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Your Position: Home > Recombinant Protein > Human Cell Expressed > Mouse SEMA5A / Semaphorin-5A / SEMAF Protein (His Tag)

Mouse SEMA5A / Semaphorin-5A / SEMAF Protein (His Tag) PDF Download

Catalog Size (Price) Quantity In Stock Operation Other Information
50972-M08H
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sema domain, seven thrombospondin repeats (type 1 and type 1-like), transmembrane domain (TM) and short cytoplasmic domain, (semaphorin) 5A Protein Datasheet

 

SEMA5A / Semaphorin-5A / SEMAF Protein Price Inquiry ( Available Sizes )

SEMA5A / Semaphorin-5A / SEMAF Protein Product Information

Synonym : SEMA5A
Protein Construction:

A DNA sequence encoding the mouse SEMA5A (Q3UPZ0) (Met1-Thr765) was expressed with a C-terminal polyhistidine tag.

Source: Mouse
Expression Host: Human Cells

SEMA5A / Semaphorin-5A / SEMAF Protein QC Testing

Purity: > 85% as determined by SDS-PAGE SDS-PAGE:
SDS-PAGE

SEMA5A / Semaphorin-5A / SEMAF 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: Pro 22
Molecular Mass:

The recombinant mouse SEMA5A comprises 755 amino acids and has a predicted molecular mass of 85.1 kDa. The apparent molecular mass of the protein is approximately 96 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.

SEMA5A / Semaphorin-5A / SEMAF 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.

SEMA5A / Semaphorin-5A / SEMAF Protein Related Products & Topics

Related Areas:

Neuroscience>>Axon Guidance>>Semaphorin & Related Molecules>>Semaphorin 5A/SEMA5A

Proteins:

Molecule Species Description //For Detailed Info. and Price------CLICK! Cat. No
Semaphorin 5A/SEMA5A Human Semaphorin 5A/SEMA5A Protein, Recombinant 11300-H02H
Semaphorin 5A/SEMA5A Human Semaphorin 5A/SEMA5A Protein, Recombinant 11300-H08H
Semaphorin 5A/SEMA5A Mouse SEMA5A / Semaphorin-5A / SEMAF Protein, Recombinant 50972-M08H

Antibodies:

SEMA5A / Semaphorin-5A / SEMAF Protein Description

Semaphorins are secreted, transmembrane, and GPI-linked proteins, defined by cysteine-rich semaphorin protein domains, that have important roles in a variety of tissues. Humans have 20 semaphorins, Drosophila has five, and two are known from DNA viruses. Semaphorins are found in nematodes and crustaceans but not in non-animals. They are grouped into eight classes on the basis of phylogenetic tree analyses and the presence of additional protein motifs. Semaphorins have been implicated in diverse developmental processes such as axon guidance during nervous system development and regulation of cell migration. Semaphorin-5A, also known as Semaphorin-F, Sema F, SEMA5A and SEMAF, is a single-pass type I membrane protein which belongs to the semaphorin family. Semaphorin5A / SEMA5A contains one PSI domain, one Sema domain and seven TSP type-1 domains. It may act as positive axonal guidance cues. Semaphorin5A / SEMA5A is an axon regulator molecule and plays major roles during neuronal and vascular development. It plays an essential role in embryonic development. Semaphorin5A / SEMA5A induces endothelial cell migration from pre-existing vessels. It also plays a role in autism, reducing the ability of neurons to form connections with other neurons in certain brain regions.

References

  1. Strausberg RL. et al., 2003, Proc Natl Acad Sci.  99 (26): 16899-903.
  2. Neufeld G. et al., 2005, Front Biosci. 10: 751-60.
  3. Fiore R. et al., 2005, Mol Cell Biol. 25 (6): 2310-9.
  4. Yazdani U. et al., 2006, Genome Biol. 7 (3): 211.
  5. Sadanandam A. et al., 2010, Microvasc Res. 79 (1): 1-9.