Semaphorin 3A, Human, Recombinant

Semaphorins are a large group of structurally related secreted, GPI-anchored and transmembrane cell signaling molecules. There are 8 major classifications (1-7) of Semaphorins characterized by the existence of a conserved 500 amino acid SEMA domain at the amino terminus. Classes 3, 4, 6, and 7 are found in vertebrates only, whilst class 5 is found in both vertebrates and invertebrates. Each class is then divided into additional subgroups based on shared structural characteristics. Semaphorins primarily function as axon growth cone guidance factors during neuronal development. Semaphorin 3A acts as a chemo-repellent to axons, and an inhibitor of the growth of axons by signaling through receptors, Neuropilin-1and Plexin-A. Recombinant human Semaphorin 3A is a 751 amino acid protein containing the SEMA domain, an immunoglobulin c2-like domain and a basic domain (Arg/Lys rich) near the C-terminus.

SEMA3A, SEMAD

CHO cells

NYQNGKNNVP RLKLSYKEML ESNNVITFNG LANSSSYHTF LLDEERSRLY VGAKDHIFSF DLVNIKDFQK IVWPVSYTRR DECKWAGKDI LKECANFIKV LKAYNQTHLY ACGTGAFHPI CTYIEIGHHP EDNIFKLENS HFENGRGKSP YDPKLLTASL LIDGELYSGT AADFMGRDFA IFRTLGHHHP IRTEQHDSRW LNDPKFISAH LISESDNPED DKVYFFFREN AIDGEHSGKA THARIGQICK NDFGGHRSLV NKWTTFLKAR LICSVPGPNG IDTHFDELQD VFLMNFKDPK NPVVYGVFTT SSNIFKGSAV CMYSMSDVRR VFLGPYAHRD GPNYQWVPYQ GRVPYPRPGT CPSKTFGGFD STKDLPDDVI TFARSHPAMY NPVFPMNNRP IVIKTDVNYQ FTQIVVDRVD AEDGQYDVMF IGTDVGTVLK VVSIPKETWY DLEEVLLEEM TVFREPTAIS AMELSTKQQQ LYIGSTAGVA QLPLHRCDIY GKACAECCLA RDPYCAWDGS ACSRYFPTAK RRTRRQDIRN GDPLTHCSDL HHDNHHGHSP EERIIYGVEN SSTFLECSPK SQRALVYWQF QRRNEERKEE IRVDDHIIRT DQGLLLRSLQ QKDSGNYLCH AVEHGFIQTL LKVTLEVIDT EHLEELLHKD DDGDGSKTKE MSNSMTPSQK VWYRDFMQLI NHPNLNTMDE FCEQVWKRDR KQRRQRPGHT PGNSNKWKHL QENKKGRNRR THEFERAPRS V

Determined by its ability to bind recombinant rat Neuropilin-1 Fc Chimera in a functional ELISA assay.

Verified by N-terminal and Mass Spectrometry analyses (when applicable).