Product Description
Type I bovine collagen, lyophilized fibrous powder, Catalog Number 5162, is extracted from bovine flexor tendon with the raw material sourced from closed/controlled herds of animals. Because the collagen is extracted from tendon, the material is more naturally crosslinked. The collagen is polymericinsolublecollagen. The manufacturing processes comply with stringent quality standards that have proven to yield a high quality product with lot-to-lot consistency. This product has a purity of >96% with Type II and Type III collagens not detectable.
This product is supplied as a lyophilized fibrous powder in a 1 gram package size. Bioburden and endotoxin levels are tested – this product is not considered sterile.
This collagen product is naturally cross-linked yielding a robust material for applications which require structure and strength. This product can be readily prepared into such forms as tissue scaffolds, foams, sponges, suspensions, coatings, putties, films and sheets butdoesnot form hydrogels.Using typical cross-linking methods, this material can be tuned for optimal in vivo resorption. This collagen product is ideal for tissue engineering applications and uses with inorganic and biomaterials.
The product is provided in user-friendly packaging for use and storage. Avoid extended open-air exposure to environment since this material is hygroscopic.
Parameter, Testing, and Method | Insoluble Type I Collagen Fibrous Powder #5162 |
Form | Lyophilized Fibrous Powder |
Package Size | 1 gram |
Storage Temperature | Room temperature |
Shelf Life | Minimum of 6 months from date of receipt |
Collagen Purity | >96% |
Endotoxin (LAL) | <20.0 EU/mL |
Bioburden | <200 cfu/gram |
Source | BovineFlexor Tendon |
Amino Acid Analysis | Characteristic |
Directions for Use
Download the full PDF versionor continue reading below:
Note: The following procedure is based on preparationof 1 gram of collagen in 100 ml to initially prepare a 10 mg/ml collagen suspension. Smaller quantities and volumes may be used but the same ratios of collagen and solutions should be used.
- Weigh out 1 gram of collagen fibrous powder.
- Reconstitute 1 gram of collagen with 50 ml of cold purified water (50% of the final volume).
- Stir the collagen with the water continuously mixing for a minimum of 15 minutes until the collagen is fully wetted and the suspension appears to be a semi-solution.
- Add 50 ml of cold 0.02 M HCl to the collagen mixture and stir for a minimum of 10 minutes. This will yield a collagen concentration of 10 mg/ml with the suspension continuing to appear as a semi-solution.
- Measure the pH – the mixture should have a pH of 2 to 3.
- Using Waring stick blender or equivalent, homogenize the collagen mixture for a minimum of 15 minute at a high speed ensuring that the collagen is fully homogenized. Ensure that the temperature of mixture does exceed 24°C. Upon completion, there should be very few visual solids in the viscous suspension. Air bubbles with be prevalent.
- To remove air bubbles, stir the solution on a stir plate and pull a vacuum on the suspension. This will remove the air bubbles.
- At this point if a collagen concentration of less than 10 mg/ml is desired, the collagen can be diluted with 0.01 M HCl.
Product Q & A
We completed a study to show that DNA is completely destroyed at pH 2, and demonstrated that our collagen products do not contain DNA.
The collagen is fully hydrolyzed. The amino acid analysis is done using the Waters AccQ-Tag derivatization method.During the acid hydrolysis step, asparagine (N) is converted to aspartic acid (D) and glutamine (Q) is converted to glutamic acid (E). Tryptophan (W), if present, is destroyed during acid hydrolysis. Experimentally, one can determine the picomoles (pmol) of each amino acid per injected detected using amino acid standards.For the concentration determination, the total number of pmol of each amino acid is summed to get the total pmol of the 18 amino acids detected. The total pmol amino acids is divided by the theoretical number of amino acid residues in collagen based on the published sequence. The result is the pmol of collagen injected. The result is then multiplied by the dilution and 300,000 is used as the collagen molecular weight to get to mg/mL. The molecular weight of collagen is not well agreed upon.
Diluting with 1X PBS (rather than water or 0.01 N HCl) would have an effect for coating purposes. It would change the pH of the diluted collagen solution from acid to neutral pH. The pH change will transform the collagen molecules from a molecular form to a fibrillar form; and then the nature of coating surface will be changed from a monomeric coating to a fibrillar coating.
We use thefollowing antibodies from SouthernBiotech:
1. 1310-02 – Goat Anti-Type I Collagen-FITC
2. 1310-08 – Goat Anti-Type I Collagen-BIOT
3. 7100-05 – Streptavidin-HRP
The major collagen molecular species in our Type I collagen products are monomers (approx. 70%), but there are dimers, trimers and a few percentages of oligomers too (approx. 30%) with some minor amounts of collagen fragments. The collagen monomer is a rod shaped molecule with 300 nm in length and 1.5 nm in diameter. The dimer, trimer and oligomer are 600 nm, 900nm and even longer in length respectively. According to the coating procedures, the collagen molecules are attached to the charged polystyrene surface randomly by charge or affinity in acid conditions during the 1-2 hrs incubation period at 37°C, and any unattached materials are removed by aspiration and rinsing. Therefore, the coated surface is a single layer of collagen monomer, dimer, trimer and oligomer mixtures.The thickness of the mono-molecular layer is dependent on how those molecules are attached on the surface. The coating density thickness would generally be characterized as a 1 molecule thickness which could be ranging from a few nanometers to a few hundred nanometers with the whole surface being covered by collagen.
The net charge of Type I collagen products’ (PureCol®, Bovine Collagen and VitroCol®, Human Collagen) molecule is directly related to the pH. At an acidic pH, the amino acids (zwitterions) along the collagen molecule are positively charged, making the entire collagen molecule positive. At the isoelectric point (or zone) of collagen, around pH 7-8, the amino acids along the collagen molecule are positively and negatively charged, making the net charge of the collagen molecule close to zero. At a basic pH, the amino acids along the collagen molecule were negatively charged, making the entire collagen molecule negative.
Further, the nature of the charge of the collagen coating surface will be dependent on the type of coating applied. For a monomeric collagen coatings when the collagen is applied under an acidic pH condition, the surface is positively charged. If the surface is rinsed with pH neutral buffer or media then it will change the charge of the collagen surface net charge close to zero. For a 3D gel coating, the collagen prepared under neutral pH; the net charge of the collagen surface is close to zero.
Using rotary shadowing technique under transmission electron microscopy, it was found that our collagen, on average, consists of approximately 80% monomers, 13% dimers, trimers, and oligomers with the remaining 7% collagen fragments.
Yes.The collagen molecule in PureCol, Nutragen, VitroCol, and all of our other Atelo collagen products were prepared from native collagen matrix by pepsin treatment under controlled conditions to remove the non-helical portion, telo-peptides, only and the helical portion is intact. In this case, the enzymatic active sites for MMP (Matrix Metalloproteinase), such as for Mammalian Collagenase Matrix Metalloproteinase 8 (MMP-8), on the molecule was preserved.
These pepsin treated collagen products should behave as native intact collagen.
TGF beta would have been digested with the pepsin enzymatic digestion step. It was undetectable by SDS PAGE silver stain as well. We didn’t do any specific measurements by ELISA however but presences of TGF betais not anticipated.
We primarily use the Biuret method, but we also use BCA, AAA, and hydroxyl-proline assays.
- Collagen solutions that are frozen tend to have issues forming 3D hydrogels, and will likely not work. The solutions should still be good for 2D coatings.
- Collagen solutions that are left out at room temperature for extended periods of time may show signs of degradation, which will affect the formation of 3D hydrogels. It is likely still fine for 2D coatings.
Our recommendation is this: If you are using the product directly for a publication, we highly suggest buying a new bottle if the one you have was compromised.
Product References
References for Insoluble Collagen:
Ahmed, Raju, Monjurul Haq, and Byung-Soo Chun. "Characterization of marine derived collagen extracted from the by-products of bigeye tuna (Thunnus obesus)."International journal of biological macromolecules(2019).
Divakar, Prajan, Kaiyang Yin, and Ulrike GK Wegst. "Values and property charts for anisotropic freeze-cast collagen scaffolds for tissue regeneration."Data in brief22 (2019): 502-507.
Divakar, Prajan, Kaiyang Yin, and Ulrike GK Wegst. "Anisotropic freeze-cast collagen scaffolds for tissue regeneration: How processing conditions affect structure and properties in the dry and fully hydrated states."Journal of the mechanical behavior of biomedical materials90 (2019): 350-364.
Product Certificate of Analysis
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Safety and Documentation
Safety Data Sheet
Certificate of Origin
Product Disclaimer
This product is for R&D use only and is not intended for human or other uses. Please consult the Material Safety Data Sheet for information regarding hazards and safe handling practices.
美国AdvancedBioMatrix(简称ABM) www.advancedbiomatrix.comAdvancedBioMatrix(简称ABM)是美国一家著名的生物公司,获得了AllerganInc的授权(Allergan用25年时间不断完善胶原蛋白相关的产品的生产工艺),将Allergan的专业和技术用于蛋白生产与检测,致力于为组织工程、细胞分析及细胞增殖等研究领域提供优质稳定的产品。AdvancedBioMatrix不断丰富已有产品线,目前可为三维细胞培养提供各种胶原蛋白、纤连蛋白、玻连蛋白、水性凝胶、不同粘度与分子量的透明质酸以及低代成纤维细胞等。在美国全部产品授权Sigma销售。AdvancedBioMatrix是组织培养,细胞分析和细胞增殖三维(3D)应用的生命科学领域的领导者。我们的产品被公认为纯度,功能性和一致性的标准。我们在生产,分离,纯化,冷冻干燥,细胞培养和蛋白质测试,粘附肽,附着因子,底物刚性和其他3D矩阵产品方面拥有丰富的专业知识。我们的专业技术和知识正在被用来确保我们的产品质量最高,批次之间一致且易于为我们的研究客户使用。
美国AdvancedBioMatrix是3D组织培养、细胞检测和细胞增殖等领域实验解决方案的佼佼者。AdvancedBioMatrix在分离、纯化、冻干、细胞培养和蛋白检测、多肽粘附、附着因子、基质硬度和其他3Dmatrix 产品开发方面有着丰富的经验。AdvancedBioMatrix的研发经验和专业知识确保其产品可达到最佳质量,并保证产品之间一致性,方便研究客户使用。以下为AdvancedBioMatrix3DMatrices 产品竞争优势:1. 提供高纯度和成分确定的胞外基质;2. 超过1000余篇文献引用PureCol产品,品质非常均一;3. 在3D培养基领域可提供最全面的产品线;4. 唯一可提供特异性刚性有机硅基板的公司(CytoSoft);5. 唯一可提供可溶性丝纤蛋白的供应商(可运用于多种3D培养);6. 如果客户首次接触3D胶原凝胶,AdvancedBioMatrix还是唯一的预制胶原蛋白(PureColEZGel)供应商;
以下产品为AdvancedBioMatrix全球畅销品:1.PureCol 牛源I型胶原蛋白 3mg/ml#5005-100ML2.Nutragen牛源I型胶原蛋白 6mg/ml#5010-50ML3.FibriCol 牛源I型胶原蛋白 10mg/ml#5133-20ML4.VitroCol 人源I型胶原蛋白 #5007-20ML5. 弹性蛋白原 #5052-1MG6.ECMSelectArraykitUltra-36#5170-1EA7.CytoSoft(刚性可变的基底,AdvancedBioMatrix最新添加产品5190-7EA)8. 人III型胶原蛋白 #5021-10MG9. 人IV型胶原蛋白 #5022-5MG10.SilkFibroin溶液 #5154-20ML11.Fibronectin#5080-5MG12.Vitronectin#5051-0.1MG
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01中西医结合治疗内科疾病丁春华①101政治②201英语一或203日语③306西医综合或307中医综合中西医结合内科学▲广州中医药大学第二临床医学院
招生简章:http://www1.gzhtcm.edu.cn/bumen/yjsc2497/showart.asp?id=1906
招生目录:http://www1.gzhtcm.edu.cn/bumen/yjsc2497/showart.asp?id=1901
科室简介和个人简介:
一广东省中医院心律失常诊疗中心位于环境优美的广州大学城内以美国加州大学心脏中心归国的丁春华主任为学科带头人与美国加州大学心脏中心合作开展最前沿的介入诊疗手术心脏电生理导管室引进国际上最先进的三维标测系统EnsitevelocityCardioLab多导电生理仪西门子大型C臂血管造影X线机等设备开展心律失常的射频消融起搏器及除颤器植入手术
二充分发挥我院传统中医中药学的技术特色和独特优势由全国名老中医被誉为“中医泰斗”的邓铁涛教授中国科学院陈可冀院士著名中医黄春林教授为学术带头人以“中西医师各自专攻特长中西医学联合诊治病人”为科室特色为病人提供个体化最优化的中西医治疗方案
三心律失常诊疗中心设有病床张正高职称人博士研究生导师人主治医师人博士后人硕士人并设有心脏电生理研究室引进国际领先的光学标测膜片钳等研究设备开展心律失常疾病研究药物研发
四开展介入手术:
心房颤动(房颤)心房扑动(房扑)房性心动过速(房速)房性早搏(房早);阵发性室上性心动过速(室上速);预激综合征;室性心动过速(室速)室性早搏(室早);晕厥或头晕/晕倒;起搏器治疗病态窦房结综合征房室传导阻滞;心室再同步治疗心力衰竭;植入性心脏转复除颤器(ICD)治疗致死性恶性心律失常;家族先天性或复杂异常心电图的心内电生理检查诊断等
五中医特色治疗:在名老中医指导和实验研究基础上采用中药方剂耳针腹针体针穴位贴敷沐足等结合药膳调理综合治疗心律失常
六.地址:广州市番禺区小谷围街大学城内环西路号电话:-网址:wwwacucbbsorg
丁春华研究员
丁春华,男,河北省任丘市人,1972年2月生,医学博士。2010年自美国旧金山加州大学(UCSF)心脏中心归国,组建并担任广州中医药大学第二临床医学院(广东省中医院)心律失常诊疗中心主任、广东省中医药科学院心脏电生理研究室主任。现任心血管内科研究员、心血管(心律失常方向)博士研究生导师,心律失常专业国际权威期刊美国《心律》杂志编委、美国心律协会会员、美国华裔心脏协会会员、北美华人生物医药协会会员、美国《循环》杂志特约审稿人。
自1995年于华西医科大学攻读硕士学位,师从黄德嘉、姜建教授,从事心律失常介入手术和心脏电生理研究工作。1998年于天津医科大学总医院心脏科工作,并于2000年赴美国克里夫兰医学中心、亚利桑那州心脏病医院深造。2004年博士毕业于天津医科大学。
2005-2010年于美国旧金山加州大学心脏中心工作,任心脏电生理博士后、助理研究员。介入手术师从于心脏中心主任JeffreyOlgin和心律失常导管消融手术创始人MelvinScheinman教授。科研方面,建立了具有光学标测、膜片钳和微电极等心脏电生理先进技术的实验室,进行抗纤维化对心律失常的影响、心律失常发病机理等方面研究。发表SCI论文6篇,累计影响因子为42.304,英文专著1本。
目前承担2项科研课题。指导硕士生和博士生各2名。
我现在手头上有“医疗器械分类规则(局令第15号)”单位没有说ⅠⅡⅢ类的事情?请教!
首先导管插入部位(腹股沟、手臂、肩膀或颈部)的皮肤消毒,局麻药进行局部麻醉;然后用穿刺针穿刺静脉/动脉血管,电生理检查导管通过血管插入心腔;心脏电生理检查所用的电极导管长而可弯的导管,能将电信号传入和传出心脏。电极导管记录心脏不同部位的电活动,并发放微弱的电刺激来刺激心脏,以便诱发心律失常,明确心动过速诊断;然后医生通过导管找到心脏异常电活动的确切部位(此过程称为“标测”),再通过消融仪发送射频电流消融治疗,从而根治心动过速。 血管穿刺并发症包括局部出血、血肿、感染、气胸、血栓形成、栓塞等,导管操作并发症包括主动脉瓣返流、心肌穿孔、心包填塞等,放电消融并发症包括房室传导阻滞、心肌梗死等。向左转|向右转
1.在没有开始记录(空跑的状态下)和开始记录时的波形的基线都不在0点而是处于负值,是因为仪器设备设置的问题还是仪器本身有损坏?
2.记录ACC场电的通道50Hz干扰特别大,接地线排干扰后仍然存在,可能是什么问题呢?
3.Brownlee440的Amplifier上有Gain,lowpassfilter,Highpassfilter的设置,这个设置对ACC场电的记录有影响吗?如果记录ACC的场电,一般常用的参数是多少啊?
4.有没有用过这个仪器记录过肌电的前辈,我用A-B模式可以记录到类似Chart5软件记录的肌电波形。可是用clampfit10.2的Analyze--statistics--Measurement--Area分析,分析出来的数值太小,与波形不符。从波形看,明显有强的肌肉收缩,但是数值却没有明显差异。有前辈分析过肌电吗?是否我的分析方法不对?或者是应为问题1中提到的基线不在0点所引起的曲线下面积分析的误差?
感谢!
谢谢啦~
编译字数:1452
Neurosurgery:神经外科术中可以同时使用磁共振与神经电生理监测
现代神经外科手术的目的,是实现最大化的肿瘤切除,同时保留神经功能。在过去的十几年间,新的技术工具如神经外科导航系统、低场强和高场强的术中核磁共振成像(iMRI)及先进的神经影像学技术(弥散张量成像技术DTI),以及术中神经电生理监测(IOM)一贯都有助于实现这一目标。但是,这几项技术集成一体化使用往往很难。
对于术中神经元系统和白质束的功能变化,IOM能够提供可靠的评估,而这些变化最终发生在手术中。在肿瘤切除过程中,高场强术中核磁共振成像(iMRI)可以提供残余肿瘤的影像图像,以及显示肿瘤转移和功能途径的形态学改变(通过DTI方式)。大脑雄辩区域的手术要求术中神经电生理监测(IOM),这在提供高场强(1.5T)iMRI的手术室可能会出现一些问题。比如安全性、失真率、IOM与iMRI之间相互干扰导致的可靠性受损。
来自意大利罗马LaSapienza大学医学心理学系神经科学和心理健康感觉器官教研室神经外科的GiancarloD’Andrea博士,为了鉴别在高场强iMRI的手术室里,哪些类型的电极更适合术中神经电生理监测,利用模型进行了一项实验研究。报告了他们在手术期间使用铱铂(Pt/Ir)电极的经验,并且证明IOM与Pt/Ir电极和高场强iMRI之间的集成一体化是安全的、可靠的。文章最近在线发表于Neurosurgery上。
研究人员使用凝胶样模型和苹果,对不同的材料(黄金、Pt/Ir,不锈钢(SS))构成的电极进行测试,以评估他们的安全性和兼容性。随后,在病人使用之前,在5例健康志愿者身上进行了电极测试。研究结果显示,这些不同的电极中,没有任何一个出现热不稳定,并且没有损害志愿者的皮肤的情况发生。
不锈钢电极造成了严重的图像失真。黄金电极没有造成图像失真,但是其高昂的费用使得他们在常规手术中使用负担不起。很明显,铂铱电极比黄金便宜,并且在高场强iMRI的手术室里,其具备完全的安全性、兼容性和适用性,可以提供出色的IOM和温和的干扰,根本不影响术中成像的质量。
因此,高场强的术中核磁共振辅助下的图像引导手术期间,核磁共振兼容的皮下铂铱针电极适用于术中神经电生理监测。在高场强iMRIBrainSuite®中使用IOM是有效的和安全的。
图1本图分为两个部分:在上半部分中,我们展示了我们手术室的照片,包括博医来公司提供的术中核磁共振辅助的脑科手术室(BrainSuite®iMRI)。在下半部分中,原理图描绘了同一手术室的设置证据,关系到逐步地增加与磁场的距离,安全线意味着磁场线使得所在区域的磁场强度逐步减少(10mT、5mT、3mT、1mT,0.5mT)。红线标记的是磁场强度为0.5mT的区域的内边界;因此,在此区域之外进行手术。病人、外科医师、麻醉医师和协助护士的理想位置,以及术中神经电生理监测设备(建议距离病人4-5米)和参与手术的神经生理学家的位置,也都按照上面提到的示意线的建议来事先设计好。附加到磁场的一个回转工作台,允许在手术期间病人的头部置放于5高斯示意线以外。在这条线以外可以使用普通的外科手术器械。术中神经电生理监测设备可以位于更远的地方,幸亏拥有足够7米长的电缆。(IOM=术中神经电生理监测,anesthesiologist=麻醉医师,m=米,mT=毫特斯拉)
图2相比较之下,铂铱电极在凝胶样模型测试期间增加了他们的差别,提供了优良的术中采集的核磁共振信号。(IntraoperativeMRIjellyphantomstudy=凝胶样模型的术中核磁共振成像研究,platinum-iridiumelectrode=铱铂电极,Steelelectrode=钢电极)
图3"苹果测试"更加证实了以前的研究结果,表明铱铂电极具备与术中强磁场最优的兼容性,相比而言,钢电极的人工产品和顺磁性的失真率都很高。(IntraoperativeMRIApplestudy=苹果的术中核磁共振成像研究,platinum-iridiumelectrode=铱铂电极,Steelelectrode=钢电极)
图4术中应用设备在"活体内"的演示图像(IntraoperativeT1VolumetricMRI=术中T1容积核磁共振成像,Intraoperative3Drendering=术中三维渲染图像)
我们一般是在心导管室内,要在特殊的X线设备,可以转动的C臂心血管造影机,影像增强设备和电视荧屏设备,多导电生理记录仪,心脏程控刺激仪等。高档可以有三维电解剖生理定位标测系统比如CARTO,EnSite3000,这仅仅国内少数顶尖医院才有。
我们做电生理检查是通过你自身的血管放入心导管,直到心脏相应部位,一般主要局部麻醉,小孩则需要全麻。手术前必须停用抗心律失常药物至少5个半衰期以上,一般至少要3天,一般抗凝药物也是需要停用的。
我们局部需要手术前备皮,也就是局部皮肤清洁,有毛发的也需要清理干净。然后铺上洞巾。仅仅暴露局部血管穿刺部位。
我们穿刺血管插入诱发电极导管是根据不同需要来的,比如通常我们需要至少放置冠状静脉窦电极,右心室电极,高位右心房电极,和His束电极,那么冠状静脉窦电极是一般通过左锁骨下静脉或者右颈内静脉穿刺放置的,而右心室、高右房和His束电极则通过右股静脉放置。这些和体表心电图构成都可以让医生在电视屏幕上看到你不同的心电图图形,这样可以更加明确你心律失常的机制,部位。那么我们就可以标定你需要消融的部位(靶点)
我们通过插入电极导管,然后我们就进行心电生理检查,也就是人工给与各种电刺激,诱发你心律失常,比如我们可以采用输出电刺激信号比如用S1S1 刺激,也可以采用S1S2刺激等等,有时候可以静脉点滴异丙肾上腺素等药物,增加诱发的成功率,术前我们停用抗心律失常药物也是这个目的,就是诱发出你心律失常,这样我们根据体表和心内心电图,可以准确判断并定位你心律失常发生机制和部位,为下一步射频导管消融作准备,其实标定,是最为关键的一步,你只有找准敌人才能准确打击。准确的标定,也就是找准敌人的位置,那么就为打击敌人,做出关键的作用。我们的射频导管就像导弹一样,但是你必须先直到敌人在哪里,把它标定好,然后我们的导弹就可以直接定点清除。
目前比较新的高档的比如CARTO,就是类似于全球定位系统GPS的原理,可以准确三维立体定位你心律失常形成的部位和路径。一般我们针对最多是折返造成的心律失常,比如最多用于房室结双径路或者房室旁路引起的阵发性室上速,成功率一般是95%以上。
如果是房扑,主要是经典房扑,那么一般我们需要用一个Halo导管,一根可以弯折的上面带有很多对电极的导管,沿着折返环,环形放置。那么成功率也可以到95%。
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