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- bs-1723P
- 2025年10月16日
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500ug
| 产品编号 | bs-1723P |
| 英文名称 | MASP Antibody Blocking Peptide |
| 中文名称 | 甘露聚糖结合凝集素丝氨酸肽酶1封闭多肽 |
| 英文别名 | MASP1/3; MASP-1; Complement factor MASP-3; Complement factor MASP3; Complement-activating component of Ra-reactive factor; CRARF; EC 3.4.21; Mannan binding lectin serine protease 1; Mannose binding lectin associated serine protease 1; Mannose binding protein associated serine protease; Mannose-binding lectin-associated serine protease 1; Mannose-binding lectin-associated serine protease-1; MASP; PRSS 5; Ra reactive factor serine protease p100; Ra-reactive factor serine protease p100; RaRF; Serine protease 5; MASP1_HUMAN. Mannan-binding lectin serine protease 1; Mannan-binding lectin serine protease 1 heavy chain; MASP1_HUMAN. |
| 纯化方法 | HPLC |
| 研究领域 | Immunology > Innate Immunity > Complement |
| 亚基 | Homodimer. Interacts with the oligomeric lectins MBL2, FCN2 and FCN3; triggers the lectin pathway of complement through activation of C3. Interacts with SERPING1. |
| 亚细胞定位 | Secreted. |
| 组织特异性 | Protein of the plasma which is primarily expressed by liver. |
| 翻译后修饰 | The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
N-glycosylated. Some N-linked glycan are of the complex-type. Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. Isoform 1 but not isoform 2 is activated through autoproteolytic processing. |
| 相似性 | Belongs to the peptidase S1 family. |
| 功能 | Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. |
| 保存条件 | Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles. |
| 注意事项 | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| 背景资料 | This gene encodes a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response. The encoded protein is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. The encoded protein is also able to cleave fibrinogen and factor XIII and may may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Apr 2010] |
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文献和实验or from the literature are missing. In this article, processing parameters for DNA, peptide, antibody, and carbohydrate microarrays are outlined. The applicability of the model experiments is demonstrated and described in detail on the example of short oligonucleotides.
Synthesis and Probing of Membrane-bound Peptide Arrays
the stringency of the blocking conditions and make sure that the primary binding partner and detection reagent (e.g., antibody) are of high purity and are used in the highest possible dilution. Stage
Mapping Protein‐Protein Interactions with Phage‐Displayed Combinatorial Peptide Libraries
. Fack, F., Deroo, S., Kreis, S., and Muller, C.P. 2000. Heteroduplex mobility assay (HMA) pre‐screening: An improved strategy for the rapid identification of inserts selected from phage‐displayed peptide
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