HPA013321
Anti-POMK antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonim(y):
Anti-FLJ23356, Anti-SgK196
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About This Item
Polecane produkty
pochodzenie biologiczne
rabbit
Poziom jakości
białko sprzężone
unconjugated
forma przeciwciała
affinity isolated antibody
rodzaj przeciwciała
primary antibodies
klon
polyclonal
linia produktu
Prestige Antibodies® Powered by Atlas Antibodies
Postać
buffered aqueous glycerol solution
reaktywność gatunkowa
human
rozszerzona walidacja
recombinant expression
Learn more about Antibody Enhanced Validation
metody
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:20-1:50
sekwencja immunogenna
TSNFSILANDLDALPLVNHSSGMLVKCGHRELHGDFVAPEQLWPYGEDVPFHDDLMPSYDEKIDIWKIPDISSFLLGHIEGSDMVRFHLFDIHKACKSQTPSERPTAQDVLETYQKVLDTL
Warunki transportu
wet ice
temp. przechowywania
−20°C
docelowa modyfikacja potranslacyjna
unmodified
informacje o genach
human ... SGK196(84197)
Immunogen
Protein kinase-like protein SgK196 recombinant protein epitope signature tag (PrEST)
Zastosowanie
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.
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.
Działania biochem./fizjol.
The SGK196 (Sugen kinase 196) gene encodes a protein called protein-O-mannose kinase (POMK) that is a glycosylation-specific O-mannose kinase that functions in the presentation of the laminin-binding O-linked carbohydrate chain of α-dystroglycan (α-DG). It catalyzes the phosphorylation of the mannose residue in the core M3 glycan. Mutations in this gene have been associated with disruption of dystroglycan receptor function leading to congenital muscular dystrophy. Loss of function, mutation in this gene has been observed in patients with Walker-Warburg syndrome (WWS).
Cechy i korzyści
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.
Powiązanie
Corresponding Antigen APREST72363
Postać fizyczna
Solution in phosphate buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide.
Informacje prawne
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
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Kod klasy składowania
10 - Combustible liquids
Klasa zagrożenia wodnego (WGK)
WGK 1
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Certyfikaty analizy (CoA)
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Masz już ten produkt?
Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Lucas T Jae et al.
Science (New York, N.Y.), 340(6131), 479-483 (2013-03-23)
Glycosylated α-dystroglycan (α-DG) serves as cellular entry receptor for multiple pathogens, and defects in its glycosylation cause hereditary Walker-Warburg syndrome (WWS). At least eight proteins are critical to glycosylate α-DG, but many genes mutated in WWS remain unknown. To identify
Ci Xu et al.
Oncogenesis, 9(1), 4-4 (2020-01-09)
SGK196 is a protein O-mannose kinase involved in an indispensable phosphorylation step during laminin-binding glycan synthesis on alpha-dystroglycan (α-DG). However, the function of SGK196 in cancer diseases remains elusive. In the current study, we demonstrated that SGK196 is primarily modified
Takako Yoshida-Moriguchi et al.
Science (New York, N.Y.), 341(6148), 896-899 (2013-08-10)
Phosphorylated O-mannosyl trisaccharide [N-acetylgalactosamine-β3-N-acetylglucosamine-β4-(phosphate-6-)mannose] is required for dystroglycan to bind laminin-G domain-containing extracellular proteins with high affinity in muscle and brain. However, the enzymes that produce this structure have not been fully elucidated. We found that glycosyltransferase-like domain-containing 2 (GTDC2)
Ameya S Walimbe et al.
eLife, 9 (2020-09-26)
Matriglycan [-GlcA-β1,3-Xyl-α1,3-]n serves as a scaffold in many tissues for extracellular matrix proteins containing laminin-G domains including laminin, agrin, and perlecan. Like-acetyl-glucosaminyltransferase 1 (LARGE1) synthesizes and extends matriglycan on α-dystroglycan (α-DG) during skeletal muscle differentiation and regeneration; however, the mechanisms
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