F1020
Anti-Factor IX antibody, Mouse monoclonal
clone HIX-5, purified from hybridoma cell culture
Synonym(s):
Anti-Factor IX antibody, Mouse monoclonal
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About This Item
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biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified from hybridoma cell culture
antibody product type
primary antibodies
clone
HIX-5, monoclonal
form
buffered aqueous solution
species reactivity
human
technique(s)
indirect ELISA: suitable
western blot: 1:500
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... F9(2158)
General description
Four and a half LIM domains protein 1 is a protein encoded by the FHL1 gene in human and located on human chromosome Xq27.2. Factor IX (or Christmas factor) is one of the serine proteases of the coagulation system. It belongs to peptidase family S1. The proteins belong to a novel family of LIM proteins that are expressed in human skeletal muscle.
Monoclonal Anti-Human Factor IX (mouse IgG1 isotype) is derived from the HIX-5 hybridoma produced by the fusion of mouse Sp2/0-Ag14 myeloma cells and splenocytes from BALB/c mice immunized with factor IX purified from human plasma. Factor IX is a 55 kDa, single chain, vitamin K-dependent plasma zymogen which plays a key role in the intrinsic and extrinsic blood coagulation systems. A disulfide bond in factor IX connects the N-terminal sequence (light chain) of factor IX to the C-terminal sequence (heavy chain).
Immunogen
Factor IX from pooled normal human plasma.
Application
Monoclonal Anti-Factor IX antibody produced in mouse is suitable for indirect ELISA and western blotting at a dilution of 1:500.
Monoclonal Anti-Factor IX has been used in circulating protein assay. It may also be used in the preparation of factor IX depleted plasma and for purification of factor IX.
Biochem/physiol Actions
Four and a half LIM domains protein 1 (FHL1) downregulation in oral squamous cell carcinoma (OSCC) occurs through DNA methylation of the promoter region rather than histone deacetylation or mutation. Upon activation of factor IX to factor IXa by factor XIa in the intrinsic system, an 11 kDa activation peptide is removed from the factor IX molecule by cleavage of two peptide bonds. These changes allow the exposure of the serine protease site on the heavy chain which can then activate factor X in the presence of factor VIII, Ca2+, and phospholipid. When patients lack Vitamin K, or take oral anticoagulants that interfere with the metabolism of vitamin K, a hypo coagulable or antithrombotic state is induced. This state stems from the diminished ability of factor IX to bind to phospholipids. Factor IX is synthesized in liver parenchymal cells and requires a post-translational, vitamin K-dependent, modification to become a mature plasma zymogen. Hereditary deficiencies or dysfunctions of factor IX cause hemophilia B or Christmas disease.
Physical form
Solution in 10 mM HEPES, pH 7.4, with 140 mM sodium chloride and 0.05% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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High-level protein secretion into blood circulation after electric pulse-mediated gene transfer into skeletal muscle
Molecular Therapy, 2(3), 204-210 (2000)
The New England journal of medicine, 371(21), 1994-2004 (2014-11-20)
In patients with severe hemophilia B, gene therapy that is mediated by a novel self-complementary adeno-associated virus serotype 8 (AAV8) vector has been shown to raise factor IX levels for periods of up to 16 months. We wanted to determine
Biochemical and biophysical research communications, 225(2), 632-638 (1996-08-14)
We have assembled the complete protein sequence of the skeletal muscle LIM-protein SLIM by aligning overlapping cDNA sequences. These cDNA sequences were identified from our own sequencing and from BLASTn searches of non-redundant cDNA databases. The predicted SLIM protein sequence
International journal of oncology, 42(1), 141-150 (2012-11-06)
The four and a half LIM domains 1 (FHL1) gene has been related to carcinogenesis. However, the expression status of FHL1 in human oral squamous cell carcinoma (OSCC) remains unclear and the detailed mechanism of gene silencing is poorly understood.
Gene, 216(1), 163-170 (1998-08-26)
We have isolated and sequenced a human heart cDNA clone encoding a novel LIM-only protein. This full-length cDNA clone has a predicted open reading frame (ORF) encoding 280 amino acids. The ORF of this cDNA codes for a LIM-only protein
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