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This document describes an experiment testing whether asparagus can inhibit the growth of yeast cells. It involved growing yeast in different broth solutions with and without asparagus, measuring absorbance over time with a spectrophotometer, and counting yeast colonies on agar plates with and without asparagus to compare growth. The results showed lower absorbance values and fewer colonies for yeast grown in broth and plated with asparagus compared to the positive control.
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Yeast cells were grown in three different mediums - a standard positive control with nutrients, a negative control with just water, and an experimental group with standard nutrients and 50mL of filtered asparagus. The asparagus experimental group showed less growth than the positive control based on absorbance measurements and fewer viable colony counts on agar plates, indicating that compounds in asparagus may inhibit yeast population growth.
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Yeast cells were grown in three different mediums - a standard positive control with nutrients, a negative control with just water, and an experimental group with standard nutrients and 50mL of filtered asparagus. The asparagus experimental group showed less growth than the positive control based on absorbance measurements and fewer viable yeast colonies on agar plates, indicating that asparagus may inhibit yeast population growth.
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Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis . The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ . Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization . Plays a key role to control cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration . The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage-independent growth, and epithelial mesenchymal transition (EMT) induction . / Isoform 2: Isoform 2 and isoform 3 can activate the C-terminal fragment (CTF) of ERBB4 (isoform 3).
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This experiment tested whether asparagus could inhibit the growth of yeast cells. Yeast was grown in three different mediums - a positive control with nutrients, a negative control with water only, and an experimental group with nutrients and asparagus. The yeast growth was measured using spectrophotometry and viable colony counts. The results showed lower absorbance and fewer colonies for yeast grown in the medium containing asparagus, indicating its growth was inhibited.
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Yeast cells were grown in three different mediums - a standard positive control with nutrients, a negative control with just water, and an experimental group with standard nutrients and 50mL of filtered asparagus. The asparagus experimental group showed less growth than the positive control based on absorbance measurements and fewer viable colony counts on agar plates, indicating that compounds in asparagus may inhibit yeast population growth.
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Yeast cells were grown in three different mediums - a standard positive control with nutrients, a negative control with just water, and an experimental group with standard nutrients and 50mL of filtered asparagus. The asparagus experimental group showed less growth than the positive control based on absorbance measurements and fewer viable yeast colonies on agar plates, indicating that asparagus may inhibit yeast population growth.
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Tyrosine phosphorylated upon stimulation with EGF. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, LIF, CNTF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha, LEP and OSM. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Phosphorylated on serine upon DNA damage, probably by ATM or ATR. Serine phosphorylation is important for the formation of stable DNA-binding STAT3 homodimers and maximal transcriptional activity.
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Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.
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Glial fibrillary acidic protein is an intermediate filament (IF) protein that is expressed by numerous cell types of the central nervous system (CNS) including astrocytes and ependymal cells. GFAP has also been found to be expressed in glomeruli and peritubular fibroblasts taken from rat kidneys Leydig cells of the testis in both hamsters and humans, human keratinocytes, human osteocytes and chondrocytes and stellate cells of the pancreas and liver in rats. First described in 1971, GFAP is a type III IF protein that maps, in humans, to 17q21.[13] It is closely related to its non-epithelial family members, vimentin, desmin, and peripherin, which are all involved in the structure and function of the cell’s cytoskeleton. GFAP is thought to help to maintain astrocyte mechanical strength,[14] as well as the shape of cells but its exact function remains poorly understood, despite the number of studies using it as a cell marker.
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Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. The ATG12-ATG5 conjugate also negatively regulates the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Also plays a role in translation or delivery of incoming viral RNA to the translation apparatus.
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Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability.
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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Cancer Cells
Tiffany Sato investigated whether asparagus can inhibit the growth of yeast cells. She used yeast (Saccharomyces cerevisiae) as a model organism to study the anti-proliferative effects of asparagus due to similarities between yeast and cancer cells. Yeast was grown in media containing asparagus extract, a control lacking nutrients, and a positive control with nutrients. Growth was measured using absorbance and colony counts. Absorbance was lowest in asparagus media, indicating decreased growth. Colony counts also showed fewer colonies with asparagus, supporting the hypothesis that asparagus inhibits yeast cell proliferation.
The Effect of Asparagus on Cancer Cell Growth
Tiffany Sato investigated whether asparagus can inhibit the population growth of yeast cells. Yeast cells were used as a model for cancer cells due to similarities in structure and uncontrolled cell division. Sato grew yeast in media containing asparagus (experimental), without nutrients (negative control), and with nutrients (positive control). Analysis using a spectrophotometer found the lowest yeast activity/growth in the experimental media. Agar plate results also showed fewer colonies forming in the experimental plates compared to the positive control. Sato's results suggest that asparagus can minimally inhibit yeast cell growth, indicating its potential as an anticancer agent.
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Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.
Anti-Caspase-8 -http://www.stjohnslabs.com/caspase-8-antibody-p-99045
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validationImmunofluorescence Antibody Validation Report for Anti-GFAP Antibody (STJ96961)
Immunofluorescence Antibody Validation Report for Anti-GFAP Antibody (STJ96961)St John's Laboratory Ltd
Glial fibrillary acidic protein is an intermediate filament (IF) protein that is expressed by numerous cell types of the central nervous system (CNS) including astrocytes and ependymal cells. GFAP has also been found to be expressed in glomeruli and peritubular fibroblasts taken from rat kidneys Leydig cells of the testis in both hamsters and humans, human keratinocytes, human osteocytes and chondrocytes and stellate cells of the pancreas and liver in rats. First described in 1971, GFAP is a type III IF protein that maps, in humans, to 17q21.[13] It is closely related to its non-epithelial family members, vimentin, desmin, and peripherin, which are all involved in the structure and function of the cell’s cytoskeleton. GFAP is thought to help to maintain astrocyte mechanical strength,[14] as well as the shape of cells but its exact function remains poorly understood, despite the number of studies using it as a cell marker.
Anti-GFAP -http://www.stjohnslabs.com/gfap-antibody-p-98596
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validation
Immunofluorescence Antibody Validation Report for Anti-ATG5 Antibody (STJ98903)
Immunofluorescence Antibody Validation Report for Anti-ATG5 Antibody (STJ98903)St John's Laboratory Ltd
Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. The ATG12-ATG5 conjugate also negatively regulates the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Also plays a role in translation or delivery of incoming viral RNA to the translation apparatus.
Anti-ATG5 - http://www.stjohnslabs.com/anti-atg5-antibody-p-104935?filter_name=STJ98903
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validation
Immunofluorescence Antibody Validation Report for Anti-eIF4A1 Antibody (STJ97...
Immunofluorescence Antibody Validation Report for Anti-eIF4A1 Antibody (STJ97...St John's Laboratory Ltd
ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. / ATP + H2O = ADP + phosphate. / Helicase activity and function in translation are inhibited by interaction with PDCD4.
Anti-eIF4A1 -http://www.stjohnslabs.com/eif4a1-antibody-p-98673
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validationImmunofluorescence Antibody Validation Report for Anti-Phospho-Stat1 (Y701) A...
Immunofluorescence Antibody Validation Report for Anti-Phospho-Stat1 (Y701) A...St John's Laboratory Ltd
Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus.
Anti-Phospho-Stat1 (Y701) -http://www.stjohnslabs.com/phospho-stat1-y701-antibody
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validation
Immunofluorescence Antibody Validation Report for Anti-Caspase 9 Antibody (ST...
Immunofluorescence Antibody Validation Report for Anti-Caspase 9 Antibody (ST...St John's Laboratory Ltd
This antibody validation report describes the validation of an anti-Caspase 9 monoclonal antibody in immunofluorescence applications on human appendix and colon tissues. The report provides the antibody information, imaging descriptions, and immunofluorescence protocol which involves tissue processing, antigen retrieval, blocking, primary and secondary antibody incubations, counterstaining, mounting and visualization under a fluorescence microscope.Immunofluorescence Antibody Validation Report for Anti-PPAR Delta Antibody (S...
Immunofluorescence Antibody Validation Report for Anti-PPAR Delta Antibody (S...St John's Laboratory Ltd
This antibody validation report describes the testing of an anti-PPAR Delta monoclonal antibody (clone 2F9) on rat and mouse spleen tissue samples. The report details the immunofluorescence protocol used, including tissue processing, antigen retrieval, primary and secondary antibody incubations, DAPI counterstaining, mounting, and visualization under a fluorescence microscope. Images show the distribution of the target protein in red fluorescence and DAPI nuclear counterstain in blue.Immunofluorescence Antibody Validation Report for Anti-Luciferase Antibody (S...
Immunofluorescence Antibody Validation Report for Anti-Luciferase Antibody (S...St John's Laboratory Ltd
Produces green light with a wavelength of 562 nm. / Photinus luciferin + O2 + ATP = oxidized Photinus luciferin + CO2 + AMP + diphosphate + light.
Anti-Luciferase -http://www.stjohnslabs.com/luciferase-antibody-2
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validationImmunofluorescence Antibody Validation Report for Anti-USP11 Antibody (STJ96193)
Immunofluorescence Antibody Validation Report for Anti-USP11 Antibody (STJ96193)St John's Laboratory Ltd
This antibody validation report from St. John's Laboratory describes testing of a polyclonal rabbit anti-USP11 antibody on human uterus and lung tissue samples. The report details the immunofluorescence protocol used, including tissue processing with antigen retrieval, primary and secondary antibody incubations, DAPI counterstaining, and visualization under a fluorescence microscope. Testing showed the anti-USP11 antibody successfully labeled USP11 protein in samples of both human uterus and lung tissues.Immunofluorescence Antibody Validation Report for Anti-HP-1α Antibody (STJ98895)
Immunofluorescence Antibody Validation Report for Anti-HP-1α Antibody (STJ98895)St John's Laboratory Ltd
Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins.
Anti-HP-1α - http://www.stjohnslabs.com/anti-hp-1a-antibody?filter_name=STJ98895
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validation
Immunofluorescence Antibody Validation Report for Anti-Collagen IV Antibody (...
Immunofluorescence Antibody Validation Report for Anti-Collagen IV Antibody (...St John's Laboratory Ltd
Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.
Anti-Collagen IV - http://www.stjohnslabs.com/anti-collagen-iv-antibody?filter_name=STJ98907
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validation
Immunofluorescence Antibody Validation Report for Anti-PR Antibody (STJ97365)
Immunofluorescence Antibody Validation Report for Anti-PR Antibody (STJ97365)St John's Laboratory Ltd
The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation. / Isoform A: inactive in stimulating c-Src/MAPK signaling on hormone stimulation. / Isoform 4: Increases mitochondrial membrane potential and cellular respiration upon stimulation by progesterone.
Anti-PR -http://www.stjohnslabs.com/pr-antibody-p-99016
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validationImmunofluorescence Antibody Validation Report for Anti-Rock-1 Antibody (STJ95...
Immunofluorescence Antibody Validation Report for Anti-Rock-1 Antibody (STJ95...St John's Laboratory Ltd
Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability.
Anti-Rock-1 -http://www.stjohnslabs.com/rock-1-antibody-p-94232
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validationImmunofluorescence Antibody Validation Report for Anti-Histone H2B Antibody (...
Immunofluorescence Antibody Validation Report for Anti-Histone H2B Antibody (...St John's Laboratory Ltd
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Anti-Histone H2B -http://www.stjohnslabs.com/histone-h2b-
antibody-p-98699
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validationImmunofluorescence Antibody Validation Report for Anti-NSE Antibody (STJ96968)
Immunofluorescence Antibody Validation Report for Anti-NSE Antibody (STJ96968)St John's Laboratory Ltd
Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity).
Anti-NSE -http://www.stjohnslabs.com/nse-antibody-p-98603
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validationImmunofluorescence Antibody Validation Report for Anti-COX IV Antibody (STJ96...
Immunofluorescence Antibody Validation Report for Anti-COX IV Antibody (STJ96...St John's Laboratory Ltd
Cytochrome c oxidase subunit 4 isoform 1, mitochondrial is an enzyme that in humans is encoded by the COX4I1 gene.
Cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. The complex consists of 13 mitochondrial- and nuclear-encoded subunits. The mitochondrially-encoded subunits perform the electron transfer and proton pumping activities.
Anti-COX IV -http://www.stjohnslabs.com/cox-iv-antibody-p-
98570
Join our Antibody Validation Project - http://www.stjohnslabs.com/services/antibody-validationanti microbial screening models
This document describes three models used to screen for antibacterial activity:
1) The mouse systemic infection model tests compounds against infections caused by E. coli, Klebsiella pneumoniae, and Staphylococcus aureus in mice. One study showed broad-spectrum activity against gram-negative and gram-positive bacteria.
2) The rabbit skin burn infection model assesses compounds' ability to reduce viable E. coli colony counts in burn wounds created on rabbits.
3) The mouse ascending urinary tract infection model evaluates compounds' dose-dependent efficacy against an E. coli bladder infection in mice. Kidneys are examined for reductions in viable bacterial counts compared to controls.
Brucella test (rose bengal test)
Brucella cause disease primarily in domestic and some wild animals and most are pathogenic for humans
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Immunofluorescence Antibody Validation Report for Anti-CK16 Antibody (STJ96958)
Immunofluorescence Antibody Validation Report for Anti-CK16 Antibody (STJ96958)
Immunofluorescence Antibody Validation Report for Anti-Phospho-Stat3 (S727) A...
Immunofluorescence Antibody Validation Report for Anti-Phospho-Stat3 (S727) A...
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Immunofluorescence Antibody Validation Report for Anti-Caspase-8 Antibody (ST...
Immunofluorescence Antibody Validation Report for Anti-GFAP Antibody (STJ96961)
Immunofluorescence Antibody Validation Report for Anti-GFAP Antibody (STJ96961)
Immunofluorescence Antibody Validation Report for Anti-ATG5 Antibody (STJ98903)
Immunofluorescence Antibody Validation Report for Anti-ATG5 Antibody (STJ98903)
Immunofluorescence Antibody Validation Report for Anti-eIF4A1 Antibody (STJ97...
Immunofluorescence Antibody Validation Report for Anti-eIF4A1 Antibody (STJ97...
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Immunofluorescence Antibody Validation Report for Anti-USP11 Antibody (STJ96193)
Immunofluorescence Antibody Validation Report for Anti-USP11 Antibody (STJ96193)
Immunofluorescence Antibody Validation Report for Anti-HP-1α Antibody (STJ98895)
Immunofluorescence Antibody Validation Report for Anti-HP-1α Antibody (STJ98895)
Immunofluorescence Antibody Validation Report for Anti-Collagen IV Antibody (...
Immunofluorescence Antibody Validation Report for Anti-Collagen IV Antibody (...
Immunofluorescence Antibody Validation Report for Anti-PR Antibody (STJ97365)
Immunofluorescence Antibody Validation Report for Anti-PR Antibody (STJ97365)
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Immunofluorescence Antibody Validation Report for Anti-NSE Antibody (STJ96968)
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Immunofluorescence Antibody Validation Report for Anti-COX IV Antibody (STJ96...
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Tiffany Sato investigated whether asparagus can inhibit the growth of yeast cells. She used yeast (Saccharomyces cerevisiae) as a model organism to study the anti-proliferative effects of asparagus due to similarities between yeast and cancer cells. Yeast was grown in media containing asparagus extract, a control lacking nutrients, and a positive control with nutrients. Growth was measured using absorbance and colony counts. Absorbance was lowest in asparagus media, indicating decreased growth. Colony counts also showed fewer colonies with asparagus, supporting the hypothesis that asparagus inhibits yeast cell proliferation.
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Tiffany Sato investigated whether asparagus can inhibit the population growth of yeast cells. Yeast cells were used as a model for cancer cells due to similarities in structure and uncontrolled cell division. Sato grew yeast in media containing asparagus (experimental), without nutrients (negative control), and with nutrients (positive control). Analysis using a spectrophotometer found the lowest yeast activity/growth in the experimental media. Agar plate results also showed fewer colonies forming in the experimental plates compared to the positive control. Sato's results suggest that asparagus can minimally inhibit yeast cell growth, indicating its potential as an anticancer agent.
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Tiffany Sato investigated whether asparagus can inhibit the population growth of yeast cells. Yeast cells were used as a model for cancer cells due to similarities in structure and uncontrolled cell division. Sato grew yeast in media containing asparagus (experimental), without nutrients (negative control), and with nutrients (positive control). Analysis using a spectrophotometer found the lowest yeast activity/growth in the experimental media. Agar plate results also showed fewer colonies forming in the experimental plates compared to the positive control. Sato concluded the asparagus decreased yeast growth, indicating its compounds may inhibit cell proliferation.
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Tiffany Sato investigated whether asparagus can inhibit the growth of yeast cells. She used yeast (Saccharomyces cerevisiae) as a model organism to study the anti-proliferative effects of asparagus due to similarities between yeast and cancer cells. Yeast was grown in media containing asparagus extract, a control lacking nutrients, and a positive control with nutrients. Growth was measured using absorbance and colony counts. Absorbance was lowest in asparagus media, indicating decreased growth. Colony counts also showed fewer colonies with asparagus, supporting the hypothesis that asparagus inhibits yeast cell proliferation.
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Tiffany Sato investigated whether asparagus could inhibit the growth of yeast cells. She used yeast (Saccharomyces cerevisiae) as a model organism to study the anti-proliferative effects of asparagus due to similarities between yeast and cancer cells. Yeast was grown in media containing asparagus extract, a control lacking nutrients, and a positive control with nutrients. Growth was measured using spectrophotometry and viable colony counts. Results showed the asparagus extract resulted in lower yeast growth than the positive control, indicating it inhibited proliferation. This supported the hypothesis that compounds in asparagus may slow the growth of cells.
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Tiffany Sato investigated whether asparagus can inhibit the population growth of yeast cells. She used yeast (Saccharomyces cerevisiae) as a model organism to study the anti-proliferative effects of asparagus due to similarities between yeast and cancer cells. Yeast growth was measured using spectrophotometry and viable colony counts. Results showed decreased yeast activity and fewer colonies with asparagus compared to positive controls, indicating asparagus can minimally inhibit yeast cell growth. This supports the hypothesis that asparagus compounds may reduce cancer cell proliferation.
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- 6. Can Asparagus inhibit population growth in yeast cells? YeastGrowth Activity with Spectrophotometer ViableColony Counts withAgar Plates
- 7. • 1%Yeast Extract • 2% Peptone • 1% Dextrose Positive (YPD+) • Water Negative (YPD-) • 1%Yeast Extract • 2% Peptone • 1% Dextrose • 50mL of Filtered Asparagus Experimental (YPDAsp)
- 8. Grow S. cerevisiae inYPD+,YPD-, YPDAsp Broths Incubated all cultures for hours Centrifuge all the different mediums Measured the absorbance of each using a spectrophotometer at Compared theYeast GrowthActivity wResults
- 9. For my agar plates, I inoculated a colony from a positive plate colony. Incubate for hours at Streak onto my three different plates: positive, negative and experimental Incubate for hours at RecordViable Colony Count Results
- 11. 0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1 0 2 4 6 8 10 12 Absorbance(600nm) Sample Numbers
- 19. Positive • Raised,Convex Surface Experimental • Flat Surface Negative • Produced no colonies
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