MANT-GTP (2'-(or-3')-O-(N-Methylanthraniloyl) Guanosine 5'-Triphosphate, Trisodium Salt)
MANT-GTP (2'-(or-3')-<i>O</i>-(<i>N</i>-Methylanthraniloyl) Guanosine 5'-Triphosphate, Trisodium Salt)
引用資料與參考文獻 (48)
Invitrogen™

MANT-GTP (2'-(or-3')-O-(N-Methylanthraniloyl) Guanosine 5'-Triphosphate, Trisodium Salt)

The nucleotide analog MANT GTP is modified on the ribose moiety. The compact mature of the MANT fluorophore and its深入閱讀
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產品號碼Quantity
M12415400 μL
產品號碼 M12415
價格 (TWD)
14,210.00
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Ends: 31-Dec-2025
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Quantity:
400 μL
價格 (TWD)
14,210.00
Online offer
Ends: 31-Dec-2025
20,300.00
您節省 6,090.00 (30%)
Each
新增至購物車
The nucleotide analog MANT GTP is modified on the ribose moiety. The compact mature of the MANT fluorophore and its attachment position results in nucleotide analogs that induce minimal perturbation of nucleotide-protein interactions. Because MANT fluorescence is sensitive to the environment of the fluorophore, nucleotide-protein interactions may be directly detectable. MANT nucleotides are valuable probes of the structure and enzymatic activity of nucleotide-binding proteins.
For Research Use Only. Not for use in diagnostic procedures.
規格
Label or DyeMANT (N-Methylanthraniloyl)
Product TypeMANT-GTP
Quantity400 μL
Shipping ConditionWet Ice
Concentration5 mM
Unit SizeEach
內容物與存放
Store in freezer -5°C to -30°C and protect from light.

引用資料與參考文獻 (48)

引用資料與參考文獻
Abstract
Authors:
Journal:
PubMed ID:11063593
Activation of the superoxide-generating NADPH oxidase by chimeric proteins consisting of segments of the cytosolic component p67(phox) and the small GTPase Rac1.
Authors:Alloul N, Gorzalczany Y, Itan M, Sigal N, Pick E
Journal:Biochemistry
PubMed ID:11724569
'Activation of the superoxide (O2(-))-generating NADPH oxidase of phagocytes is the consequence of the assembly of a membrane-associated flavocytochrome b(559) with the cytosolic proteins p47(phox) and p67(phox) and the small GTPase Rac (1 or 2). We proposed that Rac1 serves as a membrane-targeting molecule for p67(phox). This hypothesis was tested ... More
A novel function for Cyclin A2: control of cell invasion via RhoA signaling.
Authors:Arsic N, Bendris N, Peter M, Begon-Pescia C, Rebouissou C, Gadéa G, Bouquier N, Bibeau F, Lemmers B, Blanchard JM,
Journal:J Cell Biol
PubMed ID:22232705
'Cyclin A2 plays a key role in cell cycle regulation. It is essential in embryonic cells and in the hematopoietic lineage yet dispensable in fibroblasts. In this paper, we demonstrate that Cyclin A2-depleted cells display a cortical distribution of actin filaments and increased migration. These defects are rescued by restoration ... More
Low affinity interactions of GDPbetaS and ribose- or phosphoryl-substituted GTP analogues with the heterotrimeric G protein, transducin.
Authors:Zera EM, Molloy DP, Angleson JK, Lamture JB, Wensel TG, Malinski JA
Journal:J Biol Chem
PubMed ID:8662741
'We have examined the effects of three commonly used classes of guanine nucleotide analogues on the retinal G protein, transducin (Gt), and found them to be quite different from those that might be expected from results with other GTP-binding proteins. The most surprising results were with guanosine 5''-O-(2-thiodiphosphate) (GDPbetaS); rather ... More
Alanine scan mutagenesis of the switch I domain of the Caulobacter crescentus CgtA protein reveals critical amino acids required for in vivo function.
Authors:Lin B, Skidmore JM, Bhatt A, Pfeffer SM, Pawloski L, Maddock JR
Journal:Mol Microbiol
PubMed ID:11251813
'The Caulobacter crescentus CgtA protein is a member of the Obg/GTP1 subfamily of monomeric GTP-binding proteins. In vitro, CgtA displays moderate affinity for both GDP and GTP and displays rapid exchange rate constants for either nucleotide, indicating that the guanine nucleotide-binding and exchange properties of CgtA are different from those ... More
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