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N-(5-AMINO-1-CARBOXYPENTYL)IMINODIACETIC ACID, TRI-T-BUTYL ESTER is a nitrilotriacetic acid derivative characterized as a yellow oil. It is known for its metal chelating properties, which make it a valuable component in various applications.
Used in Biochemistry Industry:
N-(5-AMINO-1-CARBOXYPENTYL)IMINODIACETIC ACID, TRI-T-BUTYL ESTER is used as a metal chelating adsorbent for metal ion affinity chromatography. It plays a crucial role in the identification and rapid one-step purification of gene products expressed as fusion proteins with an oligo-histidine tag. The oligo-histidine tag has a high affinity for binding with metal chelating absorbents like N-(5-Amino-1-carboxypentyl)iminodiacetic acid, enabling efficient purification processes.

205379-08-4

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205379-08-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 205379-08-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,0,5,3,7 and 9 respectively; the second part has 2 digits, 0 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 205379-08:
(8*2)+(7*0)+(6*5)+(5*3)+(4*7)+(3*9)+(2*0)+(1*8)=124
124 % 10 = 4
So 205379-08-4 is a valid CAS Registry Number.
InChI:InChI=1/C22H42N2O6/c1-20(2,3)28-17(25)14-24(15-18(26)29-21(4,5)6)16(12-10-11-13-23)19(27)30-22(7,8)9/h16H,10-15,23H2,1-9H3/t16-/m1/s1

205379-08-4SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name amino-modified nitrilo-triacetic-acid(NTA)

1.2 Other means of identification

Product number -
Other names N-(5-Amino-1-carboxypentyl)iminodiacetic Acid Tri-t-butyl Ester

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:205379-08-4 SDS

205379-08-4Relevant academic research and scientific papers

Grid coatings for capture of proteins and other compounds

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Page/Page column 19-21, (2021/04/28)

Grids comprising a coating modified with one or more capture agents and a deactivating agent are disclosed. Methods of using such grids in connection with suitable microscopy techniques, such as for determining the structure of target compounds including proteins, are also disclosed.

Assessing changes in the expression levels of cell surface proteins with a turn-on fluorescent molecular probe

Hatai, Joydev,Prasad, Pragati Kishore,Lahav-Mankovski, Naama,Oppenheimer-Low, Noa,Unger, Tamar,Sirkis, Yael Fridmann,Dadosh, Tali,Motiei, Leila,Margulies, David

supporting information, p. 1875 - 1878 (2021/03/01)

Tri-nitrilotriacetic acid (NTA)-based fluorescent probes were developed and used to image His-tagged-labelled outer membrane protein C (His-OmpC) in liveEscherichia coli. One of these probes was designed to light up upon binding, which provided the means

Optimized reaction pair of the Cyshis tag and Ni(II)-Nta probe for highly selective chemical labeling of membrane proteins

Zenmyo, Naoki,Tokumaru, Hiroki,Uchinomiya, Shohei,Fuchida, Hirokazu,Tabata, Shigekazu,Hamachi, Itaru,Shigemoto, Ryuichi,Ojida, Akio

supporting information, p. 995 - 1000 (2019/07/18)

Chemical labeling of proteins with synthetic molecular probes offers the possibility to probe the functions of proteins of interest in living cells. However, the methods for covalently labeling targeted proteins using complementary peptide tag-probe pairs are still limited, irrespective of the versatility of such pairs in biological research. Herein, we report the new CysHis tag-Ni(II) probe pair for the specific covalent labeling of proteins. A broad-range evaluation of the reactivity profiles of the probe and the CysHis peptide tag afforded a tag-probe pair with an optimized and high labeling selectivity and reactivity. In particular, the labeling specificity of this pair was notably improved compared to the previously reported one. This pair was successfully utilized for the fluorescence imaging of membrane proteins on the surfaces of living cells, demonstrating its potential utility in biological research.

Simple and efficient knockdown of His-tagged proteins by ternary molecules consisting of a His-tag ligand, a ubiquitin ligase ligand, and a cell-penetrating peptide

Hattori, Takayuki,Okitsu, Koyo,Yamazaki, Norikazu,Ohoka, Nobumichi,Shibata, Norihito,Misawa, Takashi,Kurihara, Masaaki,Demizu, Yosuke,Naito, Mikihiko

supporting information, p. 4478 - 4481 (2017/09/12)

We designed and synthesized hybrid molecules for a protein knockdown method based on the recognition of a His-tag fused to a protein of interest (POI). The synthesized target protein degradation inducers contained three functional moieties: a His-tag liga

Protein Delivery System Containing a Nickel-Immobilized Polymer for Multimerization of Affinity-Purified His-Tagged Proteins Enhances Cytosolic Transfer

Postupalenko, Viktoriia,Desplancq, Dominique,Orlov, Igor,Arntz, Youri,Spehner, Danièle,Mely, Yves,Klaholz, Bruno P.,Schultz, Patrick,Weiss, Etienne,Zuber, Guy

supporting information, p. 10583 - 10586 (2015/09/02)

Recombinant proteins with cytosolic or nuclear activities are emerging as tools for interfering with cellular functions. Because such tools rely on vehicles for crossing the plasma membrane we developed a protein delivery system consisting in the assembly

MOLECULAR SENSOR AND METHODS OF USE THEREOF

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Paragraph 00118, (2014/07/21)

The present invention is directed to fluorescent molecular sensor based on thiazole orange as represented below for protein detection. Interaction of the protein target with the molecular sensors of this invention results in a significant increase in the fluorescence emission. The generation of light output signal enables one to detect protein biomarkers associated with different diseases or detecting the protein of interest also in living cells.

A supramolecular host-guest carrier system for growth factors employing VHH fragments

Cabanas-Dans, Jordi,Rodrigues, Emilie Dooms,Landman, Ellie,Van Weerd, Jasper,Van Blitterswijk, Clemens,Verrips, Theo,Huskens, Jurriaan,Karperien, Marcel,Jonkheijm, Pascal

supporting information, p. 12675 - 12681 (2015/01/09)

A supramolecular strategy is presented for the assembly of growth factors employing His6-tagged single-domain antibodies (VHH). A combination of orthogonal supramolecular interactions of β-cyclodextrin (βCD)-adamantyl (Ad) host-guest

Oriented insertion of phi29 N-hexahistidine-tagged gp10 connector protein assemblies into C20BAS bolalipid membrane vesicles

Hyun, Seok-Hee,Kim, Hee-Kwon,Kim, Jong-Mok,Thompson, David H.

supporting information; experimental part, p. 17053 - 17055 (2011/03/01)

Ni2+:NTA-PEG600-grafted glass surfaces are capable of immobilizing N-his6 gp10 connector protein assemblies from the phi29 DNA packaging motor and mediating their transplantation into bolalipid vesicles whose membrane thickness is co

Synthesis of a pH-sensitive nitrilotriacetic linker to peptide transduction domains to enable intracellular delivery of histidine imidazole ring-containing macromolecules

June, Ronald K.,Gogoi, Khirud,Eguchi, Akiko,Cui, Xian-Shu,Dowdy, Steven F.

supporting information; experimental part, p. 10680 - 10682 (2010/11/16)

Intracellular delivery of functional macromolecules using peptide transduction domains (PTDs) is an exciting technology with both experimental and therapeutic applications. Recent data indicate that PTD-mediated transduction occurs via fluid-phase macropi

Synthesis of nickel-chelating fluorinated lipids for protein monolayer crystallizations

Hussein, Waleed M.,Ross, Benjamin P.,Landsberg, Michael J.,Lévy, Daniel,Hankamer, Ben,McGeary, Ross P.

supporting information; experimental part, p. 1473 - 1479 (2009/07/11)

Nickel-chelating lipids have been synthesized for use as functionalized templates for 2-D crystallization of membrane proteins. These monolayer-forming lipids have been designed with three distinct components: (i) a branched hydrocarbon tail to confer flu

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