10A Protein (Fc Tag)

Name: Recombinant Human CLEC10A Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-1295
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	Fc
Host Species	Human
Accession	Q8IUN9
Synonym	CD301, CLECSF13, CLECSF14, HML, HML2, MGL
Background	CLEC1A, also known as the macrophage galactose-type calcium-type lectins (MGLs; CD31) constitute a unique class of C-type lectins because of their specificity for galactose and its structural homologues. MGLs/CD31 is a type II transmembrane glycoproteins and is expressed on macrophages and related cells of myeloid origins, particularly immature dendritic cells (DCs). There are 2 homologues: MGL1 and MGL2 (CD31a and CD31b) in mice. MGL1/CD31a induces both the production and secretion of interleukin (IL)-1. MGL1/CD31a plays a protective role against colitis by effectively inducing IL-1 production by colonic lamina propria macrophages in response to invading commensal bacteria.
Description	A DNA sequence encoding the human CLEC10A (Q8IUN9-2) (Gln61-His292) was expressed, with the fused Fc region of human IgG1 at the N-terminus.
Source	HEK293
Predicted N Terminal	Glu
AA Sequence	Gln61-His292
Molecular Weight	The recombinant human CLEC10A/Fc is a disulfide-linked homodimer. The reduced monomer comprises 492 a.a. and has a predicted molecular mass of 54.6 kDa. The apparent molecular mass of the protein is approximately 58 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity	>85% 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.