AP1173
Anti-EPHA4 Mouse mAb (6H7)
liquid, clone 6H7, Calbiochem®
别名:
Anti-Ephrin Receptor A4
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关于此项目
NACRES:
NA.41
UNSPSC Code:
12352203
Clone:
6H7, monoclonal
Species reactivity:
human, mouse
Application:
—
Citations:
2
biological source
mouse
antibody form
purified antibody
antibody product type
primary antibodies
clone
6H7, monoclonal
form
liquid
does not contain
preservative
species reactivity
human, mouse
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze, avoid repeated freeze/thaw cycles
dilution
(ELISA
Immunoblotting (1-5 µg/mL))
isotype
IgG1
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... EPHA4(2043)
General description
Anti-EPHA4, mouse monoclonal, clone 6H7, recognizes the EPHA4 protein in NIH3T3 cells. It is validated for use in ELISA and Western blotting.
Purified mouse monoclonal antibody. Recognizes the ~100 kDa EPHA4 protein.
Recognizes the EPHA4 protein in NIH3T3 cells.
Immunogen
A recombinant polypeptide corresponding to amino acids of 887-987 human EPHA4, expressed as a GST fusion protein
Application
ELISA Immunoblotting (1-5 µg/mL)
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Regulatory Review (Z)
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存储类别
12 - Non Combustible Liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Brian Hitt et al.
The Journal of biological chemistry, 287(46), 38408-38425 (2012-09-19)
BACE1 is the β-secretase enzyme that initiates production of the β-amyloid peptide involved in Alzheimer disease. However, little is known about the functions of BACE1. BACE1-deficient mice exhibit mild but complex neurological phenotypes suggesting therapeutic BACE1 inhibition may not be
Heng-Huan Lee et al.
Nature communications, 12(1), 2788-2788 (2021-05-15)
Human ribonuclease 1 (hRNase 1) is critical to extracellular RNA clearance and innate immunity to achieve homeostasis and host defense; however, whether it plays a role in cancer remains elusive. Here, we demonstrate that hRNase 1, independently of its ribonucleolytic
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