Mouse IgM (µ) (min X Hu Sr Prot), Biotin

Price:
634 EUR
760 USD
526 GBP
known as: Mouse IgM (µ) (min X Hu Sr Prot), Biotin
Catalog number: genta-BMDB69
Product Quantity: 1 ml.
Category:
Supplier: Accu

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Gene target: min x hu sr prot

Related genes to: Mouse IgM (µ) (min X Hu Sr Prot), Biotin

Symbol : biotin NIH gene
LocusTag : Bathy11g00270
chromosome : 11
description : biotin synthase
type of gene : protein-coding
Modification date : 2015-06-26
Symbol : IGM NIH gene
description : IgM constant region
type of gene : other
Modification date : 2016-04-02
Symbol : min NIH gene
Synonyms : mi
dbXrefs : FLYBASE:FBgn0002747
chromosome : 2
map location : 56E-56E|2-90 cM
description : mini
type of gene : unknown
Modification date : 2016-05-09
Symbol : Prot NIH gene
dbXrefs : MGI:MGI:107578
chromosome : 18
description : proline transporter
type of gene : protein-coding
Symbol from nomenclature authority : Prot
Full name from nomenclature authority : proline transporter
Nomenclature status : O
Modification date : 2016-07-02

Related Pathways to: Mouse IgM (µ) (min X Hu Sr Prot), Biotin

Gene about :IgM
Pathway :Rn Inflammatory Response Pathway
IgM
Gene about :biotin
Pathway :Sc Protein Modifications
biotin

Related product to: Mouse IgM (µ) (min X Hu Sr Prot), Biotin

Related Articles about: Mouse IgM (µ) (min X Hu Sr Prot), Biotin

Specific IgM and Regulation of Antibody Responses.

Specific IgM, administered together with the antigen it recognizes, enhances primary antibody responses, formation of germinal centers, and priming for secondary antibody responses. The response to all epitopes on the antigen to which IgM binds is usually enhanced. IgM preferentially enhances responses to large antigens such as erythrocytes, malaria parasites, and keyhole limpet hemocyanine. In order for an effect to be seen, antigens must be administered in suboptimal concentrations and in close temporal relationship to the IgM. Enhancement is dependent on the ability of IgM to activate complement, but the lytic pathway is not required. Enhancement does not take place in mice lacking complement receptors 1 and 2 (CR1/2) suggesting that the role of IgM is to generate C3 split products, i.e., the ligands for CR1/2. In mice, these receptors are expressed on follicular dendritic cells (FDCs) and B cells. Optimal IgM-mediated enhancement requires that both cell types express CR1/2, but intermediate enhancement is seen when only FDCs express the receptors and low enhancement when only B cells express them. These observations imply that IgM-mediated enhancement works through several, non-mutually exclusive, pathways. Marginal zone B cells can transport IgM-antigen-complement complexes, bound to CR1/2, from the marginal zone and deposit them onto FDCs. In addition, co-crosslinking of the BCR and the CR2/CD19/CD81 co-receptor complex may enhance signaling to specific B cells, a mechanism likely to be involved in induction of early extrafollicular antibody responses. - Source :PubMed

Reliability, validity, and norms of the 2-min walk test in children with and without neuromuscular disorders aged 6-12.

The 2-min walk test may be more appropriate functional exercise test for young children. This study aimed to examine the 2-min walk test's reliability; validity; and minimal clinically important difference; and to establish norms for children aged 6-12. - Source :PubMed

Click biotinylation of PLGA template for biotin receptor oriented delivery of doxorubicin hydrochloride in 4T1 cell induced breast cancer.

PLGA was functionalized with PEG and biotin using click chemistry to generate a biotin receptor targeted copolymer (Biotinylated-PEG-PLGA) which in turn was used to fabricate ultrafine nanoparticles (BPNP) of doxorubicin hydrochloride (DOX) for effective delivery in 4T1 cell induced breast cancer. However adequate entrapment of a hydrophilic bioactive like DOX in a hydrophobic polymer system made of PLGA is not usually possible. We therefore modified a conventional W/O/W emulsion method by utilizing ammonium chloride in the external phase to constrain DOX in dissolved polymer phase by supressing its inherent aqueous solubility as per common ion effect. This resulted in over eight fold enhancement in entrapment efficiency of DOX inside BPNP, which otherwise is highly susceptible to leakage due to its relatively high aqueous solubility. TEM and DLS established BPNP to be sized below 100 nm, storage stability studies showed that BPNP were stable for one month at 4°C, and in vitro release suggested significant control in drug release. Extensive in vitro and in vivo studies were conducted to propound anticancer and antiproliferative activity of BPNP. Plasma and tissue distribution study supplemented by pertinent in vivo fluorescence imaging mapped the exact fate of DOX contained inside BPNP once it was administered intravenously. A comparative safety profile via acute toxicity studies in mice was also generated to out rightly establish usefulness of BPNP. Results suggest that BPNP substantially enhance anticancer activity of DOX whilst simultaneously mitigating its toxic potential due to altered spatial and temporal presentation of drug and consequently deserve further allometric iteration. - Source :PubMed

Anti-Fas2 IgM antibodies in Fasciola hepatica infected patients with positive IgG serology.

Fascioliasis is an infectious disease caused by parasites Fasciola hepatica and F. gigantica. Humans are infected by the consumption of vegetables and water contaminated with the infective form of the parasite. - Source :PubMed

A photocrosslinkable biotin derivative of the phosphoantigen (E)-4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP) activates Vγ9Vδ2 T cells and binds to the HMBPP site of BTN3A1.

Vγ9Vδ2 T cells play an important role in the cross talk of the innate and adaptive immune system. For their activation by phosphoantigens (PAgs) both cell surface receptors the eponymous Vγ9Vδ2 T cell antigen receptors (Vγ9Vδ2 TCRs) on Vγ9Vδ2 T cells and butyrophilin 3A1 (BTN3A1) on the phosphoantigen-"presenting" cell are mandatory. To find yet undetected further contributing proteins a biotinylated, photocrosslinkable benzophenone probe BioBP-HMBPP (2) was synthesized from a known allyl alcohol in nine steps and overall 16% yield. 2 is based on the picomolar PAg (E)-4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP, 1). Laser irradiation of 2 at 308 nm initiated the photocrosslinking reaction with proteins. When the B30.2 domain of BTN3A1, which contains a positively charged PAg-binding pocket, was exposed to increasing amounts of HMBPP (1) labeling by BioBP-HMBPP (2) was reduced significantly. Since BSA labeling was not impaired, clearly 2 binds to the same site as natural ligand 1. Thus, BioBP-HMBPP (2) is a suitable tool to identify co-ligands or receptors involved in PAg-mediated T cell activation. - Source :PubMed

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