Recombinant Human TLR10 Fc Chimera Protein, CF

Catalog #: 6619-TR Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
6619-TR-050

R&D Systems Recombinant Proteins and Enzymes

1 Image

Product Details

Supplemental Products

Reviews

Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human TLR10 Fc Chimera Protein, CF Summary

Product Specifications

Purity

>85%, by SDS-PAGE under reducing conditions and visualized by silver stain

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

Activity

Measured by its binding ability in a functional ELISA. When Recombinant Human TLR10 Fc Chimera is immobilized at 1 µg/mL (100 µL/well), the concentration of Recombinant Human TLR1 Fc Chimera (Catalog # 1484-TR) that produces 50% of the optimal binding response is approximately 0.5‑3 µg/mL.

Source

Chinese Hamster Ovary cell line, CHO-derived human TLR10 protein

Human TLR10 (Asp20-Thr576) Accession # Q9BXR5	IEGRMD	Human IgG₁ (Pro100-Lys330)
N-terminus		C-terminus

Accession #

Q9BXR5

N-terminal Sequence
Analysis

Asp20

Structure / Form

Disulfide-linked homodimer

Predicted Molecular Mass

91.2 kDa (monomer)

SDS-PAGE

115-135 kDa, reducing conditions

Product Datasheets

6619-TR

Product Datasheet

COA

SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

6619-TR

Formulation	Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution	Reconstitute at 100 μg/mL in PBS.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Reconstitution Calculator

Background: TLR10

TLR10 (Toll‑like receptor 10, designated CD290) is a 90‑100 kDa type I transmembrane glycoprotein that is a member of the TLR1 subfamily within the TLR family of pathogen-associated molecular pattern (PAMP) receptors (1‑3). Human TLR10 is synthesized as a precursor with a 19 amino acid (aa) signal sequence, an extracellular domain (ECD, aa 20‑576) with 15 or more leucine‑rich repeats (LRR), an LRRCT (LRR C‑terminal) domain and nine potential sites for N‑linked glycosylation, a transmembrane domain, and a cytoplasmic region (aa 598‑811) with a TIR (Toll/IL‑1 receptor) domain (1, 3). Human TLR10 shares 71%, 81%, 82% and 83% aa sequence identity with rat, bovine, porcine and canine TLR10, respectively. The mouse TLR10 gene is nonfunctional (2). TLR10 is expressed on B cells and cell lines, except for early pre‑B cells, and is more highly expressed on activated than resting cells (2, 4). It is also expressed on FOXP3⁺ regulatory T cells, placental trophoblasts, and CD1a⁺ and plasmacytoid dendritic cells (DC), but not on monocyte‑derived DC (2, 5, 6). Among PAMPs, TLR10 is thought to recognize triacylated bacterial lipoproteins (as demonstrated by recognition of the synthetic molecule Pam₃CSK₄), gram positive bacterial peptidoglycans, and other microbially-derived agonists shared with TLR1 (3, 6, 7). It is found as a homodimer or heterodimer with TLR1 or TLR2, associating through a region within the extracellular LRR repeats (2, 3, 7). It interacts directly with MYD88, leading to production of inflammatory cytokines (2, 7).

References