Human CD46 Protein 3858

$285.00 – $950.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Cys35-Asp343

SKU: 3858parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P15529
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	CD46 was discovered in 1986 during a search for novel C3b-binding proteins. CD46 is expressed ubiquitously and functions as a co-factor in the factor I-mediated proteolytic cleavage of C3b and C4b. Its vital role in preventing complement deposition on host tissue is underpinned by the fact that deficiency of CD46 is a predisposing factor for numerous disease conditions arising from complement-mediated 'self-attack'.
molecular weight	The protein has a predicted MW of 35.4 kDa. Due to glycosylation, the protein migrates to 60-70 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human CD46 Protein 3858

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
CD46 was discovered in 1986 during a search for novel C3b-binding proteins. CD46 is expressed ubiquitously and functions as a co-factor in the factor I-mediated proteolytic cleavage of C3b and C4b. Its vital role in preventing complement deposition on host tissue is underpinned by the fact that deficiency of CD46 is a predisposing factor for numerous disease conditions arising from complement-mediated 'self-attack'.
Protein names Membrane cofactor protein (TLX) (Trophoblast leukocyte common antigen) (CD antigen CD46)
Gene names CD46,CD46 MCP MIC10
Mass 43747Da
Function FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. {ECO:0000269\|PubMed:10843656, ECO:0000269\|PubMed:12540904}.; FUNCTION: (Microbial infection) A number of viral and bacterial pathogens seem to bind MCP in order to exploit its immune regulation property and directly induce an immunosuppressive phenotype in T-cells.; FUNCTION: (Microbial infection) Acts as a receptor for Adenovirus subgroup B2 and Ad3. {ECO:0000269\|PubMed:12915534, ECO:0000269\|PubMed:14566335, ECO:0000269\|PubMed:15047806, ECO:0000269\|PubMed:15078926, ECO:0000269\|PubMed:15919905, ECO:0000269\|PubMed:16254377}.; FUNCTION: (Microbial infection) Acts as a receptor for cultured Measles virus. {ECO:0000269\|PubMed:10972291, ECO:0000269\|PubMed:20010840, ECO:0000269\|PubMed:7534417, ECO:0000269\|PubMed:8371352, ECO:0000269\|PubMed:8402913}.; FUNCTION: (Microbial infection) Acts as a receptor for Herpesvirus 6/HHV-6. {ECO:0000269\|PubMed:12663806, ECO:0000269\|PubMed:12724329}.; FUNCTION: (Microbial infection) May act as a receptor for pathogenic bacteria Neisseria and Streptococcus pyogenes (PubMed:11260136, PubMed:11971006, PubMed:7708671, PubMed:9379894).
Subellular location SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269\|PubMed:12112588, ECO:0000269\|PubMed:14597734, ECO:0000269\|PubMed:15307194}; Single-pass type I membrane protein {ECO:0000269\|PubMed:12112588, ECO:0000269\|PubMed:14597734, ECO:0000269\|PubMed:15307194}. Note=Inner acrosomal membrane of spermatozoa. Internalized upon binding of Measles virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an increased susceptibility of infected cells to complement-mediated injury. In cancer cells or cells infected by Neisseria, shedding leads to a soluble peptide.
Tissues TISSUE SPECIFICITY: Expressed by all cells except erythrocytes.
Structure SUBUNIT: Interacts with C3b (PubMed:1717583, PubMed:3260937). Interacts with C4b (PubMed:1717583). Interacts with moesin/MSN (PubMed:7884872). {ECO:0000269\|PubMed:1717583, ECO:0000269\|PubMed:3260937, ECO:0000269\|PubMed:7884872}.; SUBUNIT: (Microbial infection) Interacts (via N-terminus) with measles virus H protein; this interaction allows attachment and viral entry of vaccine and laboratory-adapted strains. {ECO:0000269\|PubMed:10972291, ECO:0000269\|PubMed:20010840}.; SUBUNIT: (Microbial infection) Interacts with human herpesvirus 6 GH protein (PubMed:12663806, PubMed:12724329). {ECO:0000269\|PubMed:12663806, ECO:0000269\|PubMed:12724329}.; SUBUNIT: (Microbial infection) Interacts with human adenovirus B/D fiber protein (PubMed:12915534, PubMed:14566335, PubMed:15047806, PubMed:15078926, PubMed:15919905, PubMed:16254377). {ECO:0000269\|PubMed:12915534, ECO:0000269\|PubMed:14566335, ECO:0000269\|PubMed:15047806, ECO:0000269\|PubMed:15078926, ECO:0000269\|PubMed:15919905, ECO:0000269\|PubMed:16254377}.; SUBUNIT: (Microbial infection) Binds to Streptococcus pyogenes M protein and to type IV pili from Neisseria (PubMed:11260136, PubMed:11971006, PubMed:7708671, PubMed:9379894). {ECO:0000269\|PubMed:11260136, ECO:0000269\|PubMed:11971006, ECO:0000269\|PubMed:7708671, ECO:0000269\|PubMed:9379894}.
Post-translational modification PTM: N-glycosylated on Asn-83; Asn-114 and Asn-273 in most tissues, but probably less N-glycosylated in testis. N-glycosylation on Asn-114 and Asn-273 is required for cytoprotective function. N-glycosylation on Asn-114 is required for Measles virus binding. N-glycosylation on Asn-273 is required for Neisseria binding. N-glycosylation is not required for human adenovirus binding.; PTM: Extensively O-glycosylated in the Ser/Thr-rich domain. O-glycosylation is required for Neisseria binding but not for Measles virus or human adenovirus binding.; PTM: In epithelial cells, isoforms B/D/F/H/J/L/3 are phosphorylated by YES1 in response to infection by Neisseria gonorrhoeae; which promotes infectivity. In T-cells, these isoforms may be phosphorylated by LCK.
Domain DOMAIN: Sushi domains 1 and 2 are required for interaction with human adenovirus B PIV/FIBER protein and with Measles virus H protein. Sushi domains 2 and 3 are required for Herpesvirus 6 binding. Sushi domain 3 is required for Neisseria binding. Sushi domains 3 and 4 are required for interaction with Streptococcus pyogenes M protein and are the most important for interaction with C3b and C4b.
Target Relevance information above includes information from UniProt accession: P15529
The UniProt Consortium

Data

Immobilized Human CD46, His Tag at 0.5µg/ml (100µl/Well) on the plate. Dose response curve for Anti-CD46 Antibody, hFc Tag with the EC50 of 4.2ng/ml determined by ELISA.

The purity of Human CD46 is greater than 95% as determined by SEC-HPLC.

Human CD46 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.