Rabbit Anti-S-tag antibody |
反应物种(预测) |
Species independent |
产品应用(已验证) |
WB |
产品应用(可尝试) |
ELISA |
推荐稀释比例 |
WB=1:1000-5000,Elisa=1:5000-10000, |
研究领域 |
细胞生物 |
标签 |
Array |
-
Sample:
Lane1: S-Tagged Fusion Protein Overexpression E.coli Lysate at 2ug
Lane2: S-Tagged Fusion Protein Overexpression E.coli Lysate at 2ug
Primary: Anti-S-tag (bs-33017R) at 1/1000 dilution
Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution
Predicted band size: 41 kD
Observed band size: 45 kD
RRID:RRID
产品名称:Rabbit Anti-S-tag antibody
别名: Stag; S tag; Ribonuclease A; KETAAAKFERQHMDS.
中文名称:S-tag标签抗体
英文名称:Rabbit Anti-S-tag antibody
抗体来源: Rabbit
克隆类型:多克隆
性 状:Liquid
亚 型:IgG
纯化方法:affinity purified by Protein A
保存条件:Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
免 疫 原:KLH conjugated synthetic peptide S-tag
Human Gene ID:S tag
S-tag is the name of an oligopeptide derived from pancreatic ribonuclease A (RNase A). If RNase A is digested with subtilisin, a single peptide bond is cleaved, but the resulting two products remain weakly bound to each other and the protein, called ribonuclease S, remains active although each of the two products alone shows no enzymatic activity. The N-terminus of the original RNase A, also called S-peptide, consists of 20 amino acid residues, of which only the first 15 are required for ribonuclease activity. This 15 amino acids long peptide is called S15 or S-tag.
The amino acid sequence of the S-tag is: Lys-Glu-Thr-Ala-Ala-Ala-Lys-Phe-Glu-Arg-Gln-His-Met-Asp-Ser. It is believed that the peptide with its abundance of charged and polar residues could improve solubility of proteins it is attached to[citation needed]. Moreover, the peptide alone is thought not to fold into a distinct structure. On DNA-level the S-tag can be attached to the N- or C-terminus of any protein. After gene expression, such a tagged protein can be detected by commercially available antibodies.
Important Note:This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.