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2 clone B3 was digested with XhoI and Not I (site from pCR2. Capping of Labeled Proteins. Cysteine and methionine at positions 35 and 37 were replaced with arginine and cysteine to increase the distance between cysteine residues and minimize the potential steric hindrance created by two dye molecules binding to cysteines residues at positions 34 and 37.

Novex Sharp Prestained Protein Standard Chartered

In some embodiments, the protein that is depleted in cysteine residues comprises fewer than one residue of cysteine per 10 kDa. In preferred embodiments, all of the protein standards of the pre-labeled standard set are separated such that the bands do not overlap the widths of the bands on a gel of each of the electrophoresed proteins of the set having a molecular weight of 10 kDa or greater do not vary by more than 2-fold and the band intensities of the proteins of the pre-labeled protein standard set having molecular weights of 10 kDa or greater do not vary by more than 2. The insulin-b chain has theoretical absorbance of 0. 5%, or 1% of one another are selectively labeled on a first amino acid. 16 mm, a difference of just under 2-fold. Prestained protein ladder novex. The dye was eluted in acetonitrile and the colored fractions were collected. In some preferred embodiments, the labeled proteins of a pre-labeled protein standard set having molecular weights between 20 kDa and 100 kDa produce visually detectable bands on electrophoresis gels having widths that do not differ by more than 50%. Invitrogen™ Novex™ Sharp Pre-stained Protein Standard by Thermo Fisher Scientific. 5%, or within 1% of the migration distance of the same proteins that are not labeled under standard protein gel electrophoresis conditions on a 4-12% Bis-Tris gel or a 4-20% Tris-glycine gel. The invention provides pre-labeled protein standard sets comprising a plurality of labeled proteins, in which one or more of the labeled proteins is selectively labeled on a first amino acid. The liquid fraction was discarded and the pellet (insoluble fraction) was resuspended in 50 μl of 1×LDS Sample buffer. The appropriate amount of compound for any protein or other component is conveniently predetermined by experimentation in which variable amounts of the compound are added to the protein, the conjugate is purified (for example, using chromatography) to separate unconjugated compound and the protein-labeling compound conjugate is tested in its desired application. Sequences depleted in lysine can be further selected based on low frequency of other potential non-target amino acids, such as, but not limited to, histidine or tryptophan.

Novex Sharp Prestained Protein Ladder

The mutation of codons can be to any non-target codon and need not be restricted to conservative mutation. In some preferred embodiments, a protein standard selectively labeled on cysteine is depleted in or has an amino acid sequence with a reduced number of residues of at least lysine relative to the corresponding wild-type amino acid sequence. The pre-labeled protein standard set can include two or more, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, twenty, or more proteins that are selectively labeled on cysteine and are depleted in lysine, in which the selectively labeled proteins comprise one or more copies of an amino acid sequence depleted in lysine. Cell Mol Life Sci 77:2235-2253 (2020). The pTrc1-2 C6 vector, containing two 50 kd inserts, was digested with Avr II and PmeI. The sample was loaded on the column and the dye was separated from the protein conjugate. Novex sharp prestained protein standard curve. The present invention provides pre-labeled protein standard sets that when electrophoresed give sharp bands that have migration distances consistent with the migration distances of the proteins of the standard set electrophoresed in unlabeled form. The reactive dye was loaded directly onto the column after adjusting the pH to 7.

Novex Sharp Prestained Protein Standard Curve

Mass spectrometry analysis of the actual molecular weight of the expressed protein revealed that it was 10 kDa larger than expected (Table 4). 4_F: |(SEQ ID NO: 28). 250 μl of 2 mg/ml 30 kDa (NL) stock solution was brought up to 1 ml volume to a final concentration of 50 mM Tris, 0. This leads to a protein standard having variable label intensity per microgram of protein, and poor resolution of the protein standard in separation techniques that rely on mass, such as, but not limited to, electrophoresis and chromatography. Tyrosine can also be a target amino acid, in which a reactive chemical group on a label to be conjugated to the protein standard is, for example, a sulfonyl fluoride or iodoacetamide. The synthesis scheme is depicted in FIG. The dye was loaded on the C-18 resin in 50 mM phosphate pH 3. Easy to identify: Includes green ~25 kDa and red ~75kDa reference bands. In some preferred embodiments, the proteins having ratios of first amino acid to molecular weight within 10%, 5%, 2. The expression clone was labeled pTrc 50. ACTCTGCCCAGAAGTCGAC. Novex™ Sharp Pre-stained Protein Standard. Induced 50 ml cell cultures (after reaching an O. D. of 0. The BenchMark™ 10 kDa protein standard (Invitrogen Corp., Carlsbad, Calif. ; U. A protein standard selectively labeled on cysteine is labeled with a labeling compound that comprises an sulfhydryl-reactive group, such as, but not limited to, vinyl sulfone, iodoacetamide, maleimide, or iodoacetic acid.

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In some embodiments, a protein of a pre-labeled protein standard set that is selectively labeled on cysteine comprises an amino acid sequence derived from an nucleotide-disulfide oxidoreductase, such as a lipoamide dehydrogenase, a glutathione reductase, or a thioredoxin. The significant reactive groups of amino acids behave as nucleophiles in chemical reactions, for example, the sulfhydryl group of cysteine; the amino group of an N-terminal amino acid or of lysine, histidine, tryptophan, or arginine; the carboxyl group of aspartate and glutamate or a C-terminal amino acid; the phenolate of tyrosine; and the thioether of methionine. A "variant" of a wild-type protein or peptide sequence is a sequence having at least 70%, preferably at least 80%, at least 90%, at least 95%, or at least 99% sequence identity with at least 20 contiguous amino acids of the wild-type protein. Novex sharp prestained protein standard chartered. As shown by the diagram of FIG. Examples of textile dyes that can be used to label protein standards include, for example, Remazol brilliant blue, Uniblue A, malachite green isothiocyanate, and Orange 16 (Remazol orange).

Prestained Protein Ladder Novex

The resin-bound dye was then washed to remove most of the acid from the coupling step. 50 ml centrifuge tubes. The set of pre-labeled protein standards of the kit can include at five, six, seven, eight, nine, ten, eleven, twelve, or more labeled protein standards that are provided as one or more mixtures of two or more labeled standards. The pre-labeled marker set of Example 11 (10 microliters) was electrophoresed alongside the same set of proteins in unlabeled form (5 microliters) in a 4-12% Bis-Tris (NuPAGE® Novex®) acrylamide gel run with 1×MES buffer. The pre-labeled protein molecular weight standard sets can comprise two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, or more labeled proteins. The column is plugged with a cap and 4 ml 8M urea, 20 mM phosphate, 500 mM NaCl pH=7. The sample is left to cool down to room temperature. For example, an engineered protein to be used for making pre-labeled protein standards can have one or more copies of an amino acid sequence with at least 70% or at least 80% identity with at least 20, at least 30, at least 40, or at least 50 contiguous amino acids of a thioredoxin sequence, in which lysine has been removed from the sequence by deletion or mutation of lysine codons in the nucleic acid sequence encoding the protein.

Novex Sharp Prestained Protein Standard.Html

In some embodiments, the protein that is depleted in cysteine residues comprises an amino acid sequence that has homology to at least 40 amino acids of a naturally-occurring protein, such as at least 70%, at least 80%, or at least 90% homology to at least 40 amino acids of a naturally-occurring protein, and has fewer cysteine residues than the amino acid sequence of the naturally-occurring protein to which has homology. A pre-labeled protein standard set of the invention can include two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, or more proteins selectively labeled on a target amino acid. The column was washed thoroughly with water after the dye was loaded. In another embodiment, a pre-labeled protein standard set of the invention comprises two or more proteins of different molecular weights that are labeled on cysteine and depleted in lysine residues. PGRMC1 phosphorylation affects cell shape, motility, glycolysis, mitochondrial form and function, and tumor growth. The resulting PCR product was Topo cloned into the pCR®-Blunt cloning vector (Invitrogen, Carlsbad, Calif., USA) using the Zero Blunt® kit (Invitrogen, Carlsbad, Calif., USA).

A negative ion mode mass spectrum was obtained to be sure that a parent peak was seen at a mass to charge ratio of 492. 50 μl of 1M iodoacetamide was added, and the sample was vortexed for 3-5 seconds and then incubated for 40-60 minutes at room temperature in the dark. 2B provides the nucleic acid sequence of BH6mer ORF (SEQ ID NO:13). 5 mm) or larger gel. The unlabeled standard set was formulated such that the 20 kDa and 80 kDa standard protein bands were more intense than the other protein bands when viewed on an electrophoresis gel, so that the user can orient the proteins readily by observation of the intense 20 kDa and 80 kD bands. Adjust the volume to 2 liters.

13/715, 812 filed Dec. 14, 2012, now U. Pat. CCGTTACGGAAAAGCAGAAG. The TCA supernatant was removed and the precipitate was spun again for 10 seconds at 2000×g to collect TCA drops from the tube wall. Convenient - a ready-to-use formulation eliminates the need to heat, reduce, or add sample buffer prior to use. In preferred embodiments, all of the protein standards of the pre-labeled standard set are separated from one another such that the bands do not overlap and such that the widths of the bands on a gel of each of the electrophoresed proteins of the set having a molecular weight of 10 kDa or greater do not vary by more than 2-fold. Tools that aid in the development of new drugs and new medical diagnostics, as well as certain diagnostics themselves, require accurate and efficient analysis of protein samples. The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user. In some preferred embodiments, the two or more labeled proteins are comprise a labeling compound bound to a first amino acid and comprise one or more copies of an amino acid sequence of or having homology to an amino acid sequence of a naturally-occurring protein, in which the amino acid sequences of the labeled proteins lacks residues of a second amino acid that can react with the labeling compound. The method includes: reducing cysteines of a protein that lacks lysine residues and adding a labeling compound to the protein under conditions that allow conjugation of the dye with cysteine. Approximately every 18th amino acid's 3rd base codon wobbled to minimize repeats when the construct was fully assembled. In one embodiment, the method includes: providing a pre-labeled protein standard set to a customer, in which at least one of the labeled proteins of the standard set is selectively labeled on a first amino acid, in exchange for revenue.

Electrophoretic migration of labeled and unlabeled forms of a protein standard is within a given percentage when the difference in the calculated molecular weights of the labeled and unlabeled forms of the protein using either curve-fitting of molecular weight to migration distances or point-to-point calculation are within the given percentage. The sample is loaded on the column (about 20 ml of sample can be applied to 100 ml column bed volume). Preferred conservative amino acid substitution groups are: valine-leucine-isoleucine; phenylalanine-tyrosine; lysine-arginine; alanine-valine; glutamic acid-aspartic acid; and asparagine-glutamine. The specificity of labeling achieved using the methods provided in the invention produces labeled proteins that are highly-resolving in separation procedures, such as electrophoresis on denaturing gels. A pre-labeled protein of a standard set of the invention can be made by recombinant methods. Methods of Using a Pre-Labeled Standard Set to Determine Molecular Weight of a Protein. CCGGCGGCCGTTCGCCGTTACGGAAAAGCA, |50. Designed for monitoring protein separation during PAGE and providing clear electro-transfer to commonly used membranes. The dye front can be a Coomassie dye front, such as a Coomassie G250 dye front. 25 lpm air, 500 rpm agitation, and the pH is controlled to 6. The width of each peak at half height was therefore divided by 11.

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