| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | Tumor necrosis factor ligand superfamily member 11; RANKL; CD254; ODF; OPGL; TNFSF11; TRANCE |
| Biological Activity | |
| Expression System | |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Protein Length | |
| Purity | |
| Shipping | |
| Species | |
| Storage | |
| Target |
Background
RANKL is supplied as a recombinant protein reagent for research use only. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.
Also known as: Tumor necrosis factor ligand superfamily member 11; RANKL; CD254; ODF; OPGL; TNFSF11; TRANCE.
Species origin: Mouse.
Mouse RANKL protein, expressed in E. coli
Endotoxin: < 1 EU per μg of the protein as determined by the LAL method
Biological significance and function
RANKL is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as Molecular & Cellular Biology.
Molecular characteristics
Molecular characteristics: Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.
- Source species: Mouse
- Molecular weight: 19 kDa
- Protein length: The recombinant Mouse sRANKL consists of 174 amino acids(N-Met) and has a predicted molecular mass of 19 kDa. The apparent molecular mass of the Mouse sRANKL protein is approximately 19 kDa in SDS-PAGE under reducing conditions.
- Expression region: Amino acid sequence derived from Mouse RANKL soluble form (O35235)(Pro143-Asp316) was expressed
- Purity: ≥ 98 % as determined by SDS-PAGE
- Biological activity: Immobilized Mouses RANKL at 1μg/mL(100μl/well)can bind Human OPG(C-Fc),The EC50 of Human OPG is 55 ng/mL.
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.
Expression and purification strategy
Expression system: E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.
Tagging: No tag tags are commonly used to streamline purification and enable capture/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.
Formulation: Lyophilized from sterile 20 mM Tris, 150 mM NaCl pH 8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.
Research interpretation
Research interpretation: Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.
What is the purity of Mouse RANKL Protein (Mouse)?
What buffer is this protein supplied in?
How should Mouse RANKL Protein (Mouse) be stored?
What expression system was used to produce this protein?
What is the molecular weight of this protein?
Is this protein biologically active?
What are the shipping conditions?
Is this protein approved for clinical or in vitro diagnostic use?
Can I request a custom size, tag variant, or formulation?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
Modulation of mammary tumour progression using murine model by ethanol root extract of Saussurea costus (falc.) lipsch(PRP1114-5.4)
Author:R Kumar, P Bhardwaj, M Soni, Publication name:Journal IF:5.4 View