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Merck
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Key Documents

HPA003084

Sigma-Aldrich

Anti-MDGA2 antibody produced in rabbit

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

동의어(들):

Anti-MAM domain-containing glycosylphosphatidylinositol anchor protein 2 antibody produced in rabbit, Anti-MAM domain-containing protein 1 precursor 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

기술

immunohistochemistry: 1:50- 1:200

면역원 서열

ALVQLIVQYPPAVEPAFLEIRQGQDRSVTMSCRVLRAYPIRVLTYEWRLGNKLLRTGQFDSQEYTEYAVKSLSNENYGVYNCSIINEAGAGRCSFLVTGKAYAPEFYYDTYNPVWQNRHRVYSYSLQWTQMNPDAV

UniProt 수납 번호

배송 상태

wet ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... MDGA2(161357)

관련 카테고리

면역원

MAM domain-containing protein 1 precursor recombinant protein epitope signature tag (PrEST)

애플리케이션

Anti-MDGA2 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.

생화학적/생리학적 작용

MDGA2 (MAM domain containing glycosylphosphatidylinositol anchor 2) gene encodes a cell adhesion molecule belonging to the IgCAM superfamily of proteins. It is abundantly expressed in dorsolaterally located (dI1) spinal interneurons. It functions in the longitudinal axonal extension. This gene is a susceptibility gene for systemic lupus erythematosus (SLE).

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 APREST70618

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

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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

Anna Hellquist et al.
PloS one, 4(12), e8037-e8037 (2009-12-10)
Systemic lupus erythematosus (SLE) is a complex autoimmune disorder with multiple susceptibility genes. We have previously reported suggestive linkage to the chromosomal region 14q21-q23 in Finnish SLE families. Genetic fine mapping of this region in the same family material, together
Pascal Joset et al.
Neural development, 6, 22-22 (2011-05-06)
Long-distance axonal growth relies on the precise interplay of guidance cues and cell adhesion molecules. While guidance cues provide positional and directional information for the advancing growth cone, cell adhesion molecules are essential in enabling axonal advancement. Such a dependence
Gregory R Johnson et al.
PLoS computational biology, 11(12), e1004614-e1004614 (2015-12-02)
Characterizing the spatial distribution of proteins directly from microscopy images is a difficult problem with numerous applications in cell biology (e.g. identifying motor-related proteins) and clinical research (e.g. identification of cancer biomarkers). Here we describe the design of a system

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