Human Interleukin-29/Interferon Lambda 1, carrier-free
- Specifications
- Tech Info / Data
- Citations
- Documentation
Specifications
| Formulation | Supplied lyophilized without a carrier protein |
| Molecular Weight | Based on N-terminal sequencing, the mature recombinant IL-29 starts at Gly 20 and has a calculated molecular mass of 21.4 kDa. As a result of glycosylation, the recombinant monomer migrates as an approximately 26-35 kDa protein in SDS-PAGE under reducing conditions. |
| Source | DNA sequence encoding the signal peptide from human CD33 was fused to the carboxyl terminally polyhistidine-tagged mature human IL-29 (Gly 20-Thr 200). The chimeric protein was expressed in a mouse myeloma cell line, NS0. |
| Purity | Greater than 95%Endotoxin level < 1 EU/μg |
| Bioactivity | Human HepG2 cells infected with encephalomyocarditis virus, ED50 1-5 ng/ml |
| Storage | For retention of full activity store at -70°C or below and avoid repeated freeze/thaw cycles |
| Synonyms | Hu IL-29; Hu IFN-λ1 |
| Accession Number | Q8IU54 |
Tech Info / Data
The IFN lambda gene family is composed of three distinct genes: IFN lambda 1 (IL-29), IFN lambda 2 (IL-28A) and IFN lambda 3 (IL-28B). All three are class II cytokine receptor ligands that are distinctly related to members of the IL-10 family and Type I family. Refer to the product specific datasheet for references associated with this information.
IL-28A, IL-28B, and IL-29, also named interferon-λ2 (IFN-λ2), IFN-λ3, and IFN-λ1, respectively, are newly identified class II cytokine receptor ligands that are distantly related to members of the IL-10 family (11-13% aa sequence identity) and type I IFN family (15 - 19% aa sequence identity).1 – 3 The genes encoding these three cytokines are localized to chromosome 19 and each is composed of multiple exons. The exon organization of these genes is also found in the IL-10 family genes but is distinct from the type I IFNs, which are encoded within a single exon. The expression of IL-28A, B, and IL-29 is induced by virus infection or double-stranded RNA. All three cytokines exert bioactivities that overlap those of type I IFNs, including antiviral activity and up-regulation of MHC class I antigen expression. The three proteins signal through the same heterodimeric receptor complex that is composed of the IL-10 receptor β (IL-10 Rβ) and a novel IL-28 receptor α (IL-28 Rα, also known as IFN-λ R1). Ligand binding to the receptor complex induces Jak kinase activation and STAT1 and STAT2 tyrosine phosphorylation. The phosphorylated STAT1 and STAT2 complex with IFN-regulatory factor 9 (IRF-9) to form the IFN-stimulated regulatory factor 3 (ISGF-3) transcription factor complex that is translocated to the nucleus. ISGF-3 binds to the IFN-stimulated response element (ISRE) present in the regulatory regions of the target genes. Human IL-29 cDNA encodes a 200 amino acid (aa) residue precursor protein with a putative 19 aa signal peptide and a 181 aa mature protein, which is a monomer in solution. It shares 67% and 69% aa sequence identity with human IL-28A and human IL-28B, respectively.
Citations
Documentation
11826 Certificate of Analysis (CoA) 11826 Safety Data Sheet (SDS)ebiomall.com
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大家好，想请教大家一个关于HPLC方法学的问题。
目前我们做的一个蛋白药，没有标准品，液相建立一个方法只想用于纯度鉴定，不去定量，这个方法所得到的图谱就一个主蛋白峰，面积归一化法相当于100%，现在就这个方法的方法学验证提出下面几点疑问：
1.因为我只做纯度鉴定，这个方法的方法学应该做系统适用性、专属性、检测限、耐用性和精密度这些，还是按照定量的全套加上定量限、线性、范围、准确度这些？
2.纯度鉴定中，我觉得应该对杂质进行定量，但是我们的这个方法只有一个主蛋白峰，几乎没有杂质峰，这样的话这个方法学我应该以什么为标准证明纯度呢？需将样品进行适当的氧化、酸、碱破坏吗？然后证明破坏后主峰能和产生的杂质分开？
3.对应生物蛋白药的杂质，应该属于无法获得的，如果通过强破坏，这个杂质也是不好鉴定的，是不是我只需要知道主峰能和强破坏的降解物分开，就可以说方法建立成功？还是生物药没有必要做这个强破坏，简单的走一下系统适用性、专属性、检测限、耐用性和精密度这样的流程就行？
说的有点乱，主要是自己对这个生物药的HPLC纯度鉴定的方法学，实在是疑惑重重，希望有经验的大侠能帮忙解答下。非常感谢！
白细胞介素、
干扰素、
肿瘤坏死因子、
生长因子、每一类里面又可以分为具体的因子。如某种细胞生长因子。
一个制造一种专一抗体的浆细胞进行培养，就可得到由单细胞经分裂增殖而形成细胞群，即单克隆。单克隆细胞将合成针对一种抗原决定簇的抗体，称为单克隆抗体。
Keyword:Cell-PenetratingPeptides,多肽修饰,分子动力学
关键词：抗原制备，电渗流，包涵体
出版时间：2015-10.ProteinExpressionandPurification118(2016)77-82.
特异性抗体是一个依赖性工具用于测定蛋白表达模式和测定蛋白在细胞内的位置。一般来说，重组抗体常作为抗原用于特异性抗体制备。然而，来源于哺乳动物和植物的重组蛋白常在大肠杆菌体内的包涵体中过表达。
因为溶解的抗原比较适合用于注射到动物体内产生抗原，所有这些包涵体的溶解是令人满意的。此外，高纯化的蛋白也被用来制备特异性抗体。为了获得纯化的蛋白(用来作为抗原)，通过制备的圆盘凝胶电泳用于从包涵体中纯化蛋白。
纯化的蛋白含有0.1%SDS的电泳缓冲液(直接注射带免疫动物体内)中作为溶解的片段被回收，所以该方法适合用于从包涵体中纯化抗原。该方法也能用于制备大批量的抗原(几十毫升)。
Estimationofanti-AccDantibodiesusingwesternblotting.
采用蛋白免疫印迹估计抗AccD抗体
原文地址：http://www.ontoresinc.cn/Blog_%E5%88%B6%E5%A4%87%E7%9A%84%E5%9C%86%E7%9B%98%E5%87%9D%E8%83%B6%E7%94%B5%E6%B3%B3%E7%94%A8%E4%BA%8E%E4%BB%8E%E5%8C%85%E6%B6%B5%E4%BD%93%E4%B8%AD%E7%BA%AF%E5%8C%96%E6%8A%97%E5%8E%9F%E7%9A%84%E5%BA%94%E7%94%A8_82.html
[作者]AnnHoeben,BartLanduyt,MartinS.Highley,HansWildiers,AllanT.VanOosterom,andErnstA.DeBruijn
[杂志]PharmacolRev200456:549-580.
Angiogenesisisahallmarkofwoundhealing,themenstrualcycle,cancer,andvariousischemicandinflammatorydiseases.Arichvarietyofpro-andantiangiogenicmoleculeshavealreadybeendiscovered.Vascularendothelialgrowthfactor(VEGF)isaninterestinginducerofangiogenesisandlymphangiogenesis,becauseitisahighlyspecificmitogenforendothelialcells.Signaltransductioninvolvesbindingtotyrosinekinasereceptorsandresultsinendothelialcellproliferation,migration,andnewvesselformation.Inthisarticle,theroleofVEGFinphysiologicalandpathologicalprocessesisreviewed.WealsodiscusshowmodulationofVEGFexpressioncreatesnewtherapeuticpossibilitiesanddescriberecentdevelopmentsinthisfield.
血管内皮生长因子(VEGF)与血管生成
血管生成是创伤治愈、月经周期、肿瘤、各种局部缺血和炎症疾病的共同特征。现已发现许多抗血管生成素分子和前体。血管内皮生长因子是血管生成和淋巴血管生成的诱导因子，它是一种对内皮细胞高度特异的促细胞分裂剂。信号转导包括酪氨酸激酶受体的结合和内皮细胞的增殖、移动，以及新的血管形成。本文重点评述了血管内皮生长因子在正常成人中的生理作用（如月经周期），以及在肿瘤、炎症等疾病的病理进程中的作用。探讨通过调控血管内皮生长因子的表达来创造新治疗途径的可能性，并综述了这一领域最近的发展情况。
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http://www.dxy.cn/bbs/user/download/2549699/549.pdf
