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500ug
| 产品编号 | bs-2435P |
| 英文名称 | ATP5F1A Antibody Blocking Peptide |
| 中文名称 | ATP5A封闭多肽 |
| 英文别名 | ATP synthase alpha chain, mitochondrial; ATP synthase subunit alpha; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, 1; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 1, cardiac muscle; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 2, non-cardiac muscle-like 2; ATP sythase (F1 ATPase) alpha subunit; ATP5A; Atp5a1; ATP5AL2; ATPA_HUMAN; ATPM; hATP1; MC5DN4; mitochondrial; Mitochondrial ATP Synthase Subunit Alpha; Mitochondrial ATP synthetase; Mitochondrial ATP synthetase oligomycin resistant; Modifier of Min 2 mouse homolog; Modifier of Min 2, mouse, homolog of; MOM2; OMR; ORM. |
| 纯化方法 | HPLC |
| 研究领域 | Metabolism > Pathways and Processes > Mitochondrial Metabolism > Mitochondrial markers Metabolism > Pathways and Processes > Mitochondrial Metabolism > Oxidative phosphorylation > Complex V Metabolism > Types of disease > Cancer Signal Transduction > Metabolism > Mitochondrial Signal Transduction > Metabolism > Plasma Membrane > ATPases Tags & Cell Markers > Subcellular Markers > Organelles > Mitochondria |
| 亚基 | F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). |
| 亚细胞定位 | Mitochondrion. Mitochondrion inner membrane. |
| 相似性 | Belongs to the eukaryotic ATPase subunit F6 family. |
| 功能 | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes. |
| 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 | ATP5J (ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6) is a multisubunit membrane-bound enzyme complex consisting of an F0 segment embedded in the membrane and an F1 segment attached to the F0. It is also a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments. Human ATP5J shares 72% sequence identity with rat ATP5J. This signal peptide is rich in basic amino acids, devoid of acidic amino acids, and amphiphilic, which allows it to be water-soluble yet capable of passage through the phospholipid membrane bilayers. Moreover, it is circulating and functions as an endogenous vasoconstrictor by inhibiting cytosolic phospholipase A2. |
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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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