추천 제품
생물학적 소스
bovine
Quality Level
Grade
for molecular biology
제품 라인
BioReagent
분석
≥98%
형태
lyophilized powder
분자량
~66 kDa
정제법
heat shock fractionation
포장
poly bottle of
기원
USA origin
기술
ELISA: suitable
electrophoresis: suitable
western blot: suitable
pH
7
solubility
water: soluble (40 mg/ml)
UniProt 수납 번호
외래 활성
Protease free
저장 온도
2-8°C
유전자 정보
bovine ... ALB(280717)
유사한 제품을 찾으십니까? 방문 제품 비교 안내
애플리케이션
A non-acetylated protein suitable as a blocking agent in Southern blotting. If your application requires nuclease-free BSA, we recommend our acetylated BSA for these critical applications.
생화학적/생리학적 작용
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.
특징 및 장점
- Protease free
- Suitable for blocking non-specific protein binding sites in hybridizations
- Heat shock fractionated
제조 메모
Prepared using heat shock fractionation
Serum albumin may be referred to as Fraction V. This naming convention is taken from the original Cohn method of fractionating serum proteins using cold ethanol precipitation. Serum albumin was found in the fifth ethanol fraction using Cohn′s method. Since then, the term "Fraction V" has been used by some to describe serum albumin regardless of the method of preparation. Others have used this term to describe serum albumin purified by ethanol fractionation methods that have been highly modified since the original Cohn method was described. Sigma-Aldrich manufactures and distributes serum albumins purified from a variety of primary methods including the true Cohn fractionation method, modified ethanol fractionation methods, heat shock and chromatography. Additional purification steps may include crystallization or charcoal filtration.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
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PloS one, 6(1), e15611-e15611 (2011-01-26)
The actin cytoskeleton of dendritic spines plays a key role in morphological aspects of synaptic plasticity. The detailed analysis of the spine structure and dynamics in live neurons, however, has been hampered by the diffraction-limited resolution of conventional fluorescence microscopy.
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