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- bs-17264P
- 2025年10月16日
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500ug
| 产品编号 | bs-17264P |
| 英文名称 | SCAMP4 Antibody Blocking Peptide |
| 中文名称 | 分泌载体膜蛋白4封闭多肽 |
| 英文别名 | FLJ33847; FLJ90105; SCAM4_HUMAN; SCAMP 4; SCAMP4; Secretory carrier membrane protein 4; Secretory carrier-associated membrane protein 4. |
| 纯化方法 | HPLC |
| 亚细胞定位 | Membrane. |
| 相似性 | Belongs to the SCAMP family. |
| 功能 | Probably involved in membrane protein trafficking. |
| 保存条件 | Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles. |
| 注意事项 | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| 背景资料 | Secretory carrier membrane proteins (SCAMPs) are widely distributed integral membrane proteins implicated in membrane trafficking. Most SCAMPs (e.g., SCAMP1; MIM 606911) have N-terminal cytoplasmic NPF (arg-pro-phe) repeats, 4 central transmembrane regions, and a short C-terminal cytoplasmic tail. These SCAMPs likely have a role in endocytosis that is mediated by their NPF repeats. Other SCAMPs, such as SCAMP4, lack the NPF repeats and are therefore unlikely to function in endocytosis (summary by Fernandez-Chacon and Sudhof, 2000 [PubMed 11050114]).[supplied by OMIM, Feb 2011] |
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文献和实验or from the literature are missing. In this article, processing parameters for DNA, peptide, antibody, and carbohydrate microarrays are outlined. The applicability of the model experiments is demonstrated and described in detail on the example of short oligonucleotides.
Synthesis and Probing of Membrane-bound Peptide Arrays
the stringency of the blocking conditions and make sure that the primary binding partner and detection reagent (e.g., antibody) are of high purity and are used in the highest possible dilution. Stage
Mapping Protein‐Protein Interactions with Phage‐Displayed Combinatorial Peptide Libraries
. Fack, F., Deroo, S., Kreis, S., and Muller, C.P. 2000. Heteroduplex mobility assay (HMA) pre‐screening: An improved strategy for the rapid identification of inserts selected from phage‐displayed peptide
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