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Rat EFNB1 / Ephrin-B1 Protein PDF Download

Catalog Size (Price) Quantity In Stock Operation Other Information
80106-R02H
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Ephrin B1 Protein Datasheet

 

EFNB1 / Ephrin-B1 Protein Price Inquiry ( Available Sizes )

EFNB1 / Ephrin-B1 Protein Product Information

Synonym : EFNB1, Eplg2, Lerk2
Protein Construction:

A DNA sequence encoding the rat EFNB1 (P52796) (Met1-Thr229) was expressed, fused with the Fc region of human IgG1 at the C-terminus.

Source: Rat
Expression Host: Human Cells

EFNB1 / Ephrin-B1 Protein QC Testing

Purity: > 98 % as determined by SDS-PAGE SDS-PAGE:
SDS-PAGE

EFNB1 / Ephrin-B1 protein

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
Stability: Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal: Ala 25
Molecular Mass:

The recombinant rat EFNB1 comprises 446 amino acids and predicts a molecular mass of 49.4 kDa. The apparent molecular mass of the rat EFNB1 is approximately 58 kDa in SDS-PAGE under reducing conditions due to glycosylation.

Formulation: Lyophilized from sterile PBS, pH7.4.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.

EFNB1 / Ephrin-B1 Protein Usage Guide

Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

EFNB1 / Ephrin-B1 Protein Related Products & Topics

Related Areas:

Neuroscience>>Axon Guidance>>Ephrin & Eph Receptor>>Ephrin-B1/EFNB1

Cancer>>Growth Factor & Receptor>>Ephrin & Eph Receptor>>Ephrin-B1/EFNB1

Proteins:

Molecule Species Description //For Detailed Info. and Price------CLICK! Cat. No
Ephrin-B1/EFNB1 Human Ephrin-B1/EFNB1 Protein, Recombinant 10894-H03H
Ephrin-B1/EFNB1 Human Ephrin-B1/EFNB1 Protein, Recombinant 10894-H08H
Ephrin-B1/EFNB1 Mouse Ephrin-B1/EFNB1/Fc Protein, Recombinant 50580-M02H
Ephrin-B1/EFNB1 Mouse Ephrin-B1/EFNB1 Protein, Recombinant 50580-M08H
Ephrin-B1/EFNB1 Rat EFNB1 / Ephrin-B1 Protein, Recombinant 80106-R02H
Ephrin-B1/EFNB1 Rat Rat EFNB1 / Ephrin-B1 Protein, Recombinant 80106-R08H

Antibodies:

Molecule Application Description //For Detailed Info. and Price------CLICK! Cat. No
Human
Ephrin-B1/EFNB1
WB, ELISA Ephrin-B1/EFNB1 Antibody, Rabbit PAb 10894-RP01
Human
Ephrin-B1/EFNB1
WB, ELISA Ephrin-B1/EFNB1 Antibody, Rabbit PAb (Antigen Affinity Purified) 10894-RP02
Mouse
Ephrin-B1/EFNB1
WB, ELISA Ephrin-B1 / EFNB1 Antibody (Antigen Affinity Purified) 50580-RP02

EFNB1 / Ephrin-B1 Protein Description

The ephrins (Eph) and Eph receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in developmental events, especially in the nervous system and in erythropoiesis. 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. All ephrins share a conserved extracellular sequence, which most likely corresponds to the receptor-binding domain. In molecular biology, ephrins and Eph receptors are components of cell signaling pathways involved in animal development, and implicated in some cancers. ephrin-B1, also known as LERK-2, ELK-L, EFL-3, Cek5-L, and STRA-1, is a member of the ephrin ligand family which binds members of the Eph receptor family. Ephrin-B1 has been shown to bind EphA3, EphB1, EphB2, EphB3, and EphB4. The extracellular domains of human and mouse ephrin-B1 share 94% amino acid identity.

References

  1. Cerretti DP. et al., 1995, Mol Immunol. 32 (16): 1197-205.
  2. Gale NW. et al.,1996, Neuron.17 (1): 9-19.
  3. Flanagan J. et al., 1998, Annual Review of Neuroscience. 21: 309-45.
  4. Holder N. et al., 1999, Development. 126 (10): 2033-44.
  5. Wilkinson DG. et al., 2001, Nat. Rev. Neurosci. 2 (3): 155-64.
  6. Murai KK. et al., 2003, Journal of Cell Science. 116 (14): 2823-32.