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Merck
모든 사진(5)

Key Documents

HPA002132

Sigma-Aldrich

Anti-ESYT2 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

동의어(들):

Anti-Chr2Syt antibody produced in rabbit, Anti-Extended synaptotagmin-2 antibody produced in rabbit, Anti-FAM62B antibody produced in rabbit, Anti-Protein FAM62B antibody produced in rabbit

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About This Item

UNSPSC 코드:
12352203
인간 단백질 도해서 번호:
NACRES:
NA.41

생물학적 소스

rabbit

결합

unconjugated

항체 형태

affinity isolated antibody

항체 생산 유형

primary antibodies

클론

polyclonal

제품 라인

Prestige Antibodies® Powered by Atlas Antibodies

형태

buffered aqueous glycerol solution

종 반응성

human

향상된 검증

RNAi knockdown
Learn more about Antibody Enhanced Validation

기술

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:500-1:1000

면역원 서열

FTLDEVPKGKLHLRLEWLTLMPNASNLDKVLTDIKADKDQANDGLSSALLILYLDSARNLPSGKKISSNPNPVVQMSVGHKAQESKIRYKTNEPVWEENFTFFIHNPKRQDLEVEVRDEQHQ

배송 상태

wet ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... FAM62B(57488)

일반 설명

ESYT2 (extended synaptotagmin protein 2), membrane-anchored extended synaptotagmin-like protein, belongs to the family of multi-C2 domain membrane proteins. It is composed of an N-terminal transmembrane domain, a central juxtamembranous domain and three or five C-terminal C2 domains. In human three ESYT genes have been found.

면역원

Protein FAM62B recombinant protein epitope signature tag (PrEST)

애플리케이션

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

생화학적/생리학적 작용

ESYT2 (extended synaptotagmin protein 2) is mainly involved in Ca2+ regulated secretion. Its C2 domain is capable of binding Ca2+ and phospholipid at micromolar concentrations. It can bind up to four Ca2+ ions.

특징 및 장점

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

결합

Corresponding Antigen APREST85126

물리적 형태

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

법적 정보

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

면책조항

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


시험 성적서(COA)

제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.

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문서 라이브러리 방문

Junjie Xu et al.
Structure (London, England : 1993), 22(2), 269-280 (2014-01-01)
Contacts between the endoplasmic reticulum and the plasma membrane involve extended synaptotagmins (E-Syts) in mammals or tricalbins in yeast, proteins with multiple C₂ domains. One of the tandem C₂ domains of E-Syt2 is predicted to bind Ca²⁺, but no Ca²⁺-dependent
Sang-Won Min et al.
Proceedings of the National Academy of Sciences of the United States of America, 104(10), 3823-3828 (2007-03-16)
C(2) domains are autonomously folded protein modules that generally act as Ca(2+)- and phospholipid-binding domains and/or as protein-protein interaction domains. We now report the primary structures and biochemical properties of a family of evolutionarily conserved mammalian proteins, referred to as
Zimple Kurlawala et al.
Journal of cellular biochemistry, 118(8), 2261-2270 (2017-01-12)
There are five Ubiquilin proteins (UBQLN1-4, UBQLN-L), which are evolutionarily conserved and structurally similar. UBQLN proteins have three functional domains: N-terminal ubiquitin-like domain (UBL), C-terminal ubiquitin-associated domain (UBA), and STI chaperone-like regions in the middle. Alterations in UBQLN1 gene have
Gerhard J Groer et al.
FEBS letters, 582(28), 3941-3947 (2008-11-04)
The protein family of membrane-anchored extended synaptotagmin-like proteins (E-Syts) was recently discovered in humans. E-Syt1 to 3 each contain at least one transmembrane domain and three or five C2 domains. To investigate the whole C2 area of murine E-Syt2, highly
Natalie Krahmer et al.
Developmental cell, 47(2), 205-221 (2018-10-24)
Lipid metabolism is highly compartmentalized between cellular organelles that dynamically adapt their compositions and interactions in response to metabolic challenges. Here, we investigate how diet-induced hepatic lipid accumulation, observed in non-alcoholic fatty liver disease (NAFLD), affects protein localization, organelle organization

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