Biotinylated Human Serum Albumin

$395.00

Catalog Number: B2010193 (5 mg)
Biotinylated Human Serum Albumin is a high quality research product used as multipurpose biotin labelled Human Serum Albumin (HSA) with applications in Molecular Biology, Cellular Biology, Assay development, Biochemistry and more. Each HSA unit contains several biotin units. This product is highly purified by size exclusion chromatography to eliminate any traces of free biotin. Custom bulk orders of this product are available upon request.

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SKU: B2010193 Categories: ,

Description

Biotinylated Human Serum Albumin
Catalog number: B2010193
Lot number: Batch Dependent
Expiration Date: Batch dependent
Volume/Weight: 5 mg
Supplied as: Ready-to-use
Appearance: Solution
Applications: multipurpose biotin labelled Human Serum Albumin (HSA) with applications in Molecular Biology, Cellular Biology, Assay development, Biochemistry and more. Each HSA unit contains several biotin units. This product is highly purified by size exclusion chromatography to eliminate any traces of free biotin.
Storage: -20C
Keywords: Human Albumin Biotin Conjugated, Native Human Serum Albumin protein (Biotin) , Serum albumin Biotin, ALB Biotin, Human serum albumin biotin, Biotinylated Human Serum Albumin, Human Serum Albumin (HSA), Biotinylated, Human serum albumin, Biotin labeled.
Grade: Biotechnology grade. All components are highly pure (minimum 99%). All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered on a 0.22 um.

References:
1: Maciążek-Jurczyk M, Szkudlarek A, Chudzik M, Pożycka J, Sułkowska A.
Alteration of human serum albumin binding properties induced by modifications: A
review. Spectrochim Acta A Mol Biomol Spectrosc. 2018 Jan 5;188:675-683.

2: Rabbani G, Ahn SN. Structure, enzymatic activities, glycation and therapeutic
potential of human serum albumin: A natural cargo. Int J Biol Macromol. 2019 Feb
15;123:979-990.

3: Ronzetti M, Baljinnyam B, Yasgar A, Simeonov A. Testing for drug-human serum
albumin binding using fluorescent probes and other methods. Expert Opin Drug
Discov. 2018 Nov;13(11):1005-1014.

4: Putri RM, Zulfikri H, Fredy JW, Juan A, Tananchayakul P, Cornelissen JJLM,
Koay MST, Filippi C, Katsonis N. Photoprogramming Allostery in Human Serum
Albumin. Bioconjug Chem. 2018 Jul 18;29(7):2215-2224.
PMC6053643.

5: Leblanc Y, Berger M, Seifert A, Bihoreau N, Chevreux G. Human serum albumin
presents isoform variants with altered neonatal Fc receptor interactions.
Protein Sci. 2019 Nov;28(11):1982-1992.

6: Padelli M, Labouret T, Labarre M, Le Reun E, Rouillé A, Kerspern H, Capaldo
C, Chauvet J, Plée-Gautier E, Carré JL, Leven C. Systematic overestimation of
human serum albumin by capillary zone electrophoresis method due to monoclonal
immunoglobulin interferences. Clin Chim Acta. 2019 Apr;491:74-80.

7: Alinovskaya LI, Sedykh SE, Ivanisenko NV, Soboleva SE, Nevinsky GA. How human
serum albumin recognizes DNA and RNA. Biol Chem. 2018 Mar 28;399(4):347-360.

8: Szkudlarek A, Pożycka J, Maciążek-Jurczyk M. Influence of Piracetam on
Gliclazide-Glycated Human Serum Albumin Interaction. A Spectrofluorometric
Study. Molecules. 2018 Dec 29;24(1):111.

9: Želonková K, Havadej S, Verebová V, Holečková B, Uličný J, Staničová J.
Fungicide Tebuconazole Influences the Structure of Human Serum Albumin Molecule.
Molecules. 2019 Sep 2;24(17):3190.

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