SAB4500696
Anti-EFNA1 antibody produced in rabbit
affinity isolated antibody
Synonym(s):
B61, ECKLG, EFL1, EPH-related receptor tyrosine kinase ligand 1, ephrin-A1
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About This Item
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA, IF, WB
Citations:
6
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 23 kDa
species reactivity
human, mouse, rat
concentration
~1 mg/mL
technique(s)
ELISA: 1:10000, immunofluorescence: 1:100-1:500, western blot: 1:500-1:1000
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... EFNA1(1942)
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General description
EphrinA1 (EFNA1), also known as angiogenesis factor, is encoded by the gene mapped to human chromosome 1q21-22. The encoded protein belongs to subclass A of ephrin family. EFNA1 is localized to cell membrane via a glycosylphosphatidylinositol (GPI) moiety. EFNA1 ligand preferentially binds to the receptor tyrosine kinase, Eph receptor 2 (EphA2).
Immunogen
The antiserum was produced against synthesized peptide derived from human EFNA1.
Immunogen Range: 66-115
Immunogen Range: 66-115
Application
Anti-EFNA1 antibody produced in rabbit has been used in western blot analysis.
Biochem/physiol Actions
EphrinA1 (EFNA1) and its primary receptor, Eph receptor 2 (EphA2) are associated with various cancers, such as urinary bladder carcinoma, breast cancer gastric cancer, glioma and malignant mesothelioma. Expression pattern of EFNA1 can be used as a potential prognostic marker in colorectal cancer (CRC) patients and other human malignancies. Experimental studies state that, EphrinA1 (EFNA1) can be involved in both tumor promotion and inhibition, based on whether ephrin-A1 is bound to the receptor in soluble or membrane bound form, respectively. Activation of EphA2, induces indirect growth signal by overcoming ‘contact inhibition′.
Features and Benefits
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Physical form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
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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Storage Class
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
低风险生物材料
常规特殊物品
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Lyka Potla et al.
Cancer letters, 175(2), 187-195 (2001-12-14)
Ephrin A1 (EFNA1) is a GPI-anchored ligand that preferentially binds to the receptor tyrosine kinase, EphA2. EphA2 is over-expressed in malignant melanocytes and in prostate carcinoma cells. Whether activation of EphA2 by EFNA1 is involved in aberrant growth or differentiation
The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3.
Cerretti DP, et al.
Genomics, 33(2), 277-282 (1996)
Amanda Beauchamp et al.
Seminars in cell & developmental biology, 23(1), 109-115 (2011-11-02)
Ephrin-A1 and its primary receptor, EphA2, are involved in numerous physiological processes and have been intensely studied for their roles in malignancy. Ephrin-Eph signalling is complex on its own and is also cell-type dependent, making elucidation of the exact role
Sho Kohara et al.
Biomedicines, 10(12) (2022-12-24)
Kupffer cells are maintained via self-renewal in specific microenvironmental niches, primarily the liver sinusoidal endothelial cells (LSECs). In this study, we propagated tissue-resident macrophages (Mø) from mouse liver using mixed culture with hepatic fibroblastic cells. Propagated liver Mø express Id3
T Tawadros et al.
British journal of cancer, 107(10), 1737-1744 (2012-10-06)
High intake of omega-6 polyunsaturated fatty acids (PUFA) has been associated with clinical progression in prostate cancer (CaP). This study investigates the signalling mechanism by which the omega-6 PUFA arachidonic acid (AA) induces prostatic cellular migration to bone marrow stroma.
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