MOUSE ANTI RAT IgD Biotin

Price:
472 EUR
566 USD
391 GBP
known as: MOUSE ANTI RAT IgD Biotin
Catalog number: genta-ABS0574
Product Quantity: 0.5 mg
Category:
Supplier: AbD

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Gene target:

Related genes to: MOUSE ANTI RAT IgD Biotin

Symbol : biotin NIH gene
LocusTag : Bathy11g00270
chromosome : 11
description : biotin synthase
type of gene : protein-coding
Modification date : 2015-06-26
Symbol : Igd NIH gene
chromosome : 6
description : immunoglobulin delta heavy chain constant region
type of gene : other
Other designations : Ig delta chain C region
Modification date : 2016-04-02

Related Pathways to: MOUSE ANTI RAT IgD Biotin

Gene about :biotin
Pathway :Sc Protein Modifications
biotin

Related product to: MOUSE ANTI RAT IgD Biotin

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Related Articles about: MOUSE ANTI RAT IgD Biotin

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

The Infatuation With Biotin Supplementation: Is There Truth Behind Its Rising Popularity? A Comparative Analysis of Clinical Efficacy versus Social Popularity.

Biotin, also known as Vitamin B7 or vitamin H, is a water-soluble B vitamin that acts as an essential cofactor for several carboxylases involved in the cellular metabolism of fatty acids, amino acids, and gluconeogenesis. Although there exists an incredible amount of social media hype and market advertising touting its efficacy for the improvement of hair quantity and quality, biotin's efficacy for hair remains largely unsubstantiated in scientific literature. We reviewed all pertinent scientific literature regarding the efficacy of biotin supplementation for hair growth and quality improvement, and we also investigated its popularity in society defined as a function of market analytics. To date, there have been no clinical trials conducted to investigate the efficacy of biotin supplementation for the treatment of alopecia of any kind, nor has there been any randomized controlled trial to study its effect on hair quality and quantity in human subjects. Because of the lack of clinical evidence, its use to improve hair quantity or quality is not routinely recommended. However, societal infatuation with biotin supplementation is not only propagated by its glamorization in popular media, its popularity is vastly disproportionate to the insufficient clinical evidence supporting it's efficacy in hair improvement. In other words, biotin supplements are quite "in vogue", without there being any real reason to be so.

J Drugs Dermatol. 2017;16(5):496-500.

. - Source :PubMed

Metabolic Reprogramming Commits Differentiation of Human CD27(+)IgD(+) B Cells to Plasmablasts or CD27(-)IgD(-) Cells.

B cells play a crucial role in the pathogenesis of autoimmune diseases, such as systemic lupus erythematosus (SLE). However, the relevance of the metabolic pathway in the differentiation of human B cell subsets remains unknown. In this article, we show that the combination of CpG/TLR9 and IFN-α markedly induced the differentiation of CD27(+)IgD(+) unswitched memory B cells into CD27(hi)CD38(hi) plasmablasts. The response was accompanied by mammalian target of rapamycin complex 1 (mTORC1) activation and increased lactate production, indicating a shift to glycolysis. However, CpG alone induced the differentiation of unswitched memory B cells into CD27(-)IgD(-) memory B cells with high cytokine production, but such differentiation was suppressed by IFN-α. AMP-activated protein kinase activation enhanced the differentiation to CD27(-)IgD(-) B cells, but it attenuated mTORC1 activation and differentiation into plasmablasts. High mTORC1 activation was noted in CD19(+) B cells of patients with SLE and correlated with plasmablast differentiation and disease activity. Taken together, differential metabolic reprogramming commits the differentiation of human unswitched memory B cells into plasmablasts (the combination of CpG and IFN-α amplifies mTORC1-glycolysis pathways) or CD27(-)IgD(-) memory B cells (CpG alone amplifies the AMP-activated protein kinase pathway). The former metabolic pathway may play a pivotal role in SLE. - Source :PubMed

A single 10mg oral dose of biotin interferes with thyroid function tests.

This letter reports a study with a single 10 mg oral dose of biotin in 19 health subjects. The acute use of biotin interferes with measurement of TSH, free T4 and T3, in a fashion similar to a hyperthyroid subject, and the changes are reversible 24 hours after the biotin ingestion. - Source :PubMed

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