C3 (基因名), Complement C3 (蛋白名), co3_human.
产品名称:
C3 Antibody
补体蛋白3
货号:
M0861Rb-h
商标:
EIAab®
监管等级:
别名:
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, CPAMD1
反应性:
human
免疫原:
corresponding to a sequence mapping at the CSVQLTEKRMDKVGKYPKEL of P01024
形态:
Liquid
存储说明:
4℃ for frequent use, -20℃ to -70℃ for 6 months
缓冲液:
0.1M×PBS,50% glycerol,pH7.5
浓度:
200ug/ml
纯化方式:
Immunogen affinity purified
克隆性:
Monoclonal
亚型:
Mouse IgG
应用:
推荐产品:
研究领域:
Immunology
R&D 技术数据
更多信息,请参阅手册,或联系我们的技术支持: tech@eiaab.com.
通用注释
亚单元:
C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). During pregnancy, C3dg exists as a complex (probably a 2:2:2 heterohexamer) with AGT and the proform of PRG2. Interacts with VSIG4. C3b interacts with herpes simplex virus 1 (HHV-1) and herpes simplex virus 2 (HHV-2) envelope glycoprotein C; this interaction inhibits the activation of the complement system. Interacts with S.aureus immunoglobulin-binding protein sbi, this prevents interaction between C3dg and CR2. Interacts with S.aureus fib. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77.
功能:
Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2 (PubMed:8376604, PubMed:2909530, PubMed:9059512, PubMed:10432298, PubMed:15833747, PubMed:16333141, PubMed:19615750).
亚细胞位置:
Secreted
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