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Merck

S1638

Streptavidin−Agarose from Streptomyces avidinii

buffered aqueous suspension

동의어(들):

streptavidin agarose beads, streptavidin agarose resin

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제품정보 (DICE 배송 시 비용 별도)

UNSPSC Code:
41106500
NACRES:
NA.56
MDL number:
기술 서비스
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도움 문의

form

buffered aqueous suspension

extent of labeling

≥1 mg per mL

technique(s)

affinity chromatography: suitable

matrix

4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

amino

matrix spacer

7 atoms

capacity

≥15 μg/mL binding capacity (biotin)

storage temp.

2-8°C

Quality Level

Application

Streptavidin−agarose from Streptomyces avidinii has been used:
  • to pull down biotinylated cell surface proteins during the quantification of plasma membrane transforming growth factor β (TGFβ) receptor II (TβRII) and Tβ
  • RII internalization
  • in biotinylated miRNA pull-down assay; as secondary antibodies in immunoprecipitation

Streptavidin-agarose is used in protein chromatography, affinity chromatography, and recombinant protein expression and analysis. Streptavidin-agarose has been used to study the oriented immobilization of the tobacco etch virus protease for the cleavage of fusion proteins. Streptavidin-agarose has also been used to develop a method for screening triplex DNA binders from natural plant extracts.
Used for the purification of biotin containing proteins or DNA binding proteins

Biochem/physiol Actions

Streptavidin is a homotetrameric protein, isolated from Streptomyces avidinii, which, like avidin, has a high affinity for biotin. Streptavidin is slightly anionic (pI ~ 5-6) and non-glycosylated. These properties contribute to its relatively low non-specific binding compared to egg white avidin. Streptavidin is also more resistant than avidin to dissociation into subunits by guanidinium chloride. Streptavidin-agarose can be used to immobilize or isolate various biotinylated macromolecules and complexes (proteins, antibodies, lectins, nucleic acids, receptors, and ligands). The inherent high-affinity streptavidin-biotin interaction requires harsh conditions to release biotinylated macromolecules. This feature makes streptavidin-agarose useful in a variety of affinity purification applications.

Physical form

Suspension in 0.01 M sodium phosphate, pH 7.2, containing 0.05 M NaCl and 0.02% sodium azide

저장 등급

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

I Gottschalk et al.
European journal of biochemistry, 267(23), 6875-6882 (2000-11-18)
Two cytochalasin B-binding states of the human red blood cell facilitative glucose transporter GLUT1 were studied, one exhibiting one cytochalasin B-binding site on every second GLUT1 monomer (state 1) and the other showing one site per monomer (state 2). Quantitative
Niusheng Xu et al.
Analytical chemistry, 84(5), 2562-2568 (2012-01-10)
A novel ligand fishing assay was established to screen triplex DNA binders from complicated samples by a combination of immobilization of triplex DNA on agarose beads and high-performance liquid chromatography-electrospray ionization-mass spectrometry (HPLC-ESI-MS). The biotinylated oligodeoxynucleotides were first bound to
O Litzka et al.
European journal of biochemistry, 251(3), 758-767 (1998-03-07)
In Aspergillus nidulans, a DNA-binding complex, PENR1, was shown to bind to two CCAAT-box-containing DNA elements located in the promoter regions of the bidirectionally oriented penicillin biosynthesis genes acvA and ipnA, and of the aat promoter. Here, partial purification of
S W Rogers et al.
The Plant journal : for cell and molecular biology, 11(6), 1359-1368 (1997-06-01)
Barley aleurain is contained within a specific type of vacuole characterized by acidic pH and the presence of other hydrolytic enzymes. The aleurain-containing vacuole is distinct from protein storage vacuoles, and anti-aleurain antibodies serve as markers for this organelle in
Behrad Derakhshan et al.
Nature protocols, 2(7), 1685-1691 (2007-07-21)
Covalent addition of nitric oxide (NO) to Cys-sulfur in proteins, or S-nitrosylation, plays pervasive roles in the physiological and pathophysiological modulation of mammalian protein functions. Knowledge of the specific protein Cys residues that undergo NO addition in different biological settings

관련 콘텐츠

친화성, GST 풀다운, TAP, 공동 면역 침전법을 활용한 풀다운 분석을 통해 in vitro 단백질-단백질 상호작용을 분석합니다.

Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.

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자사의 과학자팀은 생명 과학, 재료 과학, 화학 합성, 크로마토그래피, 분석 및 기타 많은 영역을 포함한 모든 과학 분야에 경험이 있습니다..

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