The specific formulation of this buffer is considered proprietary. However, the solution includes sodium octanoate and polysorbate-80.
A6608
Albumin human
recombinant, expressed in Saccharomyces cerevisiae, aqueous solution, 10% in aqueous buffer, ≥99% (agarose gel electrophoresis)
Synonym(s):
rHSA
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| Pack Size | SKU | Availability | Price |
|---|---|---|---|
| 100 mg | Check Cart for Availability | $355.00 |
About This Item
Empirical Formula (Hill Notation):
C2936H4624N786O889S41
CAS Number:
Molecular Weight:
66471.53
UNSPSC Code:
12352202
eCl@ss:
42010201
NACRES:
NA.25
MDL number:
Biological source:
human
Assay:
≥99% (agarose gel electrophoresis)
Form:
aqueous solution
Technique(s):
cell culture | mammalian: suitable
Concentration:
10% in aqueous buffer
biological source
human
Quality Level
recombinant
expressed in Saccharomyces cerevisiae
assay
≥99% (agarose gel electrophoresis)
form
aqueous solution
mol wt
monomer ~67 kDa
concentration
10% in aqueous buffer
technique(s)
cell culture | mammalian: suitable
UniProt accession no.
storage temp.
2-8°C
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1 of 1
This Item | |||
|---|---|---|---|
| technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable | technique(s) ELISA: suitable, tissue culture: suitable, western blot: suitable |
| biological source human | biological source human | biological source human | biological source human |
| assay ≥99% (agarose gel electrophoresis) | assay ≥90% (agarose gel electrophoresis) | assay ≥90% (SDS-PAGE) | assay ≥96% (agarose gel electrophoresis) |
| Quality Level 200 | Quality Level 300 | Quality Level 200 | Quality Level 300 |
| form aqueous solution | form lyophilized powder | form solution | form lyophilized powder |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
General description
Albumin constitutes 25% of the proteins produced by the liver and is a prominent protein found in the blood. It is a protein of a single polypeptide chain with a thiol group.
Application
Albumin human has been used:
- to study its adsorption process on model mica surface at pH 3.5 using the atomic force microscopy (AFM) and in situ streaming potential measurements[1]
- to study its proteolytic activities under reducing conditions[2]
- in the medium for stem cell cultivation[3]
This recombinant variant is recommended for use in absorption, distribution, metabolism, and excretion (ADME) pharmacological research; cell culture; drug delivery research; and cryopreservation of cells.
Biochem/physiol Actions
Albumins are soluble monomeric proteins found in the body fluids and tissues of animals and in some plant seeds. Serum albumin functions as a carrier protein for steroids, fatty acids, and thyroid hormones. Serum albumins are also vital in regulating the colloidal osmotic pressures of blood.
Albumin is a binding and transport protein that serves as a protein repository and a carrier for amino acids. Albumin binding dissolves the biomolecules in blood and ensures its effective transport. This also prevents the loss of substance through excretion. Pathological conditions like vasculitis, lymphangiectasia, glomerulonephritis, and hepatic sinusoidal hypertension might result in hypoalbuminemia. This product can be used in the pharmaceutical industry as a drug excipient and to coat medical devices.[1]
Analysis Note
Endotoxin tested
Other Notes
View more information on human serum albumin.
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Dmitry Kryndushkin et al.
Pharmaceutical research, 33(2), 526-539 (2015-10-27)
Ascorbic acid has been considered as a potential radical scavenging excipient for pharmaceutical formulations. However, under certain circumstances, ascorbic acid can generate reactive oxygen species via redox cycling. The objective of this study was to investigate ascorbic acid-induced oxidative carbonylation
Dmitry Kryndushkin et al.
Pharmaceutical research, 34(4), 765-779 (2017-02-06)
Protein carbonylation is an irreversible modification of Lys, Arg, Thr and Pro amino acids under conditions of oxidative stress. Previous studies have reported specific carbonylated residues in purified recombinant albumins, albeit with a lack of agreement between the studies. Currently
Autoreactivity against Denatured Type III Collagen Is Significantly Decreased in Serum from Patients with Cancer Compared to Healthy Controls.
Jensen, et al.
International Journal of Molecular Sciences, 24 (2023)
Marta Kujda et al.
Colloids and surfaces. B, Biointerfaces, 127, 192-199 (2015-02-14)
Recombinant human serum albumin (rHSA) in monomeric state is widely used in pharmaceutical industry as a drug excipient and for preparing coatings for medical devices. In this work the adsorption process of rHSA on model mica surface at pH 3.5
Abnormalities of plasma proteins
Scientific Foundations of Biochemistry in Clinical Practice, 464-494 (1994)
Global Trade Item Number
| SKU | GTIN |
|---|---|
| A6608-100MG | 04061833382530 |
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A6608-100MG 제품의 buffer 조성을 알고싶습니다.
1 answer-
Helpful?
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I will like to ask for the secondary structure content of this product (A6608-100MG), particularly alpha helix and beta sheets.
1 answer-
The structure of human albumin is published and readily available. Please see the UniProt and PDB websites below:
https://www.uniprot.org/uniprotkb/P02768/entry#structure
https://www.rcsb.org/structure/1AO6Helpful?
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Could you provide information on the buffer from which it is lyophilized?
1 answer-
The product is formulated without additives and is lyophilized in water
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