| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | Kallidin, lysyl-bradykinin |
| Cas No. | |
| Concentration | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Reconstitution | |
| Solubility | Centrifuge the vial before adding solvent (10,000 x g for 5 minutes) to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. The product is soluble in pure water at high micromolar concentrations (100 µM - 1 mM). For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in double-distilled water (ddH2O) at a concentration between 100-1000x of the final working concentration. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. Centrifuge all product preparations before use. It is recommended to prepare fresh solutions in working buffers just before use. Avoid multiple freeze-thaw cycles to maintain biological activity. |
| Source | Synthetic peptide |
| Storage | |
| Target |
Overview
Lys-Bradykinin is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to B2 bradykinin receptor biology and/or assay development. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Calcium imaging assay.
Key elements and design rationale
- Molecular identity: CAS: 0342-10-9, MW: 1188.38 Da, Formula: C56H85N17O12.
- Source / origin: Synthetic peptide.
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.
Biological background
Kinins are small peptides rapidly produced following tissue injury that serve as important modulators of inflammation and pain. In the periphery, the actions of kinins include vasodilatation, increased vascular permeability, stimulation of immune cells, and induction of pain. Kinins in the central nervous system (CNS) appear to initiate a similar cascade of events leading to neural tissue damage as well as long lasting disturbances affecting blood-brain barrier function1.Kinins such as Bradykinin (BK), Lys-BK, desArg9-BK, and Lys-desArg9-BK exert their action via two distinct G protein-coupled receptors (GPCR): the B1 Bradykinin receptor (BKRB1) and the B2 Bradykinin receptor (BKRB2)2.Activation of BKRB2 liberates mediators of vascular tone, fibrinolysis, and pain. BKRB2, which mediates most of the physiological effects of kinins, as well as BKRB1, represent potential therapeutic targets for treatment of inflammatory disorders and cardiovascular diseases.Expression of BKRB1 is inducible upon various types of tissue injury and by inflammatory mediators such as bacterial lipopolysaccharide (LPS) and cytokines. A low level of expression of BKRB1 in the CNS of rodent and primates was recently demonstrated3. BKRB2 is constitutively and widely expressed throughout the CNS and peripheral nervous system and on various cell types including endothelial cells, nerve fibers, leukocytes, and mast cells3-5.Lys-Bradykinin is an endogenous nonspecific agonist for BKRB1and BKRB2, with some specificity towards the BKRB26. Activation of Bradykinin receptors with Lys-Bradykinin may induce intracellular Ca2+ elevation7. 100 nM Lys-Bradykinin induced Ca2+ transients in rat aortic endothelium cells (RAEC) (see figure here and review in reference #8).
Research relevance and current trends
- Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
- Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
- Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.
Common research applications
- Calcium imaging assay: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.
Notes for experimental interpretation
- Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
- Target complexity: closely related family members, splice variants, and post-translational modifications can influence apparent specificity and potency.
- Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
- Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.
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