Streptavidin Agarose, sedimented bead suspension
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Invitrogen™

Streptavidin Agarose, sedimented bead suspension

The streptavidin conjugated to 4% beaded crosslinked agarose can be used to isolate biotinylated proteins. Additionally, biotinylated antibodies can beRead more
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Catalog NumberQuantity
S9515 mL
Catalog number S951
Price (MXN)
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Quantity:
5 mL
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The streptavidin conjugated to 4% beaded crosslinked agarose can be used to isolate biotinylated proteins. Additionally, biotinylated antibodies can be bound to streptavidin agarose to generate affinity matrices for the large-scale isolation of antigens.

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Column TypeAffinity
Label or DyeAgarose
Quantity5 mL
Shipping ConditionWet Ice
Stationary PhaseStreptavidin
FormLiquid Suspension
TypeAgarose
Unit SizeEach
Contents & Storage
Store in refrigerator (2°C to 8°C).

Frequently asked questions (FAQs)

What is the binding capacity of streptavidin agarose?

The binding capacity of streptavidin agarose is 15-20 µg (18-24 nmoles) of fluorescein biotin per mL of sedimented gel.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

Citations & References (57)

Citations & References
Abstract
Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation.
Authors:Hirsch JD, Eslamizar L, Filanoski BJ, Malekzadeh N, Haugland RP, Beechem JM, Haugland RP
Journal:Anal Biochem
PubMed ID:12419349
'The high-affinity binding of biotin to avidin, streptavidin, and related proteins has been exploited for decades. However, a disadvantage of the biotin/biotin-binding protein interaction is that it is essentially irreversible under physiological conditions. Desthiobiotin is a biotin analogue that binds less tightly to biotin-binding proteins and is easily displaced by ... More
Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH.
Authors:Kim JR, Yoon HW, Kwon KS, Lee SR, Rhee SG
Journal:Anal Biochem
PubMed ID:10906242
'A procedure for detecting proteins that contain H(2)O(2)-sensitive cysteine (or selenocysteine) residues was developed as a means with which to study protein oxidation by H(2)O(2) in cells. The procedure is based on the facts that H(2)O(2) and biotin-conjugated iodoacetamide (BIAM) selectively and competitively react with cysteine residues that exhibit a ... More
Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane.
Authors:Kaether C, Lammich S, Edbauer D, Ertl M, Rietdorf J, Capell A, Steiner H, Haass C
Journal:J Cell Biol
PubMed ID:12147673
'Amyloid beta-peptide (Abeta) is generated by the consecutive cleavages of beta- and gamma-secretase. The intramembraneous gamma-secretase cleavage critically depends on the activity of presenilins (PS1 and PS2). Although there is evidence that PSs are aspartyl proteases with gamma-secretase activity, it remains controversial whether their subcellular localization overlaps with the cellular ... More
Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport.
Authors:Tai AW, Chuang JZ, Sung CH
Journal:J Cell Biol
PubMed ID:11425878
'Despite the existence of multiple subunit isoforms for the microtubule motor cytoplasmic dynein, it has not yet been directly shown that dynein complexes with different compositions exhibit different properties. The 14-kD dynein light chain Tctex-1, but not its homologue RP3, binds directly to rhodopsin''s cytoplasmic COOH-terminal tail, which encodes an ... More
Evidence for allosteric linkage between exosites 1 and 2 of thrombin.
Authors:Fredenburgh JC, Stafford AR, Weitz JI
Journal:J Biol Chem
PubMed ID:9325262
'Investigations to date have demonstrated that ligand binding to exosites 1 or 2 on thrombin produces conformational changes at the active site. In this study, we directly compared the effect of ligand binding to exosites 1 and 2 on the structure and function of the active site of thrombin and ... More