Reporter Proteins Catalog

REPORTER PROTEINS

RNA ENCODED PROTEIN SPECIES CATALOG NUMBER FROM PRICE
BioCapTM GFP mRNA Green fluorescent protein Aequorea victoria (Jellyfish) 1500101 100 ug $275
BioCapTM GFP NLS mRNA Green fluorescent protein NLS Aequorea victoria (Jellyfish) 1500201 100 ug $325
BioCapTM mCherry mRNA mCherry Anaplasma marginale 1500301 100 ug $275
BioCapTM mCherry-NLS mRNA mCherry NLS Anaplasma marginale 1500801 100 ug $445
BioCapTM fLuc mRNA Firefly luciferase Firefly 1500401 100 ug $250
BioCapTM rLuc mRNA Renilla luciferase Renilla muelleri (Sea pansy) 1500501 100 ug $320
BioCapTM gLuc mRNA Gaussia luciferase Gaussia princeps 1500601 500 ug $1,155.50
BioCapTM GLB1 mRNA Beta-galactosidase Human 1500701 500 ug $1,155.50

REPORTER PROTEINS

A readily detectable protein that is not typically present in your research system is referred to as a reporter protein. For instance, if you were researching bacteria, you wouldn’t want to use a bacterial protein as a reporter. There are numerous widely used reporter proteins, including beta galactosidase (encoded by the bacterial gene lacZ); luciferase; chloramphenicol acetyltransferase (CAT), which is frequently used in the chapter on single genome circuits; GUS (beta glucuronidase), which is frequently used in plants; and green fluorescent protein (GFP, from jellyfish).

The bacterium gene lacZ encodes beta galactosidase, one of the first and most well-known reporter proteins. Lactose (milk sugar), a disaccharide, is broken down by bacteria’s beta galactosidase enzyme into glucose and galactose.The colorless precursor X-gal is broken down by the enzyme β-galactosidase into galactose and an insoluble blue byproduct. LacZ can be used as a reporter gene because lacZ is not present in the majority of chromosomes.

BioCapTM GFP mRNA

Protein

Green fluorescent protein

Gene

GFP

Status

UniProtKB reviewed (Swiss-Prot)

Organism

Aequorea victoria (Water jellyfish) (Mesonema victoria)

Amino acids

238

Protein existence

Evidence at protein level

A huge variety of different colored mutations, fusion proteins, and biosensors have been created using green fluorescent protein engineering. Different colors of green fluorescent protein can be produced by mutations. In order to create chimeric proteins, where they serve as a fluorescent protein tag, fluorescent proteins and their mutated allelic forms have evolved into a practical and common instrument. The majority of the time, they accept N- and C-terminal fusing to a wide range of proteins.

BioCapTM GFP NLS mRNA

Protein

Green fluorescent protein

Gene

GFP

Status

UniProtKB reviewed (Swiss-Prot)

Organism

Aequorea victoria (Water jellyfish) (Mesonema victoria)

Amino acids

238

Protein existence

Evidence at the protein level

A huge variety of different coloured mutations, fusion proteins, and biosensors have been created using green fluorescent protein engineering. It is possible to mutate green fluorescent protein to produce light at various wavelengths. They serve as acceptors of energy transmission. Using energy transfer, it converts aequorin’s blue chemiluminescence to green fluorescent light, receives energy from the Ca2+-activated photoprotein aequorin, and fluoresces in living tissue.

BioCapTM mCherry mRNA

Protein

MCherry fluorescent protein

Gene

mCherry

Status

UniProtKB unreviewed (TrEMBL)

Organism

Anaplasma marginale

Amino acids

236

Protein existence

Evidence at the protein level

The red glowing protein mCherry is encoded by the mCherry mRNA. The red fluorescent protein DsRed, which is isolated from the marine anemone, is the source of mCherry (Discosoma). The monomeric fluorescence mCherry has a maximum emission wavelength of 610 nm and a maximum absorption wavelength of 587 nm. In biology, mCherry is frequently used for cell component placement and molecular markers due to its high photostability.

BioCapTM fLuc mRNA

Protein

Luciferin 4-monooxygenase

Gene

luc

Status

UniProtKB unreviewed (TrEMBL)

Organism

Photinus pyralis (Common eastern firefly) (Lampyris pyralis)

Amino acids

550

Protein existence

Inferred from homology

The firefly luciferase protein is encoded by the FLuc mRNA, which has been specifically engineered for maximum in vitro production and luminescence. The thorough purification procedure eliminates dsRNA impurities and other reaction elements, producing highly pure mRNA that can induce extremely high amounts of protein expression in a variety of cell types with very little cellular innate immune activation (virtually undetectable).

BioCapTM rLuc mRNA

Protein

Luciferase 1

Gene

Luc1

Status

UniProtKB unreviewed (TrEMBL)

Organism

Renilla muelleri (Sea pansy)

Amino acids

311

Protein existence

Evidence at transcript level

Renilla Luciferase protein will be expressed at a high amount when R-Luc mRNA is used, according to design. They are created through in vitro transcription, and changed nucleotides capping stabilizes the 5′ end. (Cap1). These mature mRNAs are designed to produce better stability and efficacy and include a poly(A) tail at the 3′ end.

BioCapTM gLuc mRNA

Protein

Luciferase

Status

UniProtKB unreviewed (TrEMBL)

Organism

Gaussia princeps

Amino acids

185

Protein existence

Evidence at the protein level

The elevated expression level of Gaussia princeps protein is produced by the G-Luc mRNA. In vitro transcription is used to create them. 

BioCapTM GLB1 mRNA

Protein

Beta-galactosidase

Gene

GLB1

Status

UniProtKB reviewed (Swiss-Prot)

Organism

Homo sapiens (Human)

Amino acids

677

Protein existence

Evidence at protein level

Isoform 1: cleaves glycosaminoglycans, glycoproteins, and gangliosides’ beta-linked terminal galactosyl residues.

Isoform 2: has no beta-galactosidase enzymatic activity but is essential for the growth of connective tissue and the elastogenesis of extracellular elastic fibers. Among the non-integrin cell surface receptors on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and cancer cells, the elastin-binding protein (EBP) plays a critical role.