推荐产品
生物源
rabbit
品質等級
共軛
unconjugated
抗體表格
IgG fraction of antiserum
抗體產品種類
primary antibodies
無性繁殖
polyclonal
形狀
buffered aqueous solution
分子量
46 kDa
物種活性
human
濃度
0.5 mg - 1 mg/mL
技術
immunoprecipitation (IP): suitable
western blot: suitable
NCBI登錄號
UniProt登錄號
運輸包裝
wet ice
儲存溫度
−20°C
目標翻譯後修改
unmodified
基因資訊
human ... SERPINH1(871)
免疫原
Synthetic peptide directed towards the C terminal region of human SERPINH1
應用
Anti- SerPINH1 antibody produced in rabbit is suitable for western blotting at a concentration of 1 μg/ml.
生化／生理作用
SerPINH1 (Hsp47) is a molecular chaperone that regulates protein folding of type I and type IV procollagen in the endoplasmic reticulum. The activity of Hsp47 is critical for the development of well-organized cartilage and formation of normal endochondral bone.
序列
Synthetic peptide located within the following region: DIYGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRLKGDKMRDEL
外觀
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
免責聲明
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
Yusaku Masago et al.
Journal of cell science, 125(Pt 5), 1118-1128 (2012-04-12)
Heat shock protein 47 kDa (Hsp47) is considered as a molecular chaperone essential for the correct folding of type I and type IV procollagen in the ER. However, the function of Hsp47 for other types of procollagen and its importance
Christine Widmer et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(33), 13243-13247 (2012-08-01)
Collagen is the most abundant protein in animals and is a major component of the extracellular matrix in tissues such as skin and bone. A distinctive structural feature of all collagen types is a unique triple-helical structure formed by tandem
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