UltraBio™ Anti-MBP Magnetic Beads (Anti-MBP磁珠)

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货号 (SKU) 包装规格 是否现货 价格 数量
A751542-500μl
500μL 期货 Stock Image
A751542-2ml
2ml 期货 Stock Image
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蛋白纯化 (32)

基本描述

产品名称 UltraBio™ Anti-MBP Magnetic Beads (Anti-MBP磁珠)
别名 UltraBio™ 抗 MBP 磁珠
产品介绍

阿拉丁的UltraBio™ Anti-MBP Magnetic Beads,即Anti-Maltose Binding Protein (MBP)磁珠,也称Anti-MBP磁珠、Anti-MBP免疫磁珠或MBP抗体磁珠,由高质量的MBP标签小鼠单克隆抗体与纳米级氨基磁珠共价偶联而成,可特异性地与动植物或者微生物裂解液、血清、腹水等样品中含有MBP标签的蛋白结合,从而用于带有MBP标签的融合蛋白或蛋白复合物的免疫沉淀(Immunoprecipitation, IP)、免疫共沉淀(Co-IP)或纯化。MBP标签(MBP-tag)、His标签(His-tag)、Flag标签、Myc标签(Myc-tag)、HA标签(HA-tag)和GST标签等是表达载体上最常见的一些标签,通过与这些标签的融合表达可以非常方便地检测目的蛋白及与目的蛋白相互结合的蛋白,也可以非常方便地用于目的蛋白的纯化。麦芽糖结合蛋白(Maltose binding protein, MBP),是大肠杆菌(E. coli)麦芽糖(Maltose)/麦芽糊精(Maltodextrin)系统的一部分,由malE基因编码,负责麦芽糊精的摄取、分解和代谢,分子量约为42kDa 1]。MBP标签,即麦芽糖结合蛋白标签,可融合在蛋白的N端或C端,通常融合在N端。MBP标签具有以下优点:能增加外源蛋白的可溶性2],尤其适用于以不溶性形式积累的重组蛋白,如包涵体(Inclusion bodies, IBs)等;适用范围广,可在不同的宿主如大肠杆菌和酵母中表达并提高靶蛋白的表达水平;可促进蛋白的正确折叠;如果在MBP标签和目的蛋白之间含有氨基酸序列特异性蛋白酶识别位点,如PreScission Protease、TEV Protease或Thrombin等,则可用相应的蛋白酶切除MBP标签;高特异性,纯化方便且温和;MBP标签作为标签蛋白,后续通过MBP抗体、Anti-MBP磁珠即可对目的蛋白的表达、定位及功能进行检测或对目的蛋白进行纯化、免疫沉淀或免疫共沉淀等。基于以上优点,MBP标签已被广泛应用于蛋白表达、纯化、鉴定、相互作用和功能等多方面的研究。一般使用MBP标签蛋白纯化介质对MBP标签蛋白进行纯化,但对于带有MBP标签的融合蛋白或蛋白复合物的少量纯化或免疫沉淀等应用,Anti-MBP磁珠更简单、便捷。UltraBio™ Anti-MBP Magnetic Beads (Anti-MBP磁珠)可特异性地结合MBP标签融合蛋白,并可以借助磁力架等磁分离设备非常便捷地应用于带有MBP标签的融合蛋白或其蛋白复合物的免疫沉淀或纯化等实验。本产品进行免疫沉淀的流程参考图1。图1.阿拉丁UltraBio™ Anti-MBP Magnetic Beads (Anti-MBP磁珠) 免疫沉淀流程图。本产品特异性强、靶蛋白结合量高。与国内外大多数的同类产品相比,本产品抗体结合密度高,对带有MBP标签蛋白的结合具有很强的特异性,并且本产品磁珠粒径小,不易产生非特异吸附。本产品每毫升磁珠悬浊液含约10mg磁珠,含有不少于0.6mg MBP抗体,通常可结合不少于0.6mg MBP标签融合蛋白,具体的最大结合量和标签蛋白的分子量大小等相关。每500微升样品,通常仅需使用10-20微升磁珠悬浊液,就可以高效地进行免疫沉淀实验。本产品可结合多种形式的MBP标签蛋白。本产品可特异性地结合N端MBP融合蛋白(MBP-Protein)、C端MBP融合蛋白(Protein-MBP)。本产品结合目的蛋白速度快。本产品使用了纳米级磁珠(~200nm),具有超大的比表面积,便于抗体和抗原的快速有效结合。通常30分钟内即可完成抗原吸附的过程,60分钟内完成目的蛋白免疫沉淀操作。缩短操作时间可以有效避免在长时间操作过程中目的蛋白的降解或变性,充分保证目的蛋白的活性。本产品可选择多种洗脱方法。本产品根据目的蛋白的结构、生物学功能及后续应用的要求等,使用多种洗脱方法,包括SDS-PAGE上样缓冲液和酸性等洗脱液进行洗脱。本产品用于原核表达MBP融合蛋白的免疫沉淀效果参考图2。图2.UltraBio™ Anti-MBP Magnetic Beads (Anti-MBP磁珠) 用于MBP-tag融合蛋白的免疫沉淀效果图。样品1为Input,即原核表达的MBP-tag融合蛋白全细胞裂解液;样品2为UltraBio™ Mouse IgG Magnetic Beads (小鼠IgG免疫磁珠) 免疫沉淀后经SDS-PAGE蛋白上样缓冲液(1X) 洗脱后的样品,该Mouse IgG是正常的小鼠IgG (Normal Mouse IgG),为阴性对照;样品3为本磁珠免疫沉淀后使用SDS-PAGE蛋白上样缓冲液(1X)洗脱的样品。Western印迹成像由Imager 600化学发光成像系统完成。实际结果会因实验条件、检测仪器等的不同而存在差异,图中数据仅供参考。本产品的主要指标如下表:


注意事项

由于MBP标签本身的分子量较大,约42kDa,与目的基因形成融合蛋白后分子量更大,而且融合蛋白的结构复杂性可能会影响Anti-MBP磁珠对MBP标签的识别,建议先通过免疫沉淀预实验进行效果验证,如有必要可对裂解条件进行适当调整。由于MBP标签与MBP抗体的结合力非常强,酸性洗脱的效果可能比较差,建议优先使用SDS-PAGE上样缓冲液洗脱法。本产品需维持pH为6-8,避免高速离心、干燥;请勿长时间将磁珠置于磁场中,否则可能会引起磁珠聚团。本产品使用前要适当充分重悬,即颠倒若干次使磁珠混合均匀,混匀操作须轻柔,不宜剧烈涡旋震荡等,避免抗体变性等。在免疫沉淀或纯化时,建议设置阳性和阴性对照组。蛋白样品收集后宜尽快完成纯化工作,并应始终放置在4ºC或冰浴,以减缓蛋白降解或变性。为有效抑制蛋白降解,可以在蛋白样品中添加适量的蛋白酶抑制剂混合物,例如阿拉丁的P1005/P1006 蛋白酶抑制剂混合物(通用型)、P1048/P1049 蛋白酶磷酸酶抑制剂混合物(通用型, 质谱兼容, 50X)、P1010/P1011 蛋白酶抑制剂混合物(哺乳动物样品抽提用, 100X)、P1050/P1051 蛋白酶磷酸酶抑制剂混合物(哺乳动物样品抽提用, 50X)等。如果使用真空泵等仪器吸取上清液,须注意真空泵的吸液强度,以免吸力过大而吸取到聚集的磁珠。酸性溶液洗脱时磁珠可能会发生聚集,属于正常现象,不影响磁珠的正常使用。0.1%的非离子型去垢剂(如Triton X-100、Tween-20或NP-40)可有效防止磁珠聚集,并且不会影响磁珠的抗体结合效率。高浓度的DTT、巯基乙醇、盐酸胍等对本产品与标签蛋白的结合可能有一定影响,但Western及IP细胞裂解液、RIPA裂解液或NP-40裂解液等都完全适用。阿拉丁生产的不同裂解液的主要特点和差异,以及如何选择裂解液可参考我们的相关网页:http://www.aladdin-e.com/support/lysis-buffer.htm。本产品仅限于专业人员的科学研究用,不得用于临床诊断或治疗,不得用于食品或药品,不得存放于普通住宅内。为了您的安全和健康,请穿实验服并戴一次性手套操作。


使用说明

1.样品的制备:a.选择合适的裂解液,用于制备细胞或组织的裂解液。优先推荐选择阿拉丁生产的P0013 Western及IP细胞裂解液用于细胞或组织样品的裂解。根据特定的实验目的,如有必要,也可以使用阿拉丁生产的P0013B RIPA裂解液(强)、P0013C RIPA裂解液(中)或P0013D RIPA裂解液(弱)用于样品的制备。如果使用自行配制的或其它公司生产的裂解液,需要确保裂解液的pH为6-8。注:由于MBP标签本身的分子量较大,约42kDa,与目的基因形成融合蛋白后分子量更大,而且融合蛋白的结构复杂性可能会影响Anti-MBP磁珠对MBP标签的识别,建议先通过免疫沉淀预实验进行效果验证,如有必要可对裂解条件进行适当调整。b.具体的细胞或组织样品裂解的制备步骤请参考裂解液的使用说明。制备好的裂解液上清宜置于冰上或4ºC存放,随后即可用于免疫沉淀或免疫共沉淀、标签蛋白的纯化等操作。新鲜制备好的样品,建议尽量当天完成免疫沉淀等后续操作,但如果样品不能当天使用,也可以适当分装后-80ºC冻存。2.Anti-MBP免疫磁珠准备:由于Anti-MBP磁珠储存在特殊保护液中,所以需要在加入样品前用适当洗涤。a.用移液器轻轻吹打重悬Anti-MBP磁珠,按照每500μl样品10μl或20μl磁珠悬浊液,取适量Anti-MBP磁珠至一洁净离心管中,加入1X TBS 至最终体积为约0.5ml。说明:如果初始体积大于0.2ml,可以考虑先直接置于磁力架(FMS012/FMS024)上分离10秒,去除上清,然后再加入1X TBS 至最终体积为约0.5ml。b.用移液器轻轻吹打重悬Anti-MBP磁珠。置于磁力架(FMS012/FMS024)上分离10秒,去除上清。重复上述步骤两次。c.按照初始体积的量,用1X TBS 重悬Anti-MBP磁珠。3.免疫沉淀(Immunoprecipitation, IP):a.加入磁珠与孵育。按照每500μl蛋白样品加入10μl或20μl磁珠悬浊液的比例加入Anti-MBP磁珠,置于侧摆摇床或旋转混合仪上,室温孵育2小时或4ºC孵育过夜。注:孵育过程中,如果磁珠发生聚团或呈片状属正常现象,不会影响实验结果。b.磁分离。孵育完毕后,置于磁力架上分离10秒,去除上清。注:可保留部分上清液,用于检测免疫沉淀的效果。c.洗涤。加入500μl的1X TBS,用移液器轻轻吹打重悬Anti-MBP磁珠。置于磁力架上分离10秒,去除上清。重复洗涤三次。注:也可以通过检测洗涤得到的洗涤液的OD280来判断是否洗涤完全,若OD280大于0.05,应适当增加洗涤次数。4.洗脱:根据标签蛋白的特点及后续实验要求,可以选择如下2种方法之一进行洗脱。a.SDS-PAGE上样缓冲液洗脱法:本方法为变性法,得到的蛋白样品适合SDS-PAGE电泳或WB检测。(a)SDS-PAGE上样缓冲液的配制:可以直接使用阿拉丁生产的P0015A SDS-PAGE蛋白上样缓冲液(1X),或使用阿拉丁生产的P0015 SDS-PAGE蛋白上样缓冲液(5X)或自行参考《分子克隆》等配制5X或2X的SDS-PAGE蛋白上样缓冲液,然后加入水配制成1X的SDS-PAGE蛋白上样缓冲液。通常SDS-PAGE蛋白上样缓冲液含有DTT等还原剂,其洗脱得到的蛋白样品中会含有MBP抗体的轻链和重链。(b)每10-20μl原始磁珠体积的磁珠,加入100μl 1X SDS-PAGE上样缓冲液,95ºC加热5分钟。(c)置于磁力架上分离10秒,取上清进行SDS-PAGE电泳或Western检测。b.酸性洗脱法:本方法为非变性法,洗脱后的蛋白保持原有的生物活性,便于后续分析检测。(a)溶液的配制:酸性洗脱液(0.1M Glycine-HCl, pH3.0),中和液(0.5M Tris-HCl, pH7.4, 1.5M NaCl)。(b)每10-20μl原始磁珠体积,加入100μl酸性洗脱液,混匀后置于侧摆摇床或旋转混合仪上,室温孵育5分钟。注:孵育时间不要超过15分钟。(c)孵育完毕后,置于磁力架上分离10秒,将上清转移到新的离心管中,并立刻加入10μl中和液,适当混匀。(d)为了获得最大的洗脱效率,可重复步骤(b)和(c),并将相同样品合并。(e)洗脱并中和的MBP标签蛋白置于4ºC待用,或者-20ºC或-80ºC长期保存。注1:由于MBP-tag与MBP抗体的结合力非常强,酸性洗脱法的效果可能低于SDS-PAGE上样缓冲液洗脱法。注2:由于目的蛋白的差异,酸性洗脱法的洗脱效率也会存在一定的差异。如果对洗脱效率的要求比较高,可对酸性洗脱液的pH值在2.5-3.1之间进行适当的调整,相应的中和液的pH值或量也要进行适当的调整,例如100μl酸性洗脱液(0.1M Glycine-HCl, pH2.8)和15μl中和液(1M Tris-HCl, pH8.5)。常见问题: Problem Possible Causes Solution Very few or no MBP‐tagged protein exists in the eluate. Protein is not completely eluted. Change elution methods. No target protein expressed. Make sure the protein of interest contains the MBP-tag by Western blot or dot blot analyses. Very low protein expression level. 1.Use larger volume of cell lysate. 2.Optimize expression conditions to raise the protein expression level. Washes are too stringent. Reduce the time and number of washes. Incubation times are inadequate. Increase the incubation time. Interfering substance is present in sample. Lysates containing high concentration of DTT, 2-mercaptoethanol, or other reducing agents may destroy antibody function, and must be avoided. Detection system is inadequate. If Western blot detection is used:1.Check primary and secondary antibodies using proper controls to confirm binding and reactivity.2.Verify that the transfer was adequate by usingprestained protein marker or staining the membrane with Ponceau S.3.Use fresh detection substrate or try a different detection system. Background is too high. Proteins bind nonspecifically to the Anti-MBP monoclonal antibody, insufficient washing on magnetic beads, or the microcentrifuge tubes. 1.Pre-clear lysate with Mouse IgGMagnetic Beadsto remove nonspecific binding proteins.2.After suspending beads for the final wash, transfer entire sample to a clean microcentrifuge tube before centrifugation. Washes are insufficient. 1.Increase the number of washes.2.Prolong duration of the washes, incubating each wash for at least 15 minutes.3.Increase the salt and/or detergent concentrations in the wash solutions.4.Centrifuge at lower speed to avoid nonspecific trapping of denatured proteins. Multiple protein bands found in the eluate. The protein is not stable at room temperature. Purify the target protein at lower temperature, such as 4ºC. Protein degradation due to proteases activity during purification process. Add protease inhibitors to cell lysate. Non‐specific binding. 1.Prepare cell lysate again.2.Add additional wash steps. 参考文献:1.Duplay P, Bedouelle H, Fowler A, Zabin I, Saurin W, et al. J Biol Chem. 1984. 259(16):10606-13.2.Reuten R, Nikodemus D, Oliveira MB, Patel TR, Brachvogel B, et al. PLoS One. 2016. 11(3):e0152386.

Aladdin's UltraBio™ Anti-MBP Magnetic Beads are nano-scale amino magnetic beads covalently coupled with high-quality MBP mouse monoclonal antibodies. These beads can specifically bind MBP fusion proteins in lysates, serum, ascites, or other samples from animals, plants, or microorganisms. This product is mainly used for immunoprecipitation (IP), co-immunoprecipitation (Co-IP), or purification of MBP-tagged proteins or their protein complexes.Maltose binding protein (MBP) encoded by the malE gene is a component of the E. coli maltose/maltodextrin system and regulates the uptake and catabolism of maltodextrins, with a molecular weight of approximately 42kDa [1]. The MBP tag can be fused to the N- or C-terminus of a protein, with the N-terminus being the most common fusion site. The MBP tag has several advantages


Precautions

Due to the large molecular weight of the MBP tag itself (approximately 42kDa), the larger fusion protein structure may affect the recognition of the MBP tag by the Anti-MBP Magnetic Beads. We recommend performing a preliminary immunoprecipitation test to verify the effectiveness. The lysis conditions can be adjusted appropriately if necessary.Due to the strong binding affinity between the MBP tag and the MBP antibody, acidic elution may not be effective. It is recommended to use the SDS-PAGE loading buffer elution method in priority.This product should be maintained at pH of 6-8. Avoid high-speed centrifugation and drying of the magnetic beads. Long time exposure of the beads to magnetic field will cause beads to agglomerate.Properly resuspend the magnetic beads before use by gently inverting the tube several times. Do not vortex or shake the beads vigorously to avoid antibody denaturation.When performing immunoprecipitation or purification with this product, it is recommended to include both positive and negative controls.Protein samples should be purified as soon as possible after collection and should always be placed at 4℃ or on ice to minimize protein degradation or denaturation. Protein degradation can also be inhibited by adding appropriate protease inhibitors, such as Protease Inhibitor Cocktail for General Use , Protease and Phosphatase Inhibitor Cocktail for General Use (MS-safe, 50X) , Protease Inhibitor Cocktail for Mammalian Cell and Tissue Extracts , Protease and Phosphatase Inhibitor Cocktail for Mammalian Cell and Tissue Extracts , etc.If using a vacuum pump to aspirate the supernatant, the strength of the vacuum pump should be controlled properly to avoid the aspiration of magnetic beads.Containing 0.1% non-ionic detergent (such as Triton X-100, Tween-20, and NP-40) in solutions can effectively prevent aggregation of magnetic beads, without affecting the antibody binding efficiency of the beads.High concentrations of DTT, mercaptoethanol, or guanidine hydrochloride, may have a certain effect on the binding of this product to MBP fusion proteins, but Cell lysis buffer for Western and IP , RIPA Lysis Buffer and NP-40 Lysis Buffer , are fully applicable. For the selection guide of different lysis buffers from , please refer to our website at: http://www.aladdin-e.com/support/lysis-buffer.htm.This product is for R&D only. Not for drug, household, or other uses.For your safety and health, please wear a lab coat and disposable gloves during the operation


Instructions for Use

1. Preparation of protein samples:a. Lysis cells or tissues with appropriate lysis buffer. We recommend using 's Cell Lysis Buffer for Western and IP as a priority. Under certain circumstances, RIPA Strong Lysis Buffer , RIPA Medium Lysis Buffer , or RIPA Weak Lysis Buffer can be attempted. Other lysis buffers with a pH of 6-8 can also be used.b. After lysis and centrifuge, keep the supernatant at 4℃ or on ice for subsequent use. We recommend performing the subsequent procedures on the same day as the protein sample is prepared. Otherwise, make aliquots and keep them at -80℃ for future use.2. Preparation of Anti-MBP Magnetic BeadsAs Anti-MBP magnetic beads are stored in a special protective solution, they need to be washed with an appropriate wash buffer before adding to samples.a. Resuspend the Magnetic Beads in the vial (gently pipette for 10 times, do not vortex). Transfer 10-20μl of Magnetic Beads suspension into a new tube (for 500μl of protein sample). The amount of beads suspension can be scaled up or down proportionally based on the volume of the protein sample.Note: If the initial volume is greater than 0.2 ml, consider separating by placing directly on a magnetic rack (FMS012/FMS024) for 10 seconds to remove the supernatant before adding 1X TBS to a final volume of ~0.5 ml.b. Add 500μl of 1X TBS (, ST661/ST665) to the beads and pipette gently to mix. Place the tube into a magnetic stand for 10 seconds to collect the beads against the side of the tube. Remove and discard the supernatant. Repeat this step twice.c. Resuspend the Magnetic Beads with 1X TBS at an equal volume to the initial volume of beads suspension taken in step a (e.g., if 10μl of beads suspension is taken, add 10μl of 1X TBS).3. Protein bindinga. Add 500μl of cell lysate to the washed beads, pipette gently to mix well, and incubate for 2 hours at room temperature or overnight at 4℃ while gently rotating on a rotary mixer.Note: Occasional aggregation of magnetic beads during the binding process doesn't affect experimental results.b. Place the tube on a magnetic stand for 10s to collect beads against the side of the tube. Remove and discard the supernatant.Note: A small amount of supernatant can be reserved in a clean EP tube for examination of the binding results.c. Wash beads with 500μl of 1X TBS and gently pipette to mix. Place the tube on a magnetic stand for 10s to collect the beads against the side of the tube. Remove and discard the supernatant. Repeat this step 3 timesNote: The A280 of supernatant can also be measured to determine whether the beads are washed thoroughly. Repeat washing until the A280 is smaller than 0.05.4. ElutionBased on the features of the target protein and downstream applications, one of the following two elution methods can be used.a. Elution with 1X SDS-PAGE loading buffer under denaturing conditions: The protein sample obtained is suitable for SDS-PAGE electrophoresis or Western blot.(a) Prepare SDS-PAGE loading buffe, or directly use 's SDS-PAGE protein loading buffer (1X) . Typically, SDS-PAGE protein loading buffer contains reducing agents such as DTT, and the eluted protein sample will contain the light and heavy chains of the MBP antibody.(b) Add 100μl of 1X SDS-PAGE loading buffer per 10-20μl of magnetic beads, and heat at 95℃ for 5 minutes.(c) Place the magnetic beads on a magnetic stand for 10 seconds and collect the supernatant for SDS-PAGE electrophoresis or Western blot analysis.b. Elution under acidic conditions. This method is rapid and highly efficient. The eluted protein also maintains its original bioactivity, which is beneficial for subsequent activity analysis.(a) Prepare acidic elution buffer (0.1M Glycine-HCl, pH3.0) and neutralization buffer (0.5M Tris-HCl, pH7.4, 1.5M NaCl). (b) Add 100μl of acidic elution buffer to resuspend the beads by gently pipetting and incubate with gentle shaking or on a rotary mixer for 5 minutes at room temperature (no more than 15 minutes). (c) Place the tube on a magnetic stand for 10 seconds and transfer the supernatant to a new EP tube. Add 10μl of neutralization buffer immediately to neutralize the low pH, which helps preserve the bioactivity of the target protein. Mix well gently.(d) For immediate use, keep the eluates at 4℃, or store at -20℃ or -80℃ for long-term storage. (e) To obtain higher elution efficiency, repeat steps b-c and combine the eluates.Note 1: Due to the strong binding affinity between the MBP tag and the MBP antibody, the effectiveness of acidic elution may be lower than that of SDS-PAGE loading buffer elution method.Note 2: The acidic elution efficiency varies depending on the features of the target protein. To obtain a higher elution efficiency, the pH of the acidic elution buffer can be optimized from 2.5 to 3.1, and the pH or amount of neutralization buffer needs to be adjusted correspondingly.FAQ: ProblemPossible CausesSolutionsVery few or no Flag‐tagged protein in the eluate.Protein is not completely elutedChange elution methods.No target protein expressedMake sure the target protein contains the MBP-tag by Western blot or dot blot analysis.Very low protein expression level1. Use larger volume of cell lysate.Optimize expression conditions to increase the protein expression level.Washes are too stringentRReduce the wash time and number of washes.Incubation time is inadequate.Prolong the incubation time.Interfering substances present in the sample.Lysates should not contain high concentration of DTT, 2-mercaptoethanol, or other reducing agents that may interfere with antibody-antigen interaction.Low sensitivity of the detection system.For Western blot analysis:1. Check the specificity and reactivity of primary and secondary antibodies using proper controls.2. Check the protein transfer efficiency by using prestained protein marker or staining the membrane with Ponceau S.3. Use fresh ECL western substrate or try a different ECL substrate with higher sensitivity.The background is too high.Nonspecific binding of proteins to antibodies, beads, or EP tubes.1. Pre-clear lysate with Mouse IgG Magnetic Beads to remove nonspecific binding proteins.2. After suspending beads for the final wash, transfer entire sample to a clean microcentrifuge tube before centrifugation.Insufficient washing of magnetic beads after protein binding1. Increase the number of washes.2. Prolong the duration of each wash to at least 15 minutes.3. Increase the salt and/or detergent concentrations in wash buffer.Centrifuge at lower speed to avoid nonspecific trapping of denatured proteins.Multiple protein bands found in the eluate.The protein is not stable at room temperaturePurify the target protein at lower temperature, such as 4℃.Protein degradation due to protease activity during the purification process.Add protease inhibitors to cell lysate.Non‐specific binding.1. Prepare cell lysate again.2. Add additional wash steps.References:1. Duplay P, Bedouelle H, Fowler A, Zabin I, Saurin W, et al. J Biol Chem. 1984. 259(16):10606-13.2. Reuten R, Nikodemus D, Oliveira MB, Patel TR, Brachvogel B, et al. PLoS One. 2016. 11(3):e0152386.


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