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Interleukin 8 (IL8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. IL8 is also synthesized by endothelial cells, and then stored in vesicles. There are many receptors capable of binding to IL8; however, the receptors that have the greatest affinity are CXCR1 and CXCR2. As a member of the CXC chemokine family, IL8 is a player in the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils and T-cells. IL8 is often associated with inflammation and has been cited as a pro-inflammatory mediator in gingivitis and psoriasis.

Interleukin-8 (IL8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. IL8 is synthesized by endothelial cells, which stock IL8 in their storage vesicles. There are many receptors capable of binding to IL8; however, the molecules with the highest affinity to IL8 are receptors CXCR1 and CXCR2. As a member of the CXC chemokine family, one of the functions of IL8 is the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils, and T-cells. IL8 (72a.a.) has a 5-10-fold higher activity on neutrophil activation compared to IL8 (77 a.a.). IL8 is often associated with inflammation, and has been cited as a pro-inflammatory mediator in gingivitis and psoriasis.

Interleukin-8 (IL8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. There are many receptors capable of binding to IL8; however, the molecules with the highest affinity to IL8 are receptors CXCR1 and CXCR2. As a member of the CXC chemokine family, one of the functions of IL8 is the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils and T-cells. IL8 (72a.a.) has a 5-10-fold higher activity on neutrophil activation, compared to IL8 (77 a.a.). IL8 is often associated with inflammation, and has been cited as a pro-inflammatory mediator in gingivitis and psoriasis.

Interleukin-8 (IL8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. IL8 is also synthesized by endothelial cells, and then stored in vesicles. There are many receptors capable of binding to IL8; however, the receptors that have the greatest affinity are CXCR1 and CXCR2. As a member of the CXC chemokine family, IL8 is a player in the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils and T-cells. IL8 is often associated with inflammation and has been cited as a pro-inflammatory mediator in gingivitis and psoriasis.

Interleukin-8 (C-X-C motif chemokine 8) is coded by the interleukin 8 gene on chromosome 5 in Rhesus macaque (Macaca mulatta), which is not only 94% identical to human IL8, but also structurally and functionally similar with human IL8. IL8 also provides a valuable resource for a model of inflammation in primates.

Interleukin-9 (IL9) is encoded by the IL9 gene and is produced by T-cells and specifically by CD4+ helper cells. IL9 was originally identified as a cytokine found in the conditioned medium of a human T-cell leukemia virus type I (HTLVI) transformed T-cell line. IL9 functions through the IL-9 receptor, which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. IL9 can support the growth of IL-2 independent and IL4 independent helper T-cells. Human IL9 has approximately 56% amino acid sequence identity with murine IL9. The gene encoding this cytokine has been identified as a candidate gene for asthma. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.

Interleukin-9 (IL9) is encoded by the IL9 gene and is produced by T-cells and specifically by CD4+ helper cells. IL9 was originally identified as a cytokine found in the conditioned medium of a human T-cell leukemia virus type I (HTLVI) transformed T-cell line. IL9 functions through the IL-9 receptor, which activates different signal transducer and activator (STAT) proteins and thus connects this pleiotropic cytokine to various biological processes. IL9 can support the growth of IL2 independent and IL4 independent helper T-cells. The gene encoding this cytokine has been identified as a candidate gene for asthma. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.

GoldBio’s Illumination™ Renilla Luciferase Enhanced Assay Kit is specifically designed for the measurement of Renilla luciferase in transfected cell reporter gene assays. This kit is enhanced with a water soluble coelenterazine that is easier to use and store than other conventional coelenterazine products.

Renilla luciferase is a commonly used bioluminescent reporter gene that is used to study gene regulation and function both in vivo as well as in vitro. Renilla luciferase is a monomeric 36 kDa protein isolated from the sea pansy, Renilla reniformis, which catalyzes coelenterazine with oxygen to produce a blue light (480 nm). There is no need for any post-translational modifications and the protein may be used as a gene reporter immediately after translation. Our Enhanced Assay Kit includes a special buffer which is designed to yield reliable, linear measurements of Renilla luciferase activity with maximum sensitivity and minimal autoluminescence. This kit is a flash-type luminescent assay, and requires measurement immediately after adding the substrate to the sample.

One Assay can be performed in a single tube or an individual well on a 96 well plate. The kits include enough Passive Lysis Buffer to perform the stated number of assays in plate sizes ranging from 96-well to 24-well. If needed, additional 5X Passive Lysis Buffer (GoldBio Catalog # L-745) can be purchased separately.

GoldBio’s Illumination™ Dura-Luc Lyophilized Firefly HTS Assay Kit contains a proprietary formulation that modifies and stabilizes the enzymatic reaction to produce a long lasting bioluminescent signal by preventing the formation of adenyl-oxyluciferin at the enzyme surface. The Dura-Luc system is a highly sensitive and homogenous luciferase reporter assay that has a signal half-life of three hours for the best quantification of expression in mammalian cell lines, allowing for batch processing and plate to plate comparisons in high-throughput screening experiments.

Firefly Luciferase Assays are one of the leading reporter assays in the world in the measurement of gene function and gene regulation as well as being widely used in pharmaceutical screening. The luciferase assays are sensitive and convenient due to the absence of endogenous luciferase activity in most cell types and tissue. Firefly luciferase is a monomeric 62 kDa protein typically isolated from the firefly, Photinus pyralis, which catalyzes the ATP-dependent D-luciferin in the presence of oxygen and Mg2+ to oxyluciferin producing a yellow to greenish light (~560 nm).

The Dura-Luc Lyophilized Firefly Kit contains an assay buffer that is provided in a lyophilized form for economical shipping and more convenient storage. A reconstitution buffer is also provided with this kit.

GoldBio’s Illumination™ Firefly & Renilla Luciferase Enhanced Assay Kit is a combined luciferase assay allowing the sequential measurement of Firefly and Renilla luciferase activity in the same sample while still retaining the highest degree of sensitivity, reliability and linearity that you want in your assay. Firefly activity is measured first, then the Renilla Luciferase Assay Buffer is added to the sample to simultaneously extinguish all firefly luciferase activity to the level of untransformed cells and begins the Renilla luciferase activity. This great luciferase combo allows the sequential measurement of both luciferase assays in the same sample without additional hassle.

This kit is a flash-type luminescent assay, and requires measurement immediately after adding the detection reagents to the sample. The Enhanced Assay Kit includes our water soluble coelenterazine that is easier to use and store than other conventional coelenterazine products.

One Assay can be performed in a single tube or an individual well on a 96 well plate. The kits include enough Passive Lysis Buffer to perform the stated number of assays in plate sizes ranging from 96-well to 24-well.

Kit components

• 1X Passive Lysis Buffer
• Firefly Luciferase Assay Buffer
• Renilla Luciferase Assay Buffer
• GoldBio D-Luciferin
• GoldBio Enhanced Coelenterazine

GoldBio’s Illumination™ Firefly Luciferase Enhanced Assay Kit is specifically designed for the simple and efficient quantification of firefly luciferase reporter enzyme activity from cultured cells with the highest degree of sensitivity, reliability and linearity. This kit is a flash-type luminescent assay, and requires measurement immediately after adding the substrate to the sample.Our Enhanced Assay Kit includes our improved 5X Luciferase Lysis Buffer which provides a better working solution stability compared to other firefly assay kits.

One Assay can be performed in a single tube or an individual well on a 96 well plate. The kits include enough Luciferase Lysis Buffer to perform the stated number of assays in plate sizes ranging from 96-well to 24-well. If needed, additional 5X Luciferase Lysis Buffer (GoldBio Catalog # L-740) can be purchased separately.

Kit components

• 5X Luciferase Lysis Buffer
• Firefly Luciferase Assay Buffer
• GoldBio D-Luciferin

GoldBio’s Illumination™ Lyophilized Firefly Luciferase Enhanced Assay Kit is specifically designed for the simple and efficient quantification of firefly luciferase reporter enzyme activity from cultured cells with the highest degree of sensitivity, reliability and linearity. In addition, the Firefly Luciferase Assay Buffer is lyophilized for more convenient shipping and storage.

This kit is a flash-type luminescent assay, and requires measurement immediately after adding the substrate to the sample.Our Enhanced Assay Kit includes our improved 5X Luciferase Lysis Buffer which provides a better working solution stability compared to other firefly assay kits.

One Assay can be performed in a single tube or an individual well on a 96 well plate. The kits include enough Luciferase Lysis Buffer to perform the stated number of assays in plate sizes ranging from 96-well to 24-well. If needed, additional 5X Luciferase Lysis Buffer (GoldBio Catalog # L-740) can be purchased separately.

Kit components

• 5X Luciferase Lysis Buffer
• Firefly Luciferase Assay Buffer (lyophilized)
• GoldBio D-Luciferin

Imazapyr is imidazolinone family herbicide that has been used to research herbicidal resistances and biochemical pathways in an array of plants. This compound has been shown to uncompetitively inhibit acetolactate synthase (ALS) which catalyzes the production of the amino acids valine, leucine and isoleucine. Loss of these specific amino acids depletes physiologically important proteins and enzymes, eventually resulting in cell death.

Imidazole is a planar 5-membered ring. It is a highly polar, highly water soluble amphoteric compound. Imidazole is often used to elute tagged proteins bound to metal ions attached to the surface of beads in a chromatography column by displacing the His-tag from the metal ion and freeing the His-tagged proteins.

Imidazole is a planar 5-membered ring. It is a highly polar, highly water soluble amphoteric compound. Imidazole is often used to elute tagged proteins bound to metal ions attached to the surface of beads in a chromatography column by displacing the His-tag from the metal ion and freeing the His-tagged proteins.

Iminodiacetic acid is a dicarboxylic acid amine used to regulate peptide mobility through capillary electrophoresis. It forms complexes that are stronger than glycine but weaker than nitrilotriacetic acid.

Imipenem is a carbapenem β-lactam antibiotic with a broad target spectrum. It has been shown to be effective against ESBL-producing Enterobacteriaceae and gram-negative and gram-positive organisms. Imipenem has also been shown to be effective against bacteria from the genus Burkholderia. Resistance to imipenem is conferred through the loss of the OprD porin protein.

Ficin is a cysteine protease enzyme which is derived from the latex of fig trees with activity similar to other cysteine protease enzymes including endopeptidases, aminopeptidases, and dipeptidyl peptidases. Ficin cleaves mouse immunoglobulin G molecules (IgG1) in the hinge region. The concentration of cysteine changes how ficin cleaves IgG1. A F(ab’)2 fragment is formed in the presence of 1mM cysteine. The F(ab’)2 fragments are smaller than whole IgG molecules and better penetrate tissue for antigen recognition while avoiding unspecific binding to Fc receptors. In the presence of 10mM cysteine, two 2 Fab fragments are produced instead. F(ab) fragments block background from primary antibody binding, and block endogenous and exposed immunoglobulins and tissues in labeling experiments.

Immobilized Ficin Agarose Resin offers a convenient solution to the production of F(ab’)2 and Fab fragments while eliminating autolysis and protease contamination and the need to remove the enzymes following digestion. Fab and F(ab’)2 can be further separated from whole IgG with either Protein A Agarose Resin (GoldBio Product # P-400) or ion exchange chromatography.

Activity:1-1.5 mg ficin/ml of resin

Support: 6% Cross-linked Agarose

Storage/Handling: Shipped at ambient temperature. Upon receipt, store at 4°C, do NOT freeze.

Papain is a cysteine protease enzyme from papaya latex that has a wide variety of activities including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endo-peptidase activity. In particular, papain cleaves immunoglobulin G (IgG) molecules near the hinge region of the antibody, resulting in three similar, ~50 kDa, fragments; an Fc domain and two monovalent Fab domains. This papain-digested antibody is therefore unable to promote agglutination, precipitation, opsonization or lysis. The Fc fragment can then be used to determine the specificity of the Fc receptors without any typical antigen binging interference while the Fab fragments can be used in immunohistochemical studies.

Pepsin, one of the principal digestion enzymes, breaks down proteins in to smaller peptides. It is most efficient in cleaving the peptide bonds between hydrophobic and aromatic amino acids such as phenylalanine, tryptophan and tyrosine. Pepsin readily cleaves immunoglobulin G (IgG) molecules, generating F(ab’)2 fragments and small Fc peptide fragments. The smaller Fc fragments can be easily removed via gel filtration while the F(ab’)2 fragments can then be purified from any remaining, undigested IgG. The F(ab’)2 fragments are highly useful for research interests, being able to penetrate tissue better than standard IgG antibodies and facilitate better antigen recognition while avoiding unspecific binding to Fc receptors.

Immobilized Pepsin Agarose Resin is an efficient method for producing F(ab’)2 fragments from IgG molecules for antibody mimetic. Undigested IgG can be quickly removed with our Protein A Agarose Resin (GoldBio Catalog # P-400). Fc fragments can also be removed using a gel filtration system.

Resin: 6% Cross-linked Agarose

Shipping/Handling: Shipped at ambient temperature. Upon receipt, store at 4°C, do NOT freeze.