MOUSE ANTI RAT IgA HEAVY CHAIN Biotin

Price:
472 EUR
566 USD
391 GBP
known as: MOUSE ANTI RAT IgA HEAVY CHAIN Biotin
Catalog number: genta-ABS0571
Product Quantity: 0.5 mg
Category:
Supplier: AbD

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Gene target: heavy chain

Related genes to: MOUSE ANTI RAT IgA HEAVY CHAIN Biotin

Symbol : biotin NIH gene
LocusTag : Bathy11g00270
chromosome : 11
description : biotin synthase
type of gene : protein-coding
Modification date : 2015-06-26
Symbol : IGA NIH gene
dbXrefs : AnimalQTLdb:12890
chromosome : 3
description : Immunoglobulin A activity
type of gene : unknown
Modification date : 2015-01-22

Related Pathways to: MOUSE ANTI RAT IgA HEAVY CHAIN Biotin

Gene about :biotin
Pathway :Sc Protein Modifications
biotin

Related product to: MOUSE ANTI RAT IgA HEAVY CHAIN Biotin

Related Articles about: MOUSE ANTI RAT IgA HEAVY CHAIN Biotin

Association of TNFSF13 polymorphisms with IgA nephropathy in Chinese Han population.

Our previous genome-wide association study (GWAS) of IgA nephropathy (IgAN) in Chinese Han population suggested that TNFSF13 gene may be a novel susceptibility gene for IgAN. In this study, we aim to further evaluate the associations of single-nucleotide polymorphisms (SNPs) and expression level of TNFSF13 gene with the risk and clinical parameters of IgAN. - Source :PubMed

The Association of rs1047763 and rs1008898 of C1GALT1 with IgA Nephropathy Risk: A Global Meta-Analysis.

IgA nephropathy (IgAN) is a globally common primary glomerulonephritis characterized by an elevated level of serum IgA and immune complex deposition in the mesangial area. In the serum of patients with IgAN, the hinge region of IgA1 immunoglobulin contains aberrantly glycosylated O-glycans deficient in galactose, which is normally added to the core 1 O-glycan structure by core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 (C1GALT1), the key enzyme in the process of glycosylation. It is unknown if single-nucleotide polymorphisms rs1047763 and rs1008898 of C1GALT1 increase the risk of IgAN. We enrolled 5 subjects in this meta-analysis, including a total of 1693 IgAN patients and 1864 control subjects. We performed meta-analysis on associations between rs1047763, rs1008898, and IgAN using the allele model, dominant model, recessive model, and additive model. We found that there was no relationship between rs1047763 and rs1008898 in C1GALT1 and susceptibility to IgAN. - 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

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

Inducing Mucosal IgA: A Challenge for Vaccine Adjuvants and Delivery Systems.

Mucosal IgA or secretory IgA (SIgA) are structurally equipped to resist chemical degradation in the harsh environment of mucosal surfaces and enzymes of host or microbial origin. Production of SIgA is finely regulated, and distinct T-independent and T-dependent mechanisms orchestrate Ig α class switching and SIgA responses against commensal and pathogenic microbes. Most infectious pathogens enter the host via mucosal surfaces. To provide a first line of protection at these entry ports, vaccines are being developed to induce pathogen-specific SIgA in addition to systemic immunity achieved by injected vaccines. Mucosal or epicutaneous delivery of vaccines helps target the inductive sites for SIgA responses. The efficacy of such vaccines relies on the identification and/or engineering of vaccine adjuvants capable of supporting the development of SIgA alongside systemic immunity and delivery systems that improve vaccine delivery to the targeted anatomic sites and immune cells. - Source :PubMed

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