抗Human CMG-2 Phycoerythrin抗体(Anti-Human CMG-2 Phycoerythrin antibody)

• 価格
• Product Details
• Applications and Data
• Related Product & Information

価格

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Product Details

Species Reactivity	Human
Label	Phycoerythrin
Immunogen	Mouse myeloma cell line NS0-derived recombinant human CMG‑2/ANTXR2 isoform 1Gln34-Asn317Accession # P58335
Source	Polyclonal Goat IgG
Purification	Antigen Affinity-purified
Specificity	Detects human CMG‑2/ANTXR2 in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 20% cross-reactivity with recombinant mouse CMG-2 is observed.

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Applications and Data

	Recommended Concentration	Sample
Flow Cytometry	10 µL/106 cells	See below

Flow Cytometry
	Detection of CMG‑2/ANTXR2 in Human Whole Blood Monocytes by Flow Cytometry. Human whole blood monocytes were stained with Goat Anti-Human CMG‑2/ANTXR2 PE‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB2940P, filled histogram) or isotype control antibody (Catalog # IC108P, open histogram). View our protocol for Staining Membrane-associated Proteins.

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Related Product & Information

Background

CMG-2/ANTXR2

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Background: CMG-2/ANTXR2 Capillary Morphogenesis Gene-2 (CMG-2) is a widely expressed Anthrax Toxin Receptor (ATR) family protein (1‑3). CMG-2 is a 55 kDa type I transmembrane (TM) protein that contains a 33 amino acid (aa) signal sequence, a 284 aa extracellular domain (ECD), a 24 aa TM segment, and a 147 aa cytoplasmic domain. There are three additional isoforms. Isoform 4 shows a 12 aa insertion in the cytoplasmic region, isoform 2 shows a 103 aa deletion in the ECD, and isoform 3 is a truncated, 20 kDa, 289 aa soluble form. The main functional domain of CMG-2 is an extracellular integrin-like von Willebrand factor type A (VWA) domain with a metal ion dependent adhesion site (MIDAS). This domain adheres selectively to collagen type IV and laminin (1‑5). CMG-2 isoform 2 is induced in HUVEC as they undergo capillary formation in collagen matrices in vitro (3). CMG-2 is mutated in juvenile hyaline fibromatosis and infantile systemic hyalinosis disorders, and several of these mutations result in loss of laminin binding (6). CMG-2 and the related protein ATR/TEM8 serve as receptors for the protective antigen (PA) of Bacillus Anthracis (1, 2). After binding the VWA domain, PA undergoes furin-type cleavage, forms a heptameric receptor/PA pre-pore, and binds LF or EF toxin subunits (5, 7, 8). Transport to low pH endosomes, which requires CMG-2 ubiquitination and interaction with the LDL receptor related protein LRP6 (9, 10), allows PA pore formation and release of toxin to the cytoplasm (10, 11). Soluble CMG-2 VWA domain acts as a dummy receptor that can protect cultured cells from anthrax intoxication (2). Within the extracellular region, human CMG-2 shares 84%, 81%,89% and 93% amino acid sequence identity with mouse, rat, bovine, and canine CMG-2, respectively. CMG-2 VWA domain also shares 60% aa sequence identity with ATR/TEM8.

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