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Merck

MABF983

Anti-Complement C3b/iC3b/C3dg Antibody, clone 1H8

clone 1H8, from mouse

동의어(들):

Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, Complement C3 beta chain, C3-beta-c, C3bc, Complement C3 alpha chain, C3a anaphylatoxin, Acylation stimulating protein, ASP, C3adesArg, Complement C3b alpha′ chain, Complem

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제품정보 (DICE 배송 시 비용 별도)

UNSPSC 코드:
12352203
eCl@ss:
32160702
NACRES:
NA.41

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기술 서비스
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도움 문의

생물학적 소스

mouse

Quality Level

결합

unconjugated

항체 형태

purified immunoglobulin

항체 생산 유형

primary antibodies

클론

1H8, monoclonal

종 반응성

human, primate

기술

flow cytometry: suitable

동형

IgG2aκ

NCBI 수납 번호

UniProt 수납 번호

배송 상태

wet ice

타겟 번역 후 변형

unmodified

유전자 정보

human ... C3(718)

일반 설명

187 kDa calculated
Complement C3 (UniProt P01024; also known as C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1) is encoded by the C3 (also known as CPAMD1) gene (Gene ID 718) in human. C3 is initially translated with an N-terminal 22-amino acid signal peptide sequence, which is then removed to produce the 1641-amino acid mature C3. It plays a central role in the activation of complement system. Its activation is required for the activation of both classical and alternative pathway of complement (CPC and APC, respectively). C3 is cleaved into C3a and C3b during CPC activation by the C3-convertase C4b2a composed of the activated C4 and C2. In APC, C3 is cleaved by the C3-convertase C3bBb composed C3b and the activated form of factor B (Bb). C3b serves as an opsonizing agent, and can be further cleaved by Factor I into C3c and C3d. iC3b is a proteolytically inactive C3b fragment that still opsonizes target microbes or cells, but cannot further amplify/activate the complement cascade through APC. iC3b can be further cleaved to C3dg, and finally to C3d. Unregulated activation of APC can result in paroxysmal nocturnal hemoglobinuria (PNH) that is characterized by chronic intravascular hemolysis. Clinical C5-neutralizing mAb treatment prevents the formation of cytolytic membrane attack complex (MAC) of complement, but does not block APC activation. Consequently, PNH patients are left with immune-mediated hemolytic anemia and their erythrocytes become opsonized with complement C3. Monoclonal antibodies (mAbs) against C3b/iC3b are useful for monitoring and studying C3b/iC3b deposit on PNH blood cells and mAbs with neutralizing activities are useful tools for studying C3-mediated CPC and APC.

면역원

Epitope: iC3dg
Sepharose 4B beads with surface C3b/C3bi deposits via APC in normal human serum corresponding to the iC3dg of human Complement C3b/iC3b/C3dg.

애플리케이션

Flow Cytometry Analysis: A presentative lot detected C3b/iC3b/C3dg deposit on paroxysmal nocturnal hemoglobinuria (PNH) patient-derived erythrocyte ghosts due to alternative pathway of complement (APC) activation-mediated hemolysis in acidified normal human serum (aNHS; pH 6.4) (Lindorfer, M.A., et al. (2010). Blood. 115(11):2283-2291).
This mouse monoclonal Anti-Complement C3b/iC3b/C3dg Antibody, clone 1H8, Cat. No. MABF983 is validated for use in Flow Cytometry, for the detection of C3b.

생화학적/생리학적 작용

This clone binds C3b, iC3b, and C3dg, but does not block the activation of alternative pathway of complement (APC).

물리적 형태

Format: Purified

분석 메모

Flow Cytometry Analysis: This antibody (200 ug mAb/5 x 10e6 cells/mL) detected C3b/iC3b/C3dg deposit on human Burkett′s lymphoma Raji B cells opsonized with anti-CD20 mAb Rituximab (RTX) in the presence of 50% normal human serum (NHS).

기타 정보

Concentration: Please refer to lot specific datasheet.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


시험 성적서(COA)

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관련 콘텐츠

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

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