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| 货号 (SKU) | 包装规格 | 是否现货 | 价格 | 数量 |
|---|---|---|---|---|
| A743825-500μl |
500μL |
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| A743825-2ml |
2ml |
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| A743825-10ml |
10ml |
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| 产品名称 | Anti-V5 Affinity Gel (Anti-V5亲和凝胶) |
|---|---|
| 产品介绍 |
阿拉丁生产的Anti-V5 Affinity Gel (Anti-V5亲和凝胶),也称Anti-V5 IP Gel、Anti-V5免疫沉淀凝胶或Anti-V5琼脂糖凝胶,由高质量的单克隆鼠源V5抗体与琼脂糖共价偶联而成,可与常规蛋白表达系统(如哺乳动物细胞、细菌或酵母)中含有V5标签的蛋白结合,从而用于带有V5标签的融合蛋白或蛋白复合物的免疫沉淀(Immunoprecipitation, IP)或纯化。V5标签(V5-tag)、Flag标签、Myc标签(Myc-tag)、HA标签(HA-tag)、His标签(His-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。V5-tag是从猴副流感病毒V5中分离得到的由14个氨基酸(GKPIPNPLLGLDST)组成的多肽,通过基因重组技术把V5-tag的核酸序列与目的基因的5'端或3'端连接,就可以最终表达形成V5-tag的目的蛋白。V5-tag具有以下优点:V5-tag通常不会与目的蛋白相互作用,并且大多数情况下不会影响目的蛋白的功能;V5-tag作为蛋白标签,后续通过"V5抗体、Anti-V5磁珠或Anti-V5亲和凝胶即可对目的基因的表达、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,V5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。Anti-V5 Affinity Gel (Anti-V5亲和凝胶),也被称为Anti-GKPIPNPLLGLDST Affinity Gel/Beads/Resin或Anti-GKPIPNPLLGLDST IP Gel/Beads/Resin,可特异性地结合V5标签融合蛋白,广泛应用于带有V5标签的融合蛋白或蛋白复合物的免疫沉淀或纯化等实验。本产品有较高的融合蛋白结合量、特异性强:每ml纯凝胶(settled gel)含有约7.5mg V5抗体,可结合约0.5mg融合蛋白,且特异性强,非特异的杂蛋白结合少。本产品可结合多种形式的V5标签蛋白:本产品可特异性地结合N端V5融合蛋白(V5-Protein)、C端V5融合蛋白(Protein-V5)。本产品可选择多种洗脱方法:本产品根据蛋白结构的完整性、生物功能及后续应用的要求等,可使用多种洗脱方法,包括V5多肽、酸性和SDS-PAGE上样缓冲液等洗脱液进行洗脱。特别是V5多肽洗脱后不包含抗体的轻链和重链,可以有效解决免疫沉淀后Western实验中轻链和重链的干扰问题。本产品可重复使用多次,性价比高:在正常情况下,本产品用于相同蛋白的纯化时可回收使用3-5次。如果用于免疫共沉淀检测蛋白-蛋白的相互作用,不推荐重复使用。本产品的主要指标如下表:本产品为50%凝胶悬液,包装体积为总体积,每毫升本产品中共含有0.5ml纯凝胶(沉淀物)。 注意事项: 本产品使用前一定要充分重悬,即充分颠倒若干次使混合均匀。本产品含有微量的防腐剂,不会影响常规的蛋白或蛋白复合物的纯化和免疫沉淀。但如果后续涉及酶活性测定,使用本产品前宜先用TBS等适当溶液洗涤凝胶3次,以充分消除防腐剂可能产生的干扰。在免疫沉淀或纯化时,建议设计阳性和阴性对照组。蛋白样品收集后宜尽快完成纯化工作,并应始终放置在4℃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,或P1025/P1026蛋白酶抑制剂混合物(细菌抽提用)。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。若离心不能完全除去蛋白样品中的不溶物,可以将样品溶液用0.45μm的滤膜过滤。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。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4℃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-80℃冻存。2.Anti-V5 Affinity Gel (Anti-V5亲和凝胶)的准备。由于Anti-V5 Affinity Gel储存在含50%甘油的保护液中,所以需要在加入样品前适当洗涤。a.轻轻重悬Anti-V5 Affinity Gel,尽量形成均匀的凝胶悬液,按照通常每100μl细胞裂解液中加入20μl混合均匀的凝胶悬液(以下免疫沉淀法中都以20μl凝胶悬液为例),取适量Anti-V5 Affinity Gel至一洁净离心管中,加入1X TBS 至最终体积为约0.5ml。注:使用大孔径吸头(如用剪刀剪去部分吸头)吸取凝胶悬液会比较方便。b.轻轻重悬Anti-V5 Affinity Gel,6000×g在4℃离心30秒,小心去除上清,不要吸到凝胶。重复上述步骤两次。c.按照初始体积的量,用1X TBS 重悬Anti-V5 Affinity Gel。3.免疫沉淀(Immunoprecipitation, IP)。1)加入凝胶与孵育。按照每100μl蛋白样品加入20μl凝胶悬液的比例加入Anti-V5 Affinity Gel,置于侧摆摇床或旋转混合仪上,4℃孵育1-2小时。如需提高结合效率,可4℃孵育过夜。2)离心分离。孵育完毕后,6000×g在4℃离心30秒,小心去除上清,不要吸到凝胶。注:可保留部分上清液,用于检测免疫沉淀的效果。3)洗涤。加入500μl的1X TBS,轻轻重悬Anti-V5 Affinity Gel,冰浴并置于摇床上5分钟,然后6000×g在4℃离心30秒,小心去除上清,不要吸到凝胶。重复洗涤三次。样品置于冰上用于洗脱。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3种方法之一进行洗脱。1)V5竞争洗脱法:本方法为非变性法,洗脱效率高,且洗脱后的蛋白保持原有的生物活性,便于后续分析检测。a.V5多肽洗脱液的配制:取适量V5多肽溶解于1X TBS中,使其终浓度为150μg/ml,或稀释5mg/ml的V5多肽溶液至150μg/ml。b.每20μl原始凝胶悬液体积,加入100μl V5多肽洗脱液(150μg/ml),混匀后置于侧摆摇床或旋转混合仪上,室温摇晃孵育30-60分钟,或4℃孵育1-2小时。为了提高洗脱效率,可延长孵育时间或重复洗脱。V5多肽洗脱液体积一般为凝胶悬液的5倍。c.孵育完毕后,6000×g在4℃离心30秒,将上清转移到新的离心管中。上清即为洗脱的V5标签蛋白。d.洗脱的V5标签蛋白置于4℃待用,或者-20℃或-80℃长期保存。注:由于V5-tag与V5抗体的结合力非常强,V5多肽竞争洗脱的效果可能会不太理想,此时需要对V5多肽浓度及竞争条件进行一定的优化。2)酸性洗脱法:本方法为非变性法,比较快速且高效。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20μl原始凝胶悬液体积,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。酸性洗脱液体积一般为凝胶悬液的5倍。注:孵育时间不宜超过15分钟。c.孵育完毕后,6000×g在4℃离心30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V5标签蛋白置于4℃待用,或者-20℃或-80℃长期保存。注1:酸性洗脱法虽然高效,但仍可能低于竞争洗脱法或SDS-PAGE上样缓冲液洗脱法。注2:由于目的蛋白的差异可能对酸性洗脱法的洗脱效率有一定的影响,如果对洗脱效率的要求比较高,可对酸性洗脱液的pH在2.5-3.1之间进行一定的调整,相应的中和液的pH值或量也要进行一定的调整,例如100μl酸性洗脱液(0.1M Glycine-HCl, pH2.8)和15μl中和液(1M Tris-HCl, pH8.5)。3)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P0015B SDS-PAGE蛋白上样缓冲液(2X),但含有DTT等还原剂,用该上样缓冲液洗脱得到的样品中含有V5抗体的轻链和重链。也可以自行参考《分子克隆》等配制不含DTT的2X SDS-PAGE蛋白上样缓冲液。b.每20μl原始凝胶悬液体积,加入20μl 2X SDS-PAGE上样缓冲液,95℃加热5分钟。c.6000×g在4℃或室温离心30秒,取上清进行SDS-PAGE电泳或WB检测。注:由于上样缓冲液中SDS会破坏V5抗体,所以洗脱后的凝胶不能重复使用。常见问题: Problem Possible Causes Solution Large amount of tagged protein found in the flow through. Binding time is not enough. If using batch method, increase the binding time experimentally; If using column method, use a lower flow rate when loading samples. Column is overloaded. Reduce the amount of the sample added to the gel or increase the amount of gel. Tag is not accessible to gel. Expose the epitope tag by adding low amount of denaturant to the protein extract (dialysis may be needed before applying onto gel), or fuse thetag to the other terminus of the target protein. Gel has not been regenerated since last purification. Perform gel regeneration procedure prior to binding. Reagent compatibility problem. Dialyze the sample against TBS before purification procedure. The target protein has been degraded. 1.Prepare fresh lysates. Avoid using frozen lysates.2.Perform purification at lower temperature, such as 4℃.3.Use appropriate protease inhibitors in the lysate or increase their concentrations to prevent degradation of the fusion protein. Very few or notagged 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 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. 1.Reduce the number of washes.2.Avoid adding high concentrations of NaCl to the mixture.3.Use solutions that contain less or no detergent Incubation times are inadequate. Increase the incubation times with the affinity gel (from several hours to overnight). Interfering substance is present in sample. 1.Lysates containing high concentrations of DTT, 2-mercaptoethanol, or other reducing agents may destroy antibody function, and must be avoided.2.Excessive detergent concentrations may interfere with the antibody-antigen interaction. Detergent levels in buffers may be reduced by dilution. 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 staining the membrane with Ponceau S.3.Use fresh detection substrate or try a different detection system. Multiple protein bands found in the eluate. The protein is not stable at room temperature. Purify the target protein at lower temperature, such as 4℃. 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. Background is too high. Proteins bind nonspecifically to the monoclonal antibody, the gel beads, or the microcentrifuge tubes. 1.Pre-clear lysate with Mouse IgG-Agarose to 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 from the lysate during the initial centrifugation of the affinity gel complexes. Aladdin's Anti-V5 Affinity Gel, also known as Anti-V5 IP Gel, Anti-V5 immunoprecipitation gel or Anti-V5 agarose gel, is agarose gel covalently coupled with high-quality mouse monoclonal antibody that recognizes the V5 tag sequence (GKPIPNPLLGLDST). This product can specifically bind V5-tagged proteins expressed in animals, plants, and microorganisms, and can be used for immunoprecipitation (IP) and purification of V5-tag fusion proteins or their protein complexes.V5-tag is a peptide consisting of 14 amino acids (GKPIPNPLLGLDST) isolated from monkey parainfluenza virus V5, which can be fused either to the N-terminus or the C-terminus of a target protein to facilitate protein purification and immunoassays. V5-tag usually does not interact with the target protein, and in most cases does not affect the function of the target protein; With Aladdin's V5 antibodies , Anti-V5 magnetic beads , or Anti-V5 affinity gel , V5-tagged proteins can be used for examination of protein expression level and subcellular localization, protein purification, and immunoassays.This product has high binding capacity and strong specificity Precautions: This product must be fully resuspended by inverting the tube several times prior to use.This product contains a small amount of preservative, which does not affect routine IP assays and protein purification. But for special experiments that might be interfered by the preservative, the gel should be washed 3 times with appropriate solutions such as TBS prior to use.For immunoprecipitation assays, 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 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.High concentrations of DTT, mercaptoethanol, guanidine hydrochloride, etc. may have a certain effect on the binding of this product to V5-tagged proteins, but Cell lysis buffer for Western and IP , RIPA Lysis Buffer or NP-40 Lysis Buffer are applicable to this product. For the main features and differences of various lysis buffers produced by and the selection of lysis buffers, please refer to the website at http://www.aladdin-e.com/support/lysis-buffer.htm.If the insoluble substance in protein samples can not be removed completely by centrifugation, samples can be filtered with a 0.45μm filter before performing the assay.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 samplesa.Lysis cells or tissues with appropriate lysis buffer, such as ’s Cell Lysis Buffer for Western and IP . Under certain circumstances, ’s RIPA Strong Lysis Buffer , RIPA Medium Lysis Buffer , or RIPA Weak Lysis Buffer can also be used. Other lysis buffers with a pH6-8 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. Otherwise, make aliquots and store them at -80℃ for future use.2.Preparation of Anti-V5 Affinity GelAs the Anti-V5 Affinity Gel is stored in a protective solution containing 50% glycerol, it needs to be washed properly before adding protein samples.a.Gently resuspend the Anti-V5 Affinity Gel to be homogeneous. Transfer 20μl of gel suspension per 100μl of protein sample into a clean centrifuge tube . Note: It is easier to aspirate the gel suspension using a large aperture pipette tip (e.g., by cutting off part of the tip with scissors).b.Add 1X TBS to a final volume of 0.5ml, and gently resuspend the Anti-V5 Affinity Gel by pipetting or vortex. Centrifuge at 6000×g for 30 seconds at 4℃, remove the supernatant carefully without disturbing the gel. Repeat this step twice.c.Resuspend the Anti-V5 Affinity Gel with 1X TBS equal to the initial volume of gel suspension (e.g., if 20μl of gel suspension is taken, add 20μl of 1X TBS).3.Protein binding1)Add 20μl of washed Anti-V5 Affinity Gel per 100μl of protein sample, mix well, and incubate at 4℃ for 1-2 hours or overnight with gentle shaking on a rotary mixer.2)After incubation, centrifuge at 6000×g for 30sec at 4℃ and remove the supernatant carefully without disturbing the gel. Note: A portion of supernatant can be reserved in a clean microfuge tube for examination of the binding results.3)Gently resuspend the Anti-V5 Affinity Gel in 500μl of 1X TBS and place in an ice bath on a shaker for 5 minutes. Centrifuge at 6000×g for 30 seconds at 4℃ and carefully remove the supernatant. Repeat the wash thrice, then keep the sample on ice for elution. 4.ElutionBased on the features of the target protein or downstream applications, one of the following three elution methods can be used.1)Competitive elution with the V5 peptide. This is a non-denaturing elution method with a high elution efficiency, and the eluted proteins do not contain the light and heavy chains of V5 antibody.a.Preparation of V5 peptide elution buffer: Dissolve the V5 Peptide (, P9813) in 1X TBS buffer to a final concentration of 150μg/ml, or dilute the 5mg/ml V5 peptide solution with 1X TBS buffer to a final concentration of 150μg/ml. b.For every 20μl of initial gel volume, add 100μl of V5 Peptide elution buffer (150μg/ml). Resuspend the gel gently and incubate for 30-60 minutes at room temperature on a rotary mixer , or 1-2 hours at 4℃. To improve the elution efficiency, increase the incubation time or repeat the elution. c.After incubation, centrifuge at 6000×g for 30 seconds at 4℃, and transfer the supernatant to a new microfuge tube. The supernatant contains the V5-tagged protein and its protein complex.d.Store the supernatant at 4℃ for immediate use, or -20℃/ -80℃ for long-term storage. 2)Acidic elution: This method is non-denaturing, relatively fast and efficient. The eluted proteins also retain their original biological activity, which facilitates subsequent analysis and detection.a.Preparation of acidic elution buffer (0.1M Glycine-HCl, pH3.0) and neutralization buffer (0.5M Tris-HCl, pH7.4, 1.5M NaCl). b.For every 20μl of initial gel volume, add 100μl of acidic elution buffer. Resuspend the agarose gently and incubate for 5 minutes at room temperature on a rotary mixer.Note: The incubation time should not exceed 15 minutes.c.After incubation, centrifuge at 6000×g for 30 seconds at 4℃, and transfer the supernatant to a new microfuge tube. Immediately add 10μl of neutralization buffer and mix well. d.To achieve the maximum elution efficiency, repeat steps b-c and combine the supernatant containing the V5-tagged protein and its protein complex .e.Store the supernatant at 4℃ for or immediate use, or -20℃/-80℃ for long-term storage. Note 1: The elution efficiency of the acidic elution method might be lower than the other two elution methods.Note 2: The elution efficiency of the acidic elution method depends on characteristics 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. The pH or amount of neutralization buffer needed to neutralize the eluates should also be adjusted appropriately.3)Elution with the 1X SDS-PAGE loading buffer: This method is a denaturation method, and the obtained proteins are suitable for SDS-PAGE electrophoresis or WB blot analysis.a.Preparation of SDS-PAGE loading buffer: We recommend using ’s SDS-PAGE Sample Loading Buffer (2X) . Usually, the SDS-PAGE protein loading buffer contains a reducing agent such as DTT, and the eluted protein sample will contain the light chain and heavy chain of the V5 antibody.b.For every 20μl of initial gel volume, add 20μl of 2X SDS-PAGE sample loading buffer, mix well and heat at 95℃ for 5 minutes. c.Centrifuge at 6000×g or 4℃ for 30 seconds. Take the supernatant for SDS-PAGE electrophoresis or Western blot analysisNote: The Agarose cannot be reused because SDS in the loading buffer destroys V5 antibodies.FAQ: Problem Possible Causes Solution Large amount of tagged protein found in the flow through. Binding time is not enough. If using batch method, increase the binding time experimentally; If using column method, use a lower flow rate when loading samples. Column is overloaded. Reduce the amount of the sample added to the gel or increase the amount of gel. Tag is not accessible to gel. Expose the epitope tag by adding low amount of denaturant to the protein extract (dialysis may be needed before applying onto gel), or fuse thetag to the other terminus of the target protein. Gel has not been regenerated since last purification. Perform gel regeneration procedure prior to binding. Reagent compatibility problem. Dialyze the sample against TBS before purification procedure. The target protein has been degraded. 1.Prepare fresh lysates. Avoid using frozen lysates.2.Perform purification at lower temperature, such as 4℃.3.Use appropriate protease inhibitors in the lysate or increase their concentrations to prevent degradation of the fusion protein. Very few or notagged 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 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. 1.Reduce the number of washes.2.Avoid adding high concentrations of NaCl to the mixture.3.Use solutions that contain less or no detergent Incubation times are inadequate. Increase the incubation times with the affinity gel (from several hours to overnight). Interfering substance is present in sample. 1.Lysates containing high concentrations of DTT, 2-mercaptoethanol, or other reducing agents may destroy antibody function, and must be avoided.2.Excessive detergent concentrations may interfere with the antibody-antigen interaction. Detergent levels in buffers may be reduced by dilution. 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 staining the membrane with Ponceau S.3.Use fresh detection substrate or try a different detection system. Multiple protein bands found in the eluate. The protein is not stable at room temperature. Purify the target protein at lower temperature, such as 4℃. 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. Background is too high. Proteins bind nonspecifically to the monoclonal antibody, the gel beads, or the microcentrifuge tubes. 1.Pre-clear lysate with Mouse IgG-Agarose to 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 from the lysate during the initial centrifugation of the affinity gel complexes. |
| 储存温度 | -20°C储存 |
|---|---|
| 运输条件 | 超低温冰袋运输 |
| 稳定性与储存 | -20℃保存,一年有效。 |