Canine Factor VIII Matched Antibody Pair (ABPR-L008)

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

Write a review

Size
Sufficient reagent for 4 x 96 well plates
Sample
Plasma
Species Reactivity
Canine
Intended Use
This antibody pair set comes with matched antibody pair to detect and quantify protein level of Canine Factor VII
Contents of Kit
1. Capture Antibody (yellow): 0.4 ml of polyclonal purified anti-canine FVIII antibody for coating plates.
2. Detecting Antibody (neutral): Four neutral-capped tubes each containing 10 ml of pre-diluted peroxidase conjugated polyclonal anti-canine FVIII antibody for detection of captured cFVIII.
3. Sample Diluent (green): 100 ml bottle containing a green-coloured diluent optimised for dilution of samples.
Note: Reagents are sufficient for at least 4×96 well plates using recommended protocols.
Storage
2-8°C
General Description
Factor VIII is a large glycoprotein (320 kDa) synthesized in the liver. The majority of Factor VIII is cleaved during expression, resulting in a mixture of partially cleaved forms ranging in size from 200-280 kDa. The F.VIII is stabilized in circulation through non-covalent association with von Willebrand Factor. The concentration of F.VIII in normal human plasma is typically 200 ng/mL. In canine plasma, the F.VIII activity is 5-7 fold higher relative to human plasma. F.VIII is a pro-cofactor that is activated through limited proteolysis by thrombin. In this process F.VIIIa dissociates from vWF to combine with activated Factor IX, calcium and a phospholipid surface where it is an essential cofactor in the assembly of the Factor X activator complex. Hemophilia A is a congenital bleeding disorder resulting from an X-chromosome-linked deficiency of F.VIII, occurring with a frequency of 1 in 4000 males. The defect can be caused by any one of hundreds of reported mutations but are most commonly due to inversions within intron 22 of the F.VIII gene. Hemophilia A has also been reported in a variety of species including dog and mouse, with a clinical phenotype very similar to human. The genetic defect in one case of canine Hemophilia-A has been shown to also be due to a gene inversion similar to the human defect, possibly indicating a common instability of the F.VIII gene in humans and dogs.

Citations


Have you cited ABPR-L008 in a publication? Let us know and earn a reward for your research.

Customer Reviews


Write a review, share your experiences with others and get rewarded !
Product Name Cat. No. Applications Host Species Datasheet Price Add to Basket
Product Name Cat. No. Applications Host Species Datasheet Price Add to Basket

References


A Foundational Study for NormalF8-Containing Mouse Models for the miRNA Regulation of Hemophilia A: Identification and Analysis of Mouse miRNAs that Downregulate the MurineF8Gene

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

Authors: Jankowska, Katarzyna, I; Chattopadhyay, Maitreyi; Sauna, Zuben E.; Atreya, Chintamani D.

Hemophilia A (HA) is associated with defects in theF8gene, encoding coagulation factor VIII (FVIII). Our previous studies show that F8-targeting micro RNAs (miRNAs), a group of small RNAs involved in gene regulation, can downregulate F8 expression causing HA in individuals with normal F8-genotypes and increased HA severity in patients with mutations inF8. Understanding the mechanistic underpinnings of human genetic diseases caused or modulated by miRNAs require a small animal model, such as a mouse model. Here, we report a foundational study to develop such a model system. We identified the mouse 3 ' untranslated region (3 ' UTR) on murineF8-mRNA (muF8-mRNA) that can bind to murine miRNAs. We then selected three miRNAs for evaluation: miR-208a, miR-351 and miR-125a. We first demonstrate that these three miRNAs directly target the 3 ' UTR of muF8-mRNA and reduce the expression of a reporter gene (luciferase) mRNA fused to the muF8-3 ' UTR in mammalian cells. Furthermore, in mouse cells that endogenously express theF8gene and produce FVIII protein, the ectopic expression of these miRNAs downregulatedF8-mRNA and FVIII protein. These results provide proof-of-concept and reagents as a foundation for using a normalF8-containing mouse as a model for the miRNA regulation of normalF8in causing or aggravating the genetic disease HA.

Inorganic perovskite light emitting diodes with ZnO as the electron transport layer by direct atomic layer deposition

ORGANIC ELECTRONICS

Authors: Li, Wei; Xu, Yun-Xiao; Wang, Dong; Chen, Fei; Chen, Zhi-Kuan

Inorganic n-type metal oxide materials, i.e., ZnO have been developed and employed as interface layers for energy level matching and electron transport in order to achieve high performance perovskites based optoelectronic devices. In this work, we successfully apply atomic layer deposition (ALD) technique to deposit ZnO directly on top of CsPbBr3 to serve as the electron transport layer. A regular perovskite light emitting diode (PeLED) in a configuration of glass/ITO/PEDOT: PSS/CsPbBr3/ZnO/Ag was fabricated. In the CsPbBr3 emitting layer, polyethyleneimine ethoxylated (PEIE) dissolved in an anti-solvent chlorobenzene (CB) was introduced to assist the nucleation and crystal growth of perovskite films, as well as providing surface reactive sites for ALD deposition of ZnO layer particularly. The ALD deposition temperature on the growth, crystallinity and morphology of ZnO and subsequent device performance was investigated. We obtained PeLEDs of the best performance with the best current and external quantum efficiency (EQE) of 0.49 cd/A and 0.14%, respectively, which is as 14 folds high as an inorganic CsPbBr3 device using F8 as the electron transport layer reported previously.

Online Inquiry

Name:
Phone: *
E-mail Address: *
Technology Interest:
Type of Organization:
Service & Products Interested: *
Project Description:

Related Products

Related Resources

Ordering Information

Payment methods we support:
Invoice / Purchase Order
Credit card

Inquiry Basket