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Mogengel Matrix (GFR Phenol Red Free) (Acro Certified)

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产品展示(Product Show)

Mogengel PRODUCT SHOW

产品优势(Key Benefits)

  1. Organoid Function Assay Validated - Strict Quality Control Assays for every produced lot.
  2. Lot-to-lot Consistency - Strict manufacturing controls and management systems.
  3. Stable, Long-term Supply - Large-scale manufacturing capacity and ACRO’s global supply chain.
  4. Cost Effective - Bulk pricing available to meet your research needs.

产品应用(Intended Use)

Mogengel Matrix (GFR Phenol Red Free) is intended to be used in organoid/3D cell culturing and applications that require extracellular matrix scaffolding. This includes applications including maintaining cellular growth and differentiation of various cell types, including stem, endothelial, epithelial, and others. It is also intended for applications regarding a more demanding preparation of basement membrane such as tubular osteocyte signaling studies or as a base for mouse mammalian epithelial cell expression studies (basement membrane matrices can reduce the background signals triggered by external addition of growth factors).

产品描述(Product Description)

  1. Basement membranes are comprised of continuous sheets of a specialized extracellular matrix. It acts an interface between various types of cells, including muscle, neuronal, epithelial, or endothelial cells, along with adjacent stroma. Basement membranes are an essential part in the organization of tissues forming the scaffolding and support for cellular growth and cell layers. They also affect a variety of cellular mechanisms such as adhesion, migration, proliferation, and differentiation. Basement membranes are selectively degraded and regenerated during development and wound healing, forming the base scaffold for tissue reconstruction. Basement membranes also act as a major barrier to invasion by metastatic tumor cells.
  2. Mogengel Matrix GFR (Growth Factor Reduced) Phenol Red Free is a soluble form of basement membrane that is purified from gene-edited mouse tumor cells grown in LDEV-free mouse populations. Reconstitution into the original basement membrane form occurs at 37℃ and is mainly comprised of laminin, collagen IV, entactin, and heparin sulfate proteoglycan.
 

活性(Bioactivity)-Tumor Organoid Culture

Mogengel TUMOR ORGANOID CULTURE

Human tumor organoids (breast cancer organoids, hepatocellular carcinoma organoids) can grow well in greater than 70% Mogengel (Cat. No. AC-M082703).

 

活性(Bioactivity)-Mouse Organoid Culture

Mogengel MOUSE ORGANOID CULTURE

Mouse intestinal organoid, liver ductal organoid, airway organoid can also grow well in greater than 70% Mogengel (Cat. No. AC-M082703).

 

说明书(Specification)

Protein ConcentrationWithin 9 to 11 mg/mL, tested by BCA assay.
Endotoxin Level< 4.5 EU/mL, tested by LAL assay.
Organoid CultureMouse intestinal organoids, mouse liver ductal organoids and mouse airway organoids could grow well under the Mogengel matrix.
*Evaluated Mogengel Matrix: Medium Ratio = 7:3 (v/v).
AngiogenesisBlood vessel formation is observed, tested by HUVEC angiogenesis assay.
*Evaluated Mogengel Matrix: Medium Ratio = 1:0 (original formulation), 2:1, 1:1 (v/v).
SterilityNo growth observed after 14 days. Testing for the detection of bacteria, fungi, and mycoplasma through cell culture.
Viral TestingTested negative by ELISA, bacterial culture and microscope observation for a total of 19 bacterial and virus strains, and additional murine infectious agents including LDEV.
StabilityProduct is stable for at least two years from date of manufacture when stored at ≤ -20℃. See lot specific Certificate of Analysis for expiration date.
Shipping ConditionsThe product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended on the product label.
StorageStore at -20℃. Avoid multiple freeze-thaws. Do not store in frost-free freezer. KEEP FROZEN.
 

Acro Certify声明

This product is one of ACROBiosystems' Certify products. ACROBiosystems and our Certify partners have established a close partnership that includes an in-depth review of quality management and quality audits this product. Products from our Certify partners have been qualified by ACROBiosystems to be included under Acro Certify. ACROBiosystems may provide Product information, including technical information, specifications, recommendations, literature, and other material (collectively, "Product Information") for customer's convenience. The accuracy and completeness of Product Information is not guaranteed and is subject to change without notice. ACROBiosystems is not responsible for the intellectual property or impact to intellectual property for products sold under Acro Certify.

 
评论(0)
  1. 198XXXXXXX5
  2. 0人赞
  3. 在试剂盒开发过程中,elisa的方法开发与优化使用了S1N C52Hv 这个蛋白,很顺利的完成了方法开发并交付。
  4. 2024-3-11
 
ACRO质量管理体系
 
 

前沿进展

Alveolar epithelial type 2 cell specific loss of IGFBP2 activates inflammation in COVID-19
Pujadas, Chin, Sankpal et al
Respir Res (2025) 26 (1), 111
Abstract: The coronavirus disease 2019 (COVID-19) global pandemic is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). However, our understanding of SARS-CoV-2-induced inflammation in alveolar epithelial cells remains very limited. The contributions of intracellular insulin-like growth factor binding protein-2 (IGFBP2) to SARS-CoV-2 pathogenesis are also unclear. In this study, we have uncovered a critical role for IGFBP2, specifically in alveolar epithelial type 2 cells (AEC2), in the immunopathogenesis of COVID-19. Using bulk RNA sequencing, we show that IGFBP2 mRNA expression is significantly downregulated in primary AEC2 cells isolated from fibrotic lung regions from patients with COVID-19-acute respiratory distress syndrome (ARDS) compared to those with idiopathic pulmonary fibrosis (IPF) alone or IPF with a history of COVID-19. Using multicolor immunohistochemistry, we demonstrated that IGFBP2 and its selective ligands IGF1 and IGF2 were significantly reduced in AEC2 cells from patients with COVID-ARDS, IPF alone, or IPF with COVID history than in those from age-matched donor controls. Further, we demonstrated that lentiviral expression of Igfbp2 significantly reduced mRNA expression of proinflammatory cytokines-Tnf-α, Il1β, Il6, Stat3, Stat6 and chemokine receptors-Ccr2 and Ccr5-in mouse lung epithelial cells challenged with SARS-CoV-2 spike protein injury (S2; 500 ng/mL). Finally, we demonstrated higher levels of cytokines-TNF-α; IL-6 and chemokine receptor-CCR5 in AEC2 cells from COVID-ARDS patients compared to the IPF alone and the IPF with COVID history patients. Altogether, these data suggest that anti-inflammatory properties of IGFBP2 in AEC2 cells and its localized delivery may serve as potential therapeutic strategy for patients with COVID-19.© 2025. The Author(s).
The fusion peptide of the spike protein S2 domain may be a mimetic analog of β-coronaviruses and serve as a novel virus-host membrane fusion inhibitor
Safiriyu, Hussain, Dewangan et al
Antiviral Res (2025) 237, 106144
Abstract: Coronavirus has garnered more attention recently, particularly in the aftermath of the 2019 pandemic. The β genus of the coronavirus family has demonstrated a significant threat to humanity. Current mitigation strategies involve the development of vaccines and repurposing drugs for symptomatic management of coronavirus infection, specifically SARS-Cov 2. Fusion inhibitors that are available as antiviral drugs for coronavirus have targeted the heptad repeat (HR) 1 and 2 in the S2 domain of the spike protein. The current study identified a fusion peptide (FP) upstream of HR1 as a potential target for developing membrane fusion inhibitors, and mimetic peptides analogous to the FP segment were tested for antiviral activity. Four mimetic fusion peptides (MFPs) (RSA59PP (MFP633), RSA59P (MFP634), RSMHV2P (MFP635), and RSMHV2PP (MFP636)) that are analogous to the FP of murine β coronavirus mouse hepatitis virus (MHV), MHV-A59/RSA59 (PP) and MHV-2/RSMHV2 (P) with central proline mutations, were tested. Results show the ability of MFPs to reduce cell-to-cell fusion and viral replication in vitro. MFP633, which contains a central double proline, exhibited the most potent inhibitory effect in spike protein-mediated membrane fusion assays. Biophysical experiments also demonstrated the strongest interactions between double-proline containing MFPs (MFP633 and MFP636) with biomimetic liposomes. In vivo studies using a liposome-mediated delivery system in mice confirmed the antiviral activity of MFP633. These findings suggest that targeting FPs could develop effective fusion inhibitors against coronaviruses. MFPs act on the host cell membrane by competing with the viral FP during the early stage of host-viral membrane fusion events. MFP633 is a promising peptide drug candidate that warrants future examination to assess whether this and other dual-proline containing peptides may exert similar anti-viral effects in other coronaviruses with conserved FP structures.Copyright © 2025. Published by Elsevier B.V.
SARS CoV-2 spike adopts distinct conformational ensembles in situ
Gramm, Braet, Srinivasu et al
bioRxiv (2025)
Abstract: Engineered recombinant Spike (S) has been invaluable for determining S structure and dynamics and is the basis for the design of most prevalent vaccines. While these vaccines have been highly efficacious for short-term protection from infection, protection waned with the emergence of variants (alpha through omicron). Here we report differences in conformational dynamics between native, membrane-embedded full-length S and recombinant S. Our virus-like particle (VLP) model mimics the native SARS CoV-2 virion by displaying S assembled with auxiliary E, M, and N proteins in a native membrane environment that captures the entirety of quaternary interactions mediated by S. Display of S on VLP obviates the requirement for stabilizing modifications that have been engineered into recombinant S for enhanced expression and solubility. Amide hydrogen/deuterium exchange mass spectrometry (HDXMS) reveals altered interprotomer contacts in VLP S trimers attributable to the presence of auxiliary proteins, membrane anchoring, and lack of engineered modifications. Our results reveal decreased dynamics in the S2 subunit and at sites spanning interprotomer contacts in VLP S with minimal differences in the N-terminal domain (NTD) and receptor binding domain (RBD). This carries implications for display of epitopes beyond NTD and RBD. In summary, despite affording efficient structural characterization, recombinant S distorts the intrinsic conformational ensemble of native S displayed on the virus surface.
Targeting the early life stages of SARS-CoV-2 using a multi-peptide conjugate vaccine
Myburgh, Karsjens, Blanas et al
Vaccine (2025) 54, 126989
Abstract: The spike glycoprotein is a key factor in the infection cycle of SARS-CoV-2, as it mediates both receptor recognition and membrane fusion by the virus. Therefore, in this study, we aimed to design a multi-peptide conjugate vaccine against SARS-CoV-2, targeting the early stages of the virus's life cycle. We used iBoost technology, which is designed to induce immune responses against low- or non-immunogenic epitopes. We selected six peptide sequences, each representing a key domain of the spike protein (i.e., receptor binding domain (RBM), subdomain 1 (SD1), subdomain 2 (SD2), S1/S2, fusion peptide and the S2' sequences (FP + S2'), heptad repeat 1 (HR1)). Immunization studies in mice displayed targeted humoral and cellular immune responses against specific peptides of the spike protein simultaneously, while inducing cross-protection against the Delta and Omicron coronavirus variants. Moreover, vaccinated hamsters challenged with SARS-CoV-2 elicited high antibody levels against key peptides, induced early neutralizing antibody responses and resulted in less weight loss compared to controls. This highlights the potential for improving viral control and disease outcomes when utilizing this strategy. Therefore, by using iBoost technology in conjunction with our peptide design strategy, we were able to successfully target non-immunodominant regions in the spike protein while activating both arms of the adaptive immune system.Copyright © 2024. Published by Elsevier Ltd.
Showing 1-4 of 1461 papers.
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