Human Factor VII Matched Antibody Pair

Name: Human Factor VII Matched Antibody Pair
SKU: ABPR-L006
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Sample

Plasma

Species Reactivity

Human

Detection Method

Sandwich ELISA

Intended Use

This antibody pair set comes with matched antibody pair to detect and quantify protein level of Human Factor VI

Contents of Kit

1. Capture Antibody (yellow): 0.5 ml of purified monoclonal anti-FVII antibody for coating plates.
2. Detecting Antibody (red): 0.5 ml of peroxidase-conjugated polyclonal anti-FVII antibody for detection of captured FVII.
Note: Reagents are sufficient for at least 5×96 well plates using recommended protocols. Antibodies are supplied in a 50% (v/v) glycerol solution for storage at –10 to -20°C. Keep vials tightly capped. Do not store in frost-free freezers.

Storage

-10 to -20°C

General Description

Factor VII (F.VII, also known as Stable Factor and Proconvertin) is a vitamin K-dependent glycoprotein produced in the liver. Plasma concentration of F.VII is normally ~0.5 μg/ml (10 nM) in plasma. A deficiency of F.VII is associated with bleeding in a clinical pattern similar to haemophilia, but is inherited as an autosomal recessive trait. The deficiency can be characterized by a quantitative (low activity and low antigen) or a qualitative (low activity and normal antigen) defect in F.VII function. In its zymogen form F.VII is a single chain molecule of ~50 kDa. It contains two EGF-like domains and an amino-terminal domain containing 10 γ-carboxyglutamic acid (Gla) residues. These Gla residues allow F.VII to bind divalent metal ions and participate in calcium-dependent binding interactions. F.VII and activated F.VII (F.VIIa) bind to tissue factor exposed at the site of vascular injury. F.IXa, F.Xa or F.VIIa rapidly activate tissue factor-bound F.VII to F.VIIa in the presence of calcium and phospholipid. Thrombin and F.XIIa are able to activate F.VII in the fluid phase in the absence of cofactors. The activation of the single chain zymogen F.VII occurs by proteolysis after residue Arg152, resulting in a two-chain active serine protease consisting of a 30 kDa heavy chain and an 18 kDa light chain. In complex with tissue factor, phospholipid and calcium, F.VIIa is able to activate F.X and F.IX. Free F.VIIa in plasma is remarkably stable, but the activity of F.VIIa/TF complex is regulated by Tissue Factor Pathway Inhibitor (TFPI) in the presence of F.Xa, and also by Antithrombin (ATIII) in the presence of heparin.

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Documents

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QA & Reviews

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References

Super Canola: Newly Developed High Yielding, Lodging and Drought Tolerant Double Zero Cultivar of Rapeseed (Brassica napus L.)

GENETICS AND MOLECULAR RESEARCH

Authors: Mahmood, Tariq; Bin Mustafa, Hafiz Saad; Aftab, Muhammad; Ali, Qurban; Malik, Arif

Abstract

The aim of present research was to develop a high yielding rapeseed cultivar having good quantitative and qualitative characteristics under the scenario of climate change. The research was initiated during 2005 and successfully completed during 2018 by Oilseeds Research Institute, Faisalabad Pakistan. Super Canola (RBN-13018) is an outcome of hybridization (Rainbow x RBN-03052) in 2005-06 and subsequently following by the pedigree method of selection. Homozygous progenies from F7 were bulked in 2013-14 for yield evaluation in replicated trials. Its performance was evaluated in the station and outstation yield trials at different agro-climatic conditions. RBN-13018 performed well in all yield trials by giving 44% better yield in Station Yield Trials, 9% better yield in Micro Yield Trials and 23% to 29% better yield in National Uniform Rapeseed Yield Trials conducted during 2015 to 2017 than the check Canola varieties. It also gave 6% higher yield than the widespread rapeseed hybrid Hyola 401 in National Uniform Rapeseed Yield Trials. RBN-13018 showed good tolerance against Alternaria blight and White rust and also exhibited better lodging tolerance. It also performed well in Polyethylene Glycol (PEG 6000) induced drought and showed good genetic potential against drought stress. Oil quality analysis through Near Infrared (NIR) Spectroscopy showed that it has a best ratio of saturated and unsaturated fatty acids for human consumption and its meal is also fit for animals. Agronomic studies revealed that this variety thrives well with the prevailing rate of inputs and agronomic practices. Considering the qualitative and quantitative performance of RBN-13018 Punjab Seed Council (Pakistan) approved this strain as commercial variety for general cultivation with the name of Super Canola.

Torsemide Fast Dissolving Tablets: Development, Optimization Using Box-Bhenken Design and Response Surface Methodology, In Vitro Characterization, and Pharmacokinetic Assessment

AAPS PHARMSCITECH

Authors: El-Shenawy, Ahmed A.; Ahmed, Mahmoud M.; Mansour, Heba F.; Abd El Rasoul, Saleh

Abstract

The present study planed to develop new fast dissolving tablets (FDTs) of torsemide. Solid dispersions (SDs) of torsemide and sorbitol (3:1) or polyvinylpyrrolidone (PVP) k25 were prepared. The prepared SDs were evaluated for in-vitro dissolution. Fourier transform infrared spectroscopy and differential scanning calorimetry for SDs revealed no drug/excipient interactions and transformation of torsemide to the amorphous form. Torsemide/sorbitol SD was selected for formulation of torsemide FDTs by direct compression method. Box-Bhenken factorial design was employed to design 15 formulations using croscarmellose sodium and crospovidone at different concentrations. The response surface methodology was used to analyze the effect of changing these concentrations (independent variables) on disintegration time (Y-1), percentage friability (Y-2), and amount torsemide released at 10 min. The physical mixtures of torsemide and the used excipients were evaluated for angle of repose, Hausner's ratio, and Carr's index. The prepared FDTs tablets were evaluated for wetting and disintegration time, weight variation, drug content, percentage friability, thickness, hardness, and in vitro release. Based on the in-vitro results and factorial design characterization, F10 and F7 were selected for bioavailability studies following administration to Albino New Zealand rabbits. They showed significantly higher C-max and (AUC(0-12)) and shorter T-max than those obtained after administration of the corresponding ordinary commercial Torseretic (R) tablets. Stability study was conducted for F10 that showed good stability upon storage at 30 degrees C/75% RH and 40 degrees C/75% RH for 3 months.