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Recombinant Proteins / Fusion Proteins
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ALX-201-230 Revised 26-Apr-06
Endonuclease G (rat) (recombinant)
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SYNONYMS EndoG (rat) (recombinant)
PRODUCT LINE Cell Death / Apoptosis / Autophagy
PRODUCT CATEGORY HtrA2 / Omi, ARTS, EndoG / Related Products
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ALX-201-230-C020   20 µg 190.00 USD Add To Cart
Product Specification
CONCENTRATION: 0.4mg/ml
PURITY: ≥90% (SDS-PAGE)
FORMULATION: Liquid. In 50mM TRIS-HCl, pH 8.0, containing 500mM sodium chloride, 0.05% Tween 20, 5mM β-mercaptoethanol, 500mM imidazole and 20% glycerol.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
HANDLING: Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
Further Categories Containing This Product:
Recombinant Proteins / Fusion ProteinsDNA Endonucleases / Related Products
 
 
ALX-201-006 Revised 04-Sep-08
N-Acetyl-eglin C (recombinant)
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PRODUCT LINE Cancer
PRODUCT CATEGORY Cathepsin Inhibitors
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ALX-201-006-MC01   0.1 mg 95.00 USD Add To Cart
ALX-201-006-MC05   0.5 mg 380.00 USD Add To Cart
ALX-201-006-M001   1 mg 670.00 USD Add To Cart
Product Specification
SEQUENCE: Ac-Thr-Glu-Phe-Gly-Ser-Glu-Leu-Lys-Ser-Phe-Pro-Glu-Val-Val-Gly-Lys-Thr-Val-Asp-Gln-Ala-Arg-Glu-Tyr-Phe-Thr-Leu-His-Tyr-Pro-Gln-Tyr-Asn-Val-Tyr-Phe-Leu-Pro-Glu-Gly-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-Asp-Arg-Val-Arg-Val-Phe-Tyr-Asn-Pro-Gly-Thr-Asn-Val-Val-Asn-His-Val-Pro-His-Val-Gly-OH
FORMULA: C377H552N96O107
MW: 8141.1
CAS NUMBER: 96380-69-7
SOURCE/HOST: Produced in E. coli.
PURITY: ≥97% (HPLC)
APPEARANCE: White to off-white powder.
SOLUBILITY: Soluble in water.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
Product Description
Eglin C was originally isolated from the leech Hirudo medicinalis [1]. Recombinant N-acetyl-eglin C is a 70 amino acid peptide with identical biological activity to native eglin C. An effective inhibitor of chymotrypsin and subtilisin as well as of leukocyte elastase and cathepsin G.
Product Specific Literature References
[1] Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis: U. Seemüller, et al.; Hoppe-Seyler's Z. Physiol. Chem. 361, 1841 (1980) Abstract
[2] A large fragment approach to DNA synthesis: total synthesis of a gene for the protease inhibitor eglin c from the leech Hirudo medicinalis and its expression in E. coli: H. Rink, et al.; Nucl. Acids Res. 12, 6369 (1984) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P01051: Eglin C (Hirudo medicinalis)
Further Categories Containing This Product:
Recombinant Proteins / Fusion ProteinsProteases Other Products
 
 
ALX-201-002 Revised 11-May-06
Furin Convertase (human) (recombinant)
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SYNONYMS Furin (human) (recombinant)
PACE (human) (recombinant)
PRODUCT LINE Signal Transduction
PRODUCT CATEGORY Convertases / Related Products / Furin
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ALX-201-002-U050   50 U 240.00 USD Add To Cart
Product Specification
MW: ~81kDa.
EC: 3.4.21.75
SOURCE/HOST: Produced in Drosophila melanogaster Schneider 2 cells. Corresponds to aa 108-714 of the human preproenzyme. Does not contain the C-terminal and transmembrane domains.
QUANTITY: ~50U/vial. One unit is defined as the amount of enzyme that releases 1pmol AMC from Boc-Arg-Val-Arg-Arg-AMC (Prod. No. ALX-260-040) per minute.
CONCENTRATION: 1U/µl
PURITY: ~90% (one major band at ~83kDa)
FORMULATION: Liquid. In 100mM HEPES, pH 7.5, containing 25% glycerol, 150mM sodium chloride and 1mM calcium dichloride.
BIOLOGICAL ACTIVITY: Cleaves precursor proteins C-terminal to an Arg-X-X-Arg motif.
SPECIFIC ACTIVITY: One unit cleaves 24pmol (2µg) of protective antigen or 100pmol (2.5µg) of human proendothelin-1 per hour at 30°C in 100mM HEPES, pH 7.6, containing 1mM calcium dichloride, 0.5% Triton X-100 and 1mM 2-mercaptoethanol.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
USE/STABILITY: Do not aliquot. Keep vial on ice during use and put immediately back in -80°C freezer.
HANDLING: Do not freeze/thaw.
Product Specific Literature References
Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage: R. Leduc, et al.; J. Biol. Chem. 267, 14304 (1992) Abstract; Full Text
Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen: S.S. Molloy, et al.; J. Biol. Chem. 267, 16396 (1992) Abstract; Full Text
Purification of recombinant soluble forms of furin produced in Chinese hamster ovary cells: K. Nakayama; Meth. Enzymol. 244, 167 (1994) Abstract
Internally quenched fluorogenic substrate for furin: H. Angliker, et al.; Anal. Biochem. 224, 409 (1995) Abstract
Processing of proendothelin-1 by human furin convertase: J.-B. Denault, et al.; FEBS Lett. 362, 276 (1995) Abstract
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Recombinant Proteins / Fusion ProteinsEnzymes
 
 
ALX-201-023 Revised 06-Aug-07
Cyclophilin A (human) (recombinant)
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SYNONYMS CyPA (human) (recombinant)
Peptidyl-prolyl cis-trans Isomerase A (human) (recombinant)
PRODUCT LINE Immunology
PRODUCT CATEGORY Immunophilins / Related Products
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ALX-201-023-C100   100 µg 586.00 USD Add To Cart
Product Specification
MW: ~18kDa.
EC: 5.2.1.8
SOURCE/HOST: Produced in E. coli.
CONCENTRATION:  
PURITY: ≥90%
FORMULATION: Liquid. In 20mM TRIS-HCl, pH 7.8.
BIOLOGICAL ACTIVITY: Catalyzes cis-trans-isomerization of X-Pro-peptide bonds. Accelerates protein folding reactions that are limited by the isomerization of X-Pro-peptide bonds.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: +4°C
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P05092: Cyclophilin A (human)
AfCS Signalling Gateway link A000735: Cyclophilin A (mouse)
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Recombinant Proteins / Fusion Proteins
 
 
ALX-201-024 Revised 24-Feb-05
HSF1 (human) (recombinant)
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SYNONYMS Heat Shock Factor 1 (human) (recombinant)
PRODUCT LINE Stress & Heat Shock Proteins
PRODUCT CATEGORY Stress & Heat Shock Proteins Other Products
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ALX-201-024-C150   150 µg 343.00 USD Add To Cart
Product Specification
SOURCE/HOST: Produced in E. coli.
FORMULATION: Liquid. Sonicated E. coli extract at a total protein concentration of 6mg/ml in 25mM HEPES, pH 7.9, 12.5mM MgCl, 0.1mM EDTA, 10% glycerol, 1mM DTT, 0.1% NP-40 and 300mM KCl and protease inhibitors.
APPLICATION: Positive control in gel shift assays (25 tests) or Western blot (50 tests) with PAb to HSF1 (Prod. No. ALX-210-129). DNase I footprinting and in vitro transcription assays.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -20°C
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link Q00613: HSF 1 (human)
Further Categories Containing This Product:
Recombinant Proteins / Fusion ProteinsTranscription Factors Other Products
 
 
ALX-201-028 Revised 23-Apr-08
Nitric Oxide Synthase (Neuronal) (rat) (recombinant) (high purity)
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SYNONYMS nNOS (rat) (recombinant) (high purity)
NOS I (rat) (recombinant) (high purity)
PRODUCT LINE Nitric Oxide Pathway
PRODUCT CATEGORY NOS
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ALX-201-028-R050   50 µl 130.00 USD Add To Cart
Product Specification
MW: ~160kDa/subunit; homodimer.
EC: 1.14.13.39
SOURCE/HOST: Produced in Sf9 cells.
CONCENTRATION: ~1mg/ml
PURITY: ≥98% (SDS-PAGE)
FORMULATION: Liquid. In 20mM TRIS/HCl (pH 7.5), 150mM sodium chloride, 4mM EGTA and 10mM 2-mercaptoethanol.
SPECIFIC ACTIVITY: ~0.7µmol L-citrulline/mg/min. Amount assayed: 0.1-0.3µl. Optimal conditions: pH 7.0; 37°C; 0.1mM L-arginine, 0.2mM NADPH, 10µM BH4, 5µM FAD/FMN, 10µg/ml calmodulin, 10-500µM CaCl2.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
USE/STABILITY: Dilute stock solutions with buffer containing 10mM 2-mercaptoethanol and 1mM CHAPS.

nNOS is relatively unstable. K
eep stock vial on ice at all times when performing experiments! Enzyme loses approx. 10-15% of activity during a single freeze/thaw cycle.
HANDLING: Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
Product Specific Literature References
Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme: D.S. Bredt & S.H. Snyder; PNAS 87, 682 (1990) Abstract
Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- and interdomain electron transfer: H.M. Abu-Soud, et al.; J. Biol. Chem. 269, 32047 (1994) Abstract; Full Text
Electron transfer in the nitric-oxide synthases. Characterization of L- arginine analogs that block heme iron reduction: H.M. Abu-Soud, et al.; J. Biol. Chem. 269, 32318 (1994) Abstract; Full Text
Expression of rat brain nitric oxide synthase in baculovirus-infected insect cells and characterization of the purified enzyme: C. Harteneck, et al.; Biochem. J. 304, 683 (1994) Abstract
Molecular mechanisms of inhibition of porcine brain nitric oxide synthase by the antinociceptive drug 7-nitro-indazole [published erratum appears in Neuropharmacology 1995 Feb;34(2):243]: B. Mayer, et al.; Neuropharmacology 33, 1253 (1994) Abstract
Characterization of neuronal nitric oxide synthase and a C415H mutant, purified from a baculovirus overexpression system: M.K. Richards & M.A. Marletta; Biochemistry 33, 14723 (1994) Abstract
Evidence for a bidomain structure of constitutive cerebellar nitric oxide synthase: E.A. Sheta, et al.; J. Biol. Chem. 269, 15147 (1994) Abstract; Full Text
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P29476: nNOS (rat)
AfCS Signalling Gateway link A001658: nNOS (mouse)
Further Categories Containing This Product:
Recombinant Proteins / Fusion ProteinsEnzymes
 
 
ALX-201-032 Revised 08-Feb-06
Proendothelin-1 (human) (recombinant)
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SYNONYMS ProET-1 (human) (recombinant)
PRODUCT LINE Signal Transduction
PRODUCT CATEGORY Endothelins [ETs] & Endothelin Receptors / Related Products
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ALX-201-032-C004   4 µg 190.00 USD Add To Cart
Product Specification
MW: ~26kDa.
SOURCE/HOST: Produced in XL1-Blue cells. Human proendothelin-1 (aa 18-212) is fused to a His-tag. The N-terminal peptide sequence Met-Arg-Gly-Ser-(His)6 replaces the signal peptide.
PURITY: ~80% (SDS-PAGE)
FORMULATION: Lyophilized. Contains no preservatives.
RECONSTITUTION: Reconstitute in sterile water.
BIOLOGICAL ACTIVITY: 4µg (160pmoles) of recombinant human proendothelin-1 when cleaved with furin and chymosin has been shown to produce endothelin-1 mediated vasoconstriction of rat vas deferens and rabbit carotid artery.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: +4°C
Product Specific Literature References
Processing of proendothelin-1 by human furin convertase: J.-B. Denault, et al.; FEBS Lett. 362, 276 (1995) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P25101: Endothelin-1 (human) (precursor)
AfCS Signalling Gateway link A000062: Endothelin-1 (mouse)
Further Categories Containing This Product:
Recombinant Proteins / Fusion Proteins
 
 
ALX-201-034 Revised 02-May-06
Leptin (human) (recombinant)
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SYNONYMS OB Gene Product (human) (recombinant)
PRODUCT LINE Obesity & Adipokines
PRODUCT CATEGORY Leptin / Related Products
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ALX-201-034-M001   1 mg 190.00 USD Add To Cart
Product Specification
MW: ~16kDa.
MERCK INDEX: 14: 5443
SOURCE/HOST: Produced in E. coli. Homologous to human serum leptin.
PURITY: ≥98% (SDS-PAGE)
FORMULATION: Lyophilized from sterile filtered solution in 10mM sodium citrate, pH 4.0.
ENDOTOXIN CONTENT: <0.1EU/µg purified protein.
RECONSTITUTION: Reconstitute with sterile water or 0.4% sodium bicarbonate, pH 8-9. Do not reconstitute to less than 0.1mg/ml. Further dilutions should be made with medium containing 0.1% HSA or BSA.
BIOLOGICAL ACTIVITY: Induces proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
USE/STABILITY: Reconstituted protein is stable for 4 weeks when stored at +4°C.
HANDLING: Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and freeze in liquid nitrogen.
General Information
Leptin, the product of the ob (obese) gene, is a 16kDa protein consisting of 146 amino acid residues. Leptin is produced in the adipose tissue, and is considered to play an important role in appetite control, fat metabolism and regulation of body weight. It targets the central nervous system, particularly hypothalamus, affecting food intake. Leptin levels are high in most obese individuals. Studies have shown that it may also influence reproductive function.
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P41159: Leptin (human) (precursor)
General Literature References
Leptin and the regulation of body weight in mammals: J.M. Friedman and J.L. Halaas; Nature 395, 763 (1998), review Abstract
Mutation screening and identification of a sequence variation in the human ob gene coding region: R.V. Considine, et al.; BBRC 220, 735 (1996) Abstract
Serum immunoreactive leptin concentrations in normal-weight and obese humans  : R.V. Considine, et al. ; New Engl. J. Med. 334, 292 (1996) Abstract
Leptin levels in human and rodent: measurement of plasma leptin and ob RNA in obese and weight-reduced subjects  : M. Maffei, et al.; Nature Medicine 1, 1155 (1995) Abstract
Effects of the obese gene product on body weight regulation in ob/ob mice  : M.A. Pelleymounter, et al. ; Science 269, 540 (1995) Abstract
Evidence against either a premature stop codon or the absence of obese gene mRNA in human obesity  : R.V. Considine, et al. ; J. Clin. Invest 95, 2986 (1995) Abstract
Overexpression of the obese (ob) gene in adipose tissue of the human subjects  : F. Lönnqvist, et al. ; Nature Medicine 1, 950 (1995) Abstract
Positional cloning of the mouse obese gene and its human homologue  : Y. Zhang, et al.; Nature 372, 425 (1994) Abstract
Further Categories Containing This Product:
Recombinant Proteins / Fusion Proteins
 
 
ALX-201-035 Revised 18-May-06
Leptin (mouse) (recombinant)
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SYNONYMS OB Gene Product (mouse) (recombinant)
PRODUCT LINE Obesity & Adipokines
PRODUCT CATEGORY Leptin / Related Products
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ALX-201-035-M001   1 mg 190.00 USD Add To Cart
Product Specification
MW: ~16kDa.
MERCK INDEX: 14: 5443
SOURCE/HOST: Produced in E. coli. Homologous to mouse serum leptin.
PURITY: ≥98% (SDS-PAGE)
FORMULATION: Lyophilized from 0.0045mM sodium bicarbonate.
ENDOTOXIN CONTENT: <0.1EU/µg purified protein.
RECONSTITUTION: Reconstitute with sterile water or 0.4% sodium bicarbonate, pH 8-9. Do not reconstitute to less than 0.1mg/ml. Further dilutions should be made with medium containing a carrier protein.
BIOLOGICAL ACTIVITY: Induces proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
USE/STABILITY: Reconstituted protein is stable for 4 weeks when stored at +4°C.
HANDLING: After reconstitution, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles.
General Information
Leptin, the product of the ob (obese) gene, is a 16kDa protein consisting of 146 amino acid residues. Leptin is produced in the adipose tissue, and is considered to play an important role in appetite control, fat metabolism and regulation of body weight. Studies have shown that it may also influence reproductive function. Mice with ob/ob genotype develop a form of diabetes similar to type II in humans.
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link 41160: Leptin (mouse) (precursor)
AfCS Signalling Gateway link A001397: Leptin (mouse)
General Literature References
Positional cloning of the mouse obese gene and its human homologue: Y. Zhang, et al.; Nature 372, 425 (1994) Abstract
Effects of the obese gene product on body weight regulation in ob/ob mice: M.A. Pelleymounter, et al.; Science 269, 540 (1995) Abstract
Leptin levels in human and rodent: measurement of plasma leptin and ob RNA in obese and weight-reduced subjects: M. Maffei, et al.; Nature Med. 1, 1155 (1995) Abstract
Weight-reducing effects of the plasma protein encoded by the obese gene: J.L. Halaas, et al.; Science 269, 543 (1995) Abstract
Further Categories Containing This Product:
Recombinant Proteins / Fusion Proteins
 
 
ALX-201-038 Revised 24-Jan-05
Caspase-3 (active) (human) (recombinant)
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PRODUCT LINE Cell Death / Apoptosis / Autophagy
PRODUCT CATEGORY Caspases
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ALX-201-038-C005   5 µg 255.00 USD Add To Cart
Product Specification
EC: 3.4.22.-
SOURCE/HOST: Produced in E. coli.
FORMULATION: Liquid. 5µg in 25µl of 50mM TRIS (pH 8.0) containing 100mM sodium chloride and 50mM imidazole.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
USE/STABILITY: Stable for at least one week when stored at +4°C.
HANDLING: Avoid freeze/thaw cycles.
Product Specific Literature References
[1] Biochemical characteristics of caspases-3, -6, -7 and -8: H.R. Stennicke & G.S. Salvesen; J. Biol. Chem. 272, 25719 (1997) Abstract; Full Text
General Information
When expressed in E. coli, caspase-3 spontaneously undergoes autoprocessing to yield the subunits characteristic of the active enzyme.
The rate of caspase-3 enzymatic hydrolysis can be measured by the release of AMC from the caspase substrate Ac-DEVD-AMC (Prod.No. ALX-260-031) as emission at 440nm and excitation at 380nm using a spectrofluorometer [1].
BACKGROUND/TECHNICAL INFORMATION
Enzyme Evaluation Protocol
This protocol is used to measure caspase enzyme activity [1]. The synthetic fluorogenic peptide Ac-DEVD-AMC (Prod. No. ALX-260-031) is used as the caspase enzyme substrate. The enzyme cleaves the substrate releasing the fluorescent AMC (7-amino-4-methylcoumarin). AMC release can be measured by spectrofluorometry using UV.

1. Add 20mM of Ac-DEVD-AMC (Prod. No. ALX-260-031) to 1ml of assay buffer (20mM PIPES, 100mM sodium chloride, 10mM DTT, 1mM EDTA, 0.1% (w/v) CHAPS, 10% sucrose, pH 7.2). Add the appropriate amount of  active caspase to the mixture (50ng/ml).
2. Incubate for 1 hour at 37°C.
3. Measure the AMC liberated from the Ac-DEVD-AMC using a spectrofluorometer with an excitation wavelength of 380nm and an emission wavelength of 440nm.

Note: Enzyme activity can also be measured using the caspase enzyme substrate Ac-DEVD-pNA (Prod. No. ALX-260-033) at 37°C in a spectromax at 405nm wavelength.

Swiss-Prot link P42574: Caspase-3 (human) (precursor)
AfCS Signalling Gateway link A000498: Caspase-3 (mouse)
Further Categories Containing This Product:
Recombinant Proteins / Fusion ProteinsEnzymes
 
 
ALX-201-039 Revised 24-Jan-05
Caspase-6 (active) (human) (recombinant)