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SDS-PAGE

EphB1 / EPHT2 recombinant protein

Recombinant Human EphB1 / EPHT2 Protein (aa 565-984, His & GST tag)

Gene Names
EPHB1; ELK; NET; Hek6; EPHT2
Purity
> 95 % as determined by SDS-PAGE
Synonyms
EphB1 / EPHT2; Recombinant Human EphB1 / EPHT2 Protein (aa 565-984; His & GST tag); EPHB1; ELK; EPHT2; HEK6; NET; EphB1 / EPHT2 recombinant protein
Ordering
For Research Use Only!
Host
Baculovirus-Insect Cells
Purity/Purification
> 95 % as determined by SDS-PAGE
Form/Format
Supplied as sterile 20mM Tris, 500mM NaCl, 3mM DTT, pH 8.0, 10% gly
Sequence Length
984
Application Notes
The recombinant human EPHB1 /GST chimera consists of 657 amino acids and has a calculated molecular mass of 75.3 kDa. The recombinant protein migrates as an approximately 66 kDa band in SDS-PAGE under reducing conditions.
Predicted N Terminal
Met
Endotoxin
< 1.0 EU per mug of the protein as determined by the LAL method
Preparation and Storage
Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

SDS-PAGE
Related Product Information for EphB1 / EPHT2 recombinant protein
Background: Ephrin type -B receptor 1, also known as EphB1, belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family which 16 known receptors (14 found in mammals) are involved: EPHA1, EPHA2, EPHA3, EPHA4, EPHA5, EPHA6, EPHA7, EPHA8, EPHA9, EPHA10, EPHB1, EPHB2, EPHB3, EPHB4, EPHB5, EPHB6. EphB2 receptor tyrosine kinase phosphorylates syndecan-2 and that this phosphorylation event is crucial for syndecan-2 clustering and spine formation. The Eph family of receptor tyrosine kinases (comprising EphA and EphB receptors) has been implicated in synapse formation and the regulation of synaptic function and plasticity6. Ephrin receptors are components of cell signalling pathways involved in animal growth and development, forming the largest sub-family of receptor tyrosine kinases (RTKs). Ligand-mediated activation of Ephs induce various important downstream effects and Eph receptors have been studied for their potential roles in the development of cancer. EphB receptor tyrosine kinases are enriched at synapses, suggesting that these receptors play a role in synapse formation or function. We find that EphrinB binding to EphB induces a direct interaction of EphB with NMDA-type glutamate receptors. This interaction occurs at the cell surface and is mediated by the extracellular regions of the two receptors, but does not require the kinase activity of EphB.

Description: A DNA sequence encoding the human EPHB1 (AAI11745.1) (Arg565-Ala984) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
Molecular Weight
26,906 Da
NCBI Official Full Name
EPH receptor B1
NCBI Official Synonym Full Names
EPH receptor B1
NCBI Official Symbol
EPHB1
NCBI Official Synonym Symbols
ELK; NET; Hek6; EPHT2
NCBI Protein Information
ephrin type-B receptor 1
UniProt Protein Name
Ephrin type-B receptor 1
UniProt Gene Name
EPHB1
UniProt Synonym Gene Names
ELK; EPHT2; HEK6; NET; EK6; hEK6; NET

NCBI Description

Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members. [provided by RefSeq, Jul 2008]

Uniprot Description

EphB1: a receptor tyrosine kinase of the Eph family. Receptor for members of the ephrin-B family: ephrin-B1, -B2 and -B3. The Eph receptor tyrosine kinase family, the largest in the tyrosine kinase group, has fourteen members. They bind membrane-anchored ligands, ephrins, at sites of cell-cell contact, regulating the repulsion and adhesion of cells that underlie the establishment, maintenance, and remodeling of patterns of cellular organization. Eph signals are particularly important in regulating cell adhesion and cell migration during development, axon guidance, homeostasis and disease. EphA receptors bind to GPI-anchored ephrin-A ligands, while EphB receptors bind to ephrin-B proteins that have a transmembrane and cytoplasmic domain. Interactions between EphB receptor kinases and ephrin-B proteins transduce signals bidirectionally, signaling to both interacting cell types. Eph receptors and ephrins also regulate the adhesion of endothelial cells and are required for the remodeling of blood vessels. The ligand-activated form of EphB1 interacts with GRB2, GRB10 and NCK through their respective SH2 domains. Four alternatively spliced isoforms are known.

Protein type: EC 2.7.10.1; Eph family; Kinase, protein; Membrane protein, integral; Protein kinase, TK; Protein kinase, tyrosine (receptor); TK group

Chromosomal Location of Human Ortholog: 3q22.2

Cellular Component: cytosol; early endosome membrane; extracellular region; integral to plasma membrane; plasma membrane

Molecular Function: protein binding; transmembrane-ephrin receptor activity

Biological Process: angiogenesis; axon guidance; cell-substrate adhesion; central nervous system projection neuron axonogenesis; detection of temperature stimulus involved in sensory perception of pain; ephrin receptor signaling pathway; establishment of cell polarity; neurogenesis; positive regulation of synaptogenesis; protein amino acid autophosphorylation; regulation of JNK cascade; retinal ganglion cell axon guidance

Research Articles on EphB1 / EPHT2

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Product Notes

The EphB1 / EPHT2 ephb1 (Catalog #AAA2545045) is a Recombinant Protein produced from Baculovirus-Insect Cells and is intended for research purposes only. The product is available for immediate purchase. The recombinant human EPHB1 /GST chimera consists of 657 amino acids and has a calculated molecular mass of 75.3 kDa. The recombinant protein migrates as an approximately 66 kDa band in SDS-PAGE under reducing conditions. Researchers should empirically determine the suitability of the EphB1 / EPHT2 ephb1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "EphB1 / EPHT2, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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