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Merck
모든 사진(1)

주요 문서

Q4990

Sigma-Aldrich

QBP1

≥95% (HPLC)

동의어(들):

L-Seryl-L-asparaginyl-L-tryptophyl-L-lysyl-L-tryptophyl-L-tryptophyl-L-prolylglycyl-L-isoleucyl-L-phenylalanyl-L-aspartic acid trifluoroacetate salt

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크기 선택

1 MG
₩321,349

₩321,349


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벌크 견적 요청

크기 선택

보기 변경
1 MG
₩321,349

About This Item

실험식(Hill 표기법):
C72H90N16O16 · xC2HF3O2
CAS Number:
Molecular Weight:
1435.58 (free base basis)
UNSPSC 코드:
12352203
PubChem Substance ID:
NACRES:
NA.25

₩321,349


구입 가능 여부는 고객센터에 문의하십시오.
기존과 동일한 품질을 인하된 가격으로 - 어려운 예산 상황을 머크와 함께 극복하세요

벌크 견적 요청

분석

≥95% (HPLC)

양식

powder

색상

white

solubility

H2O: >1 mg/mL

저장 온도

−20°C

SMILES string

OC(=O)C(F)(F)F.CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc2c[nH]c3ccccc23)NC(=O)[C@H](Cc4c[nH]c5ccccc45)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc6c[nH]c7ccccc67)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](Cc8ccccc8)C(=O)N[C@@H](CC(O)=O)C(O)=O

InChI

1S/C72H90N16O16.C2HF3O2/c1-3-39(2)62(70(101)84-52(28-40-16-5-4-6-17-40)65(96)86-57(72(103)104)33-61(92)93)87-60(91)37-79-69(100)58-25-15-27-88(58)71(102)56(31-43-36-78-50-23-12-9-20-46(43)50)85-67(98)54(30-42-35-77-49-22-11-8-19-45(42)49)82-64(95)51(24-13-14-26-73)80-66(97)53(29-41-34-76-48-21-10-7-18-44(41)48)83-68(99)55(32-59(75)90)81-63(94)47(74)38-89;3-2(4,5)1(6)7/h4-12,16-23,34-36,39,47,51-58,62,76-78,89H,3,13-15,24-33,37-38,73-74H2,1-2H3,(H2,75,90)(H,79,100)(H,80,97)(H,81,94)(H,82,95)(H,83,99)(H,84,101)(H,85,98)(H,86,96)(H,87,91)(H,92,93)(H,103,104);(H,6,7)/t39-,47-,51-,52-,53-,54-,55-,56-,57-,58-,62-;/m0./s1

InChI key

VSUBSHMCMRUEAG-IQVZWRNHSA-N

애플리케이션

QBP1, an oligopeptide inhibitor of polyglutamine protein aggregation, may be used to study the physicochemical processes of polyglutamine-dependent protein misfolding, aggregation and precipitation. QBP1 may be used to study the role polyglutamine protein aggregation in causing or aggravating polyglutamine diseases including neurodegenerative diseases such as Huntington′s dentatorubral pallidoluysian atrophy, spinobulbar muscular atrophy, and spinocerebellar ataxia.[1][2]

생화학적/생리학적 작용

QBP1 is an inhibitor of polyglutamine protein aggregation and cell death.
QBP1 is an inhibitor of polyglutamine protein aggregation and cell death. QBP1 inhibits polyglutamine aggregation in COS-7 cells at a concentration of 25 μM, as shown by complete inhibition of thioredoxin-Q62 aggregation assayed by turbidity at 405 nm. QBP1 reduces cell death of these cells by 50% and increases median life span from 5.5-52 days in Drosophilla melanogaster that expresses the expanded polyglutamine; can be shortened to 8 amino acids (Trp-Ley-Trp-Trp-Pro-Gly-Ile-Phe) without the loss of ability to inhibit polyglutamine aggregation. Several inherited neurodegenerative diseases, Huntington′s dentatorubral pallidoluysian atrophy, spinobulbar muscular atrophy, and spinocerebellar ataxia are caused by the expanded CAG repeats in the coding region of the gene, leading to accumulation of polyglutamine.

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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시험 성적서(COA)

Lot/Batch Number

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문서 라이브러리 방문

Peter O Bauer et al.
Nature biotechnology, 28(3), 256-263 (2010-03-02)
Huntington's Disease (HD) is a dominantly inherited pathology caused by the accumulation of mutant huntingtin protein (HTT) containing an expanded polyglutamine (polyQ) tract. As the polyglutamine binding peptide 1 (QBP1) is known to bind an expanded polyQ tract but not
Miguel Mompeán et al.
Archives of biochemistry and biophysics, 675, 108113-108113 (2019-10-01)
Transactive Response DNA-Binding Protein of 43 kDa (TDP-43) is an essential human protein implicated in Amyotrophic Lateral Sclerosis (ALS) and common dementias. Its C-terminal disordered region, composed of residues 264-414 includes a hydrophobic segment (residues 320-340), which drives physiological liquid/liquid phase
H Akiko Popiel et al.
PloS one, 7(11), e51069-e51069 (2012-12-12)
The polyglutamine (polyQ) diseases such as Huntington's disease (HD), are neurodegenerative diseases caused by proteins with an expanded polyQ stretch, which misfold and aggregate, and eventually accumulate as inclusion bodies within neurons. Molecules that inhibit polyQ protein misfolding/aggregation, such as
Amit Mishra et al.
The Journal of biological chemistry, 283(12), 7648-7656 (2008-01-19)
The accumulation of intracellular protein deposits as inclusion bodies is the common pathological hallmark of most age-related neurodegenerative disorders including polyglutamine diseases. Appearance of aggregates of the misfolded mutant disease proteins suggest that cells are unable to efficiently degrade them

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