Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | XP_005556540.2 |
express system | HEK293 |
product tag | C-His |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Factor XI (FXI) is the zymogen of a plasma protease (FXIa) that contributes to hemostasis by activating factor IX (FIX). In the original cascade model of coagulation, FXI is converted to FXIa by factor XIIa (FXIIa), a component, along with prekallikrein and high-molecular-weight kininogen (HK), of the plasma kallikrein-kinin system (KKS). |
molecular weight | The protein has a predicted MW of 69.05 kDa. Due to glycosylation, the protein migrates to 70-85 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Cynomolgus Coagulation factor XI Protein 2586
$1,050.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Glu44-Ala650
Cynomolgus Coagulation factor XI Protein 2586
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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Factor XI (FXI) is the zymogen of a plasma protease (FXIa) that contributes to hemostasis by activating factor IX (FIX). In the original cascade model of coagulation, FXI is converted to FXIa by factor XIIa (FXIIa), a component, along with prekallikrein and high-molecular-weight kininogen (HK), of the plasma kallikrein-kinin system (KKS). |
Protein names Coagulation factor XI (FXI) (EC 3.4.21.27) (Plasma thromboplastin antecedent) (PTA) [Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain] |
Protein family Peptidase S1 family, Plasma kallikrein subfamily |
Mass 70109Da |
Function Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. |
Catalytic activity CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.; EC=3.4.21.27; |
Subellular location Secreted. |
Tissues Isoform 2 is produced by platelets and megakaryocytes but absent from other blood cells. |
Structure Homodimer; disulfide-linked. Forms a heterodimer with SERPINA5. After activation the heavy and light chains are also linked by a disulfide bond. Interacts with Anopheles gambiae D7L2 (PubMed:35460690). {ECO:0000269|PubMed:18510371, ECO:0000269|PubMed:1998667, ECO:0000269|PubMed:35460690}. |
Post-translational modification N-glycosylated on both chains. N-glycosylated sites mainly consist of nonfucosylated sialylated biantennary (in high abundance) and/or triantennary (in low abundance) complex structures. Glycosylation at Asn-163 uses a rare non-canonical Asn-X-Cys glycosite. {ECO:0000269|PubMed:25092234}.; Activated by factor XIIa (or XII), which cleaves each polypeptide after Arg-387 into the light chain, which contains the active site, and the heavy chain, which associates with high molecular weight (HMW) kininogen. |
Target Relevance information above includes information from UniProt accession: P03951 |
The UniProt Consortium |
Data
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