计算溶液所需的质量、体积或浓度。
His标签蛋白纯化试剂盒 (Ni-IDA, pH 6.0)
有货
为什么选择此级别
BioReagent,用于蛋白分析 级 ，适用于对基线干扰要求严格的色谱和分析工作流程。
储存与运输
2-8°C储存,室温,禁止冷冻。低温运输,禁止冷冻 。请查阅批次 COA 获取详细规格。
质量文档
SDS、COA、产品数据表及规格说明书均可下载。可通过批号查询获取批次 COA。
文献证明
在色谱分析、有机合成和交叉偶联反应领域已被 0 篇同行评审文献引用。
概述
背景介绍：
本试剂盒提供了一种快速、高效、便捷的方案，用于从大肠杆菌、酵母、昆虫，哺乳细胞表达系统的裂解液中，一步纯化带有6×His、8×His或10×His等组氨酸标签的重组蛋白。其核心成分为亚氨基二乙酸-镍离子(Ni-IDA)亲和介质。IDA配基以三齿形式螯合镍离子，留有较多空位与组氨酸标签结合，具有载量高、价格经济的特点，特别适合大规模纯化和初筛实验。
产品特点
1、快速、高效：试剂盒使用了IDA螯合的镍离子，挂柱效率高，缩短操作时间的同时可以有效的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。
2、便捷：提供了His标签蛋白纯化时所需的相关试剂，为His标签蛋白的纯化带来了极大的便利。
3、载量高：动态载量达35 mg /mL。
4、用途广泛：不仅可以用于在非变性条件纯化His标签蛋白，也可用于在变性条件纯化His标签蛋白，试剂盒提供了非变性和变性条件下纯化His标签蛋白所需的不同的裂解液、洗涤液和洗脱液，可以很好地满足不同实验的需要。
使用方法
变性与非变性纯化时需根据试剂盒内提供的试剂选择相对应的缓冲体系。
一、样品准备
A. 适用于非变性缓冲体系
1、细菌或酵母表达的可溶性蛋白
(1) 挑取单菌落到含有适合抗性的培养基中，根据载体使用说明，加入相应浓度的诱导剂诱导相应的时间。
(2) 表达结束后，将培养液转移到离心瓶中，7000 rpm (7500 ×g)，离心15 min收集菌体，然后按照菌体与裂解液比例为1 : 10 (W/V) 加入非变性裂解液，根据蛋白易降解性质可选择性加入终浓度为1 mM的PMSF，也可加入其他蛋白酶抑制剂，但不能影响目的蛋白与填料的结合 。根据需求可加入溶菌酶（如果表达的宿主细胞内含pLysS或pLysE，可以不加溶菌酶）。
(3) 将菌体沉淀悬浮起来 (如果菌液浓度高，也可考虑加入10 μg/mL RNaseA和5 μg/mL DNaseI)，混匀，放置于冰上，然后冰水混合物上超声破碎细胞，至菌液基本保持澄清。
(4) 将澄清的破碎液转移至离心管中，10000 rpm (15000 ×g)，4℃离心20-30 min。取上清，置于冰上备用，进行下一步纯化。
2、酵母、昆虫和哺乳细胞分泌表达可溶性蛋白
将细胞培养液转移至离心瓶，5000 rpm (3800 ×g)，离心10 min，收集上清，如上清中不含EDTA、组氨酸和还原剂等物质，即可直接加入柱子使用；如含有EDTA、组氨酸和还原剂等物质，需用平衡液透析后才能上柱。对于大量体积的上清，可加入硫酸铵进行沉淀浓缩后，用平衡液透析后才能上柱。
B. 适用于变性缓冲体系
1、细菌表达的包涵体蛋白
(1) 挑取单菌落到含有适合抗性的培养基中，根据载体使用说明，加入相应浓度的诱导剂诱导相应的时间。
(2) 表达结束后，将培养液转移到离心瓶中，7000 rpm (7500 ×g)，离心15 min收集菌体，然后按照菌体与裂解液比例为1 : 10 (W/V) 加入非变性裂解液，根据蛋白易降解性质可选择性加入终浓度为1 mM的PMSF，也可加入其他蛋白酶抑制剂，但不能影响目的蛋白与填料的结合。 根据需求可加入溶菌酶（如果表达的宿主细胞内含pLysS或pLysE，可以不加溶菌酶）。
(3) 将菌体沉淀悬浮起来（如果菌液浓度高，也可考虑加入10 μg/mL RNaseA和5 μg/mL DNaseI），混匀，放置于冰上，然后冰水混合物上超声破碎细胞，至菌液基本保持澄清。
(4) 将澄清的破碎液转移至离心管中，10000 rpm (15000 ×g)，4℃离心20-30 min。取沉淀，加入变性裂解液重悬， 并在室温下孵育约60 min，可能需要均质或超声将沉淀完全溶解。
(5) 12000 rpm离心30 min去除剩余的不溶物，小心的将上清转移到干净的管中而不触碰下面的沉淀，置于冰上备用，进行下一步纯化。
二、样品纯化
样品在上样前建议离心或用0.22μm或0.45μm滤膜过滤，减少杂质，提高蛋白纯化效率和防止堵塞柱子。缓冲液在使用前最好用0.22μm或者0.45μm滤膜过滤。
A. 重力柱法纯化
1、重力柱的装填
(1) 取层析空柱，装入下垫片，加入适量纯水润洗柱管和垫片，关闭下出口。
(2) 将Ni-IDA 亲和树脂充分混匀，用移液器吸取适量浆液加入重力柱中（填料实际体积约占悬液的一半，如吸取1 mL悬液，其实际体积为0.5 mL，则最大载量约为17.5 mg），打开下出口流干保护液。
(3) 加入适量纯水冲洗填料，待柱管中液体重力流干后，关闭下出口。
(4) 加入润洗后的上垫片，确保垫片与填料之间没有空隙，且保持水平。
(5) 装填好的重力柱可以直接加入洗涤液进行平衡，暂不使用时则加入保护液，4℃保存。
2、平衡
将装填好Ni-IDA亲和树脂的重力柱用2-5 CV（CV是指沉降后的树脂体积，以下内容提到的CV不再做此注解）洗涤液进行平衡，重复2-3次。
3、上样
将样品加到平衡好的重力柱中，样品缓慢流出，保证样品和填料充分接触，收集流出液，可以反复上样增加结合效率（如果目标蛋白不稳定，建议样品置于冰上）。
4、洗杂
用5 CV的洗涤液进行洗杂，去除非特异性吸附的杂蛋白，收集洗杂液。必要时可以调整咪唑的浓度进行洗杂。洗柱及下一步洗脱过程中可以用Bradford法简单快速地检测每次洗涤液和洗脱液中的蛋白含量，从而考虑增加或减少洗涤和洗脱的次数。
5、洗脱
洗脱液含有竞争试剂咪唑，可以使用洗涤剂稀释，采用阶梯式梯度（如10 mM，20 mM，50 mM，100 mM，250 mM，500 mM）洗脱方式进行洗脱，加入5 CV的洗脱液，分段收集，每1-5个CV收集一管，分别检测，既可以保证所有结合的目的蛋白被洗脱，又可以得到高纯度和高浓度的蛋白。
B.孵育法纯化
1、树脂准备
将Ni-IDA亲和树脂充分混匀，使用移液器取适量的介质悬浮液，置于离心管中，1000 xg 离心2 min后，小心的去除上清（保持低速离心，以免损坏树脂填料）；也可加入重力柱中，流干保护液。
2、树脂平衡
加入2-5 CV洗涤液，轻柔上下翻动混匀，1000 xg 离心2 min后，小心的去除上清；如使用重力柱，则直接在重力柱中清洗，直接重力流干洗涤液；重复操作2-3次。
3、树脂结合目的蛋白
将准备好的样品加入到平衡好的树脂中，封闭离心管或重力柱管，旋转振荡混匀，室温30 min或2-8℃ 1h，可适当延长时间，使混合液与树脂充分混匀（如果目标蛋白不稳定，建议置于2-8℃环境中结合）。1000 xg 离心2 min后，小心的吸出上清，将上清留存进行检测分析。
4、洗杂
使用 2-5 CV的洗涤液洗涤柱子，轻柔上下翻动混匀，1000 xg 离心2 min后，小心的吸出上清，将上清留存进行检测分析。如使用重力柱，则直接在重力柱中清洗，直接重力流干洗涤液。
5、洗脱目标蛋白
洗脱缓冲液中含有竞争试剂咪唑，可以使用洗涤剂稀释，采用阶梯式梯度（如10mM，20mM，50mM，100mM，250 mM，500mM）洗脱方式进行。用2-5 CV的Elution Buffer洗脱，轻柔上下翻动混匀，1000 xg 离心2 min后，小心的吸出上清， 将上清留存进行检测分析。如使用重力柱，直接重力流出收集洗脱液。
三、样品检测与树脂处理
1、SDS-PAGE 检测
将纯化过程中得到的样品（包括原始样品、流出组分、洗杂及洗脱组分等）利用 SDS-PAGE 进行检测，判定其纯化效果。
2、填料清洗
在位清洗：为了避免不同样品间的相互干扰，或者当介质污染比较严重时（反压增加），需要对介质进行在位清洗。
(1) 对于以离子键结合的蛋白，可用2-3 CV以上的2 M NaCl清洗，并用3 CV以上的纯水冲洗。
(2) 对沉淀蛋白、以疏水性结合的蛋白或脂蛋白，可用2-3 CV的1 M NaOH清洗（10-20 min），并用纯水冲洗，直至pH中性 。
(3) 对疏水性结合的蛋白、脂蛋白和脂类物质，可用5-10 CV的70%乙醇或30%异丙醇清洗（15-20 min），并用10 CV的纯水冲洗。此外，也可用2 CV含去污剂的碱性或酸性溶液清洗。如用0.1-0.5%的非离子去污剂+0.1 M乙酸冲洗1-2 h，并用5-10 CV的70%乙醇冲洗去除去污剂，然后用10 CV的纯水冲洗。 清洗后，可立即使用，也可保存在 20%乙醇中，置于 4℃备用。
3、 填料再生
His 标签蛋白亲和纯化填料所带的镍离子不需要经常螯合去除和重新挂镍离子。当填料使用过程中发现颜色变浅，或填料载量明显变低时，需要对其进行镍离子剥离及重新挂镍处理，即填料再生。按照下面操作流程进行：
(1) 使用5CV去离子水清洗填料；
(2) 使用5CV 50 mM EDTA（pH 8.0）剥落镍离子；
(3) 使用10 CV去离子水清洗填料；
(4) 使用0.5 M NaOH 清洗5 CV，停留10-15 min；
(5) 使用去离子水清洗填料，直至pH中性；
(6) 使用3-5 CV 100 mM NiSO₄再生挂镍；
(7) 使用10CV去离子水清洗。 填料再生后，可立即使用，也可保存在 20%乙醇中，置于 4℃备用。
注意事项：
1. 请勿冷冻保存本产品。
2. Ni-IDA 亲和树脂 ( Ni-IDA Affinity Resin) 使用前一定要充分颠倒若干次，使琼脂糖珠混合均匀。
3. 试剂盒提供的试剂适用于大多数His标签蛋白的纯化。
4. 试剂盒中的Ni-IDA亲和树脂在使用过程中，缓冲试剂如Tris、HEPES、MOPS等的浓度不宜过高，避免含有EDTA或EGTA等螯合剂成分，避免含有Glycine和DTT、DTE等还原剂成分，Triton、Tween、NP-40的常用浓度最佳为1%，盐酸胍浓度可以高达6M，尿素浓度可以高达8M。虽然IDA-Ni介质可以耐受6M盐酸胍或8M尿素，但在高浓度变性剂条件下，载量会有所降低。
5. 试剂盒中的Ni-IDA 树脂悬浊液，每毫升含约50%的固体沉淀，每毫升固体沉淀的动态载量最大达35 mg /mL，即每毫升树脂悬液可结合约10-17.5 mg蛋白，最终的最大结合量与标签蛋白的分子量大小等也有关系。
6. 为了您的安全和健康，请穿实验服并戴一次性手套操作实验。
Background Introduction
This kit provides a rapid, efficient, and convenient protocol for the one-step purification of recombinant proteins tagged with 6×His, 8×His, or 10×His from lysates of Escherichia coli, yeast, insect, and mammalian expression systems. Its core component is Nickel-Iminodiacetic Acid (Ni-IDA) affinity resin. The IDA ligand chelates Ni²⁺ ions in a tridentate manner, leaving sufficient coordination sites for binding to histidine tags. Featuring high binding capacity and cost-effectiveness, this resin is especially suitable for large-scale purification and initial screening experiments.
Product Features
1. Rapid and Efficient: The kit uses IDA-chelated nickel resin with high binding efficiency, which shortens operation time and effectively prevents degradation or denaturation of the target protein during prolonged handling, fully preserving protein activity.
2. Convenient: All necessary reagents for His-tagged protein purification are included, greatly facilitating the purification process.
3. High Binding Capacity: The dynamic binding capacity reaches 35 mg/mL resin.
4. Wide Applicability: The kit supports purification of His-tagged proteins under both native and denaturing conditions. It provides separate lysis buffers, wash buffers, and elution buffers optimized for native and denaturing conditions, satisfactorily meeting diverse experimental requirements.
Instruction For Use
Choose the appropriate buffer system for native or denaturing purification from the reagents provided in the kit.
I. Sample Preparation
A. For Native Buffer System
1. Soluble Protein Expressed in Bacteria or Yeast
(1) Pick a single colony into medium containing the appropriate antibiotic. Induce expression with inducer at the recommended concentration and duration according to the vector instructions.
(2) After expression, transfer the culture to a centrifuge bottle and centrifuge at 7000 rpm (7500 ×g) for 15 min to harvest cells. Resuspend the cell pellet in Native Lysis Buffer at a ratio of 1:10 (w/v). Optionally add PMSF to a final concentration of 1 mM or other protease inhibitors if the protein is prone to degradation, provided they do not interfere with binding to the resin. Lysozyme may be added as needed (not required if the host strain contains pLysS or pLysE).
(3) Fully resuspend the cell pellet. If the cell suspension is concentrated, add 10 μg/mL RNase A and 5 μg/mL DNase I. Mix well, keep on ice, and lyse by sonication in an ice-water bath until the lysate becomes clear.
(4) Transfer the lysate to a centrifuge tube and centrifuge at 10000 rpm (15000 ×g) at 4 °C for 20-30 min. Collect the supernatant, keep on ice, and proceed to purification.
2. Soluble Protein Expressed in Yeast, Insect, or Mammalian Cells
Transfer the cell culture to a centrifuge bottle and centrifuge at 5000 rpm (3800 ×g) for 10 min. Collect the supernatant. If the supernatant contains no EDTA, histidine, or reducing agents, it may be loaded directly. If EDTA, histidine, or reducing agents are present, dialyze against wash buffer before loading. For large volumes, concentrate by ammonium sulfate precipitation and dialyze against wash buffer before loading.
B. For Denaturing Buffer System
1. Inclusion Body Protein Expressed in Bacteria
(1) Pick a single colony into medium containing the appropriate antibiotic. Induce expression with inducer at the recommended concentration and duration according to the vector instructions.
(2) After expression, transfer the culture to a centrifuge bottle and centrifuge at 7000 rpm (7500 ×g) for 15 min to harvest cells. Resuspend the cell pellet in Native Lysis Buffer at a ratio of 1:10 (w/v). Optionally add PMSF to a final concentration of 1 mM or other protease inhibitors if the protein is prone to degradation, provided they do not interfere with binding to the resin. Lysozyme may be added as needed (not required if the host strain contains pLysS or pLysE).
(3) Fully resuspend the cell pellet. If the cell suspension is concentrated, add 10 μg/mL RNase A and 5 μg/mL DNase I. Mix well, keep on ice, and lyse by sonication in an ice-water bath until the lysate becomes clear.
(4) Centrifuge at 10000 rpm (15000 ×g) at 4 °C for 20-30 min. Discard the supernatant and resuspend the pellet in Denaturing Lysis Buffer. Incubate at room temperature for approximately 60 min. Homogenization or sonication may be required to fully dissolve the pellet.
(5) Centrifuge at 12000 rpm for 30 min to remove insoluble debris. Carefully transfer the supernatant to a clean tube without disturbing the pellet, keep on ice, and proceed to purification.
II. Sample Purification
A. Gravity Column Purification
1. Column Packing
(1) Take an empty gravity column, insert the bottom frit, rinse with purified water, and close the bottom outlet.
(2) Mix the Ni-IDA affinity resin thoroughly. Pipette the slurry into the column. The settled resin volume is approximately half of the slurry volume (e.g., 1 mL slurry yields ~0.5 mL resin, with a maximum capacity of ~17.5 mg protein). Open the outlet to drain the storage solution.
(3) Wash the resin with purified water. Drain completely and close the outlet.
(4) Insert the top frit, ensuring no air gap between frit and resin and that the frit is level.
(5) The packed column may be equilibrated immediately with wash buffer. If not used immediately, add storage solution and store at 4 °C.
2. Equilibration
Equilibrate the column with 2-5 CV Wash Buffer (CV = settled resin volume; this definition applies throughout the protocol). Repeat 2-3 times.
3. Sample Loading
Apply the sample to the equilibrated column. Allow the sample to flow slowly to ensure sufficient binding. Collect the flow-through; reloading may increase binding efficiency. Keep samples on ice if the target protein is unstable.
4. Washing
Wash with 5 CV Wash Buffer to remove non-specifically bound proteins. Collect the wash fraction. Imidazole concentration may be adjusted if needed. During the column washing and subsequent elution steps, the protein concentration in each wash and elution fraction can be quickly and simply determined using the Bradford method, allowing you to adjust the number of washing and elution steps accordingly.
5. Elution
Elution buffer contains imidazole as a competitive agent and may be diluted to form step gradients (e.g., 10 mM, 20 mM, 50 mM, 100 mM, 250 mM, 500 mM). Elute with 5 CV Elution Buffer, collect fractions every 1-5 CV, and analyze individually. This ensures complete elution and yields highly pure, concentrated protein.
B. Batch Purification
1. Resin Preparation
Mix the Ni-IDA affinity resin thoroughly. Pipette the desired slurry volume into a centrifuge tube. Centrifuge at 1000 ×g for 2 min and carefully remove the supernatant (low speed to avoid damaging the resin). Alternatively, drain the storage solution in a gravity column.
2. Resin Equilibration
Add 2-5 CV Wash Buffer, mix gently by inversion, centrifuge at 1000 ×g for 2 min, and remove the supernatant. For gravity columns, wash and drain by gravity. Repeat 2–3 times.
3. Binding
Add the prepared sample to the equilibrated resin. Seal the tube or column and mix by rotation. Incubate at room temperature for 30 min or at 2-8 °C for 1 h (longer if needed). Keep at 2-8 °C if the protein is unstable. Centrifuge at 1000 ×g for 2 min and collect the supernatant for analysis.
4. Washing
Wash with 2-5 CV Wash Buffer, mix gently, centrifuge at 1000 ×g for 2 min, and collect the supernatant. For gravity columns, wash and drain by gravity.
5. Elution
Elute using a step imidazole gradient (10 mM, 20 mM, 50 mM, 100 mM, 250 mM, 500 mM). Add 2-5 CV Elution Buffer, mix gently, centrifuge at 1000 ×g for 2 min, and collect the supernatant. For gravity columns, collect eluate by gravity flow.
III. Sample Detection and Resin Handling
1. SDS-PAGE
Analyze samples from the purification process (starting material, flow-through, wash, and elution fractions) by SDS-PAGE to evaluate purification efficiency.
2. Resin Cleaning (In-Place Cleaning)
Cleaning is required to avoid cross-contamination or if backpressure increases due to contamination.
(1) For ionically bound proteins: Wash with 2-3 CV of 2 M NaCl, then flush with ≥3 CV purified water.
(2) For precipitated, hydrophobic, or lipoprotein contaminants: Wash with 2-3 CV of 1 M NaOH for 10-20 min, then flush with water until neutral.
(3) For hydrophobic proteins, lipids, and lipoproteins: Wash with 5-10 CV of 70% ethanol or 30% isopropanol for 15-20 min, then flush with 10 CV water. Alternatively, clean with 2 CV of acidic or alkaline buffer containing detergent (e.g., 0.1-0.5% non-ionic detergent + 0.1 M acetic acid for 1-2 h), then wash with 5-10 CV of 70% ethanol to remove detergent, followed by 10 CV water. After cleaning, the resin may be used immediately or stored in 20% ethanol at 4 °C.
3. Resin Regeneration
Stripping and re-charging with Ni²⁺ is not routinely required. Perform regeneration if the resin becomes pale or binding capacity decreases significantly.
(1) Wash with 5 CV deionized water.
(2) Strip Ni²⁺ with 5 CV of 50 mM EDTA, pH 8.0.
(3) Wash with 10 CV deionized water.
(4) Clean with 0.5 M NaOH (5 CV) and incubate 10-15 min.
(5) Wash with deionized water until neutral.
(6) Re-charge with 3-5 CV of 100 mM NiSO₄.
(7) Wash with 10 CV deionized water. After regeneration, the resin may be used immediately or stored in 20% ethanol at 4 °C.
Matters needing attention
1. Do not freeze this product.
2. The Ni-IDA Affinity Resin must be mixed thoroughly by inversion before use to fully resuspend the agarose beads.
3. Reagents provided are suitable for the purification of most His-tagged proteins.
4. During purification, avoid high concentrations of Tris, HEPES, or MOPS. Do not use chelating agents such as EDTA or EGTA, or reducing agents such as glycine, DTT, or DTE. Optimal concentrations: Triton, Tween, NP-40 up to 1%; guanidine hydrochloride up to 6 M; urea up to 8 M. Although Ni-IDA resin tolerates 6 M guanidine·HCl or 8 M urea, binding capacity is reduced under high denaturant conditions.
5. The Ni-IDA resin slurry contains approximately 50% settled solids per mL. The dynamic binding capacity of the settled resin is up to 35 mg/mL, so each mL of slurry binds approximately 10-17.5 mg protein. Actual maximum binding depends on the molecular weight and properties of the tagged protein.
6. For your safety and health, wear a lab coat and disposable gloves during all experiments.
规格
别名
His标签蛋白纯化试剂盒(Ni-IDA 亲和介质, pH 6.0) | His标签蛋白纯化试剂盒 (Ni-IDA) | Ni-IDA纯化试剂盒
英文别名
His-Tag Protein Purification Kit (Ni-IDA Affinity Beads, pH 6.0) | Ni-IDA-Beadose Resin Kit | His-Tag Protein Purification Kit with IDA-Ni Agarose Beads
规格或纯度
BioReagent,用于蛋白分析
英文名称
His-Tag Protein Purification Kit (Ni-IDA, pH 6.0)
应用
Protein purification, 蛋白质组样品前处理
储存与运输
储存条件
2-8°C储存,室温,禁止冷冻
运输条件
低温运输,禁止冷冻
稳定性与储存
各组分在相应的储存条件下保质期1年。
组分与储存
H15058017 | 组分 | 10T | 储存 | 每次测试的数量 |
H15058017A | Ni-IDA 亲和树脂 | 10 mL | 2-8℃ | 1 mL |
H15058017B | 非变性裂解液 | 120 mL | 2-8℃ | 12 mL |
H15058017C | 非变性洗涤液 | 250 mL | 2-8℃ | 25 mL |
H15058017D | 非变性洗脱液 | 60 mL | 2-8℃ | 6 mL |
H15058017E | 变性裂解液 | 120 mL | 2-8℃ | 12 mL |
H15058017F | 变性洗涤液 | 250 mL | 2-8℃ | 25 mL |
H15058017G | 变性洗脱液 | 60 mL | 2-8℃ | 6 mL |
H15058017H | 层析空柱，3 mL(盖，塞，膜) | 10 EA | Room Temperature | 1 EA |
技术文档
高级数据
质检证书（CoA,COO,BSE/TSE 和分析图谱)
C of A & Other Certificates(BSE/TSE, COO):
输入批号以搜索分析图谱:
技术文档和文章
溶液计算器
常见问题
什么是「用于蛋白分析」？
「用于蛋白分析」表示该产品经过加工和检测，适用于分子生物学和蛋白质组学。典型规格包括：低或不可检测的核酸酶/蛋白酶活性、低内毒素、受控的微生物限度，以及高批间重现性。
本产品应如何储存？
请于2–8 °C条件下保存。请勿冷冻。冷冻可能对本品造成不可逆的损坏。
什么是「BioReagent」？
「BioReagent」表示该产品经过加工和检测，适用于生物和生化应用。规格可能包括内毒素限值、微生物控制、无菌性、低 DNase/RNase/蛋白酶活性，以及在相关情况下的生物活性验证。
本产品如何运输？
本产品采用湿冰冷藏运输。收货后请立即拆包，并按上述储存条件保存。
如何获取批次专用COA？
每个订单都会随附分析证书（COA），您也可以从账户订单历史中下载。如需订购前的COA，请联系您的客户代表，或使用PDP上的"申请COA"按钮——我们将提供代表性批次的COA。
产品仅提供给经过验证的企业、机构和合格的专业人员用于研发。不适用于人类、动物、诊断或治疗。
Copyright © 2023至今 上海阿拉丁生化科技股份有限公司 保留所有权利。
危险品化学品经营许可证（带存储）