Recombinant Human Ephrin B1 protein (denatured) (ab111630)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant Human Ephrin B1 protein (denatured)
See all Ephrin B1 proteins and peptides -
Purity
> 90 % SDS-PAGE. -
Expression system
Escherichia coli -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
MGSSHHHHHHSSGLVPRGSHMLAKNLEPVSWSSLNPKFLSGKGLVIYPKI GDKLDIICPRAEAGRPYEYYKLYLVRPEQAAACSTVLDPNVLVTCNRPEQ EIRFTIKFQEFSPNYMGLEFKKHHDYYITSTSNGSLEGLENREGGVCRTR TMKIIMKVGQDPNAVTPEQLTTSRPSKEADNTVKMATQAPGSRGSLGDSD GKHETVNQEEKSGPGASGGSSGDPDGFFNSK -
Predicted molecular weight
25 kDa including tags -
Amino acids
28 to 237 -
Tags
His tag N-Terminus
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab111630 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
pH: 8.00
Constituents: 2.4% Urea, 0.32% Tris HCl, 5% Glycerol (glycerin, glycerine)
General Info
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Alternative names
- CFND
- CFNS
- Craniofrontonasal syndrome (craniofrontonasal dysplasia)
see all -
Function
Binds to the receptor tyrosine kinases EPHB1 and EPHA1. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons. -
Tissue specificity
Heart, placenta, lung, liver, skeletal muscle, kidney, pancreas. -
Involvement in disease
Defects in EFNB1 are a cause of craniofrontonasal syndrome (CFNS) [MIM:304110]; also known as craniofrontonasal dysplasia (CFND). CFNS is an X-linked inherited syndrome characterized by hypertelorism, coronal synostosis with brachycephaly, downslanting palpebral fissures, clefting of the nasal tip, joint anomalies, longitudinally grooved fingernails and other digital anomalies. -
Sequence similarities
Belongs to the ephrin family. -
Post-translational
modificationsInducible phosphorylation of tyrosine residues in the cytoplasmic domain. -
Cellular localization
Membrane. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab111630 has not yet been referenced specifically in any publications.