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AFP Recombinant Human Protein, His tag

Alpha-Fetoprotein (AFP), recombinant human protein is supplied as a lyophilized powder. In general, recombinant proteins can be used as protein stucture analysis and in cell biology research applications.

This recombinant protein was expressed from a DNA sequence encoding the human AFP (P02771) (Met 1-Val 609) fused to a polyhistidine tag at the C-terminus.

Activity: This recombinant protein has not been tested.

Formulation: 140 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, pH7.4, 5% Mannitol, 5% Trehalose, 0.02% Tween80.

Reconstitution: Dissolve the protein in sterile double distilled water to a concentration of 0.2 mg/ml or lower. It is recommended that the protein be aliquoted and be used as soon as possible. Store aliquots under sterile conditions at -20°C. Avoid repeated freeze-thaw cycles.

Expiration Date: Expires one year from date of receipt when stored as instructed.



This protein is manufactured by SINO Biological.

β Amyloid [1 42] PTD Human Protein (Invitrogen™)

Major constituent of plaques and tangles that occur in Alzheimer's disease (AD) patients.

Format/Formulation: Lyophilized trifluoroacetate salt

Molecular Weight: 4515

KEAP1 Recombinant Human Protein, N-His.GST.AVI Tag

Kelch-like ECH-Associated Protein 1 (KEAP1), recombinant human protein is supplied in frozen format. In general, recombinant proteins can be used as protein standard and in cell biology research applications.

This recombinant protein was expressed from a DNA sequence encoding the human KEAP1 (Q14145) (Gln 2-Cys 624) fused to the N-terminal polyhistidine-tagged GST tag at the N-terminus linked by the AVI tag.

Activity: This recombinant protein has not been tested.

Formulation: 20 mM Tris, 500 mM NaCl, 10% glycerol, pH 7.4.

Reconstitution: No reconstitution needed. Store at -80°C. Thaw protein on ice before use and avoid repeated freeze-thaw cycles.

Expiration Date: Expires one year from date of receipt when stored as instructed.

This protein is manufactured by Sino Biologica Inc.

DLL4 Recombinant Human Protein, hIgG1-Fc Tag

Manufactured by Sino Biological (China); Distributed by Life Technologies.

Delta-like 4 (Drosophila) (DLL4) recombinant human protein is supplied as a lyophilized powder. This protein is suitable for use in protein studies such as protein structure analysis and protein-protein interactions. In general, recombinant proteins can also be used as an immunogen, as a protein standard, or in cell biology research applications.

This recombinant human protein is expressed from a DNA sequence encoding the extracellular domain (Met 1-Pro 524) of human DLL4 pre-protein (NP_061947.1) fused to the Fc region of human IgG1 at the C-terminus.

N-terminal Sequence Analysis: Ser 27.

Activity: measured by its binding ability in a functional ELISA. Immobilized human DLL4 at 10 µg/mL (100 µL/well) has been shown to bind biotinylated mouse NOTCH1-His. The EC50 of biotinylated mouse NOTCH1-His is 40 ng/mL.

Formulation: lyophilized in 140 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, pH 7.4, 5% mannitol, 5% trehalose, 0.02% Tween®-80.

Reconstitution: Dissolve the protein in sterile double-distilled water to a concentration of 0.2 mg/mL or lower. It is recommended that the protein be aliquoted and used as soon as possible. Store aliquots under sterile conditions at -20°C. Avoid repeated freeze-thaw cycles.

Expiration Date: expires one year from date of receipt when stored as instructed.

Background
Delta-like protein 4 (DLL4) is a type I membrane-bound Notch ligandcharacterized by an extracellular region containing several EGF-likedomains and a DSL domain required for receptor binding, and issuggested to play a key role in vascular development and tumorangiogenesis. The Notch pathway is an evolutionary conservedintercellular signaling pathway involved in numerous biological processesincluding cell fate determination, cellular differentiation, proliferation, survival, and apoptosis. In mammalian cells, five Notch ligands (Jagged1, 2, DLL1, 3, 4) and four Notch receptors (Notch1-4) have been identified, and ligand-receptor interactions results in proteolysis and translocation of the Notch intracellular domain. As a ligand for Notch1 and Notch 4, DLL4 is selectively expressed in the developing endothelium and in some tumor endothelium, and is induced by vascular endothelial growth factor (VEGF)-A and hypoxia. In recent studies, it has been revealed that this DLL4 inhibition may paradoxically lead to increased angiogenesis but poor tumor growth because of the non-functional neovascularization, and constitutive expression of DLL4 may leads to a lethal lymphoproliferative disease. Accordingly, this may provide a new therapeutic approach for certain carcinomas.

You may also be interested in the following DLL4 products:
Gene Expression Assays

Frizzled 1 Recombinant Human Protein (Gibco™)

Recombinant Frizzled 1 is a bioactive protein intended for use in cell culture applications. FZD1 is a member of the Frizzled family, which are 7-transmembrane domain proteins that are receptors for Wnt signaling proteins. Wnt signaling is involved in several developmental processes.

Beta-Lactamase (TEM-1) Protein

TEM-1 beta-lactamase is the most widespread enzyme to confer beta-lactam antibiotic resistance to gram-negative bacteria. It is a monomeric protein that requires no metals or cofactors for activity. TEM-1 beta-lactamase efficiently hydrolyzes most penicillin and cephalosporin substrates, including nitrocefin and fluorescent derivates. This protein is intended to be used as a positive control for enzyme-dependent substrate hydrolysis and for use on immunoblots. Other uses include kinetic studies with novel substrates or identification of inhibitors of beta-lactamase as part of an antimicrobial program.

Noggin Recombinant Human Protein (Gibco™)

Recombinant Human Noggin is a bioactive protein intended for use in cell culture applications. Noggin binds and inactivates members of the transforming growth factor-beta (TGF-β) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-β superfamily, this protein may have a principal role in creating morphogenic gradients. The protein appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of the ortholog suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation.

High purity—no interference from other proteins or contaminants
High biological activity—more results with less protein
Proven compatibility—Gibco® proteins bioassayed with Gibco® media

High Purity Recombinant Bioactive Protein
Recombinant Human Noggin is one of our more than 250 available Gibco® recombinant proteins. To help ensure Gibco® growth factors are of the highest quality, each protein is analyzed for purity along with structural homogeneity to ensure a biologically active protein.

High Biological Activity
In-house activity testing of Gibco® Recombinant Proteins includes cell proliferation, cytotoxicity, chemotaxis, calcium flux, secondary cytokine up-regulation, induction of surface antigen expression, antiviral, and protease assays. Recombinant Human Noggin specific activity is determined by measuring the dose dependent inhibition of the 5 ng/ml BMP-4-induced alkaline phosphatase production by ATDC-5 chondrogenic cells.

Proven Compatibility
Gibco® proteins are bioassayed with Gibco® media. Since 1962, Gibco® has been the consistent provider of high quality media, reagents, and sera for reliable cell culture.

See our selection of recombinant Gibco® growth factors.

For Research Use Only. Not intended for animal or human diagnostic or therapeutic use.

Annexin V Recombinant Protein, FITC, eBioscience™ (Invitrogen™)

Annexin V Recombinant Protein for Flow, Ctrl

Recombinant Protein G (Invitrogen™)

Recombinant protein G is produced in a strain of E. coli which contains the gene for protein G from Streptococcus sp. It is supplied as a salt-free lyophilized powder.

Recombinant protein G binds to the Fc region of many types of immunoglobulin G including:

• all four subclasses of human IgG
• mouse IgG
• rabbit IgG
• guinea pig IgG
• rat IgG
• goat IgG
• sheep IgG
• cow IgG
• horse IgG

Recombinant protein G does not bind to IgG from chicken or cat, or to human IgA, IgM, or serum albumin. It binds weakly to IgG from dog.

β Amyloid [1 40] PTD Human Protein (Invitrogen™)

Major constituent of plaques and tangles that occur in Alzheimer's disease (AD) patients.

Format/Formulation: Lyophilized trifluoroacetate salt, >96% purity by HPLC.

Molecular Weight: 4331

Protein A-HRP (Invitrogen™)

Protein A from Staphylococcus aureus, Cowan I Strain conjugated with highly purified horseradish peroxidase (RZ > 3.0).

The product is liquid containing 10 mM phosphate, 0.15 M NaCl buffer, pH 7.4, 1% ovalbumin, 40% glycerol, and 0.19% Kathon CG/ICP.

CA9 Recombinant Human Protein, His tag

Carbonic Anhydrase 9 (CA9), recombinant human protein is supplied as a lyophilized powder. It is suitable for use in analysis of protein structure. In general, recombinant proteins can also be used as an immunogen, as a protein standard, or in cell biology research applications.

This recombinant protein was expressed from a DNA sequence encoding the human carbonic anhydrase 9 (CA9) precursor (NP_001207.2) (Met 1-Asp 414) fused to the polyhistidine tag at the C-terminus.

Activity: Measured by its esterase activity. The specific activity is >30 pmoles/min/µg, as measured with 1 mM 4-Nitrophenyl acetate and 2.5 µg enzyme at 400 nm in 100 µl of 12.5 mM Tris, 75 mM NaCl, pH 7.5.

Formulation: Lyophilized in 25mM Tris, 150 mM NaCl, pH 7.4, 5% Mannitol, 5% Trehalose, 0.02% Tween 80.

Reconstitution: Dissolve the protein in sterile double distilled water to a concentration of 0.2 mg/ml or lower. It is recommended that the protein be aliquoted and be used as soon as possible. Store aliquots under sterile conditions at -20°C. Avoid repeated freeze-thaw cycles.

Expiration Date: Expires one year from date of receipt when stored as instructed.

This protein is manufactured by Sino Biological Inc.

protein A, Alexa Fluor™ 546 conjugate (Invitrogen™)

Our Alexa Fluor 546 protein A conjugate binds to the Fc portion of various immunoglobulins from several different species. This exceptionally bright, orange-fluorescent probe (absorption/emission maxima ~556/573 nm) can be used to visualize antibodies in a manner analogous to a labeled species-specific secondary antibody.

RSPO1 Recombinant Human Protein, His Tag

R-Spondin 1 (RSPO1), recombinant human protein is supplied as a lyophilized powder. It is suitable for use in protein studies such as protein structure analysis and protein-protein interactions. In general, recombinant proteins can also be used as an immunogen, as a protein standard, or in cell biology research applications.

This recombinant protein was expressed from a DNA sequence encoding the human RSPO1 (NP_001033722.1) (Met 1-Ala 263) fused to a polyhistidine tag at the C-terminus.

Activity: Measured by its binding ability in a functional ELISA.

1. Immobilized human RSPO1 at 20 µg/ml (100 µl/well) can bind human LIMPII with a linear ranger of 32-800 ng/ml.

2. Immobilized human RSPO1 at 20 µg/ml (100 µl/well) can bind mouse CD36 with a linear ranger of 6.4-800 ng/ml.

Formulation: Lyophilized in 140 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, pH 7.4, 5% Mannitol, 5% Trehalose, 0.02% Tween 80.

Reconstitution: Dissolve the protein in sterile double distilled water to a concentration of 0.2 mg/ml or lower. It is recommended that the protein be aliquoted and be used as soon as possible. Store aliquots under sterile conditions at -20°C. Avoid repeated freeze-thaw cycles.

Expiration Date: Expires one year from date of receipt when stored as instructed.

This protein is manufactured by Sino Biological Inc.

MBP Bovine Protein, Natural (Gibco™)

Myelin Basic Protein (MBP) was purified from bovine brain by a modification of the method of Deibler et al. (1). The protein is supplied lyophilized.