Bovine Albumin(Alb) ELISA kit
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中文名稱:牛白蛋白(ALB)酶聯(lián)免疫試劑盒
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貨號(hào):CSB-E08664b
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規(guī)格:96T/48T
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價(jià)格:¥4200/¥3000
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其他:
產(chǎn)品詳情
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產(chǎn)品描述:牛白蛋白(ALB)酶聯(lián)免疫試劑盒(CSB-E08664b)為競(jìng)爭(zhēng)法ELISA試劑盒,定量檢測(cè)血清、血漿、組織勻漿樣本中的ALB含量。ALB(白蛋白)是一種在人體血液中廣泛存在的蛋白質(zhì),主要功能是調(diào)節(jié)血漿膠體滲透壓,并作為多種內(nèi)源分子的載體。研究顯示,ALB在肝癌治療中具有重要作用,特別是在ALB基因低表達(dá)型肝癌中,通過激活A(yù)LB基因可以有效抑制肝癌細(xì)胞的增殖。其研究機(jī)制涉及檢測(cè)肝癌樣株中ALB的表達(dá)水平,識(shí)別低表達(dá)肝癌株,并利用ALB激動(dòng)劑進(jìn)行治療。試劑盒檢測(cè)范圍為0.313 μg/mL-80 μg/mL,靈敏度為0.148 μg/mL。該產(chǎn)品主要用于科研領(lǐng)域,例如牛源性生物制品的質(zhì)量控制、疫苗或抗體生產(chǎn)過程中血清蛋白的監(jiān)測(cè),以及畜牧研究中牛只健康狀態(tài)評(píng)估等場(chǎng)景,為蛋白表達(dá)水平研究提供可靠工具。本品僅用于科研,不用于臨床診斷,產(chǎn)品具體參數(shù)及操作步驟詳見產(chǎn)品說明書。
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別名:ALB ELISA Kit; Serum albumin ELISA Kit; BSA ELISA Kit; allergen Bos d 6 ELISA Kit
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縮寫:
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Uniprot No.:
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種屬:Bos taurus (Bovine)
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樣本類型:serum, plasma, tissue homogenates
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檢測(cè)范圍:0.313 μg/mL-80 μg/mL
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靈敏度:0.148 μg/mL
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反應(yīng)時(shí)間:1-5h
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樣本體積:50-100ul
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檢測(cè)波長(zhǎng):450 nm
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研究領(lǐng)域:Metabolism
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測(cè)定原理:quantitative
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測(cè)定方法:Competitive
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精密度:
Intra-assay Precision (Precision within an assay): CV%<8%
Three samples of known concentration were tested twenty times on one plate to assess.
Inter-assay Precision (Precision between assays): CV%<10%
Three samples of known concentration were tested in twenty assays to assess.
Intra-Assay Precision
Inter-Assay Precision
Sample
1
2
3
1
2
3
n
20
20
20
20
20
20
Mean(μg/ml)
5.265
5.989
5.270
5.475
5.510
4.853
SD
0.038
0.033
0.038
0.041
0.044
0.048
CV(%)
6.463
5.546
6.179
6.732
7.237
7.643
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線性度:
To assess the linearity of the assay, samples were spiked with high concentrations of Bovine Alb in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
Sample
Serum(n=4)
1:2000
Average %
96
Range %
89-113
1:4000
Average %
92
Range %
86-107
1:8000
Average %
98
Range %
85-108
1:16000
Average %
90
Range %
83-98
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回收率:
The recovery of Bovine Alb spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
Sample Type
Average % Recovery
Range%
Serum (n=5)
93
88-95
EDTA plasma (n=4)
93
89-97
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標(biāo)準(zhǔn)曲線:
These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
μg/ml
OD1
OD2
Average
80
0.309
0.289
0.299
20
0.443
0.423
0.433
5
0.579
0.568
0.573
1.25
0.857
0.848
0.853
0.313
1.504
1.498
1.501
0
2.242
2.238
2.240
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數(shù)據(jù)處理:
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貨期:3-5 working days
相關(guān)產(chǎn)品
靶點(diǎn)詳情
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最新研究進(jìn)展:ALB,全稱為白蛋白,是一種重要的血漿蛋白。最近的研究表明,ALB在多種疾病的發(fā)生和發(fā)展中發(fā)揮著重要作用,包括肝病、腎病和心血管疾病等。ALB參與了細(xì)胞內(nèi)外的物質(zhì)轉(zhuǎn)運(yùn)、細(xì)胞凋亡和免疫反應(yīng)等生物學(xué)過程。
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功能:Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (Probable). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner. The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (Probable). The rank order of affinity is zinc > calcium > magnesium (Probable). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli. Does not prevent iron uptake by the bacterial siderophore aerobactin.
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基因功能參考文獻(xiàn):
- The interaction of DRV with bovine serum albumin (BSA), a major carrier protein, has been studied under simulated physiological conditions (pH7.4) by multi-spectroscopic techniques in combination with molecular modeling. PMID: 28753530
- hese obtained results provide an in-depth understanding of the interaction of the acid azo dye AO10 with serum albumins. PMID: 29126006
- that thiamine hydrochloride (TA) is located in site I of bovine serum albumin (BSA). PMID: 27550086
- The molecular dynamics results show how the negatively charged BSA at pH7 adsorbs to the negatively charged silica surface, and reveal a unique orientation with preserved secondary and tertiary structure. The experiments then show that the protein forms complete monolayers at approximately pH6, just above the protein's isoelectric point (pH5.1). PMID: 28350173
- Molecular dynamics (MD) simulation results demonstrate that the "hard protein" lysozyme retains much of its secondary structure during adsorption, whereas BSA loses it almost completely. BSA has a considerably larger adsorption energy compared to that of lysozyme, which does not scale with chain length. Desorption simulations are carried out using classical steered MD. PMID: 27421144
- identified a total of 125 carbonylated residues in bovine serum albumin after extensive in vitro metal ion-catalysed oxidation PMID: 28062376
- Degradation of BSA by serine proteases was monitored with Fourier transform infrared (FT-IR) and ultraviolet circular dichroism (UV-CD). alpha-Helical structure of BSA was converted into unordered structure upon digestion. PMID: 26926394
- Data show that the maximum adsorption occurred at the isoelectric point (pH 4.7) of bovine serum albumin (BSA). PMID: 26673525
- The ITC results indicated that the interaction between the protein (BSA and BHb) and QDs-612 was spontaneous and the predominant force was hydrophobic interaction PMID: 25143002
- Data (including data from biophysical studies using Langmuir lipid monolayer technique) suggest that human/bovine ALB exhibits minimal electrostatic repulsion and inserts effectively into phospholipid monolayers. [REVIEW] PMID: 24267981
- data indicate that conjugation of carboxyl groups with monosaccharide generates functional BSA with membrane-perturbing activities on the lipid-water interface. PMID: 25449061
- Data suggest that native BSA samples can be dehydrated to approximately 450 waters per protein molecule via microglassification and then reverted to native-like conformation upon rehydration with only minor irreversible aggregation. PMID: 24415208
- molecular modeling approaches were employed to determine the interaction between lysionotin and bovine serum albumin (BSA) at physiological pH PMID: 24398555
- Bovine Serum Albumine aqueous solutions in the presence of NaCl are investigated for different protein concentrations and low to intermediate ionic strengths. Protein interactions are modeled via a charge-screened colloidal model. PMID: 23534667
- A crystallographic structural study allows identification of serum albumin fragments responsible for immunogenicity and the postulation of a mechanism for antigen-antibody recognition in cattle. PMID: 22993082
- Glass transition and dynamics in BSA-water mixtures over wide ranges of composition studied by thermal and dielectric techniques. PMID: 21798376
- The dynamics of bovine serum albumin (BSA) and human fibrinogen (Fg) at low concentrations were observed at the solid-aqueous interface as a function of temperature. PMID: 22713578
- serum albumin possesses chaperone-like properties and that this activity is maintained under a number of physiologically relevant conditions. PMID: 22549788
- Interaction between 2',4-dihydroxychalcone and the N, f, e conformers of albumin was exothermic and spontaneous. PMID: 22450828
- The results showed that the riboflavin could efficiently bind to BSA in aqueous solution. PMID: 22154267
- The unfolding and refolding of BSA appear to proceed through intermediates and both the processes are sequential in nature. PMID: 21993230
- The results indicated that the binding abilities of vitamin B12 to BSA in the acidic and basic pH regions (pH 2.5, 3.5, 5.0, and 9.0) were lower than that at simulating physiological condition (pH 7.4). PMID: 21955947
- new insights on bovine serum albumin self-assembly process PMID: 21303653
- Data indicate that CD spectroscopy of the HSA and BSA released in solution after desorption from the matrices shows that, while both proteins partially regain their helical structure, they show a distinct behaviour in their tertiary structure. PMID: 20692819
- Data show that the fluorescence quenching process may occur through energy transfer from singlet excited state of tryptophan in BSA to the corresponding level of ASP. PMID: 20667434
- L-Arginine does not prevent amyloid-like fibril formation by BSA. PMID: 20204431
- Our data suggest that the efficacy of this detoxication system is based on the high concentration of albumin in plasma (and in the rest of the body), and not on the catalytic efficacy itself, which is low for albumin. PMID: 20211614
- The shortest binding distance and energy transfer efficiencies between donor BSA and acceptor methyl pheophorbide-a were obtained by Forster's nonradiative energy transfer mechanism. PMID: 16128079
- Data show that the apparent complexation constant of Pb2 x BSA is lgK = 11.61, and the nitrogen in BSA could coordinate with lead in Pb2-BSA. PMID: 15852867
- Data show that the binding constants of serum albumin and ZnPc(COOH)16 were 2.25-2.94 x 10(6) L x mol(-1). PMID: 17058928
- Data show that the binding power between BLFX and BSA is electrostatic effect. PMID: 17058955
- Data show that the combination reaction of AYR with BSA was a static quenching process. PMID: 17058958
- Data show that in long interaction period or at high concentration of SDS, SDS unfolded BSA by decreasing the alpha-helix structure and increasing the random coil. PMID: 17112025
- Data show that the binding constants (KA) between quercetin and BSA were 2.8 x 10(8) (26 degrees C) and 3.1 x 10(8) (36 degrees C), and the binding sites (n) were 1.7+/-0.02. PMID: 17112044
- Data show that the binding constant of this compound with bovine serum albumin (BSA) in aqueous solution was is Ka = 1.995 x 10(5) dm3 x mol(-1) and the binding site number is n = 1.12. PMID: 16201357
- results indicated that the binding reaction between BSA and purpure-18-imide was a single static quenching process. PMID: 16097695
- Data indicate that the hydrophobic force was the main binding force of TIF with bovine serum albumin in aqueous solution. PMID: 16329500
- Data show that the interaction of the umbelliferone-BSA was driven mainly by electrostatic force which was enhanced by Cu2+ and Zn2+. PMID: 16329506
- glycation and oxidation effects on the structure of serum albumin; the partial unfolding of the tertiary structure which accompanies the aggregation process is similar both in native and glycated BSA PMID: 20006741
- Structural analysis showed that lipids bind BSA via both hydrophilic and hydrophobic contacts. PMID: 19961210
- association constant and thermodynamic parameters and binding characterisitics for interaction of nigerloxin with bovine serum albumin. PMID: 15134145
- Temperature-dependent secondary structure and conformational changes to serum albumin occur twice, around 57 and 75 degrees C., and reveal that the alpha-helix and turn structures of serum albumin are cooperatively denatured by heating. PMID: 15350138
- Albumin up-regulates ligand-binding TGF-beta receptors on cultured proximal tubular cells. Albumin-induced activation of local Ang II production appears to be responsible for this effect. PMID: 15496155
- The results from the models show that there are at least two different binding sites located in the BSA protein with different water accessibility PMID: 16382334
- Human preadipocytes and freshly isolated adipocytes incubated with bovine serum albumin (BSA) in vitro secrete significantly higher amounts of cytokines IL-6, -8, and -10, and TNF-alpha compared with cells incubated without BSA. PMID: 16452161
- Serum albumin and serum retinol-binding protein(sRBP) are not components of bovine interphotoreceptor matrix(IPM). Serum albumin and sRBP can not participate in binding and transport of visual cycle retinoids in IPM of bovine retina. PMID: 17200663
- Bovine serum albumin is common allergen responsible for cow's milk allergy. Cross reactivity with serum albumins in meat/epithelial cells of other mammals results. PMID: 17680908
- BSA is able to form well-ordered beta-sheet rich aggregates which nevertheless do not possess the same structural rigidity as classical fibrils. PMID: 17689306
- interaction of bovine serum albumin with isoxazolcurcumin and diacetylcurcumin yielded binding constants, minor BSA conformation changes, and binding site PMID: 18037556
- The present study shows that GM1 has a strong effect on the conformation of BSA depending on the conformational states of the protein that would relate to a physiological function of GM1 such as acting as the receptor of proteins in the cell membrane. PMID: 18205315
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亞細(xì)胞定位:Secreted.
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蛋白家族:ALB/AFP/VDB family
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組織特異性:Plasma.
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