KingFisher™ mL Purification System
KingFisher™ mL Purification System
Thermo Scientific™

KingFisher™ mL Purification System

Thermo Scientific™ KingFisher mL Purification System을 이용하여 실험실 워크플로 내에서 처리량이 낮은 시료 전처리를 자동화하십시오.
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카탈로그 번호수량
5400050Each
카탈로그 번호 5400050
제품 가격(KRW)
-
견적 요청하기
수량:
Each
유연성을 높이기 위해 최적화된 Thermo Scientific™ KingFisher mL Purification System을 이용하여 실험실 워크플로 내에서 처리량이 낮은 시료 전처리를 자동화하십시오. 최대 1mL 용량의 시료를 처리하기 위해 선택한 이 자성 입자 프로세서는 다섯 개의 튜브로 구성된 하나의 스트립에서 모든 정제 단계를 완료하고 1회 작동 시 15개의 시료를 처리할 수 있습니다. 또한 50μL로 이동하여 타겟 분자를 방출할 수 있는 기능이 있으므로 DNA 또는 RNA와 같은 시료는 더 큰 시작 용량에서 분리하고 동시에 농축할 수 있습니다.
특징:
  • 다양한 유형의 다운스트림 응용 분야를 위해 고품질 DNA, RNA, 단백질 및 세포의 빠르고 재현성 있는 정제
  • 개방적이고 유연한 시스템에서 자성 입자 기반의 키트를 사용해 응용 분야의 요구사항 충족
  • 사용하기 쉬운 Thermo Scientific™ BindIt™ 소프트웨어를 통한 기기 제어, 프로토콜 생성 및 수정
  • 다른 유형의 응용 분야에 바로 사용할 수 있는 프로토콜

권장 용도:

유전체학 및 단백체학, 신약 개발, 법의학, 생물지표 개발, 품질 관리, 수의학 분석

For research use only. Not for use in diagnostic procedures.
사양
Collection Efficiency of Particles95%
깊이(영국식 단위)11.4 in.
깊이(미터법)29cm
설명KingFisher mL Purification System, 100-240V, 50/60Hz 공칭 값
디스플레이시작/중지/커서 키 2개/LCD
전기 요구사항100 ∼ 240V, 50/60Hz
용도(애플리케이션)유전체학 및 단백체학, 신약 개발, 법의학, 생물지표 개발, 품질 관리, 수의학 분석
높이(영국식 단위)12.2 in.
높이(미터법)31cm
자기봉3 x 5 형태
입자 크기(미터법)대략 >1µm
수량Each
팁 콤보특수 설계, 1 x 5 형태
베슬 유형특수 튜브 스트립, 1 x 5 튜브
중량(영국식 단위)23 lb.
중량(미터법)10kg
폭(영국식 단위)11.4 in.
폭(미터법)29cm
용량1회 작동 시 15개 시료
부피(미터법) 프로세싱50 ∼ 1000µL
Unit SizeEach

자주 묻는 질문(FAQ)

Do you have scripts for using the MagMAX kits on the KingFisher mL instrument?

We do not have prewritten scripts for using MagMAX kits on the KingFisher mL instrument. We recommend adapting scripts written for the KingFisher Flex or KingFisher Presto instruments. You will still need to validate the scripts on your KingFisher mL instrument.

Find additional tips, troubleshooting help, and resources within our Automated Nucleic Acid Purification Support Center.

Can I use the MagMAX Express-96 Deep Well Head (Cat. No. 4388435) on the KingFisher 96 instrument?

Yes, the MagMAX Express-96 Deep Well Head can be used on the KingFisher 96 instrument. However, it is not compatible with the KingFisher Flex instrument.

Find additional tips, troubleshooting help, and resources within our Automated Nucleic Acid Purification Support Center.

What should I do if the tip comb does not load correctly onto my Thermo Scientific KingFisher system?

If the tip does not load correctly onto a Thermo Scientific KingFisher magnetic head, we recommend that you try manually flexing the tips both lengthwise and widthwise to level the tip comb. A video of flexing the tip comb can be found here: https://www.thermofisher.com/us/en/home/life-science/dna-rna-purification-analysis/automated-purification-extraction/kingfisher-systems/resources.html. The video is under "KingFisher Flex" and titled "How to install the magnet head and check the tip comb." Flexing of the tip comb is demonstrated at timepoint 1:35. If that does not work, try a different box or lot of tips. This applies to all KingFisher instruments.

인용 및 참조 문헌 (6)

인용 및 참조 문헌
Abstract
Characterization of human cytochrome P450s involved in the bioactivation of tri-ortho-cresyl phosphate (ToCP).
Authors:Reinen J, Nematollahi L, Fidder A, Vermeulen NP, Noort D, Commandeur JN
Journal:
PubMed ID:25706813
'Tri-ortho-cresyl phosphate (ToCP) is a multipurpose organophosphorus compound that is neurotoxic and suspected to be involved in aerotoxic syndrome in humans. It has been reported that not ToCP itself but a metabolite of ToCP, namely, 2-(ortho-cresyl)-4H-1,2,3-benzodioxaphosphoran-2-one (CBDP), may be responsible for this effect as it can irreversibly bind to human ... More
Characterization of the postsynaptic protein neurogranin in paired cerebrospinal fluid and plasma samples from Alzheimer's disease patients and healthy controls.
Authors:Kvartsberg H, Portelius E, Andreasson U, Brinkmalm G, Hellwig K, Lelental N, Kornhuber J, Hansson O, Minthon L, Spitzer P, Maler JM, Zetterberg H, Blennow K, Lewczuk P
Journal:
PubMed ID:26136856
'Synaptic dysfunction and degeneration are central events in Alzheimer''s disease (AD) pathophysiology that are thought to occur early in disease progression. Synaptic pathology may be studied by examining protein biomarkers specific for different synaptic elements. We recently showed that the dendritic protein neurogranin (Ng), including the endogenous Ng peptide 48 ... More
Brain amyloid-beta fragment signatures in pathological ageing and Alzheimer's disease by hybrid immunoprecipitation mass spectrometry.
Authors:Portelius E, Lashley T, Westerlund A, Persson R, Fox NC, Blennow K, Revesz T, Zetterberg H
Journal:
PubMed ID:25591542
'Senile plaques in Alzheimer''s disease (AD) are composed of amyloid-ß (Aß), especially N-truncated forms including Aß4-42. These are thought to be neurotoxic. However, individuals may live for decades with biomarker evidence of cerebral ß-amyloidosis (positive amyloid PET imaging and/or low cerebrospinal fluid levels of the 42 amino acid form of ... More
APP metabolism regulates tau proteostasis in human cerebral cortex neurons.
Authors:Moore S, Evans LD, Andersson T, Portelius E, Smith J, Dias TB, Saurat N, McGlade A, Kirwan P, Blennow K, Hardy J, Zetterberg H, Livesey FJ
Journal:
PubMed ID:25921538
'Accumulation of Aß peptide fragments of the APP protein and neurofibrillary tangles of the microtubule-associated protein tau are the cellular hallmarks of Alzheimer''s disease (AD). To investigate the relationship between APP metabolism and tau protein levels and phosphorylation, we studied human-stem-cell-derived forebrain neurons with genetic forms of AD, all of ... More
Highly potent soluble amyloid-ß seeds in human Alzheimer brain but not cerebrospinal fluid.
Authors:Fritschi SK, Langer F, Kaeser SA, Maia LF, Portelius E, Pinotsi D, Kaminski CF, Winkler DT, Maetzler W, Keyvani K, Spitzer P, Wiltfang J, Kaminski Schierle GS, Zetterberg H, Staufenbiel M, Jucker M
Journal:
PubMed ID:25212850
The soluble fraction of brain samples from patients with Alzheimer's disease contains highly biologically active amyloid-ß seeds. In this study, we sought to assess the potency of soluble amyloid-ß seeds derived from the brain and cerebrospinal fluid. Soluble Alzheimer's disease brain extracts were serially diluted and then injected into the ... More