T9549
トロンビン ウシ血漿由来
powder, suitable for cell culture, ≥1,500 NIH units/mg protein (E1%/280 = 19.5)
別名:
第 IIa因子
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この商品について
CAS番号:
UNSPSC Code:
12352204
EC Number:
232-648-7
MDL number:
Specific activity:
≥1,500 NIH units/mg protein (E1%/280 = 19.5)
form
powder
specific activity
≥1,500 NIH units/mg protein (E1%/280 = 19.5)
mol wt
heavy chain ~31 kDa, light chain ~6 kDa
technique(s)
cell culture | mammalian: suitable
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
cow ... F2(280685)
General description
Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects.
Application
Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags. Thrombin has been used in a study to assess an expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization.
Biochem/physiol Actions
Arg-Glyを選択的に切断するセリンプロテア-ゼは、フィブリノ-ゲン内に結合し、フィブリンおよびfibrinopeptide A、Bを形成します。
Preparation Note
1 mLの水で復元すると、0.15 M塩化ナトリウム、0.05 Mクエン酸ナトリウム溶液(pH 6.5)中に標記の活性を有する溶液となります。
Analysis Note
NIHのアッセイでは、Biggs法の変法に基づいて、トロンビンサンプル(1%バッファ-アルブミン溶液で安定化)0.1 mLと、基質として希釈血漿(同量の生理食塩水で希釈)0.2 mLを用います。 凝固時間15~25秒の範囲でトロンビン濃度を決定します。
活性は、NIIHトロンビン標準品(ロットK)との直接比較によって得られたNIH単位で表しています。
Other Notes
より詳細な情報につきましては、www.sigma-aldrich.com/enzymeexplorerのthrombinをご覧ください。
Activity is expressed in NIH units, and is measured by direct comparison to an NIH thrombin reference standard.
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signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
保管分類
11 - Combustible Solids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
関連コンテンツ
Instructions
Andrew F Uehlin et al.
Pharmaceutics, 14(2) (2022-02-27)
In this study, we report a biohybrid oriented fibrous scaffold based on nanofibers of poly(l-lactic acid) (PLLA)/fibrin produced by electrospinning and subsequent post-treatment. Induced hydrolytic degradation of the fibers in 0.25 M NaOH solution for various time periods followed by
Zachary T Britton et al.
Protein expression and purification, 84(2), 224-235 (2012-06-23)
Biophysical and structural characterization of G protein-coupled receptors (GPCRs) has been limited due to difficulties in expression, purification, and vitro stability of the full-length receptors. "Divide and conquer" approaches aimed at the NMR characterization of peptides corresponding to specific regions
Yuya Nakatani et al.
Archives of oral biology, 73, 172-178 (2016-10-25)
Platelet-rich plasma (PRP) is typically isolated and applied immediately after preparation, making it both a time- and labor-intensive addition to the operative procedure. Thus, it would be convenient if PRP could be preserved. We evaluated the efficacy of freeze-dried PRP