Auf der Bindungsreaktion von Loratadin mit humanem Serum Akut – Phase – Protein alpha – 1-saures Glyco protein
Loratadin ist ein wichtiges antiallergisches Medikament. Es ist ein Antihistaminikum der zweiten Generation zur Behandlung von allergischer Rhinitis, Heuschnupfen und Urtikaria. Humanes Alpha-1-Säure-Glykoprotein (AG) ist ein wichtiges Akute-Phase-Protein, dessen Serumkonzentration bei Entzündungen und akuten Reaktionen ansteigt. Die Bindungswechselwirkung zwischen Loratadin und AG wird mit Spektroskopie und molekularen Docking-Techniken untersucht. Die aus Fluoreszenzlöschungsexperimenten erhaltenen Ergebnisse zeigten, dass die Fluoreszenzintensität von AG durch Loratadin gelöscht wird. Loratadin bindet AG mit einer Bindungskonstante von ≈10 4 bei 298 K.
Es wurde festgestellt, dass die Änderung der freien Energie nach Gibb für die Wechselwirkung von Loratadin mit AG negativ ist, was darauf hindeutet, dass der Bindungsprozess spontan ist. Die Bindung von Loratadin an AG induzierte geordnete Strukturen im Protein. Wasserstoffbrückenbindungen und hydrophobe Wechselwirkungen waren die Hauptbindungskräfte zwischen AG-Loratadin, wie durch molekulare Docking-Ergebnisse gezeigt wurde. Diese Studie legt die Bedeutung der räumlichen Bindung eines antiallergischen Arzneimittels an AG bei Erkrankungen nahe, bei denen die Plasmakonzentration von AG um ein Vielfaches ansteigt und die Wechselwirkung mit diesem Protein signifikant wird. Diese Studie wird bei der Gestaltung der Arzneimitteldosierung und der entsprechenden Anpassung helfen, um ein optimales Behandlungsergebnis zu erzielen. Übermittelt von Ramaswamy H. Sarma.
Gezielte Protein – Abbau durch schnelle o
Schnell wachsende SARS-CoV-2 B.1.1.7 Unter Linie in den Vereinigten Staaten von Amerika mit Spike – Protein D178H und Membranprotein V70L Mutationen
Zusammenfassung Die SARS-CoV-2 B.1.1.7-Linie ist hoch ansteckend und machte im April 2021 92 % der COVID-19-Fälle in Europa und 59 % der COVID-19-Fälle in den USA aus. Sie wird durch die N501Y-Mutation definiert defined in der Rezeptorbindungsdomäne (RBD) des Spike (S)-Proteins und einigen anderen Mutationen. Dazu gehören zwei Mutationen in der N-terminalen Domäne (NTD)des S-Proteins, HV69-70del und Y144del (aufgrund der Anwesenheit von Tyrosin an beiden Positionen auch als Y145del bekannt). Wir haben kürzlich mehrere neue bedenkliche SARS-CoV-2-Varianten identifiziert, die durch Mutationen des Membranproteins (M) gekennzeichnet sind, einschließlich I82T und V70L. Wir identifizieren nun eine Unterlinie von B.1.1.7, die durch sequentielle Akquisitionen von M:V70L im November 2020 entstanden ist, gefolgt von einer neuartigen S:D178H-Mutation, die erstmals Anfang Februar 2021 beobachtet wurde.
Der Anteil der B.1.1.7-Isolate in den USA, die zu dieser Unterlinie gehören, stieg von 0,15 % im Februar 2021 auf 1,8 % im April 2021. Bis heute scheint diese Unterlinie US-spezifisch zu sein, mit gemeldeten Fällen in 31 Staaten, einschließlich Hawaii. Im April 2021 machte es 36,8% aller B.1.1.7-Isolate in Washington aus. Die phylogenetische Analyse und die Übertragungsinferenz mit Nextstrain legen nahe, dass diese Unterlinie wahrscheinlich ihren Ursprung in Kalifornien oder Washington hat . Die Strukturanalyse ergab, dass die S:D178H-Mutation in der NTD des S-Proteins und in der Nähe von zwei anderen Signaturmutationen von B.1.1.7, HV69-70del und Y144del liegt. Es ist oberflächenexponiert und kann die tertiäre Konfiguration oder Zugänglichkeit von NTD verändern und hat daher das Potenzial, die Neutralisation durch NTD-gerichtete Antikörper zu beeinflussen.
Description: A polyclonal antibody for detection of CSP from Human, Mouse, Rat. This CSP antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human CSP at AA range: 100-180
Description: A polyclonal antibody for detection of CSP from Human, Mouse, Rat. This CSP antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human CSP at AA range: 100-180
Description: A polyclonal antibody for detection of CSP from Human, Mouse, Rat. This CSP antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human CSP at AA range: 100-180
Description: A polyclonal antibody raised in Goat that recognizes and binds to Human DNAJC5 / CSP (aa177-191). This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody against CSPG4. Recognizes CSPG4 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC; Recommended dilution: WB:1:1000-1:5000, IHC:1:20-1:200
Description: A polyclonal antibody against CSPG4. Recognizes CSPG4 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB
Description: A polyclonal antibody against CSPG5. Recognizes CSPG5 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB
Description: A polyclonal antibody against CSPP1. Recognizes CSPP1 from Human, Mouse. This antibody is Unconjugated. Tested in the following application: ELISA, WB
Description: A polyclonal antibody against CSPG5. Recognizes CSPG5 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: WB, ELISA;WB:1/500-1/2000.ELISA:1/40000
Description: A polyclonal antibody against CSPG4. Recognizes CSPG4 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:2000-1:5000, WB:1:500-1:2000, IHC:1:20-1:100
Description: A polyclonal antibody against CSPG5. Recognizes CSPG5 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB;WB:1:500-1:3000
Description: A polyclonal antibody against CSPG5. Recognizes CSPG5 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB;WB:1:500-1:3000
Description: A polyclonal antibody against CSPP1. Recognizes CSPP1 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC; Recommended dilution: IHC:1:20-1:200
Description: A polyclonal antibody against CSPP1. Recognizes CSPP1 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC; Recommended dilution: WB:1:1000-1:5000, IHC:1:20-1:200
Description: This gene is a member of the septin gene family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is mapped to 22q11, the region frequently deleted in DiGeorge and velocardiofacial syndromes. A translocation involving the MLL gene and this gene has also been reported in patients with acute myeloid leukemia. Alternative splicing results in multiple transcript variants. The presence of a non-consensus polyA signal (AACAAT) in this gene also results in read-through transcription into the downstream neighboring gene (GP1BB; platelet glycoprotein Ib), whereby larger, non-coding transcripts are produced.
Description: This gene encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae. The protein also shares similarity with Diff 6 of Drosophila and with H5 of mouse. Each of these similar proteins, including the yeast CDC10, contains a GTP-binding motif. The yeast CDC10 protein is a structural component of the 10 nm filament which lies inside the cytoplasmic membrane and is essential for cytokinesis. This human protein functions in gliomagenesis and in the suppression of glioma cell growth, and it is required for the association of centromere-associated protein E with the kinetochore. Alternative splicing results in multiple transcript variants. Several related pseudogenes have been identified on chromosomes 5, 7, 9, 10, 11, 14, 17 and 19.
Description: This gene is a member of the septin family of GTPases. Members of this family are required for cytokinesis and the maintenance of cellular morphology. This gene encodes a protein that can form homo- and heterooligomeric filaments, and may contribute to the formation of neurofibrillary tangles in Alzheimer's disease. Alternatively spliced transcript variants have been found but the full-length nature of these variants has not been determined. [provided by RefSeq, Dec 2012]
Description: This gene is a member of the septin family of GTPases. Members of this family are required for cytokinesis. One version of pediatric acute myeloid leukemia is the result of a reciprocal translocation between chromosomes 11 and X, with the breakpoint associated with the genes encoding the mixed-lineage leukemia and septin 2 proteins. This gene encodes four transcript variants encoding three distinct isoforms. An additional transcript variant has been identified, but its biological validity has not been determined.
Description: This gene is a member of the septin family involved in cytokinesis and cell cycle control. This gene is a candidate for the ovarian tumor suppressor gene. Mutations in this gene cause hereditary neuralgic amyotrophy, also known as neuritis with brachial predilection. A chromosomal translocation involving this gene on chromosome 17 and the MLL gene on chromosome 11 results in acute myelomonocytic leukemia. Multiple alternatively spliced transcript variants encoding different isoforms have been described.
Description: This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is highly expressed in brain and heart. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. One of the isoforms (known as ARTS) is distinct; it is localized to the mitochondria, and has a role in apoptosis and cancer.
Description: This gene encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae. The protein also shares similarity with Diff 6 of Drosophila and with H5 of mouse. Each of these similar proteins, including the yeast CDC10, contains a GTP-binding motif. The yeast CDC10 protein is a structural component of the 10 nm filament which lies inside the cytoplasmic membrane and is essential for cytokinesis. This human protein functions in gliomagenesis and in the suppression of glioma cell growth, and it is required for the association of centromere-associated protein E with the kinetochore. Alternative splicing results in multiple transcript variants. Several related pseudogenes have been identified on chromosomes 5, 7, 9, 10, 11, 14, 17 and 19.
Description: This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Description: This gene is a member of the septin gene family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is mapped to 22q11, the region frequently deleted in DiGeorge and velocardiofacial syndromes. A translocation involving the MLL gene and this gene has also been reported in patients with acute myeloid leukemia. Alternative splicing results in multiple transcript variants. The presence of a non-consensus polyA signal (AACAAT) in this gene also results in read-through transcription into the downstream neighboring gene (GP1BB; platelet glycoprotein Ib), whereby larger, non-coding transcripts are produced.
Description: This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Protozoan Plasmodium vivax Circumsporozoite Protein (P. vivax CSP) Protein
Description: This gene encodes a guanine-nucleotide binding protein and member of the septin family of cytoskeletal GTPases. Septins play important roles in cytokinesis, exocytosis, embryonic development, and membrane dynamics. Multiple transcript variants encoding different isoforms have been found for this gene.
Description: Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. [UniProt]
Description: Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. [UniProt]
Description: Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. [UniProt]
Description: Chondroitin sulfate proteoglycan 4, also known as melanoma-associated chondroitin sulfate proteoglycan (MCSP) or neuron-glial antigen 2 (NG2), is a chondroitin sulfate proteoglycan that in humans is encoded by the CSPG4 gene. CSPG4 plays a role in stabilizing cell-substratum interactions during early events of melanoma cell spreading on endothelial basement membranes. It represents an integral membrane chondroitin sulfate proteoglycan expressed by human malignant melanoma cells.
Rabbit Anti-(NANP)5 peptide (25-aa, repeat-sequence peptide of the P. falciparum circumsporozoite protein), CSP IgG, aff pure
Description: This is Competitive Enzyme-linked immunosorbent assay for Antibody Detection.detection of Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) in serum, plasma and other biological fluids.
Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) ELISA Kit
Description: This is Competitive Enzyme-linked immunosorbent assay for Antibody Detection.detection of Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) in serum, plasma and other biological fluids.
Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) ELISA Kit
Description: This is Competitive Enzyme-linked immunosorbent assay for Antibody Detection.detection of Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) in serum, plasma and other biological fluids.
Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) ELISA Kit
Description: This is Competitive Enzyme-linked immunosorbent assay for Antibody Detection.detection of Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) in serum, plasma and other biological fluids.
Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) ELISA Kit
Description: Enzyme-linked immunosorbent assay based on the Competitive Inhibition method for detection of Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) in samples from serum, plasma and other biological fluids with no significant corss-reactivity with analogues from other species.
Description: A polyclonal antibody for detection of CSPG4 from Human, Mouse, Rat. This CSPG4 antibody is for IHC-P. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human CSPG4 protein at amino acid sequence of 1910-1990
Description: A polyclonal antibody for detection of CSPG4 from Human, Mouse, Rat. This CSPG4 antibody is for IHC-P. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human CSPG4 protein at amino acid sequence of 1910-1990
Description: A polyclonal antibody for detection of CSPG4 from Human, Mouse, Rat. This CSPG4 antibody is for IHC-P. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human CSPG4 protein at amino acid sequence of 1910-1990
Description: A polyclonal antibody for detection of CSPP1 from Human. This CSPP1 antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human CSPP1 protein
Description: A polyclonal antibody for detection of CSPP1 from Human. This CSPP1 antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human CSPP1 protein
Description: A polyclonal antibody for detection of CSPP1 from Human. This CSPP1 antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human CSPP1 protein
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Schnelle dreidimensionale Formbestimmung von globulären Proteinen durch Mobilitätskapillarelektrophorese und native Massenspektrometrie
Etablierte Hochdurchsatz-Proteomik-Methoden liefern nur begrenzte Informationen über die Stereostrukturen von Proteinen. Herkömmliche Technologien zur Bestimmung der Proteinstruktur erfordern typischerweise mühsame Schritte und können nicht mit hohem Durchsatz durchgeführt werden. Hier berichten wir über eine neue Methode mit mittlerem Durchsatz durch die Kombination von Mobilitätskapillarelektrophorese (MCE) und nativer Massenspektrometrie (MS) zur dreidimensionalen (3D) Formbestimmung von globulären Proteinen in der flüssigen Phase , die sowohl die geometrische Struktur als auch die molekularen Masseninformation von Proteinen.
Es wurde eine Theorie aufgestellt , um den hydrodynamischen Ionenradius und die Ladungszustandsverteilung im nativen Massenspektrum mit geometrischen Parametern des Proteins zu korrelieren , wodurch eine niedrigaufgelöste Struktur (Form) des Proteins bestimmt werden konnte. Unsere Testdaten von 11 verschiedenen globulären Proteinen zeigten, dass wir mit diesem Ansatz die Formen einzelner Proteine, Proteinkomplexe und Proteine in einer Mischung bestimmen und Protein-Konformationsänderungen verfolgen können. Neben der Bereitstellung komplementärer Proteinstrukturinformationen und der Fähigkeit zur Mischungsanalyse ist diese auf MCE und nativer MS basierende Methode schnell und hat einen geringen Probenverbrauch, was sie potenziell in der Top-Down-Proteomik und Strukturbiologie für intakte globuläre Protein- oder Proteinkomplexanalysen einsetzbar macht.
Schnelle Oberflächenimmobilisierung nativer Proteine durch katalysatorfreie Amino-In-Klick-Biokonjugation
Die Oberflächenimmobilisierung bietet eine nützliche Plattform für Biosensorik, Wirkstoffscreening, Tissue Engineering und andere chemische und biologische Anwendungen. Allerdings sind einige der verwendeten Reaktionen ineffizient und / oder kompliziert, die Begrenzung ihrer Anwendungen in der Immobilisierung. Hier verwenden wir eine spontane und katalysatorfreie Amino-In-Klick-Biokonjugation , um mit aktivierten Ethinylgruppen funktionalisierte Oberflächen für die schnelle Immobilisierung nativer Proteine und Zellen zu erzeugen .
Biomoleküle wie Rinderserumalbumin (BSA) , humanes IgG und ein Peptid von C(RGDfK) konnten in nur 30 min kovalent auf den Oberflächen immobilisiert werden. Insbesondere bleibt die Bioaktivität der verankerten Biomoleküle intakt, was durch effizientes Einfangen von Zielantikörpern und -zellen aus den Massenlösungen bestätigt wird. Diese Strategie stellt eine Alternative für eine hocheffiziente Oberflächenbiofunktionalisierung dar.
ptogenetische Aktivierung und seine Anwendung auf die Steuerung von Cell Signaling
Die Entwicklung von Methoden für den optisch ausgelösten Proteinabbau ermöglicht die Untersuchung dynamischer Proteinfunktionen, wie sie beispielsweise an der Zellsignalübertragung beteiligt sind und die mit herkömmlichen genetischen Techniken nur schwer untersucht werden können. Hier beschreiben wir das Design und die Implementierung eines neuartigen lichtgesteuerten Peptid-Degrons, das den Abbau des N-Ende-Wegs zu seinem Proteinziel überträgt. Das Degron umfasst eine photoaktivierbare N-terminale Aminosäure und einen lysinreichen 13-Reste-Linker. Durch das Einschließen des N-terminalen Rests konnten wir die N-Degron-Erkennung durch eine E3-Ligase optisch kontrollieren und somit die Ubiquitinierung und den proteasomalen Abbau des Zielproteins kontrollieren.
Wir demonstrieren eine breite Anwendbarkeit, indem wir diesen Ansatz auf eine Vielzahl von Zielproteinen anwenden , darunter EGFP, Glühwürmchen-Luciferase, die Kinase MEK1 und die Phosphatase DUSP6 (auch bekannt als MKP3). Das Käfig-Degron kann mit minimalem Protein-Engineering verwendet werden und bietet einen praktisch vollständigen, lichtgesteuerten Proteinabbau im Sekunden- bis Minutenbereich.
Description: A DNA sequence encoding the mature variant of ovVEGF-E isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020) was expressed in E. coli as a 132 amino acid residue fusion protein with an N-terminal His-tag sequence and a thrombin cleavage site. Recombinant VEGF-E homodimer was dimerized in vitro and has a predicted mass of approximately 35 kDa.
