추천 제품
생물학적 소스
mouse
Quality Level
결합
unconjugated
항체 형태
purified immunoglobulin
항체 생산 유형
primary antibodies
클론
2A11, monoclonal
양식
buffered aqueous solution
종 반응성
human
기술
indirect ELISA: suitable
western blot: 1-5 μg/mL
동형
IgG1κ
GenBank 수납 번호
UniProt 수납 번호
배송 상태
dry ice
저장 온도
−20°C
타겟 번역 후 변형
unmodified
유전자 정보
human ... AKTIP(64400)
일반 설명
Fused toes homolog (FTS), also known as AKT interacting protein (AKTIP)/Ft1, is encoded by the gene mapped to human chromosome 16q12.2. Ft1 is a member of ubiquitin E2 variant (UEV) enzyme subfamily, characterized with a ubiquitin conjugation (UBC) domain lacking the catalytic cysteine involved in ubiquitin transfer.
The mouse homolog of this gene produces fused toes and thymic hyperplasia in heterozygous mutant animals while homozygous mutants die in early development. This gene may play a role in apoptosis as these morphological abnormalities are caused by altered patterns of programmed cell death. The protein encoded by this gene is similar to the ubiquitin ligase domain of other ubiquitin-conjugating enzymes but lacks the conserved cysteine residue that enables those enzymes to conjugate ubiquitin to the target protein. This protein interacts directly with serine/threonine kinase protein kinase B (PKB)/Akt and modulates PKB activity by enhancing the phosphorylation of PKB?s regulatory sites. Alternative splicing results in two transcript variants encoding the same protein. (provided by RefSeq)
면역원
FTS (AAH01134, 1 a.a. ~ 292 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Sequence
MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT
Sequence
MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT
생화학적/생리학적 작용
Fused toes homolog (FTS) interacts with the shelterin component telomeric repeat factor 1 (TRF1) and facilitates proper telomere replication. In addition, the protein also plays a vital role in regulation of protein kinase B/AKT signaling and vesicle trafficking. Deletion of the gene leads to general impairment of DNA synthesis and defective telomere replication. FTS control radioresistance of cervical cancer.
물리적 형태
Solution in phosphate buffered saline, pH 7.4
법적 정보
GenBank is a registered trademark of United States Department of Health and Human Services
면책조항
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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Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
가장 최신 버전 중 하나를 선택하세요:
시험 성적서(COA)
Lot/Batch Number
Fused Toes Homolog modulates radiation cytotoxicity in uterine cervical cancer cells.
Anandharaj A, et al.
Molecular Biology Reports, 5361-70 null
The telomeric protein AKTIP interacts with A- and B-type lamins and is involved in regulation of cellular senescence
Burla R, et al.
Open Biology null
AKTIP/Ft1, a New Shelterin-Interacting Factor Required for Telomere Maintenance
Burla R, et al.
PLoS Genetics null
CD5(-) diffuse large B-cell lymphoma with peculiar cyclin D1+ phenotype. Pathologic and molecular characterization of a single case.
Lucioni M, et al.
Human Pathology, 1204-8 null
Miho Yoshioka-Nishimura et al.
Plant & cell physiology, 55(7), 1255-1265 (2014-06-04)
Under light stress, the reaction center-binding protein D1 of PSII is photo-oxidatively damaged and removed from PSII complexes by proteases located in the chloroplast. A protease considered to be responsible for degradation of the damaged D1 protein is the metalloprotease
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