Recombinant Human CLEC17A Fc Chimera Protein, CF

Catalog #: 10147-CL Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
10147-CL-050

Recombinant Human CLEC17A Fc Chimera Protein Bioactivity

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

Recombinant Human CLEC17A Fc Chimera Protein, CF Summary

Product Specifications

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

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

Activity

Measured by the ability of the immobilized protein to support the adhesion of the MCF‑7 human breast cancer cells. The ED₅₀ for this effect is 1.5-9 μg/mL.

Source

Chinese Hamster Ovary cell line, CHO-derived human CLEC17A protein

MD	Human IgG₁ (Pro100-Lys330)	IEGR	Mouse CLEC17A (Lys194-Cys378) Accession # Q6ZS10-1
N-terminus			C-terminus

Accession #

Q6ZS10-1

N-terminal Sequence
Analysis

Met

Structure / Form

Disulfide-linked homodimer

Predicted Molecular Mass

48 kDa

SDS-PAGE

54-66 kDa, under reducing conditions

Product Datasheets

10147-CL

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.

10147-CL

Formulation	Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution	Reconstitute at 500 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.

Scientific Data

Bioactivity

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Immobilized Recombinant Human CLEC17A Fc Chimera (Catalog # 10147-CL) supports the adhesion of the MCF‑7 human breast cancer cells. The ED₅₀ for this effect is 1.5-9 μg/mL.

SDS-PAGE

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2 μg/lane of Recombinant Human CLEC17A Fc Chimera (Catalog # 10147-CL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 54-66 kDa and 110-130 kDa, respectively.

Reconstitution Calculator

Background: CLEC17A

C-type lectin domain family 17, member A (CLEC17A), also known as Prolectin, is type II transmembrane protein that is expressed mainly on dividing B cells found in the germinal centers of secondary lymphoid organs, including lymph nodes, tonsils, stomach, intestine, appendix and spleen (1, 2). CLEC17A binds preferentially to epithelial rather than to mesenchymal cells, and it behaves as a cell adhesion molecule for epithelial cells (2). It has high specificity towards mannose and was found to form disulfide-linked oligomers (1, 3). Human CLEC17A is synthesized as a 378 amino acid (aa) protein that includes a 172 aa cytoplasmic domain, a 21 aa transmembrane segment, and a 185 aa extracellular domain (ECD). Within the ECD, human CLEC17A shares 84% aa sequence identity with canine CLEC17A. C-type lectins are Ca²⁺-depending sugar-binding proteins that are involved in several immune-related and other physiological functions. Presently, 17 groups within the C-type lectin superfamily have been recognized (4), with more C-type lectins being constantly discovered based on the presence of a conserved 115-130 amino acid domain along their sequences - the C-type carbohydrate recognition domain (CRD). However, for most of the recently identified C-type lectins, their interactions with carbohydrates, intracellular functions and molecular mechanisms still remain unclear (3).

References