P_Products

The 1 kb PLUS™ is composed of 14 individual DNA fragments: 25K, 10K, 8K, 6K, 5K, 4K, 3K, 2.5K, 2K, 1500, 1000, 750, 500, 250 base pairs. This product contains two enhanced bands (3K and 1K bp) for easy reference. The ladder is ready-to-use, and is premixed with loading buffer dye for direct loading on gel.

A unique combination of PCR products and a number of proprietary plasmids digested with appropriate restriction enzymes to yield 12 fragments, suitable for use as molecular weight standards for agarose gel electrophoresis. The DNA includes fragments ranging from 100-3,000 base pairs. The 500 and 1,500 base pair bands have increased intensity to serve as reference points. The approximate mass of DNA in each band is provided (0.5 μg a load) for approximating the mass of DNA in comparably intense samples of similar size.The ladder is ready-to-use, and is premixed with loading buffer dye for direct loading on gel.

5X Passive Lysis Buffer is a concentrated cell lysis buffer that is designed for use with GoldBio’s Illumination™ Renilla Luciferase Enhanced Assay Kit.The kit is supplied with enough lysis buffer to perform the stated number of assays.This 5X Passive Lysis Buffer is sold separately for use with the kits when more lysis buffer is required.

5X Passive Lysis Buffer is not compatible with Firefly Luciferase or the Illumination™ Luciferase Enhanced Assay Kit.For Firefly luciferase assays, use 5X Luciferase Lysis Buffer (GoldBio Catalog # L-740).

This Buffer Set consists of:

- 5X Phosphate Buffer, pH8 (250 mM Phosphate buffer pH 8, 1.5 M NaCl)
- 25 mL 3M Recrystallized Imidazole Solution, pH 6.0

This Buffer set allows researchers to develop, wash and elute buffers for His-tag protein purification.

5X Phosphate Buffer, pH8 (250 mM Phosphate buffer pH 8, 1.5 M NaCl).

Phosphate Buffer, pH8 is a mix of Sodium Phosphate dibasic (Na2HPO4) and Monosodium Phosphate (NaH2PO4). This buffer is the basis for wash and elution buffers for protein purification through His-tag.

Biotin‐PEG4‐NHS Ester is a pegylated, highly hydrophilic biotinylation reagent for simple and efficient biotin labeling of antibodies, proteins and other primary amine-containing biomolecules.

Biotin‐PEG4‐NHS Ester reacts specifically and efficiently with primary amines (e.g., side chain of lysine residues or aminosilane-coated surfaces) at pH 7-9 to form covalent bonds. The hydrophilic polyethylene glycol (PEG) spacer arm of this reagent imparts water solubility that is transferred to the labeled molecule, thus reducing aggregation of labeled proteins stored in solution. The PEG spacer arm also gives the reagent a long and flexible connection to minimize steric hindrance involved with binding to avidin molecules.

Blazin' Blue™ Protein Gel Stain is a ready-to-use protein gel staining solution that is a safer and more effective replacement for traditional Coomassie stains. Blazin' Blue™ offers a faster alternative to protein staining (5-60 minutes) in a single step without the need for fixation or washing. Protein bands can be detected through visible blue staining or by near-infrared fluorescence. And since Blazin' Blue™ is aqueous based, there are no hazardous chemicals like methanol or acetic acid to worry about. Blazin' Blue™ Protein Gel Stain is certified under CCR Title 22 as non-toxic to the environment for drain disposal after a simple pH neutralization step.

Blazin' Bright™ Luminescent Protein Gel Stain is a ready-to-use luminescent protein gel staining solution that is a safer and more effective replacement for traditional fluorescent staining. Blazin' Bright™ offers a faster alternative to protein staining (5-60 minutes) in a single step without the need for fixation (destaining is optional). The Blazin' Bright™ gel stains are aqueous based, there are no hazardous chemicals like methanol or acetic acid to worry about. Blazin' Bright™ Protein Gel Stain is certified under CCR Title 22 as non-toxic to the environment for drain disposal after a simple pH neutralization step.

Blazin' Bright™ has a detection limit around 1-10 ng, depending on the detection method used (staining intensity varies between proteins) and does not cause gel shrinkage. Blazin' Bright™ staining is also fully compatible with mass spectrometry (MS) and Edman-based sequencing.

Blazin' Bright™ Luminescent UV Protein Gel Stain is a ready-to-use luminescent protein gel staining solution that is a safer and more effective replacement for traditional fluorescent staining. Gels stained with our Blazin' Bright™ Luminescent UV Protein Gel Stain can be visualized rapidly (5-30 minutes) in a single step without fixation (destaining is optional). The Blazin' Bright™ gel stains are aqueous based, there are no hazardous chemicals like methanol or acetic acid to worry about. Blazin' Bright™ Protein Gel Stain is certified under CCR Title 22 as non-toxic to the environment for drain disposal after a simple pH neutralization step.

Blazin' Bright™ Luminescent UV has a detection limit around 1-10 ng, depending on the detection method used (staining intensity varies between proteins) and does not cause gel shrinkage. Blazin' Bright™ staining is also fully compatible with mass spectrometry (MS) and Edman-based sequencing.

The BLUEstain™ 2 Protein ladder is a three-color protein standard with 13 prestained proteins, covering a wide range molecular weights from 3.5 to 245 kDa. Proteins are covalently coupled with a blue chromophore except for two reference bands (one green and one red band at 25 kDa and 75 kDa respectively) when separated on SDS-PAGE (Tris-glycine buffer).

The BLUEstain™ 2 Protein ladder is designed for monitoring protein separation during SDS-polyacrylamide gel electrophoresis, verification of Western transfer efficiency on membranes (PVDF, nylon, or nitrocellulose) and for approximating the size of proteins. The ladder is supplied in gel loading buffer and is ready to use. Do not heat, dilute or add reducing agent before loading.

The BLUEstain™ Protein ladder is a three-color protein standard with 12 prestained proteins covering a wide range molecular weights from ~11 to 245 kDa. Proteins are covalently coupled with a bluechromophore except for two reference bands (one green and one red band at 25 kDa and 75 kDa respectively) when separated on SDS-PAGE (Tris-glycine buffer). The BLUEstain™ Protein ladder, is designed for monitoring protein separation during SDS-polyacrylamide gel electrophoresis, verification of Western transfer efficiency on membranes (PVDF, nylon, or nitrocellulose) and for approximating the size of proteins. The ladder is supplied in gel loading buffer and is ready to use.

Proline and its derivatives are often used as asymmetric catalysts in organic reactions. The CBS reduction and proline catalysed aldol condensation are prominent examples. L-Proline is an osmoprotectant, and therefore is used in many pharmaceutical, biotechnological applications.

Hepatitis B virus (HBV) is an infectious, and potentially fatal, human disease that causes serious liver disease. There are three start codons on the Gene S HBV surface protein antigen (HBsAg) that divide the gene into three sections: pre-S1, pre-S2, and S. These start sites create three carboxyl, coterminal polypeptides that are called large (LHB, the order from surface to the inside: pre-S1, pre-S2, and S), middle (MHB, containing the pre-S2 and S portion) and small (SHB, covering only the S portion). The pre-S1 amino acid region of LHBs consists of 119 amino acids and has been shown to interact with its human binding partner, γ2-adaptin, to subvert the membrane-trafficking apparatus to mediate virion export. HBsAg-PreS1 can be used for Immunochromatography, monoclonal and polyclonal antibody preparation or for ELISA analysis.

Horseradish peroxidase (HRP) is the most commonly used antibody-conjugated enzyme. Substrates for HRP are luminol and benzidine substrates. Tetramethylbenzidine (TMB) and similar substrates are oxidized by HRP in the presence of hydrogen peroxide, or nontoxic substitutes, to yield a chinoid structure of intense blue color.

Interleukin-1 beta (IL1B) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological and hematopoietic activities, and plays one of the central roles in the regulation of immune responses. Both IL1A and IL1B bind to the same receptor and have similar biological properties. Recombinant porcine IL1B shares 63-70% amino acid sequence identity with canine, cotton rat, equine, feline, human, mouse, rat and rhesus IL1B.

IL1RN, initially called the IL1 inhibitor, is encoded by the IL1RN gene and is a member of the interleukin 1 cytokine family. IL1RN is secreted by various types of cells including immune cells, epithelial cells, and adipocytes. ILRN functions to inhibit the activity of IL1 by binding to receptor IL1R1, preventing its association with the co-receptor IL1RAP for signaling. IL1RN is also used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL1 plays a key role. The porcine IL1RN is a single non-glycosylated polypeptide chain that has been shown to block the inflammatory responses induced by IL1 both in vitro and in vivo.

IL2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. It is expressed by CD4+ and CD8+ T-cells, γδ T-cells, B-cells, dendritic cells, and eosinophils. The receptor for IL2 (IL2R) consists of three subunits (55 kDa IL2RI, 75 kDa IL2RJ, 64 kDa common gamma chain Gc/IL2RG) that are present on the cell surface in varying preformed complexes. IL2/IL2R signaling is required for T-cell proliferation and other fundamental functions which are essential for an immune response. Recombinant porcine IL2 shares about 72% amino acid sequence identity with mouse, human and rat IL2. It also shares 60% and 67% acid sequence identity with rhesus macaque and Equus caballus IL2, respectively.

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.

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.