Recombinant Human Siglec-5 Fc Chimera Protein, CF

Name: Recombinant Human Siglec-5 Fc Chimera Protein, CF
Brand: R&D Systems
SKU: 1072-SL

R&D Systems, Inc. a Bio-Techne Brand

Catalog # 1072-SL

Citations (7)

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Key Product Details

Source:	NS0
Accession #:	O15389
Structure / Form:	Disulfide-linked homodimer
Applications:	Bioactivity

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Product Specifications for Recombinant Human Siglec-5 Fc Chimera Protein, CF

Source

Mouse myeloma cell line, NS0-derived human Siglec-5/CD170 protein

Human Siglec-5 (Glu17-Thr434) Accession # O15389	IEGRID	Human IgG₁ (Pro100-Lys330)
N-terminus		C-terminus

Purity

>90%, 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.

N-terminal sequence Analysis

Glu17

Predicted Molecular Mass

73 kDa (monomer)

SDS-PAGE

100-110 kDa, reducing conditions

Activity

Measured by the ability of the immobilized protein to support the adhesion of human red blood cells. Kelm, S. et al. (1994) Current Biology 4:965. The ED₅₀ for this effect is 1‑4 µg/mL.

Formulation, Preparation and Storage

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.

1072-SL

Formulation	Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution	Reconstitute at 100 μg/mL in sterile PBS. Reconstitution Buffer Available: Size / Price Qty Loading... RB01:
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.

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Background: Siglec-5/CD170

Siglecs (1) (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins (2) belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding (3), followed by varying numbers of Ig-like C2-type domains (1, 4). Eleven human Siglecs have been cloned and characterized (1, 4). They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and the Siglec-5 to 11 (4, 5, 7). To date, no Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Siglec-5 to 11 share a high degree of sequence similarity with CD33/Siglec-3 both in their extracellular and intracellular regions. They are collectively referred to as CD33-related Siglecs. One remarkable feature of the CD33-related Siglecs is their differential expression pattern within the hematopoietic system (4, 5). This fact, together with the presence of two conserved immunoreceptor tyrosine-based inhibition motifs (ITIMs) in their cytoplasma tails, suggests that CD33-related Siglecs are involved in the regulation of cellular activation within the immune system.

Human Siglec-5 cDNA encodes a 551 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, three Ig-like C2-type domains, a transmembrane region and a cytoplasma tail (6). Siglec-5 exists as a disulfide-linked homodimer on the cell surface and is expressed on monocytes, neutrophils and B cells (4, 5, 6). It binds equally well to both alpha 2,3- and alpha 2,6-linked sialic acid (6).

Item	Value
References	Crocker, P.R. et al. (1998) Glycobiology 8:v. Powell, L.D. et al. (1995) J. Biol. Chem. 270:14243. May, A.R. et al. (1998) Mol. Cell 1998. 1:719. Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337. Crocker, P.R. et al. (2001) Immunology 103:137. Cornish, A.L. et al. (1998) Blood 92:2123. Angata, T. et al. (2002) J. Biol Chem. 277:24466.
Long Name	Sialic Acid Binding Ig-like Lectin 5
Entrez Gene IDs	8778 (Human)
Alternate Names	CD170, CD170 antigen, CD33 antigen-like 2, CD33L2, CD33L2OB binding protein-2, OB-BP2OB-binding protein 2, OBBP2, OBBP2sialic acid-binding Ig-like lectin 5, Obesity-binding protein 2, Siglec-5, Siglec5, sialic acid binding Ig-like lectin 5, sialic acid-binding immunoglobulin-like lectin 5

Citations for Recombinant Human Siglec-5 Fc Chimera Protein, CF (7)

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Citations are publications that use Bio-Techne products. Selected citations for Recombinant Human Siglec-5 Fc Chimera Protein, CF include:

Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay

E Michaud et al. (2022), Alteration of microbiota antibody-mediated immune selection contributes to dysbiosis in inflammatory bowel diseases Embo Molecular Medicine, 0(0):e15386.
PMID: 35785473
Species: Human
Sample Types: Natural Protein
Applications: Bioassay

J Terävä et al. (2019), Lectin nanoparticle assays for detecting breast cancer-associated glycovariants of cancer antigen 15-3 (CA15-3) in human plasma PLoS ONE, 14(7):e0219480.
PMID: 31344060
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

(2016), Soluble Siglec-5 associates to PSGL-1 and displays anti-inflammatory activity Sci Rep, 6(0):37953.
PMID: 27892504
Species: Human
Sample Types: Cell Lysates
Applications: Bioassay

Chen et al. (2014), Broad and direct interaction between TLR and Siglec families of pattern recognition receptors and its regulation by Neu1. Elife, 3(0):e04066.
PMID: 25187624
Species: Virus
Sample Types: Virus
Applications: Surface Plasmon Resonance

Zou Z et al. (2011), Siglecs facilitate HIV-1 infection of macrophages through adhesion with viral sialic acids. PLoS ONE, 6(9):e24559.
PMID: 21931755
Species: Bacteria
Sample Types: Protein
Applications: Surface Plasmon Resonance

Nordstrom T et al. (2011), Human Siglec-5 inhibitory receptor and immunoglobulin A (IgA) have separate binding sites in streptococcal beta protein. J. Biol. Chem., 286(39):33981-91.
PMID: 21795693
Species: Human
Sample Types: Carbohydrates
Applications: Surface Plasmon Resonance

Zhuravleva MA et al. (2007), Structural implications of Siglec-5-mediated sialoglycan recognition. J. Mol. Biol., 375(2):437-47.
PMID: 18022638

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Showing 1 - 7 of 7 citations Showing All

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