A0764
Albumin from rabbit serum
lyophilized powder, essentially globulin free, ≥99% (agarose gel electrophoresis)
Sign Into View Organizational & Contract Pricing
All Photos(4)
About This Item
Recommended Products
biological source
rabbit
Quality Level
Assay
≥99% (agarose gel electrophoresis)
form
lyophilized powder
technique(s)
surface plasmon resonance (SPR): suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
rabbit ... ALB(100009195)
Looking for similar products? Visit Product Comparison Guide
General description
Albumins are major serum proteins in mammals. They are glycosylated and correspond to a molecular weight of 66 kDa. Rabbit albumin shares sequence homology with bovine and horse albumin. It has IIA, IIB and IIIB subdomains along with an uncharacterized ligand binding site.
Application
Albumin from rabbit serum has been used in:
- the generation of advanced glycation end-products (AGEs)
- the vaccine antigen generation
- surface plasmon resonance studies with antibody fragments
Biochem/physiol Actions
Serum albumins are multifunctional as they bind and transport various biomolecules. They have allergenic potential.
Preparation Note
Prepared from albumin (A0639).
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
B Cell Competition for Restricted T Cell Help Suppresses Rare-Epitope Responses
Woodruff MC, et al.
Testing, 25(2), 321-327 (2018)
Serhat Sibar et al.
Annals of plastic surgery, 78(4), 436-442 (2017-01-13)
Today, botulinum toxin is commonly used for cosmetic purposes throughout the world. Despite various agents reducing the efficiency of toxin are well defined, the studies related to increasing the bioavailability are limited. The purpose of our study is to assess
Extending the half-life of a fab fragment through generation of a humanized anti-human serum albumin Fv domain: An investigation into the correlation between affinity and serum half-life
Adams R, et al.
MAbs, 8(7), 1336-1346 (2016)
Holger Fuchs et al.
Journal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics, 33(2), 115-122 (2017-01-06)
The ocular half-life of intravitreally (IVT) injected drugs is of major relevance for the suitability of a drug intended for chronic intraocular treatment, as the half-life determines the dosing frequency. Thus, half-life extension principles are very attractive as they can
Fumiko Okazaki et al.
Shokuhin eiseigaku zasshi. Journal of the Food Hygienic Society of Japan, 55(2), 65-72 (2014-07-06)
A direct competitive (dc)-ELISA was developed for rapid and simple determination of chlorothalonil residue in vegetables. A carboxylic acid derivative of pentachlorophenol was used to prepare an anti-chlorothalonil monoclonal antibody (MoAb) that showed adequate reactivity for dc-ELISA. Before homogenization of
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service