
Thermo Fisher Scientific Human NUP107 Synthetic Peptide
인간 NUP107 단백질의 카복시 말단 15개 아미노산 서열에 해당하는 합성 펩타이드입니다. 항체 PA5-20563과 함께 블로킹 펩타이드로 사용 가능합니다. 핵공복합체 연구 및 HIV 관련 단백질 분석에 적합합니다. 연구용으로만 사용됩니다.
- 카탈로그번호
- PEP0683
- 판매단위
- pk
카탈로그
1개 옵션 · 카탈로그 번호를 클릭하면 복사됩니다Thermo Fisher Scientific · Thermo Fisher Scientific Human NUP107 Synthetic Peptide
Applications
Control (Ctrl)
- Assay-dependent
Blocking Assay (BLOCK)
- Assay-dependent
Product Specifications
| 항목 | 내용 |
|---|---|
| Species Reactivity | Human |
| Class | Synthetic |
| Type | Peptide |
| Conjugate | Unconjugated |
| Form | Liquid |
| Concentration | 200 µg/mL |
| Purification | Purified |
| Storage Buffer | PBS, pH 7.2, with 0.1% BSA |
| Contains | 0.02% sodium azide |
| Storage Conditions | -20°C |
Product Specific Information
This peptide corresponds to 15 amino acids near the carboxy terminus of human NUP107.
PEP-0683 can be used as a blocking peptide with polyclonal antibody PA5-20563.
Target Information
The nuclear pore complex (NPC) is a protein assembly localized at the nuclear rim and mediates macromolecular transport between the nucleus and the cytoplasm.
The mammalian nucleoporin (NUP107) is part of the hetero-oligomeric complex that also contains NUP160, NUP133, NUP96, and mammalian homolog of yeast sec13p.
While the majority of the NUP107-160 nuclear pore sub-complex localizes to the nuclear pore, a small fraction is observed at kinetochores and pro-metaphase spindle poles in mitotic cells in association with proteins such as Mad1, Mad2, Bub3, and Cdc20.
Immunodepletion of the NUP107-160 complex resulted in defective spindle assembly, indicating that it has multiple functions.
NUP107 has recently been identified as an HIV dependency factor (HDF), suggesting that NUP107 may be an important drug target in HIV treatment.
Multiple isoforms of NUP107 are known to exist.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Thermo Fisher Scientific 상품 둘러보기
전체보기문의
0개 · 배송·재고 문의는 실시간 상담이 빠릅니다아직 등록된 문의가 없어요.
