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Index / Bioassays / QuantiChrom™ Protein Assay Kit / Product Detail : QCPR-500 QuantiChrom™ Protein Assay Kit
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#QCPR-500 QuantiChrom™ Protein Assay Kit

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Product name : QuantiChrom™ Protein Assay Kit

Catalog number : QCPR-500

Quantity: 500

Availability: Yes

Supplier name : Bioassays

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About this Product :

QuantiChrom™ Protein Assay Kit antibody storage GENTAUR recommends for long therm storage to freeze at -24 C. For short time storage up to 30 days we suggest fridge storage at 1 to 10 C. Prevent multiple freeze taw cycles of QuantiChrom™ Protein Assay Kit.

More Details about

For quantitative determination of total protein.
Method: OD595nm (Bradford).
Samples: biological, food, agriculture etc.
Species: all.
Procedure: 2 min.
Size: 500 tests.
Detection limit: 60 μg/mL.

The protein is known as the "building blocks of life" and is one of the
most important macromolecules in life science. Proteins are polypeptides
made up of amino acids and play various key roles in all aspects of
biology. Protein quantitation is a very common practice for life scientists.
Simple, direct and automation-ready procedures for measuring protein
concentration are very desirable. BioAssay Systems' QuantiChromTM
protein assay kit is based on an improved Coomassie Blue G method.
The dye forms a blue complex specifically with protein, and the intensity
of color, measured at 595nm, is directly proportional to the protein
concentration in the sample. The optimized formulation substantially
reduces interference by substances in the raw samples and exhibits
increased sensitivity towards peptides.
Direct Assays: total protein concentration.
Sensitive and accurate. Use 10 μL samples. Detection range 0.06 – 1.0
mg /mL protein in 96-well plate assay.
Simple and high-throughput. The “mix-and-read” procedure involves
addition of a single working reagent and reading the optical density. Can
be readily automated as a high-throughput assay in 96-well plates for
thousands of samples per day.
Low interference. Glucose, Tris, vitamins, and amino acids, DNA, RNA,
salts, EDTA (< 12 mM), phenol (< 50 mM), urea (< 0.6 M), Triton (<
0.1%) and SDS (< 0.1% SDS) do not interfere in the assay.
Versatility: assays can be executed in 96-well plate or cuvet.
KIT CONTENTS (500 tests in 96-well plates)
Reagent: 20 mL 5 x concentrate
Protein standard: 1 mL 1.0 mg/mL BSA
Storage conditions. The kit is shipped at room temperature. Store the
reagent at 4°C and standard at -20°C, respectively. Shelf life: 12 months
after receipt.
Precautions: reagents are for research use only. Normal precautions for
laboratory reagents should be exercised while using the reagents.
Please refer to Material Safety Data Sheet for detailed information.

Pipeting devices and accessories.
Procedure using 96-well plate:
Blank 96-well plates (e.g. Corning Costar).
Plate reader for 96-well plate.
Procedure using cuvette:
Cuvets and spectrophotometer.


Sample Type: p450 enzymes

Species: bacteria


References: Aldag C et al (2009). Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine. PNAS 106(14):5481-6

Pubmed ID: 19293375

Pubmed link:

Abstract: he unique monooxygenase activity of cytochrome P450cam has been attributed to coordination of a cysteine thiolate to the heme cofactor. To investigate this interaction, we replaced cysteine with the more electron-donating selenocysteine. Good yields of the selenoenzyme were obtained by bacterial expression of an engineered gene containing the requisite UGA codon for selenocysteine and a simplified yet functional selenocysteine insertion sequence (SECIS). The sulfur-to-selenium substitution subtly modulates the structural, electronic, and catalytic properties of the enzyme. Catalytic activity decreases only 2-fold, whereas substrate oxidation becomes partially uncoupled from electron transfer, implying a more complex role for the axial ligand than generally assumed.

PMID: 19293375 [PubMed - indexed for MEDLINE] PMCID: PMC2657087


Sample Type: cells

Species: bacteria


References: Sharifuzzaman SM et al (2011). Subcellular components of probiotics Kocuria SM1 and Rhodococcus SM2 induce protective immunity in rainbow trout (Oncorhynchus mykiss, Walbaum) against Vibrio anguillarum. Fish Shellfish Immunol. 30(1):347-53.

Pubmed ID: 21078398

Pubmed link:

Abstract: The efficacy of cellular components of probiotics Kocuria SM1 and Rhodococcus SM2 to protect rainbow trout (Oncorhynchus mykiss, Walbaum) against vibriosis was assessed. Groups of fish (average weight = 10-15 g) were immunized intraperitoneally (i.p.) with 0.1 ml of subcellular materials, i.e., 0.2 ± 0.05 mg protein per fish, comprising extracellular proteins (ECPs), cell wall proteins (CWPs) and whole cell proteins (WCPs) of SM1 and SM2, respectively, or with 0.1 ml of phosphate-buffered saline (PBS) to serve as the control. Seven days after administration, fish from each group were challenged i.p. with 0.1 ml of a suspension in PBS of 3 × 10(5) cells ml(-1) per fish of Vibrio anguillarum. Use of CWPs and WCPs demonstrated significantly (P < 0.05) better protection against V. anguillarum insofar as mortalities were reduced to 11-17% [relative percent survival (RPS) = 80-87%], although ECPs fared less well (mortalities = 33-38%; RPS = 56-62%; P > 0.05), compared to 86% mortalities of the controls. The mode of action reflected activation of innate immune factors by CWPs and WCPs, demonstrating significantly (P < 0.05) increased expression of respiratory burst (optical density; OD(550 nm)) from 0.039 to 0.043-0.045, peroxidase (OD(550 nm)) from 0.26 to 0.37-0.55, and bacterial killing activities (i.e., percentage of surviving bacteria reduced from 79% to 56-57% for SM2). Moreover, an elevation of leucocyte number (from 1.93% to 1.98-2.93%; P > 0.05) and immunoglubolin level (from 27 mg ml(-1) to 28.5-33 mg ml(-1); P > 0.05) were observed with the experimental groups. These results indicate that cell components of the probiotics stimulate an immune response.

Copyright © 2010 Elsevier Ltd. All rights reserved.

PMID: 21078398 [PubMed - indexed for MEDLINE]



Sample Type: tissue

Species: rat


References: Verty AN et al (2009). The effects of rimonabant on brown adipose tissue in rat: implications for energy expenditure. Obesity (Silver Spring) 17(2):254-61.

Pubmed ID: 19057531

Pubmed link:

Abstract: The cannabinoid CB1 receptor antagonist rimonabant (SR 141716) produces a sustained decrease in body weight on a background of a transient reduction in food intake. An increase in energy expenditure has been implicated, possibly mediated via peripheral endocannabinoid system; however, the role of the central endocannabinoid system is unclear. The present study investigates this role. Rimonabant (10 mg/kg IP) was administered for 21 days to rats surgically implanted with biotelemetry devices to measure temperature in the interscapular brown adipose tissue (BAT). BAT temperature as a putative measure of thermogenesis in the BAT, physical activity, body weight, food intake, as well as changes in UCP1 messenger RNA (mRNA) and protein were measured. In addition, role of the CNS in mediating these actions of rimonabant was determined in rats where the BAT was sympathetically denervated. As expected, chronic administration of rimonabant significantly reduced body weight for the entire treatment period despite only a transient decrease in food intake. There was a profound increase in BAT temperature, particularly during the dark phase of each circadian cycle throughout the treatment period. A corresponding increase in uncoupling protein (UCP1) was also observed following chronic rimonabant treatment. The rimonabant-induced elevation in BAT temperature and decrease in body weight were significantly attenuated following denervation, indicating an involvement of the CNS. These findings suggest that the long-term weight loss associated with rimonabant treatment is due at least in part to an elevation in energy expenditure, represented here by elevated temperature recorded in the BAT, which is mediated primarily by the central endocannabinoid system.

PMID: 19057531 [PubMed - indexed for MEDLINE]


References: Lai, M et al (2007). 2007 AAPS Annual Meeting & Exposition. Development of an In-Vitro Screening Method to Determine Enzymatic Release Rates from a Homologous Series of Novel SN-38 Conjugates. Sonus Pharmaceuticals

Pubmed ID: conference

Pubmed link:

Abstract: N/A


Sample Type: brown fat tissue

Species: rat


References: Stefanidis A et al (2009). The role of thermogenesis in antipsychotic drug-induced weight gain. Obesity (Silver Spring) 17(1):16-24.

Pubmed ID: 19107124

Pubmed link:

Abstract: The administration of antipsychotic drugs to human patients or experimental animals leads to significant weight gain, which is widely presumed to be driven by hyperphagia; however, the contribution from energy expenditure remains unclear. These studies aim to examine the contribution of shifts in energy expenditure, particularly those involving centrally mediated changes in thermogenesis, to the body weight gain associated with the administration of olanzapine to female Sprague Dawley rats. Olanzapine (6 mg/kg/day orally) caused a transient increase in food intake but a maintained increase in body weight. When pair-fed rats were treated with olanzapine, body weight continued to rise compared to vehicle-treated rats, consistent with a reduction in energy expenditure. Brown adipose tissue (BAT) temperature, measured using biotelemetry devices, decreased immediately after the onset of olanzapine treatment and remained depressed, as did physical activity. UCP1 expression in interscapular BAT was reduced following chronic olanzapine treatment. An acute injection of olanzapine was preceded by an injection of a retrograde tracer into the spinal cord to evaluate the nature of the olanzapine-activated neural pathway. Levels of Fos protein in a number of spinally projecting neurons within discrete hypothalamic and brainstem sites were elevated in olanzapine-treated rats. Some of these neurons in the perifornical region of the lateral hypothalamus (LHA) were also Orexin A positive. These data collectively show a significant impact of thermogenesis (and physical activity) on the weight gain associated with olanzapine treatment. The anatomical studies provide an insight into the central neuroanatomical substrate that may subserve the altered thermogenic responses brought about by olanzapine.

PMID: 19107124 [PubMed - indexed for MEDLINE]


Sample Type: serum

Species: fish


References: Sharifuzzaman SM, Austin B (2010). Kocuria SM1 controls vibriosis in rainbow trout (Oncorhynchus mykiss, Walbaum). J Appl Microbiol. 108(6):2162-70.

Pubmed ID: 21098866

Pubmed link:


To develop probiotics for the control of vibriosis caused by Vibrio anguillarum and Vibrio ordalii in finfish.

Kocuria SM1, isolated from the digestive tract of rainbow trout, was administered orally to rainbow trout (Oncorhynchus mykiss) for 2 weeks at a dose equivalent to c. 10(8) cells per g of feed and then challenged intraperitoneally with V. anguillarum and V. ordalii. Use of SM1 led to a reduction in mortalities to 15-20% compared to 74-80% mortalities in the controls. SM1 stimulated both cellular and humoral immune responses in rainbow trout, by elevation of leucocytes (5.5 +/- 0.8 x 10(6) ml(-1) from 3.7 +/- 0.8 x 10(6) ml(-1)), erythrocytes (1.2 +/- 0.1 x 10(8) ml(-1) from 0.8 +/- 0.1 x 10(8) ml(-1)), protein (23 +/- 4.4 mg ml(-1) from 16 +/- 1.3 mg ml(-1)), globulin (15.7 +/- 0.2 mg ml(-1) from 9.9 +/- 0.1 mg ml(-1)) and albumin (7.3 +/- 0.2 mg ml(-1) from 6.1 +/- 0.1 mg ml(-1)) levels, upregulation of respiratory burst (0.05 +/- 0.01 from 0.02 +/- 0.01), complement (56 +/- 7.2 units ml(-1) from 40 +/- 8.0 units ml(-1)), lysozyme (920 +/- 128.8 units ml(-1) from 760 +/- 115.3 units ml(-1)) and bacterial killing activities.

Kocuria SM1 successfully controlled vibriosis in rainbow trout, and the mode of action reflected stimulation of the host innate immune system.

Probiotics can contribute a significant role in fish disease control strategies, and their use may replace some of the inhibitory chemicals currently used in fish farms.

PMID: 19929950 [PubMed - indexed for MEDLINE]


Sample Type: tissue

Species: trout


References: Sharifuzzaman SM, Austin B (2009). Influence of probiotic feeding duration on disease resistance and immune parameters in rainbow trout. Fish Shellfish Immunol. 27(3):440-5.

Pubmed ID: 19555765

Pubmed link:

Abstract: The effect of feeding the probiotic Kocuria SM1 to rainbow trout (Oncorhynchus mykiss, Walbaum) on disease resistance was evaluated. Thus, rainbow trout were fed Kocuria SM1 supplemented diets at concentrations of approximately 10(8) cells g(-1) feed for up to four weeks, and then challenged intraperitoneally with Vibrio anguillarum at weekly intervals. A two-week feeding regime led to the maximum reduction in mortalities, i.e. 16%, compared to mortalities of 62, 30 and 22% for one, three and four week feeding regimes, respectively. These compared to 70-90% mortalities of the controls. An enhanced cellular and humoral immune response, notably greater head kidney macrophage phagocytic and peroxidase activities, and higher serum lysozyme and total protein levels were recorded after two weeks of probiotic administration. These results reveal that a two-week feeding regime with Kocuria SM1 leads to higher disease protection in rainbow trout, with protection linked to stimulation of immune parameters.

2009 Elsevier Ltd.

PMID: 19555765 [PubMed - indexed for MEDLINE]


Sample Type: spermatozoa

Species: camel


References: Waheed MM et al (2011). Some Biochemical Characteristics and Preservation of Epididymal Camel Spermatozoa (Camelus dromedarius). Theriogenology 2011 Jul 13.

Pubmed ID: 21762979

Pubmed link:

Abstract: Testicles were isolated from thirty five apparently healthy dromedary camels (Camelus dromedarius), aged between 5 to 18 years, in a local slaughterhouse during the rutting season. Epididymal fluid was collected from one epididymis for determination of twelve biochemical and antioxidant parameters using ELISA commercial kits. Spermatozoa were harvested from each region of the other epididymis (head, body and tail) and stored in SHOTOR(®), Green buffer(®) + 20% egg yolk and INRA-96(®) extenders at 5 and 30 °C. Results revealed that, in the epididymal fluid, concentrations of testosterone, glucose, albumin, total protein, cholesterol, fatty acids, iron, aspartate aminotransferase (AST) and alanine aminotransferase (ALT) were 5.19 ± 1.69 ng/mL, 3.10 ± 0.41 mmol/L, 6.26 ± 1.26 g/dL, 0.50 ± 0.07 mg/dL, 1.74 ± 0.09 mmol/L, 6.62 ± 0.81 nmol/ul, 926.20 ± 100.18 ug/dL, 51.17 ± 7.74 mIU/ml, and 143.16 ± 18.67 mIU/ml, respectively. The antioxidants activities of catalase, glutathione peroxidase (GPx) and superoxide dismutase (SOD) in the epididymal fluid were 121.55 ± 6.57 nmol/min/ml, 59.35 ± 10.98 nmol/min/ml and 0.18 ± 0.03 U/ml, respectively. Epididymal sperm motility and concentration were higher (P < 0.05) in the body and tail than the head. The viability indices of total and forward sperm motility, at 5 and 30 °C, obtained from the tail region were superior (P < 0.05) in both SHOTOR(®) and INRA-96(®) extenders than Green buffer extender. It may be concluded that INRA-96(®) extender is the best for storing dromedary epididymal spermatozoa at 5 and 30 °C.

Crown Copyright © 2011. Published by Elsevier Inc. All rights reserved.

PMID: 21762979 [PubMed - in process]


Sample Type: urine

Species: human



Pubmed ID: N/A

Pubmed link: N/A

Abstract: N/A

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