IGF-1LR3 (0.1mg)
$100.00
Additional information
| Weight | 0.0625 lbs |
|---|
Published Scientific Research
Explore the full library of peer-reviewed studies, clinical data, mechanism breakdowns, and molecular specifications for IGF-1LR3 (0.1mg).
All research is sourced from PubMed-indexed journals for informational and educational purposes only. For Research Use Only (RUO). Not for human use.
View Full Research Library →Storage Instructions
All products from Apex Health Performance are manufactured using a lyophilization (freeze-drying) process. This method is designed to maintain product integrity and allows vials to remain stable during shipping for approximately 3–4 months.
Once a vial is reconstituted with bacteriostatic water, it should be stored in the refrigerator to help maintain stability. Under these conditions, reconstituted material is generally considered stable for up to 30 days.
Lyophilization is a dehydration technique in which compounds are frozen and then exposed to low pressure. This causes the water in the vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure. This powder can be kept at room temperature until reconstitution.
Upon receipt, products should be stored away from heat and light. For short-term use, refrigeration at approximately 4°C (39°F) is suitable. For long-term storage (several months to years), vials may be placed in a freezer at approximately -80°C (-112°F). Freezing is the preferred method for preserving product stability over extended periods.
⚠️ Important Notice:
These products are intended for research use only. Not for human consumption.
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Research Use Only
The following peer-reviewed publications reference compounds for laboratory and in vitro research purposes only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease or condition.
Published Scientific Research
Peer-reviewed laboratory studies investigating growth factor peptides
Chemoenzymatic Synthesis and in Vitro Selection of De Novo Thiazole-Containing Macrocyclic Peptides.
Backbone thiazole (Thz) moieties prevail in bioactive peptidic natural products and play important roles in their biological functions. However, the de novo discovery of artificial Thz-containing peptide ligands remains challenging. Here, we report an mRNA display-based selection platform for Thz-containing macrocyclic peptides (teMP), established through a dedicated posttranslational chemoenzymatic transformation. This method exploits the unique reactivity of ribosomally incorporated thioamides
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Recently, owing to their special spatial structures, peptide-based macrocycles have shown tremendous promise and aroused great interest in multidisciplinary research ranging from potent antibiotics against resistant strains to functional biomaterials with novel properties. Besides traditional monocyclic peptides, many fascinating polycyclic and remarkable higher-order cyclic, spherical and cylindric peptidic systems have come into the limelight owing to breakthroughs in various chemical (, nativ
View Full Study on PubMedBioinformatic prediction and experimental validation of RiPP recognition elements.
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View Full Study on PubMedLeveraging peptide-cellulose interactions to tailor the hierarchy and mechanics of peptide-polymer hybrids.
The addition of nanofiller with hydrogen bonding sites was used as another pathway towards hierarchical tuning matrix-filler interactions.
View Full Study on PubMedIn silico mutagenesis-based designing of oncogenic SHP2 peptide to inhibit cancer progression.
The SHP2 plays a major role in regulation of cell growth, proliferation, and differentiation, and functional upregulation of this enzyme is linked to oncogenesis and developmental disorders. We generated several peptides from the native wild peptide using an in silico mutagenesis method, which showed that changes (P302W, Y304F, E306Q, and Q303A) might boost the peptide's affinity for binding to SHP2.
View Full Study on PubMedStructural modeling of peptide toxin-ion channel interactions using RosettaDock.
Peptidic toxins from animal venoms target ion channels and provide useful scaffolds for the rational design of novel channel modulators with enhanced potency and subtype selectivity. We tested this approach on 10 structures of peptide toxin-ion channel complexes and demonstrated that it can sample near-native structures in all tested cases.
View Full Study on PubMedResearch Use Only
The following peer-reviewed publications reference compounds for laboratory and in vitro research purposes only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease or condition.
Published Scientific Research
Peer-reviewed laboratory studies investigating growth factor peptides
Chemoenzymatic Synthesis and in Vitro Selection of De Novo Thiazole-Containing Macrocyclic Peptides.
Backbone thiazole (Thz) moieties prevail in bioactive peptidic natural products and play important roles in their biological functions. However, the de novo discovery of artificial Thz-containing peptide ligands remains challenging. Here, we report an mRNA display-based selection platform for Thz-containing macrocyclic peptides (teMP), established through a dedicated posttranslational chemoenzymatic transformation. This method exploits the unique reactivity of ribosomally incorporated thioamides
View Full Study on PubMedRecent advances in peptide macrocyclization strategies.
Recently, owing to their special spatial structures, peptide-based macrocycles have shown tremendous promise and aroused great interest in multidisciplinary research ranging from potent antibiotics against resistant strains to functional biomaterials with novel properties. Besides traditional monocyclic peptides, many fascinating polycyclic and remarkable higher-order cyclic, spherical and cylindric peptidic systems have come into the limelight owing to breakthroughs in various chemical (, nativ
View Full Study on PubMedBioinformatic prediction and experimental validation of RiPP recognition elements.
Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a family of natural products for which discovery efforts have rapidly grown over the past decade. There are currently 38 known RiPP classes encoded by prokaryotes. Half of the prokaryotic RiPP classes include a protein domain called the RiPP Recognition Element (RRE) for successful installation of post-translational modifications on a RiPP precursor peptide. In most cases, the RRE domain binds to the N-terminal "leade
View Full Study on PubMedLeveraging peptide-cellulose interactions to tailor the hierarchy and mechanics of peptide-polymer hybrids.
The addition of nanofiller with hydrogen bonding sites was used as another pathway towards hierarchical tuning matrix-filler interactions.
View Full Study on PubMedIn silico mutagenesis-based designing of oncogenic SHP2 peptide to inhibit cancer progression.
The SHP2 plays a major role in regulation of cell growth, proliferation, and differentiation, and functional upregulation of this enzyme is linked to oncogenesis and developmental disorders. We generated several peptides from the native wild peptide using an in silico mutagenesis method, which showed that changes (P302W, Y304F, E306Q, and Q303A) might boost the peptide's affinity for binding to SHP2.
View Full Study on PubMedStructural modeling of peptide toxin-ion channel interactions using RosettaDock.
Peptidic toxins from animal venoms target ion channels and provide useful scaffolds for the rational design of novel channel modulators with enhanced potency and subtype selectivity. We tested this approach on 10 structures of peptide toxin-ion channel complexes and demonstrated that it can sample near-native structures in all tested cases.
View Full Study on PubMedResearch Use Only
The following peer-reviewed publications reference compounds for laboratory and in vitro research purposes only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease or condition.
Published Scientific Research
Peer-reviewed laboratory studies investigating growth factor peptides
Chemoenzymatic Synthesis and in Vitro Selection of De Novo Thiazole-Containing Macrocyclic Peptides.
Backbone thiazole (Thz) moieties prevail in bioactive peptidic natural products and play important roles in their biological functions. However, the de novo discovery of artificial Thz-containing peptide ligands remains challenging. Here, we report an mRNA display-based selection platform for Thz-containing macrocyclic peptides (teMP), established through a dedicated posttranslational chemoenzymatic transformation. This method exploits the unique reactivity of ribosomally incorporated thioamides
View Full Study on PubMed →Recent advances in peptide macrocyclization strategies.
Recently, owing to their special spatial structures, peptide-based macrocycles have shown tremendous promise and aroused great interest in multidisciplinary research ranging from potent antibiotics against resistant strains to functional biomaterials with novel properties. Besides traditional monocyclic peptides, many fascinating polycyclic and remarkable higher-order cyclic, spherical and cylindric peptidic systems have come into the limelight owing to breakthroughs in various chemical (, nativ
View Full Study on PubMed →Bioinformatic prediction and experimental validation of RiPP recognition elements.
Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a family of natural products for which discovery efforts have rapidly grown over the past decade. There are currently 38 known RiPP classes encoded by prokaryotes. Half of the prokaryotic RiPP classes include a protein domain called the RiPP Recognition Element (RRE) for successful installation of post-translational modifications on a RiPP precursor peptide. In most cases, the RRE domain binds to the N-terminal "leade
View Full Study on PubMed →Leveraging peptide-cellulose interactions to tailor the hierarchy and mechanics of peptide-polymer hybrids.
The addition of nanofiller with hydrogen bonding sites was used as another pathway towards hierarchical tuning matrix-filler interactions.
View Full Study on PubMed →In silico mutagenesis-based designing of oncogenic SHP2 peptide to inhibit cancer progression.
The SHP2 plays a major role in regulation of cell growth, proliferation, and differentiation, and functional upregulation of this enzyme is linked to oncogenesis and developmental disorders. We generated several peptides from the native wild peptide using an in silico mutagenesis method, which showed that changes (P302W, Y304F, E306Q, and Q303A) might boost the peptide's affinity for binding to SHP2.
View Full Study on PubMed →Structural modeling of peptide toxin-ion channel interactions using RosettaDock.
Peptidic toxins from animal venoms target ion channels and provide useful scaffolds for the rational design of novel channel modulators with enhanced potency and subtype selectivity. We tested this approach on 10 structures of peptide toxin-ion channel complexes and demonstrated that it can sample near-native structures in all tested cases.
View Full Study on PubMed →Important Research Notice: These products are research chemicals intended exclusively for in vitro laboratory research by qualified professionals. Not for human or animal consumption. Not approved by the FDA for any therapeutic purpose. Sold strictly for scientific research applications only.