
- Species ReactivityHuman
- SpecificityDetects human Coagulation Factor II/Thrombin in direct ELISAs and Western blots. In direct ELISAs, approximately 10% cross-reactivity with recombinant human (rh) PROC is observed, and less than 1% cross-reactivity with rhFactor X, recombinant mouse (rm) Factor X and rmPROC is observed.
- SourcePolyclonal Goat IgG
- PurificationAntigen Affinity-purified
- ImmunogenMouse myeloma cell line NS0-derived recombinant human Coagulation Factor II/Thrombin
- FormulationLyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
- LabelUnconjugated
- Western Blot0.1 µg/mLHuman Coagulation Factor II/Thrombin (Catalog # 2196-SE)
- Simple Western10 µg/mLSee below
- Flow Cytometry2.5 µg/106 cellsSee below
- CyTOF-readyReady to be labeled using established conjugation methods. No BSA or other carrier proteins that could interfere with conjugation.
- ReconstitutionReconstitute at 0.2 mg/mL in sterile PBS.
- ShippingThe product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
- Stability & StorageUse 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.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
- Entrez Gene IDs:2147 (Human)
- Alternate Names:coagulation factor II (thrombin) receptor-like 2; Coagulation factor II receptor-like 2 (protease-actovated receptor 3); Coagulation factor II receptor-like 2; Coagulation Factor II; F2; PAR-3; PAR3proteinase-activated receptor 3; protease-activated receptor 3; proteinase-activated receptor-3; PT; serine protease; Thrombin receptor-like 2; Thrombin
Background:
Coagulation Factor II, commonly known as thrombin, is an essential component of the coagulation cascade in which it converts fibrinogen to fibrin, activates factors V, VII, VIII, XIII and forms complexes with protein C and thrombomodulin (1). It also activates platelets and regulates the behavior of additional cells through protease‑activated receptors (PARs) (2). It may have either protective or deleterious functions, depending on the level and location (3). Its activity is regulated by endogenous inhibitors such as anti-thrombin III (serpin C1) or heparin cofactor II (serpin D1). A plasma serine protease, thrombin is synthesized in the liver as a 622 amino acid precursor with a 24 amino acid signal peptide. Cleavage by itself or by similar enzymes converts the proenzyme to three forms designated asalpha -,beta - andgamma -thrombin. Composed of a disulfide bond-linked dimer of the light chain (A) (residues 328‑363) and the heavy chain (B) (residues 364‑622),alpha -thrombin displays the diverse functions as described above. In comparison, the further processed B chains ofbeta - andgamma -thrombin have no known physiological function, but retain most of the activity towards small synthetic substrates (4).
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