Human Semaphorin 4A/SEMA4A/Semaphorin B (Fc Tag) recombinant protein

Human Semaphorin 4A/SEMA4A/Semaphorin B (Fc Tag) recombinant protein

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\Semaphorin-4A, also known as Semaphorin-B, SEMA4A, Sema B and SEMAB, is a single-pass type I  membrane protein which belongs to the semaphorin family. It inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons. Semaphorin-4A / SEMA4A contains one Ig-like C2-type (immunoglobulin-like) domain, one PSI domain and one Sema domain. Defects in SEMA4A are the cause of retinitis pigmentosa type 35 (RP35) which leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Defects in SEMA4A are also the cause of cone-rod dystrophy type 10 (CORD10) which are inherited retinal dystrophies belonging to the group of pigmentary retinopathies. CORDs are characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration.\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-4A

SEMAPHORIN 4A; AI132332; SEMB; FLJ12287; SEMAPHORIN-B; CORD10; SEMAB; SEMA B; SEMA4A; RP11-54H19.2; RP35

Q9H3S1

SEMA4A; SEMAB; SEMB; UNQ783/PRO1317

Human Cells

A DNA sequence encoding the human SEMA4A (NP_071762.2) extracellular domain (Met 1-His 683) was fused with the Fc region of human IgG1 at the C-terminus.

Human

The secreted recombinant human SEMA4A/Fc chimera is a disulfide-linked homodimer. The reduced monomer consists of 893 amino acids and predictes a molecular mass of 99 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh SEMA4A/Fc monomer is approximately 110 kDa due to glycosylation.

> 90 % as determined by SDS-PAGE

Measured by its ability to bind mouse SEMA4D in a functional ELISA.