HPA002132
抗ESYT2 ウサギ宿主抗体
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
別名:
抗Chr2Syt抗体 ウサギ宿主抗体, 抗FAM62Bタンパク質抗体 ウサギ宿主抗体, 抗FAM62B抗体 ウサギ宿主抗体, 抗延長型シナプトタグミン2抗体 ウサギ宿主抗体
製品名
抗ESYT2 ウサギ宿主抗体, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
product line
Prestige Antibodies® Powered by Atlas Antibodies
form
buffered aqueous glycerol solution
species reactivity
human
enhanced validation
RNAi knockdown
Learn more about Antibody Enhanced Validation
technique(s)
immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:500-1:1000
immunogen sequence
FTLDEVPKGKLHLRLEWLTLMPNASNLDKVLTDIKADKDQANDGLSSALLILYLDSARNLPSGKKISSNPNPVVQMSVGHKAQESKIRYKTNEPVWEENFTFFIHNPKRQDLEVEVRDEQHQ
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... FAM62B(57488)
Legal Information
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Application
Prestige抗体®は、Human Proteome Resource (HPR)プロジェクト (www.proteinatlas.org)によって開発・実証されたAtlas抗体です。Prestige抗体はすべて、数百の正常組織・疾病組織に対する免疫組織染色試験を行っています。これらの染色画像はHuman Protein Atlas (HPA)サイトで[Image Gallery]リンクをクリックするとご覧いただけます。Prestige抗体はプロテインアレイおよびウェスタンブロッティングの試験も行っています。試験の プロトコ-ル およびPrestige抗体、HPAに関する情報は sigma.com/prestigeをご覧ください。
Immunogen
FAM62Bタンパク質のPrEST (protein epitope signature tag)抗原リコンビナントタンパク質。
Physical form
PBS溶液 (pH 7.2, 40%グリセロ-ルおよび0.02%アジ化ナトリウム含有)。
Biochem/physiol Actions
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.
Disclaimer
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.
Features and Benefits
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:
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.
General description
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.
Other Notes
Corresponding Antigen APREST85126
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保管分類
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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
ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.
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