SCP0058
Bradykinin Peptide
≥95% (HPLC), lyophilized powder
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About This Item
Formule empirique (notation de Hill):
C59H89N17O14
Poids moléculaire :
1260.44
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32
Produits recommandés
product name
Bradykinin Ile-Ser, T-Kinin,
Pureté
≥95% (HPLC)
Forme
lyophilized
Composition
Peptide Content, ≥65%
Conditions de stockage
protect from light
Température de stockage
−20°C
Amino Acid Sequence
Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Application
Bradykinin, a nonapeptide, is a potent endothelium-dependent vasodilator that operates via bradykinin receptors B1 and B2. Bradykinin Ile-Ser (T-Kinin) has a biological profile similar but not identical to bradykinin which is more resistant to degradation by kininase angiotensin converting enzyme (ACE). Bradykinin Ile-Ser is used to differentiate bradykinin receptor specificity and function.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Anna Bernhold Brechter et al.
Regulatory peptides, 103(1), 39-51 (2001-12-12)
Bradykinin receptor subtypes linked to prostaglandin release have been assessed in a human osteosarcoma cell line with osteoblastic phenotype (MG-63). Bradykinin (BK; 1 micromol/l) caused a burst of prostaglandin E(2) release that was maximal at 10 min. When the effect
D G Sawutz et al.
European journal of pharmacology, 227(3), 309-315 (1992-11-02)
[3H]Bradykinin binds to intact human IMR-90 fetal lung fibroblasts in a time and dose-dependent manner. Binding equilibrium was attained by 120 minutes at 4 degrees C. [3H]Bradykinin binding was saturable; Scatchard analysis of saturation binding data demonstrated a single binding
Prashant Desai et al.
European journal of medicinal chemistry, 37(2), 135-146 (2002-02-23)
T-kinin (Ile-Ser-BK) is related to BK in its biological profile, but unlike BK, is more resistant to the action of ACE. A detailed NMR and molecular modeling study of T-kinin has been carried out in three diverse media: water (pH
Clare Davis et al.
European journal of pharmacology, 450(2), 123-130 (2002-09-11)
T-kinin and its putative carboxypeptidase product des-Arg(11)-T-kinin are members of the kinin family that are unique to the rat. Primary cultures of rat bladder smooth muscle cells were used to investigate the pharmacology of these peptides. Calcium imaging experiments showed
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