Bovine Albumin(Alb) ELISA kit

ALB，全稱(chēng)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(guò)程。

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.

1. 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
2. hese obtained results provide an in-depth understanding of the interaction of the acid azo dye AO10 with serum albumins. PMID: 29126006
3. that thiamine hydrochloride (TA) is located in site I of bovine serum albumin (BSA). PMID: 27550086
4. 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
5. 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
6. identified a total of 125 carbonylated residues in bovine serum albumin after extensive in vitro metal ion-catalysed oxidation PMID: 28062376
7. 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
8. Data show that the maximum adsorption occurred at the isoelectric point (pH 4.7) of bovine serum albumin (BSA). PMID: 26673525
9. 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
10. 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
11. data indicate that conjugation of carboxyl groups with monosaccharide generates functional BSA with membrane-perturbing activities on the lipid-water interface. PMID: 25449061
12. 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
13. molecular modeling approaches were employed to determine the interaction between lysionotin and bovine serum albumin (BSA) at physiological pH PMID: 24398555
14. 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
15. 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
16. Glass transition and dynamics in BSA-water mixtures over wide ranges of composition studied by thermal and dielectric techniques. PMID: 21798376
17. 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
18. serum albumin possesses chaperone-like properties and that this activity is maintained under a number of physiologically relevant conditions. PMID: 22549788
19. Interaction between 2',4-dihydroxychalcone and the N, f, e conformers of albumin was exothermic and spontaneous. PMID: 22450828
20. The results showed that the riboflavin could efficiently bind to BSA in aqueous solution. PMID: 22154267
21. The unfolding and refolding of BSA appear to proceed through intermediates and both the processes are sequential in nature. PMID: 21993230
22. 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
23. new insights on bovine serum albumin self-assembly process PMID: 21303653
24. 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
25. 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
26. L-Arginine does not prevent amyloid-like fibril formation by BSA. PMID: 20204431
27. 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
28. 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
29. 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
30. 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
31. Data show that the binding power between BLFX and BSA is electrostatic effect. PMID: 17058955
32. Data show that the combination reaction of AYR with BSA was a static quenching process. PMID: 17058958
33. 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
34. 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
35. 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
36. results indicated that the binding reaction between BSA and purpure-18-imide was a single static quenching process. PMID: 16097695
37. Data indicate that the hydrophobic force was the main binding force of TIF with bovine serum albumin in aqueous solution. PMID: 16329500
38. Data show that the interaction of the umbelliferone-BSA was driven mainly by electrostatic force which was enhanced by Cu2+ and Zn2+. PMID: 16329506
39. 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
40. Structural analysis showed that lipids bind BSA via both hydrophilic and hydrophobic contacts. PMID: 19961210
41. association constant and thermodynamic parameters and binding characterisitics for interaction of nigerloxin with bovine serum albumin. PMID: 15134145
42. 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
43. 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
44. 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
45. 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
46. 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
47. 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
48. 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
49. interaction of bovine serum albumin with isoxazolcurcumin and diacetylcurcumin yielded binding constants, minor BSA conformation changes, and binding site PMID: 18037556
50. 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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Secreted.

ALB/AFP/VDB family

Plasma.

KEGG: bta:280717

STRING: 9913.ENSBTAP00000022763

UniGene: Bt.106669