Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | NP_001994.2 |
express system | HEK293 |
product tag | C-His |
purity | > 95% as determined by Tris-Bis PAGE |
background | The ficolins are members of a recently discovered family of host innate opsonins that can activate the lectin pathway of complement. The ficolins bind many ligands, although they are typically described as binding acetylated sugars. Ficolin-1 is the least-described of the Ficolins and is expressed by monocytes, granulocytes, and in the lungs. Ficolin-1 is found circulating at low concentrations in serum but is regarded primarily as a secretory molecule that exerts its function locally in inflamed tissues. |
molecular weight | The protein has a predicted MW of 33.11 kDa. Due to glycosylation, the protein migrates to 34-38 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human ficolin 1/FCN1 Protein 2322
$270.00 – $900.00
Summary
- Expression: HEK293
- Pure: Yes (SDS-PAGE)
- Amino Acid Range: Ala30-Ala326
Human ficolin 1/FCN1 Protein 2322
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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The ficolins are members of a recently discovered family of host innate opsonins that can activate the lectin pathway of complement. The ficolins bind many ligands, although they are typically described as binding acetylated sugars. Ficolin-1 is the least-described of the Ficolins and is expressed by monocytes, granulocytes, and in the lungs. Ficolin-1 is found circulating at low concentrations in serum but is regarded primarily as a secretory molecule that exerts its function locally in inflamed tissues. |
Protein names Ficolin-1 (Collagen/fibrinogen domain-containing protein 1) (Ficolin-A) (Ficolin-alpha) (M-ficolin) |
Protein family Ficolin lectin family |
Mass 35078Da |
Function Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8 (PubMed:21037097). Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage. {ECO:0000269|PubMed:20032467, ECO:0000269|PubMed:21037097}. |
Subellular location Secreted {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}. Cell membrane {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}; Peripheral membrane protein {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}; Extracellular side {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}. Note=Found on the monocyte and granulocyte surface (PubMed:20400674). |
Tissues Peripheral blood leukocytes, monocytes and granulocytes. Also detected in spleen, lung, and thymus, may be due to the presence of tissue macrophages or trapped blood in these tissues. Not detected on lymphocytes. {ECO:0000269|PubMed:20400674}. |
Structure Homotrimer (PubMed:17897951). Interacts with elastin/ELN. Interacts (via Fibrinogen C-terminal domain) with FFAR2. Interacts with CRP; may regulate monocyte activation by FCN1. {ECO:0000269|PubMed:17148457, ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467, ECO:0000269|PubMed:21037097}. |
Domain The fibrinogen C-terminal domain mediates calcium-dependent binding to carbohydrates and tet |
Target Relevance information above includes information from UniProt accession: O00602 |
The UniProt Consortium |
Publications
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