Human Semaphorin 5A/SEMA5A (Fc Tag) recombinant protein

Human Semaphorin 5A/SEMA5A (Fc Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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.

Semaphorin-5A

9130201M22RIK; SEMF; SEMAPHORIN F; SEMA5A; AI464145; FLJ12815; M-SEMA D; SEMAF; 5930434A13; SEMAPHORIN 5A; SEMA F

X5DR95

SEMA5A; SEMAF

Human Cells

A DNA sequence encoding the amino acids (Met 1-Thr 765) of human SEMA5A (NP_003957.2) extracellular domain was fused with Fc region of human IgG1 at the C-terminus.

Human

The recombinant human SEMA5A (aa 1-765)/Fc is a disulfide-linked homodimer. The reduced monomer consists of 984 amino acids and predictes a molecular mass of 110.7 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh SEMA5A/Fc monomer is approximately 125-135 kDa due to glycosylation.

> 90 % as determined by SDS-PAGE