NuPAGE™ 4 ∼ 12%, Bis-Tris, 1.0–1.5 mm, Mini Protein Gels

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NuPAGE™ 4 &sim; 12%, Bis-Tris, 1.0–1.5 mm, Mini Protein Gels

인용 및 참조 문헌 (4)

Invitrogen™

NuPAGE™ 4 ∼ 12%, Bis-Tris, 1.0–1.5 mm, Mini Protein Gels

Name: NuPAGE™ 4 &sim; 12%, Bis-Tris, 1.0–1.5 mm, Mini Protein Gels
SKU: NP0330BOX
Price: 295000 KRW

Invitrogen NuPAGE Bis-Tris 단백질 겔은 고분해능 및 시료 무결성과 함께 광범위한 분자량 단백질 분리를 제공하는 프리캐스트 폴리아크릴아마이드 겔입니다.

보기 방식 변경

카탈로그 번호	웰	Gel Thickness	수량
NP0330BOX	IPG-well	1.0 mm	10 Gels/Box
NP0321BOX	10-웰	1.0 mm	10 Gels/Box
NP0321PK2	10-웰	1.0 mm	2 Gels/Box
NP0322BOX	12-웰	1.0 mm	10 Gels/Box
NP0322PK2	12-웰	1.0 mm	2 Gels/Box
NP0323BOX	15-웰	1.0 mm	10 Gels/Box
NP0323PK2	15-웰	1.0 mm	2 Gels/Box
NP0324BOX	1-웰	1.0 mm	10 Gels/Box
NP0326BOX	2D-웰	1.0 mm	10 Gels/Box
NP0327BOX	9-웰	1.0 mm	10 Gels/Box
NP0329BOX	17-웰	1.0 mm	10 Gels/Box
NP0329PK2	17-웰	1.0 mm	2 Gels/Box
NP0335BOX	10-웰	1.5mm	10 Gels/Box
NP0335PK2	10-웰	1.5mm	2 Gels/Box
NP0336BOX	15-웰	1.5mm	10 Gels/Box
NP0336PK2	15-웰	1.5mm	2 Gels/Box

16 개 옵션

카탈로그 번호 NP0330BOX

제품 가격(KRW)

295,000

Online offer

Ends: 31-Mar-2026

337,000

할인액 42,000 (12%)

Each

카트에 추가하기

웰:

IPG-well

Gel Thickness:

1.0 mm

수량:

10 Gels/Box

제품 가격(KRW)

295,000

Online offer

Ends: 31-Mar-2026

337,000

할인액 42,000 (12%)

Each

카트에 추가하기

Invitrogen NuPAGE Bis-Tris 단백질 겔은 고분해능 및 시료 무결성을 통해 광범위한 분자량 단백질 분리를 제공하는 프리캐스트 폴리아크릴아마이드 겔입니다. 이 프리캐스트 겔은 단백질 무결성이 중요한 응용 분야에 이상적입니다. 기존 Tris-glycine gel과 달리 NuPAGE Bis-Tris gel은 중성 pH로 단백질 변형을 최소화합니다. NuPAGE Bis-Tris gel을 사용하여 단백질 무결성이 중요한 염기서열 분석, 질량분석법 등 여러 주요 기법을 위해 단백질 분리를 수행할 수 있습니다.

NuPAGE Bis-Tris 겔의 주요 특징:
• 더 나은 단백질 무결성—최적화된 시료 준비 프로세스로 단백질 보존
• 광범위한 분자량 분리—최적의 단백질 분리를 위해 올바른 겔 및 런닝 버퍼 선택
• 더 빨라진 실행 시간—35분 만에 단백질 분리
• 더 긴 유효기간—NuPAGE Bis-Tris 겔은 실온에서 최소 12개월 동안 보관할 수 있습니다.

단백질 분리에 적합한 NuPAGE Bis-Tris 겔 선택
겔과 런닝 버퍼의 올바른 조합을 선택하여 단백질을 최적으로 분리하십시오. NuPAGE Bis-Tris 단백질 겔은 다음의 4가지 폴리아크릴아마이드 농도로 제공됩니다: 8%, 10%, 12%, 4–12% 농도구배. 겔은 mini(8cm x 8cm)와 midi(8.7cm x 13.3cm) 두 가지 사이즈로 제공되며 두께는 1.0mm(mini 및 midi gel) 또는 1.5mm(mini gel format만)입니다. NuPAGE Bis-Tris 겔은 또한 다중 웰 형태로도 제공됩니다.

NuPAGE Bis-Tris 겔은 변성 겔 전기영동 응용 분야에 맞게 제조됩니다. 최적의 시료 전처리를 위해 NuPAGE LDS Sample Buffer(NP0007) 및 NuPAGE Sample Reducing Agent(NP0004)를 사용하십시오. 러닝 버퍼에 NuPAGE Antioxidant(NP0005)를 사용하여 실행 중 단백질의 환원 상태를 유지하고 밴드 선명도를 최대화할 수 있습니다. 겔은 작은 단백질을 더 잘 분리하기 위해 NuPAGE MES SDS Running Buffer(NP0002)를 사용하거나 중간 크기에서 큰 크기의 단백질을 분리하기 위해 NuPAGE MOPS SDS Running Buffer(NP000102)를 사용하여 분리할 수 있습니다.

단백질을 멤브레인으로 트랜스퍼하려면 기존의 wet 트랜스퍼 방식을 위한 NuPAGE Transfer Buffer(NP00061) 를 사용하여 Mini Blot Module(B1000) 또는 XCell II Blot Module(EI9051)에서 수행하는 것이 좋습니다. 또는 Invitrogen Power Blotter 를 사용하여 급속 semi-dry 트랜스퍼를 하거나 iBlot 2 Gel Transfer Device(IB21001)를 사용하여 급속 dry 트랜스퍼를 할 수 있습니다.

For Research Use Only. Not for use in diagnostic procedures.

사양

용도(장비)XCell SureLock Mini-Cell

Gel Thickness1.0 mm

길이(미터법)8 cm

분리 모드분자량

수량10 Gels/Box

샘플 로딩 부피7 cm 스트립

유통 기한12개월

배송 조건실온

보관 요구 사항보관 온도: 4–25°C 냉동하지 마십시오.

폭(미터법)8 cm

젤 비율4 ∼ 12%

젤 크기Mini

젤 유형Bis-Tris

제품라인NuPAGE, ZOOM

분리 범위3.5 ∼ 260kDa

분리 유형변성

웰IPG-well

Unit SizeEach

자주 묻는 질문(FAQ)

Can I prepare my protein sample with the reducing agent and store it for future use?

DTT is not stable, so it must be added and the reduction performed just prior to loading your samples.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

My LDS or SDS sample buffer precipitates when stored at 4 degrees C. Can I warm it up? Can I store it at room temperature?

Precipitation of the LDS or SDS at 4 degrees C is normal. Bring the buffer to room temperature and mix until the LDS/SDS goes into solution. If you do not want to wait for it to dissolve, you can store the sample buffer at room temperature.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

How are Bolt gels different than NuPAGE gels?

While they are both Bis-Tris based gels, the chemistries are very different since Bolt gels are optimized for western blotting. Another key difference is the wedge well design of the Bolt gels, which allows larger sample volumes to be loaded.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

What is the advantage of NuPAGE Gels over regular Tris-Glycine gels?

The neutral operating pH of the NuPAGE Gels and buffers provides following advantages over the Laemmli system:
-Longer shelf life of 8-12 months due to improved gel stability
-Improved protein stability during electrophoresis at neutral pH resulting in sharper band resolution and accurate results (Moos et al, 1998)
-Complete reduction of disulfides under mild heating conditions (70 degrees C for 10 min) and absence of cleavage of asp-pro bonds using the NuPAGE LDS Sample buffer (pH > 7.0 at 70 degrees C)
-Reduced state of the proteins maintained during electrophoresis and blotting of the proteins by the NuPAGE Antioxidant
Please refer to the following paper: Moos M Jr, Nguyen NY, Liu TY (1988) Reproducible High Yield Sequencing of Proteins Electrophoretically Separated and Transferred to an Inert Support. J Biol Chem 263:6005-6008.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

What may cause streaking on the 2nd dimension gel after IEF?

There are several reasons why streaking may occur.

(1) Sample is not completely solubilized prior to application.

(2) Sample is poorly soluble in rehydration solution.

(3) Non-protein impurities in the sample can interfere with IEF, causing horizontal streaking in the final 2-D result, particularly toward the acidic side of the gel.

(4) Ionic impurities are present in sample.

(5) Ionic detergent is present in sample.

(6) Sample load is too high.

(7) Underfocusing. Focusing time was not long enough to achieve steady state focusing.

(8) Overfocusing. Extended focusing times (over 100,000 Vh) may result in electroendosmotic water and protein movement, which can produce horizontal smearing.

What should be done?

(1) Be sure that the sample is completely and stably solubilized. Note: Repeated precipitation-resolubilization cycles produce or increase horizontal streaking.

(2) Increase the concentration of the solubilizing components in the rehydration solution.

(3) Modify sample preparation to limit these contaminants or dialyze protein.

(4) Reduce salt concentration to below 10 mM by dilution or desalt the sample by dialysis. Precipitation with TCA and acetone and subsequent resuspension is another effective desalting technique that removes lipids, nucleotides and other small molecules.
Note: Specific and non-specific losses of proteins can occur with dialysis, gel chromatography, and precipitation/resuspension of samples. If the sample preparation cannot be modified, the effect of ionic impurities can be reduced by modifying the IEF protocol. Limit the voltage to 100-150 V for 2 hours, then resume a normal voltage step program. This pre-step allows the ions in the sample to move to the ends of the IPG strip.

(5) If the ionic detergent SDS is used in sample preparation, the final concentration must not exceed 0.25% after dilution into the rehydration solution. Additionally, the concentration of the non-ionic detergent present must be at least 8 times higher than the concentration of any ionic detergent to ensure complete removal of SDS from the proteins.

(6) Extend focusing time. Load less sample.

(7) Prolong focusing time.

(8) Reduce focusing time.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

View all NuPAGE™ 4 ∼ 12%, Bis-Tris, 1.0–1.5 mm, Mini Protein Gels FAQs

인용 및 참조 문헌 (4)

인용 및 참조 문헌

Abstract

Sero-epidemiology as a tool to screen populations for exposure to Mycobacterium ulcerans.

Authors:Yeboah-Manu D, Röltgen K, Opare W, Asan-Ampah K, Quenin-Fosu K, Asante-Poku A, Ampadu E, Fyfe J, Koram K, Ahorlu C, Pluschke G,

Journal:PLoS Negl Trop Dis

PubMed ID:22253937

'Previous analyses of sera from a limited number of Ghanaian Buruli ulcer (BU) patients, their household contacts, individuals living in BU non-endemic regions as well as European controls have indicated that antibody responses to the M. ulcerans 18 kDa small heat shock protein (shsp) reflect exposure to this pathogen. Here, ... More

Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease.

Authors:Zheng L, Nukuna B, Brennan ML, Sun M, Goormastic M, Settle M, Schmitt D, Fu X, Thomson L, Fox PL, Ischiropoulos H, Smith JD, Kinter M, Hazen SL,

Journal:J Clin Invest

PubMed ID:15314690

In recent studies we demonstrated that systemic levels of protein-bound nitrotyrosine (NO(2)Tyr) and myeloperoxidase (MPO), a protein that catalyzes generation of nitrating oxidants, serve as independent predictors of atherosclerotic risk, burden, and incident cardiac events. We now show both that apolipoprotein A-I (apoA-I), the primary protein constituent of HDL, is ... More

Akt-mediated valosin-containing protein 97 phosphorylation regulates its association with ubiquitinated proteins.

Authors:Klein JB, Barati MT, Wu R, Gozal D, Sachleben LR, Kausar H, Trent JO, Gozal E, Rane MJ,

Journal:J Biol Chem

PubMed ID:16027165

Hypoxia is a common environmental stress that influences signaling pathways and cell function. Previous studies from our laboratory have identified significant differences in cellular responses to sustained or intermittent hypoxia with the latter proving more cytotoxic. We hypothesized that differences in susceptibility of neurons to intermittent (IH) and sustained hypoxia ... More

Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1.

Authors:Asai R, Kato A, Kato K, Kanamori-Koyama M, Sugimoto K, Sairenji T, Nishiyama Y, Kawaguchi Y,

Journal:J Virol

PubMed ID:16698993

Epstein-Barr virus (EBV) BGLF4 is a viral protein kinase that is expressed in the lytic phase of infection and is packaged in virions. We report here that BGLF4 is a tegument protein that dissociates from the virion in a phosphorylation-dependent process. We also present evidence that BGLF4 interacts with and ... More