Name: Recombinant Bovine albumin (ALB)
Brand: CUSABIO
SKU: CSB-YP001561BO

Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Target Names

ALB

Uniprot No.

P02769

Research Area

Cardiovascular

Species

Bos taurus (Bovine)

Source

Yeast

Expression Region

25-607aa

Target Protein Sequence

DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

70.1 kDa

Protein Length

Full Length of Mature Protein

Tag Info

C-terminal 6xHis-Myc-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

The process of synthesizing the recombinant bovine ALB protein includes transfecting yeast cells with a DNA expression vector containing the gene for the ALB protein. Subsequently, the cells are cultured to induce the expression of the intended protein. The recombinant bovine ALB protein is then collected and purified from the cell lysate through affinity purification. It exhibits a purity exceeding 85%, as verified by SDS-PAGE.

Albumin, a crucial protein in the human body, plays various essential roles due to its unique properties [2]. It acts as a physiological buffer, maintaining colloid oncotic pressure in healthy individuals [1]. Human serum albumin (HSA), the most abundant protein in blood circulation, exhibits extraordinary ligand binding capacity, making it a transporter for a wide range of substances [3][4]. Albumin is involved in critical processes such as endocytosis, which is particularly relevant in neurons [5].

Albumin interacts with various molecules and undergoes modifications, as observed in the increased clearance of glycated albumin by proximal tubule cells [6]. The evolution of albumin can be traced back to early vertebrates, indicating its fundamental presence in mammalian plasma [7]. The production of serum albumin increases significantly after birth, becoming the predominant protein in adult serum [8].

References:
[1] S. Haque, F. Kabir, & K. Haque, Albumin infusion therapy in critical patients, Bangladesh Critical Care Journal, vol. 6, no. 2, p. 88-91, 2018. https://doi.org/10.3329/bccj.v6i2.38584
[2] R. García-Martinez, P. Caraceni, M. Bernardi, P. Ginès, V. Arroyo, & R. Jalan, Albumin: pathophysiologic basis of its role in the treatment of cirrhosis and its complications, Hepatology, vol. 58, no. 5, p. 1836-1846, 2013. https://doi.org/10.1002/hep.26338
[3] K. Neelofar, Z. Arif, J. Ahmad, & K. Alam, Non-enzymatic glucosylation induced neo-epitopes on human serum albumin: a concentration based study, Plos One, vol. 12, no. 2, p. e0172074, 2017. https://doi.org/10.1371/journal.pone.0172074
[4] K. Majorek, P. Porebski, A. Dayal, M. Zimmerman, K. Jablonska, A. Stewartet al., Structural and immunologic characterization of bovine, horse, and rabbit serum albumins, Molecular Immunology, vol. 52, no. 3-4, p. 174-182, 2012. https://doi.org/10.1016/j.molimm.2012.05.011
[5] L. Rasgado, A. Urbieta, & J. Jiménez, Affected albumin endocytosis as a new neurotoxicity mechanism of amyloid beta, Aims Neuroscience, vol. 7, no. 3, p. 344-359, 2020. https://doi.org/10.3934/neuroscience.2020021
[6] M. Wagner, J. Myslinski, S. Pratap, B. Flores, G. Rhodes, S. Campos-Bilderbacket al., Mechanism of increased clearance of glycated albumin by proximal tubule cells, Ajp Renal Physiology, vol. 310, no. 10, p. F1089-F1102, 2016. https://doi.org/10.1152/ajprenal.00605.2015
[7] A. Bujacz, Structures of bovine, equine and leporine serum albumin, Acta Crystallographica Section D Biological Crystallography, vol. 68, no. 10, p. 1278-1289, 2012. https://doi.org/10.1107/s0907444912027047
[8] L. Jagodzinski, T. Sargent, M. Yang, C. Glackin, & J. Bonner, Sequence homology between rnas encoding rat alpha-fetoprotein and rat serum albumin., Proceedings of the National Academy of Sciences, vol. 78, no. 6, p. 3521-3525, 1981. https://doi.org/10.1073/pnas.78.6.3521

Customer Reviews and Q&A

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■ Q&A

Is the protein free of animal components?

We guarantee that all proteins produced are 100% animal-free, as we do not use any animal components in our raw materials and no animal components are added during the production process. Serum-free media is also used in the expression of our Mammalian proteins. If you need it, we can provide a declaration of no animal component.

Is it soluble?

All proteins that we expressed recombinantly are soluble proteins.

We're thinking about modifying the protein, so I need a construct that is expressed in bacteria preferably.

You could choose the E. coli expression system (product code: CSB-EP001561BO).

We need the rBSA (Recombinant Bovine Serum albumin) for large volumes of cell culture media. This media will be used on bovine cells and the final product is for human food NOT clinical or diagnostic use. Although, the culture vessels will be using anything from100-2000L medium with 0.5% rBSA. This means each run would need between 0.5kg and 10kg per vessel and several bioreactors would be needed for each run. Obviously, large quantities would only be needed once the process is perfected. Do you provide bigger quantities such as 5-50kg?

Yes, we have 50L, 500L and much larger fermenters, and have successfully prepared 50mg, 100mg, 200mg, 500mg and other large-scale proteins for many customers.

We have the ability to achieve large-scale protein production, from mg to g, even kg.

I am preparing a research proposal (as part of a class to learn the theory) to study the efficacy of recombinant Bovine Serum Albumin (rBSA) compared to recombinant albumin that is derived from human genes for the purpose of bovine satellite cell culture. Can I get the quotation for 1mg and 1g protein? And I would also like to know if CUSABIO also sells recombinant albumin (from human genes), and if I could get a price comparison for that too.

For your experiment, do you need endotoxin removal and aseptic processing? We can provide it for free. Just put a note on your order so we will know.

As for rBSA, the quotation was already sent to you through email, you can order a small size to test first. If the test result is good then you can place bulk orders.

As for Recombinant Human Albumin, please check the product information listed below:

Uniport link: https://www.uniprot.org/uniprot/P02768
CSB-YP001561HU >> Yeast
CSB-EP001561HU >> E.coli
CSB-BP001561HU >> Baculovirus
CSB-MP001561HU >> Mammalian cell
Expression Region: 25-609aa; Full Length of Mature Protein
Tag information: Tag type will be determined during the manufacturing process.

Target Protein Sequence (The complete sequence will be provided upon request, including tag sequence, target protein sequence, and linker sequence):

DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL

I see the purity level of the product is 85%, is it good for cell culture usage? Also what is the other 15% what are the contaminants?

We guarantee a minimum purity standard of >85%. If the initial purification does not meet this standard or you have a higher purity requirement, we also have AKATA purification instrument, which is highly automated, precise control, combining the use of various columns, to ensure that the purity of our protein product is further enhanced and the final purity test results are displayed on the COA report.

The other 15% may be impurities such as nucleic acids, carbohydrates, lipids, unrelated proteins, isoenzymes, inactive proteins, etc.

In theory, CSB-YP001561BO is suitable for cell culture. Generally, we recommend you to choose endotoxin removed and aseptic process services if you plan to use a protein in cell culture or cell-related experiments. It normally needs a high purity. Please remark your requirement for purity when you place the order.

How is the protein purified? Is the purity guaranteed?

We will design the optimal purification scheme according to the tag type of the fusion protein and the physicochemical properties of the protein itself.

Purification methods: affinity chromatography, hydrophobic chromatography, ion-exchange chromatography, molecular sieve, salting out, etc.

We guarantee a minimum purity standard of >85%. The purity is comprehensively evaluated by SDS-PAGE Coomassie Brilliant Blue staining detection and Bandscan software analysis. Our QC standard of purity for all recombinant proteins is higher than 85% as determined by SDS-PAGE. We will decide if it needs a secondary AKTA-SEC purification by the SDS-PAGE result of the initial purity. If the initial purity is already qualified for the QC standard (>85%), and you don’t remark any strict requirement on the purity, generally we will not conduct AKTA-SEC for secondary purification. If the initial purification does not meet this standard or you have a higher purity requirement, we also have AKATA purification instrument, however, this AKTA-SEC purification requires an additional cost, and the delivery time will be extended by 3-5 working days.

Although we guarantee a minimum purity standard of >85%, some of the proteins we prepared can reach a purity of 95% or even 97%.

I would like to know If you could highlight a few things about the bovine recombinant albumin produced in E. coli and Yeast:
What is the smallest packing size for this product?
How is the endotoxin level, and purity of each of the recombinant expression systems?

The smallest packing size for CSB-EP001561BO and CSB-YP001561BO is 20ug. And the other sizes such as 100ug, 500ug, 1mg are also available. We have the ability to achieve large-scale protein production, from mg to g, even kg.

We guarantee a minimum purity standard of >85% for each expression system, if you have a higher purity requirement, we can also try to meet your demand through AKTA-SEC purification, please communicate with us during the pre-sales inquiry.

If you have a requirement for endotoxin level, please remark this information when placing the order and we could offer endotoxin removal service free of charge. We use conjugated PMB affinity filler adsorption to remove endotoxin and guarantee endotoxin level within 0.1ng/ug (1EU/ug). Generally, the delivery time will be extended for 2-3 days. Endotoxin removal result will be shown in COA as follows “<1.0 EU per 1μg of the protein by the LAL method.”

We noticed that this protein is C-terminal 6xHis-Myc-tagged, however, we don’t need any tag, can you provide this protein as tag-free?

If you need to remove the tag or tag-free protein, please communicate with us in advance, otherwise, we won't remove the tag. Usually, for most proteins with N-terminal tags, there is an enzyme cleavage site, and we can directly try to remove the tag by enzyme cleavage.

However, the tag of this protein is C-terminal 6xHis-Myc-tagged. It doesn't have any enzyme cleavage site. In such a case, if you need the tag-free version. We need to construct another new vector to express this protein and then try tag removal, the production cost will be much higher, please inquire for quotation.

Not all protein tags can be removed as some proteins will be very unstable after tag removal.

If we fail in removing the tag, we won’t charge for any extra cost, and remark this information in the datasheet as follows “Note: The laboratory determined that the Tag on your protein could not be removed with standard laboratory procedures. Your protein is being supplied with the Tag intact.”

Which validations have you performed for your proteins? Can you provide a free sample of this protein?

We carry out the following procedures, codon-optimized whole-gene synthesis → subcloning → construct expression plasmid → transformation and strain screening (small expression, optimization of expression conditions, determine the optimal expression conditions →scale-up expression→ protein purification→ If the expressed protein is inclusion body, it will adopt a variety of inclusion body renaturation to ensure the final supply of soluble protein→ QC test for purity, concentration, etc., and provide QC report. This series of production links will involve a variety of tests, 100% quality assurance:

(1) Sequencing → Ensure sequence correctness.
(2) Protein concentration detection.
(3) Molecular weight detection.
(4) Purity detection.
(5) Endotoxin removal will be performed upon request to ensure the final endotoxin level is less than 0.1 ng ug (1 EU/ug).
(6) Secondary activity test will be performed for Active Protein before the shipment.
(7) We will regularly perform Mass Spectrometry for mixed protein samples. If there are customers who need mass spectrometry results later, we can feedback the test results. For customers who require a separate mass spectrometry, we charge the customer for the appropriate cost and provide a single protein mass spectrometry.
(8) We can also carry out tag-antibody Western Blot for free. If the customer has this requirement, please remark this request when sending your PO and the test results will be shown in the COA report.

At present, our protein validation mainly includes SDS-PAGE and free tag-antibody WB verification.

In addition, if you have other verification requirements, you can always give us feedback. We can evaluate based on your needs and help you to perform further verification. Extra cost will be charged.

For some in-stock proteins, we could offer a small sample for free. If you need a free sample, please check with us during the pre-sales inquiry.

Why is the activity of this protein not guaranteed?

A: We have accumulated more than 15 years of experience in the expression of recombinant proteins and active proteins, and have produced more than 9000 recombinant proteins and more than 660 active proteins. A protein from the expression to the establishment of the activity test system to complete the activity verification requires a lot of cost and time investment.

This protein is not included in our activity verification plan currently. We are sorry that we have not tested it for a while and do not guarantee 100% activity. In theory, we are doing the full length of the protein, using affinity chromatography, and purifying the protein in a mild environment, which should be active in theory. We recommend that this customer can order a small size of this protein expressed by the eukaryotic expression system, which is more likely to be active.

(If our technical support can find relevant literature, the literature will be referred to customers.)

We will refer to the relevant literature on the preparation method of the active protein on the market, or if you have consulted the relevant literature and hope that we can prepare according to the methods in the literature, we will ensure the activity to the maximum according to the preparation methods mentioned in the literature.

Considering that the establishment of the protein measurement system requires a lot of time and cost to complete the measurement, although many of our proteins have not been verified by activity yet, many customers have detected very good activity and feedback to us after purchase, and even some customers have detected activity and successfully published literature.

I know activity isn’t measured – but in general –what is the impact of a given Tag type and any potential biological activity of the protein? Is a certain tag more or less likely to preserve biological activity – or does the Tag type not really make a difference? Or don’t you know?

Theoretically small tags generally have a very small influence on protein activity. However, the specific impact on protein activity can't be concluded (There is no impact on some proteins, small impact on some proteins, and relatively great impact on some proteins).

We should conduct specific analyses for specific proteins and specific tags. In the early stage, we could check related literatures. In the later stage, we will mainly validate by designing a control group.

We could design a parallel experiment for Fusion Protein & Tag-removed Protein or Fusion Protein & Tag-protein. We haven't done a relevant test for protein biological activity at present. So we can't 100% guarantee that the proteins have activity. (We will build up the detection of activity in a later stage)

Is it possible for you to provide your recombinant bovine albumin (CSB-YP001561BO) in a glycerol-free liquid format?

If the protein needs to be in a glycerol free liquid format, it must be shipped with dry ice. We could offer it as requested.

Target Background

Function

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.

Gene References into Functions

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

Hide All

Subcellular Location

Secreted.

Protein Families

ALB/AFP/VDB family

Tissue Specificity

Plasma.

Database Links

KEGG: bta:280717

STRING: 9913.ENSBTAP00000022763

UniGene: Bt.106669

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Code	CSB-YP001561BO
MSDS	MSDS Datasheet
Size	$436
	Order now
Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Bovine albumin (ALB)

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