Biosystems RapidFinder Shiga Toxin-Producing E. coli
Parameter identifiability evaluation and visualization in large-scale kinetic fashions of biosystems.
BACKGROUND
Kinetic fashions of biochemical methods normally include odd differential equations which have many unknown parameters. A few of these parameters are sometimes virtually unidentifiable, that’s, their values can’t be uniquely decided from the out there knowledge.
Attainable causes are lack of affect on the measured outputs, interdependence amongst parameters, and poor knowledge high quality. Uncorrelated parameters might be seen as the important thing tuning knobs of a predictive mannequin. Due to this fact, earlier than making an attempt to carry out parameter estimation (mannequin calibration) it is very important characterize the subset(s) of identifiable parameters and their interaction. As soon as that is achieved, it’s nonetheless essential to carry out parameter estimation, which poses further challenges.
METHODS
We current a technique that (i) detects high-order relationships amongst parameters, and (ii) visualizes the outcomes to facilitate additional evaluation. We use a collinearity index to quantify the correlation between parameters in a gaggle in a computationally environment friendly method. Then we apply integer optimization to search out the biggest teams of uncorrelated parameters. We additionally use the collinearity index to establish small teams of extremely correlated parameters. The outcomes recordsdata might be visualized utilizing Cytoscape, exhibiting the identifiable and non-identifiable teams of parameters along with the mannequin construction in the identical graph.
RESULTS
Our contributions alleviate the difficulties that seem at totally different levels of the identifiability evaluation and parameter estimation course of. We present easy methods to mix world optimization and regularization methods for calibrating medium and huge scale organic fashions with average computation occasions.
Then we consider the sensible identifiability of the estimated parameters utilizing the proposed methodology. The identifiability evaluation methods are applied as a MATLAB toolbox known as VisId, which is freely out there as open supply from GitHub ( https://github.com/gabora/visid ).
CONCLUSIONS
Our strategy is geared in the direction of scalability. It permits the sensible identifiability evaluation of dynamic fashions of enormous dimension, and accelerates their calibration. The visualization device permits modellers to detect elements which might be problematic and want refinement or reformulation, and offers experimentalists with info that may be useful within the design of recent experiments.
Validation of the Utilized Biosystems RapidFinder Shiga Toxin-Producing E. coli (STEC) Detection Workflow.
The Utilized Biosystems™ RapidFinder™ STEC Detection Workflow (Thermo Fisher Scientific) is a whole protocol for the speedy qualitative detection of Escherichia coli (E. coli) O157:H7 and the “Huge 6” non-O157 Shiga-like toxin-producing E. coli (STEC) serotypes (outlined as serogroups: O26, O45, O103, O111, O121, and O145).
The RapidFinder STEC Detection Workflow makes use of both the automated preparation of PCR-ready DNA utilizing the Utilized Biosystems PrepSEQ™ Nucleic Acid Extraction Package along side the Utilized Biosystems MagMAX™ Specific 96-well magnetic particle processor or the Utilized Biosystems PrepSEQ Speedy Spin equipment for handbook preparation of PCR-ready DNA.
Two separate assays comprise the RapidFinder STEC Detection Workflow, the Utilized Biosystems RapidFinder STEC Screening Assay and the Utilized Biosystems RapidFinder STEC Affirmation Assay. The RapidFinder STEC Screening Assay contains primers and probes to detect the presence of stx1 (Shiga toxin 1), stx2 (Shiga toxin 2), eae (intimin), and E. coli O157 gene targets. The RapidFinder STEC Affirmation Assay contains primers and probes for the “Huge 6″ non-O157 STEC and E. coli O157:H7. Using these two assays in tandem permits a person to detect precisely the presence of the “Huge 6” STECs and E. coli O157:H7. The efficiency of the RapidFinder STEC Detection Workflow was evaluated in a technique comparability research, in inclusivity and exclusivity research, and in a robustness analysis.
The assays had been in comparison with the U.S. Division of Agriculture (USDA), Meals Security and Inspection Service (FSIS) Microbiology Laboratory Guidebook (MLG) 5.09: Detection, Isolation and Identification of Escherichia coli O157:H7 from Meat Merchandise and Carcass and Environmental Sponges for uncooked floor beef (73% lean) and USDA/FSIS-MLG 5B.05: Detection, Isolation and Identification of Escherichia coli non-O157:H7 from Meat Merchandise and Carcass and Environmental Sponges for uncooked beef trim. No statistically important variations had been noticed between the reference methodology and the person or mixed kits forming the candidate assay utilizing both of the DNA preparation kits (handbook or automated extraction). For the inclusivity and exclusivity analysis, the RapidFinder STEC Detection Workflow, comprising each RapidFinder STEC screening and affirmation kits, accurately recognized all 50 goal organism isolates and accurately excluded all 30 nontarget strains for each of the assays evaluated.
The outcomes of those research reveal the sensitivity and selectivity of the RapidFinder STEC Detection Workflow for the detection of E. coli O157:H7 and the “Huge 6” STEC serotypes in each uncooked floor beef and beef trim. The robustness testing demonstrated that minor variations within the methodology parameters didn’t influence the accuracy of the assay and highlighted the significance of following the right incubation temperatures.
Description: Thymus chemokine-1 (TCK-1 or CXCL7)) is a member of the CXC subfamily of chemokines. Mouse TCK-1 shares 72% amino acid sequence identity with rat TCK-1.
Description: NAP-2 or CXCL7 is a CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is produced in leukocytes by enzymatic processing of a precursor called platelet basic protein (PBP). NAP-2 chemoattracts and activates neutrophils. Recombinant human NAP-2 protein is a 7.6 kDa protein containing 70 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines, and also including the ELR motif common to CXC chemokines that bind to CXCR1 and CXCR2.
Description: NAP-2 is a CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is produced in leukocytes by enzymatic processing of a precursor called platelet basic protein (PBP). NAP-2 chemoattracts and activates neutrophils. Recombinant human NAP-2 protein is a 7-8 kDa protein containing 70 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines, and also including the ELR motif common to CXC chemokines that bind to CXCR1 and CXCR2.
Description: Neutrophil Activating Peptide 2 (NAP2), Connective Tissue Activating Protein III (CTAPIII) and βthrombogulin ( βTG), are proteolytically processed carboxylterminal fragments of platelet basic protein (PBP) which is found in the alphagranules of human platelets. NAP2 is a member of the CXC chemokines. Similar to other ELR domain containing CXC chemokines such as IL8 and the GRO proteins, NAP2 has been shown to bind CXCR2 and to chemoattract and activate neutrophils. Although CTAPIII, βTG and PBP represent aminoterminal extended variants of NAP 2 and possess the same CXC chemokine domains, these proteins do not exhibit NAP2 activity. It has been shown that the additional aminoterminal residues of CTAP III masks the critical ELR receptor binding domain that is exposed on NAP2 and may account for lack of NAP2 activity.
Description: NAP-2 is a CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is produced in leukocytes by enzymatic processing of a precursor called platelet basic protein (PBP). NAP-2 chemoattracts and activates neutrophils. Recombinant human NAP-2 protein is a 7-8 kDa protein containing 70 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines, and also including the ELR motif common to CXC chemokines that bind to CXCR1 and CXCR2.
Mouse Pro-Platelet Basic Protein (CXCL7) ELISA Kit
Description: A sandwich ELISA kit for quantitative measurement of Mouse ?TG/PBP/CXCL7/NAP2 (Thromboglobulin, Beta) in samples from Serum, Plasma, Cell supernatant
Description: Chemokine (C-X-C motif) ligand 7 (CXCL7), also known as NAP-2 or Pro-Platelet basic protein (PPBP), is a human gene. The protein encoded by this gene is a platelet-derived growth factor that belongs to the CXC chemokine family. This growth factor is a potent chemoattractant and activator of neutrophils. It has been shown to stimulate various cellular processes including DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by synovial cells. Furthermore, the protein is an antimicrobial protein with bactericidal and antifungal activity.
Description: Recombinant NAP-2 is a disulfide-linked monomeric protein consisting of 71 amino acid residues and migrates as an approximately 8 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human NAP-2 (CXCL7) mature chain was expressed in E. coli.
Description: Recombinant NAP-2 is a disulfide-linked monomeric protein consisting of 71 amino acid residues and migrates as an approximately 8 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human NAP-2 (CXCL7) mature chain was expressed in E. coli.
Description: Human Chemokine (C-X-C motif) Ligand 7 (CXCL7), also known as neutrophil activating peptide 2 (NAP-2), is a member of the CXC chemokines containing an ELR domain (Glu-Leu-Arg tripeptide motif). Similar to other ELR domain containing CXC chemokines, such as IL-8 and the GRO proteins, CXCL7 binds CXCR2, chemoattracts and activates neutrophils. CXCL7, Connective Tissue Activating Protein III (CTAPIII) and beta thrombogulin ( beta TG), are proteolytically processed carboxylterminal fragments of platelet basic protein (PBP) which is found in the alphagranules of human platelets. Although CTAPIII, beta TG, and PBP represent amino-terminal extended variants of NAP2 and possess the same CXC chemokine domains, these proteins do not exhibit CXCL7/NAP2 activity. CXCL7 induces cell migration through the G-protein-linked receptor CXCR-2.
Description: Human Chemokine (C-X-C motif) Ligand 7 (CXCL7), also known as neutrophil activating peptide 2 (NAP-2), is a member of the CXC chemokines containing an ELR domain (Glu-Leu-Arg tripeptide motif). Similar to other ELR domain containing CXC chemokines, such as IL-8 and the GRO proteins, CXCL7 binds CXCR2, chemoattracts and activates neutrophils. CXCL7, Connective Tissue Activating Protein III (CTAPIII) and beta thrombogulin ( beta TG), are proteolytically processed carboxylterminal fragments of platelet basic protein (PBP) which is found in the alphagranules of human platelets. Although CTAPIII, beta TG, and PBP represent amino-terminal extended variants of NAP2 and possess the same CXC chemokine domains, these proteins do not exhibit CXCL7/NAP2 activity. CXCL7 induces cell migration through the G-protein-linked receptor CXCR-2.
Description: Chemokine (C-X-C motif) ligand 7 (CXCL7), also known as NAP2 or Pro-Platelet basic protein (PPBP), is a human gene. The protein encoded by this gene is a platelet-derived growth factor that belongs to the CXC chemokine family. This growth factor is a potent chemoattractant and activator of neutrophils. It has been shown to stimulate various cellular processes including DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by synovial cells. Furthermore, the protein is an antimicrobial protein with bactericidal and antifungal activity.
Description: The EC50 value of Rat NAP-2/CXCL7on Caˆ2+ mobilization assay in CHO-K1/Gα15/rCXCR2 cells (human Gα15 and Rat CXCR2 stably expressed in CHO-K1 cells) is less than 200 ng/ml.
Description: The EC50 value of rat Thymus Chemokine‑1/CXCL7 on Caˆ2+ mobilization assay in CHO-K1/Gα15/rCXCR2 cells (human Gα15 and rat CXCR2 stably expressed in CHO-K1 cells) is less than 300 ng/ml.
Validation of the Utilized Biosystems 7500 Quick Instrument for Detection of Listeria monocytogenes with the SureTect Listeria monocytogenes PCR Assay.
In 2013, the Thermo Scientific™ SureTect™ Listeria monocytogenes Actual-Time PCR Assay was licensed by the AOAC Analysis Institute (RI) Efficiency Examined Strategies(SM) program as a speedy methodology for the detection of L. monocytogenes from a variety of meals matrixes and floor samples.
This report particulars the tactic modification research undertaken to increase the evaluation of this PCR assay to the Utilized Biosystems™ 7500 Quick PCR Instrument and Utilized Biosystems RapidFinder™ Specific 2.zero software permitting the usage of the SureTect assay on a 96 effectively format PCR cycler along with the present workflow, which makes use of the 24 effectively Thermo Scientific PikoReal™ PCR Instrument and Thermo Scientific SureTect software program.
As a result of this research was deemed by AOAC-RI to be a degree 2 methodology modification research, a consultant vary of meals matrixes overlaying uncooked floor turkey, 2% fats pasteurized milk, and bagged lettuce in addition to chrome steel floor samples had been analyzed with the Utilized Biosystems 7500 Quick PCR Instrument and RapidFinder Specific 2.zero software program.
All testing was carried out compared to the reference methodology detailed in Worldwide Group for Standardization (ISO) 6579:2002. No important distinction by likelihood of detection statistical evaluation was discovered between the SureTect Listeria monocytogenes PCR Assay or the ISO reference methodology strategies for any of the matrixes analyzed throughout the research.
Validation of the Utilized Biosystems 7500 Quick Instrument for the Detection of Salmonellae with SureTect Salmonella Species PCR Package.
The Thermo Scientific SureTect™ Salmonella species real-time PCR assay is a speedy various methodology designed for the detection of salmonellae in a variety of meals, animal feeds, and production-environment samples. The assay has beforehand been validated in accordance with the AOAC Analysis Institute Efficiency Examined Strategies(SM) program utilizing Thermo Scientific PikoReal PCR cycler and Thermo Scientific SureTect Software program Efficiency Examined Methodology 051303).
This report particulars the method-modification research carried out to validate an up to date assay format, using a diminished goal probe focus and an extension of the PCR cycler platform to allow the usage of the equipment with a Utilized Biosystems 7500 Quick PCR cycler and Utilized Biosystems RapidFinder™ Specific 2.zero software program.
Throughout this validation research, a matrix research was carried out on a subset of the tactic’s claimed matrixes, evaluating the efficiency of the modified SureTect Salmonella species equipment (a diminished goal probe focus with a 7500 Quick platform) to the reference methodology detailed in ISO 6579:2002.
No important distinction by likelihood of detection statistical evaluation was discovered between SureTect or Worldwide Group for Standardization strategies for any of the matrixes analyzed throughout the research. Inclusivity and exclusivity research utilizing the modified methodology demonstrated correct outcomes for the 117 Salmonella and 36 non-Salmonella strains examined. A number of manufacturing plenty of the newly formatted equipment had been evaluated and located to be in step with the present assay. Robustness research confirmed that the change to the equipment had no influence on the assay’s efficiency when alterations had been made to methodology parameters having the best potential influence on assay efficiency.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 26.1 kDa protein consisting of 238 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 26.1 kDa protein consisting of 238 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
*Manufactured using (BTI-Tn-5B1-4) cells under license from the Boyce Thompson Institute for Plant Research, Inc.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 565.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 633.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 655.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 680.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 700.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to APC/Cy7.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 350.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 405.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 488.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 594.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 633.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to PE/ATTO 594.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Streptavidin.
Insulin-Like Growth Factor II, Recombinant, Human (Human IGF-II, IGF-II, IGFII, IGFII, IGF2, IGF-2, IGF 2)
Description: Recombinant Human Cytotoxic T-lymphocyte Protein 4 is produced by our Mammalian expression system and the target gene encoding Lys36-Asp161 is expressed with a Flag tag at the C-terminus.
