推荐产品
生物来源
bovine
质量水平
无菌性
aseptically filled
检测方案
28-32% (biuret)
形式
solution
质量
high avidity, contains azide and caprylate
纯化方式
heat shock fractionation
包含
0.1% sodium azide as preservative
10-15 mg/gram protein octanoic acid as stabilizer
来源
USA origin
浓度
28-32% (biuret)
30% in saline
技术
blocking: suitable
UniProt登记号
异质活性
BT Virus, none detected
VSV Virus, none detected
储存温度
2-8°C
基因信息
bovine ... ALB(280717)
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一般描述
Bovine serum albumin (BSA) belongs to the serum albumin family. It comprises three domains with two sub-domains under each. It is an α-helical, globular and non-glycosylated protein. BSA has 17-disulfide bonds.
应用
Bovine Serum Albumin solution has been used in the blocking of nonspecific binding in brain sections prior to light microscopy studies.
生化/生理作用
Bovine Serum Albumin (BSA) is a transporter for drugs, hormones and fatty acids. It is a crucial component of the cell culture media and favors embryonic stem cells (hESC) differentiation. BSA displays high solubility and is exploited in the cosmetic and pharmaceutical industry.It is used as a blocking agent in enzyme-linked immunosorbent assay (ELISA).
分析说明
与已知不完全抗体（遇盐不凝集）的亲和性经过测试。
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
法规信息
含少量动物源组分生物产品
Cystic fibrosis transmembrane conductance regulator protein expression in the male excretory duct system during development
Marcorelles P, et al.
Human Pathology, 43(3), 390-397 (2012)
Binding of fatty acid amide amphiphiles to bovine serum albumin: role of amide hydrogen bonding
Ghosh S and Dey J
The Journal of Physical Chemistry B, 119(25), 7804-7815 (2015)
Enzyme-linked immunosorbent assay (ELISA) and blocking with bovine serum albumin (BSA)?not all BSAs are alike
Xiao Y and Isaacs SN
Journal of Immunological Methods, 384(1-2), 148-151 (2012)
Albumin and mammalian cell culture: implications for biotechnology applications
Francis GL
Cytotechnology, 62(1), 1-16 (2010)
Structural changes during the unfolding of Bovine serum albumin in the presence of urea: A small-angle neutron scattering study
Das A, et al.
Pramana, 63(2), 363-368 (2004)
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