Search: 1000 results found for "heparanase"

Description:

Heparin Sodium Porcine

Heparin, Porcine Heparin, Heparin Pig.

Product # :

PRO-2811

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Description

Heparin Sodium Porcine is a natural native protein.

Source

Porcine Mucosa.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Biological Activity

200IU/mg.

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Synonyms
Heparin, Porcine Heparin, Heparin Pig.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Heparin Sodium Porcine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heparin Sodium Porcine should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Heparin Sodium Porcine in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Heparin sodium, a highly sulfated glycosaminoglycan, has long been recognized for its pivotal role as an anticoagulant. In porcine systems, the study of Heparin Sodium takes on significance not only for its therapeutic applications in veterinary medicine but also for its potential translational impact on human health. This research embarks on an exploration of Heparin Sodium in porcine contexts, unraveling its structural intricacies, pharmacological attributes, and broader implications for health and biomedical interventions. By delving into the properties of Heparin Sodium in porcine models, scientists aim to deepen our understanding of its anticoagulant mechanisms, therapeutic potential, and the potential avenues for cross-species applications in healthcare.
Structural Insights into Porcine Heparin Sodium:
Porcine-derived Heparin Sodium, similar to its counterparts in other species, possesses a complex and highly sulfated structure. Understanding the nuances of its structure is fundamental for deciphering how Heparin Sodium interacts with antithrombin, leading to the inhibition of clotting factors and preventing the formation of blood clots. Structural insights contribute to optimizing its therapeutic efficacy.
Pharmacological Attributes and Anticoagulant Mechanisms:
Heparin Sodium's pharmacological attributes are central to its anticoagulant effects. In porcine systems, Heparin Sodium acts as an indirect anticoagulant by accelerating the activity of antithrombin, a natural inhibitor of clotting factors. Elucidating the specific mechanisms by which porcine Heparin Sodium modulates coagulation pathways contributes to refining its dosage and application in veterinary medicine.
Therapeutic Potential in Veterinary Medicine:
Porcine Heparin Sodium holds significant therapeutic potential in veterinary medicine, where clotting disorders and thrombotic events are prevalent. Understanding its pharmacokinetics, dosage requirements, and potential interactions with other drugs is crucial for optimizing its use in porcine healthcare. Additionally, exploring its safety profile in porcine models contributes to ensuring the well-being of animals under treatment.
Cross-Species Applications and Translational Insights:
Beyond its veterinary applications, porcine Heparin Sodium provides insights into potential cross-species applications, particularly in translational medicine. Understanding the similarities and differences in its anticoagulant mechanisms between porcine and human systems may open avenues for therapeutic innovations with relevance to both animal and human health.
Challenges and Future Directions:
While porcine Heparin Sodium presents opportunities for advancements in veterinary medicine and translational research, challenges persist. Fine-tuning its applications, addressing potential variations in its anticoagulant properties across different porcine breeds, and ensuring its safety and efficacy in diverse clinical scenarios are critical considerations for translational success.
Porcine Heparin Sodium emerges as a key player in the landscape of anticoagulation, offering a bridge between veterinary and translational medicine. Its structural insights, pharmacological attributes, and therapeutic potential in porcine systems contribute not only to veterinary care but also offer translational insights with implications for human health. As researchers continue to unravel the molecular intricacies of porcine Heparin Sodium, they not only deepen our understanding of anticoagulation in veterinary contexts but also pave the way for innovative biomedical applications, shaping the future of healthcare for both animals and humans.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant

NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.

Product # :

ENZ-384

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Description

NMNAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-279 a.a.) and having a molecular mass of 36 kDa. The NMNAT1 is fused to a 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NMNAT1 Human solution containing 20mM Tris pH-8, 0.1M NaCl, 1mM DTT, 1mM EDTA & 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.
Synonyms
NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMENS EKTEVVLLAC GSFNPITNMH LRLFELAKDY MNGTGRYTVV KGIISPVGDA YKKKGLIPAY HRVIMAELAT KNSKWVEVDT WESLQKEWKE TLKVLRHHQE KLEASDCDHQ QNSPTLERPG RKRKWTETQD SSQKKSLEPK TKAVPKVKLL CGADLLESFA VPNLWKSEDI TQIVANYGLI CVTRAGNDAQ KFIYESDVLW KHRSNIHVVN EWIANDISST KIRRALRRGQSIRYLVPDLV QEYIEKHNLY SSESEDRNAG VILAPLQRNT AEAKT.

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Description:

Acetyl-COA Acyltransferase Human Recombinant

ACAA, PTHIO, THIO.

Product # :

ENZ-251

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ACAA1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (27-424 a.a.) and having a molecular mass of 43.8 kDa. The ACAA1 is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ACAA1 1mg/ml protein solution contains 20mM Tris pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
ACAA1 is part of the thiolase family of enzymes and is takes part in lipid metabolism. ACAA1 enzyme is localized to the peroxisome and catalyzes the conversion of acyl-CoA and acetyl-CoA to 3-oxoacyl-CoA in the fatty acid oxidation pathway. ACAA1 shows high enzymatic activity in liver, kidney, intestine and white adipose tissue in rats. ACAA1 deficiency causes pseudo-Zellweger syndrome.
Synonyms
ACAA, PTHIO, THIO.
Physical Appearance
Sterile Filtered clear solution.
Stability
ACAA1 Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLSGAPQASA ADVVVVHGRR TAICRAGRGG FKDTTPDELL SAVMTAVLKD VNLRPEQLGD ICVGNVLQPG AGAIMARIAQ FLSDIPETVP LSTVNRQCSS GLQAVASIAG GIRNGSYDIG MACGVESMSL ADRGNPGNIT SRLMEKEKAR DCLIPMGITS ENVAERFGIS REKQDTFALA SQQKAARAQS KGCFQAEIVP VTTTVHDDKG TKRSITVTQD EGIRPSTTME GLAKLKPAFK KDGSTTAGNS SQVSDGAAAI LLARRSKAEE LGLPILGVLR SYAVVGVPPD IMGIGPAYAI PVALQKAGLT VSDVDIFEIN EAFASQAAYC VEKLRLPPEK VNPLGGAVAL GHPLGCTGAR QVITLLNELK RRGKRAYGVV SMCIGTGMGA AAVFEYPGN.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Chymotrypsinogen-B1, Human Recombinant

Product # :

ENZ-1016

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Description

Recombinant Human CTRB1 expressed in E.coli containing 245 amino acids having a Mw of 27kDa is purified by standard chromatography techniques.

Source

E.coli

Formulation

The Human CTRB1 was lyophilized without any additives.

Purity

Greater than 95% as determined by HPLC.

Biological Activity

1100 units/mg protein.
One unit is defined as the amount of enzyme that will hydrolyze 1.0 μmole of N-alpha-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 7.0 at 25°C.

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Introduction
Chymotrypsinogen-B1 (CTRB1) belongs to the serine protease family of enzymes and forms a main precursor of the pancreatic proteolytic enzymes. CTRB1 is located next to a related chymotrypsinogen gene. CTRB1 is a protein coding gene which encodes different isoforms which may undergo similar processing to generate the mature protein.
Physical Appearance
Sterile Filtered lyophilized powder.
Stability
Recombinant Human CTRB1 although stable at room temp for 1 week, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Human CTRB1 in 1ml 50mM HAc which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND ITLLKLATPA RFSQTVSAVC LPSADDDFPAGTLCATTGWG KTKYNANKTP DKLQQAALPL LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSDTCST SSPGVYARVTKLIPWVQKIL AAN.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Asparagine Synthetase Mouse Recombinant

Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.

Product # :

ENZ-1100

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Description

ASNS produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 567 amino acids (1-561a.a.) and having a molecular mass of 65.1 kDa.ASNS is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

ASNS protein solution ( 0.25mg/ml ) contains PBS (pH 7.4) and 40% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.
Synonyms
Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPDMRIPK NGIEKHLLRE TFEDCNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDEMMSA SQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK WINATDPSAR TLTHYKS AAK AHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Phosphoglycerate Mutase 2 Human Recombinant, Active

Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.

Product # :

ENZ-981

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Description

PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PGAM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 100units/mg, in which One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37C.

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Introduction
Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.
Synonyms
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK.

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Description:

Glutamic-Oxaloacetic Transaminase 1 Human Recombinant, Active

EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

Product # :

ENZ-1001

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Description

GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GOT1 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8.0, 2mM DTT, 0.1M NaCl & 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 50 units/mg, and is defined as the amount of enzyme that converts 1umole of a-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C.

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Introduction
GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.
Synonyms
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Pyrroline-5-Carboxylate Reductase 1 Human Recombinant

P5C, PRO3, P5CR 1, Pyrroline-5-Carboxylate Reductase 1 mitochondrial, ARCL2B, PYCR, PIG45, PP222, Proliferation-Inducing Protein 45.

Product # :

ENZ-035

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Description

PYCR1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-319a.a.) and having a molecular mass of 35.5kDa.PYCR1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PYCR1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl Buffer (pH 8.5) and 10% Glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
PYCR1 is a universal housekeeping enzyme which catalyzes the NAD(P)H-dependent conversion of pyrroline-5-carboxylate to proline. PYCR1 enzyme also takes a physiologic part in the generation of NADP(+) in certain cell types. PYCR1 forms a homopolymer and localizes to the mitochondrion. Mutations in PYCR1 are the source of cutis laxa autosomal recessive type 2B (ARCL2B).
Synonyms
P5C, PRO3, P5CR 1, Pyrroline-5-Carboxylate Reductase 1 mitochondrial, ARCL2B, PYCR, PIG45, PP222, Proliferation-Inducing Protein 45.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV KLTPHNKETV QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT ISSIEKKLSA FRPAPRVIRC MTNTPVVVRE GATVYATGTH AQVEDGRLME QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH ALHVLESGGF RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL SPSGHTKLLP RSLAPAGKD

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Branched Chain Amino-Acid Transaminase 1 Human Recombinant

Branched chain amino-acid transaminase 1 cytosolic, BCT1, BCATC, Protein ECA39, placental protein 18, PP18, PNAS121, MECA39, EC 2.6.1.42.

Product # :

ENZ-597

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Description

BCAT1 Recombinant produced in E. coli is a single polypeptide chain containing 409 amino acids (1-386) and having a molecular mass of 45.4kDa.BCAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The BCAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
BCAT1 catalyzes the leading reaction in the catabolism of the indispensable branched chain amino acids isoleucine, leucine and valine.
Synonyms
Branched chain amino-acid transaminase 1 cytosolic, BCT1, BCATC, Protein ECA39, placental protein 18, PP18, PNAS121, MECA39, EC 2.6.1.42.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKDCSNG CSAECTGEGG SKEVVGTFKA KDLIVTPATI LKEKPDPNNL VFGTVFTDHM LTVEWSSEFG WEKPHIKPLQ NLSLHPGSSA LHYAVELFEG LKAFRGVDNK IRLFQPNLNM DRMYRSAVRA TLPVFDKEEL LECIQQLVKL DQEWVPYSTS ASLYIRPTFI GTEPSLGVKK PTKALLFVLL SPVGPYFSSG TFNPVSLWAN PKYVRAWKGG TGDCKMGGNY GSSLFAQCEA VDNGCQQVLW LYGEDHQITE VGTMNLFLYW INEDGEEELA TPPLDGIILP GVTRRCILDL AHQWGEFKVS ERYLTMDDLT TALEGNRVRE MFGSGTACVV CPVSDILYKG ETIHIPTMEN GPKLASRILS KLTDIQYGRE ESDWTIVLS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fatty Acid Amide Hydrolase 2 Human Recombinant

Fatty acid amide hydrolase 2, AMDD, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2.

Product # :

ENZ-777

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Description

FAAH2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 524 amino acids (32-532a.a) and having a molecular mass of 57.4kDa. FAAH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FAAH2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Fatty Acid Amide Hydrolase 2 (FAAH2) shares a conserved protein motif with the amidase signature family of enzymes. FAAH2 catalyzes the hydrolysis of a broad range of bioactive lipids, including those from the 3 main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. FAAH2 is also degrades bioactive fatty acid amides to their corresponding acids, thus helping to end the signaling functions of these molecules. FAAH2 prefers monounsaturated acyl chains as a substrate.
Synonyms
Fatty acid amide hydrolase 2, AMDD, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGGPKFAS KTPRPVTEPL LLLSGMQLAK LIRQRKVKCI DVVQAYINRI KDVNPMINGI VKYRFEEAMK EAHAVDQKLA EKQEDEATLE NKWPFLGVPL TVKEAFQLQG MPNSSGLMNR RDAIAKTDAT VVALLKGAGA IPLGITNCSE LCMWYESSNK IYGRSNNPYD LQHIVGGSSG GEGCTLAAAC SVIGVGSDIG GSIRMPAFFN GIFGHKPSPG VVPNKGQFPL AVGAQELFLC TGPMCRYAED LAPMLKVMAG PGIKRLKLDT KVHLKDLKFY WMEHDGGSFL MSKVDQDLIM TQKKVVVHLE TILGASVQHV KLKKMKYSFQ LWIAMMSAKG HDGKEPVKFV DLLGDHGKHV SPLWELIKWC LGLSVYTIPS IGLALLEEKL RYSNEKYQKF KAVEESLRKE LVDMLGDDGV FLYPSHPTVA PKHHVPLTRP FNFAYTGVFS ALGLPVTQCP LGLNAKGLPL GIQVVAGPFN DHLTLAVAQY LEKTFGGWVC PGKF.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Gamma-Glutamyl Hydrolase Human Recombinant

Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.

Product # :

ENZ-242

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Description

GGH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (25-318) and having a molecular mass of 35.9kDa.GGH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GGH solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
GGH is a homodimeric protein which catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates. GGH is a vital enzyme in folyl and antifolyl poly-gamma-glutamate metabolism and it has a significant part in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of antifolates and pteroylpolyglutamates.
Synonyms
Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRPHGDTAKK PIIGILMQKC RNKVMKNYGR YYIAASYVKY LESAGARVVP VRLDLTEKDY EILFKSINGI LFPGGSVDLR RSDYAKVAKI FYNLSIQSFD DGDYFPVWGT CLGFEELSLL ISGECLLTAT DTVDVAMPLN FTGGQLHSRM FQNFPTELLL SLAVEPLTAN FHKWSLSVKN FTMNEKLKKF FNVLTTNTDG KIEFISTMEG YKYPVYGVQW HPEKAPYEWK NLDGISHAPN AVKTAFYLAE FFVNEARKNN HHFKSESEEE KALIYQFSPI YTGNISSFQQ CYIFD

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glyoxylate Reductase/Hydroxypyruvate Reductase Human Recombinant

EC 1.1.1.79, GLXR, GLYD, GRHPR, PH2.

Product # :

ENZ-521

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Description

GRHPR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-328 a.a.) and having a molecular mass of 37.8 kDa. The GRHPR is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GRHPR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 5mM DTT and 0.2M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GRHPR located in the cytosol, belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family of proteins. GRHPR is widely expressed in liver. GRHPR has widespread tissue expression and is involved in metabolism. GRHPR is an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities.
Synonyms
EC 1.1.1.79, GLXR, GLYD, GRHPR, PH2.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA GAHGLLCLLS DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV GYTPDVLTDT TAELAVSLLL TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF LYTGRQPRPE EAAEFQAEFV STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF INISRGDVVN QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR TRNTMSLLAA NNLLAGLRGE PMPSELKL.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Ribulose-5-Phosphate-3-Epimerase Human Recombinant

Ribulose-phosphate 3-epimerase, Ribulose-5-phosphate-3-epimerase, RPE, HUSSY-17, RPE2-1.

Product # :

ENZ-584

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Description

RPE Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-228) and having a molecular mass of 27.5kDa.RPE is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RPE solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 30% glycerol and 200mM NaCl.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Ribulose-phosphate 3-epimerase (RPE) is a member of the ribulose-phosphate 3-epimerase family. RPE is the enzyme which converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. Therefore, the RPE enzyme has one substrate, D-ribulose 5-phosphate, and one product, D-xylulose 5-phosphate. RPE participates in three metabolic pathways: pentose phosphate pathway, pentose and glucuronate interconversions, and carbon fixation.
Synonyms
Ribulose-phosphate 3-epimerase, Ribulose-5-phosphate-3-epimerase, RPE, HUSSY-17, RPE2-1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMASGCK IGPSILNSDL ANLGAECLRM LDSGADYLHL DVMDGHFVPN ITFGHPVVES LRKQLGQDPF FDMHMMVSKP EQWVKPMAVA GANQYTFHLE ATENPGALIK DIRENGMKVG LAIKPGTSVE YLAPWANQID MALVMTVEPG FGGQKFMEDM MPKVHWLRTQ FPSLDIEVDG GVGPDTVHKC AEAGANMIVS GSAIMRSEDP RSVINLLRNV CSEAAQKRSL DR.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Carbonic Anhydrase XIV Human Recombinant

Carbonic anhydrase 14, Carbonate dehydratase XIV, Carbonic anhydrase XIV, CA-XIV, CA14, CAXiV.

Product # :

ENZ-761

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Description

CA14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (16-290 a.a.) and having a molecular mass of 33.2kDa. CA14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CA14 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
CA14 is a part of the Carbonic anhydrases family. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They present wide variety in tissue distribution and in their subcellular localization. CA14 is a type I membrane protein which shares highest sequence similarity with the other transmembrane CA isoform, CA XII. Nevertheless, they have different patterns of tissue-specific expression and therefore take different physiologic parts.
Synonyms
Carbonic anhydrase 14, Carbonate dehydratase XIV, Carbonic anhydrase XIV, CA-XIV, CA14, CAXiV.
Physical Appearance
Sterile Filtered colorless solution.
Stability
NPL Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSADGGQHW TYEGPHGQDH WPASYPECGN NAQSPIDIQT DSVTFDPDLP ALQPHGYDQP GTEPLDLHNN GHTVQLSLPS TLYLGGLPRK YVAAQLHLHW GQKGSPGGSE HQINSEATFA ELHIVHYDSD SYDSLSEAAE RPQGLAVLGI LIEVGETKNI AYEHILSHLH EVRHKDQKTS VPPFNLRELL PKQLGQYFRY NGSLTTPPCY QSVLWTVFYR RSQISMEQLE KLQGTLFSTE EEPSKLLVQN YRALQPLNQR MVFASFIQAG SSYTTGEM.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cathepsin-Z Human Recombinant

Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.

Product # :

ENZ-748

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Description

CTSZ Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (62-303) and having a molecular mass of 29.5kDa.CTSZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CTSZ solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.
Synonyms
Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLPKSWDW RNVDGVNYAS ITRNQHIPQY CGSCWAHAST SAMADRINIK RKGAWPSTLL SVQNVIDCGN AGSCEGGNDL SVWDYAHQHG IPDETCNNYQ AKDQECDKFN QCGTCNEFKE CHAIRNYTLW RVGDYGSLSG REKMMAEIYA NGPISCGIMA TERLANYTGG IYAEYQDTTY INHVVSVAGW GISDGTEYWI VRNSWGEPWG ERGWLRIVTS TYKDGKGARY NLAIEEHCTF GDPIV.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Acetylcholinesterase Human Recombinant

AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6

Product # :

ENZ-1174

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Description

ACHE Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (32-614 a.a) containing a total of 592 amino acids, having a molecular mass of 65.6 kDa. ACHE is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The ACHE solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 6,000 nmol/min/ug. Defined by the amount of enzyme that cleaves 1 nmole of acetylthiocholine per minute at pH 7.5 at 25˚C.

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Introduction
Acetylcholinesterase (ACHE) belongs to the type-B carboxylesterase/lipase family. ACHE catalyzes the breakdown of acetylcholine and other choline esters that play a role as neurotransmitters. During neurotransmission, ACH is released from the presynaptic neuron into the synaptic cleft and binds ACH receptors on the post-synaptic membrane, transmitting the signal from the nerve. ACHE is located on the post-synaptic membrane, terminates the signal transmission by hydrolyzing ACH.
Synonyms
AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSEGREDAE LLVTVRGGRL RGIRLKTPGG PVSAFLGIPF AEPPMGPRRF LPPEPKQPWS GVVDATTFQS VCYQYVDTLY PGFEGTEMWN PNRELSEDCL YLNVWTPYPR PTSPTPVLVW IYGGGFYSGA SSLDVYDGRF LVQAERTVLV SMNYRVGAFG FLALPGSREA PGNVGLLDQR LALQWVQENV AAFGGDPTSV TLFGESAGAA SVGMHLLSPP SRGLFHRAVL QSGAPNGPWA TVGMGEARRR ATQLAHLVGC PPGGTGGNDT ELVACLRTRP AQVLVNHEWH VLPQESVFRF SFVPVVDGDF LSDTPEALIN AGDFHGLQVL VGVVKDEGSY FLVYGAPGFS KDNESLISRA EFLAGVRVGV PQVSDLAAEA VVLHYTDWLH PEDPARLREA LSDVVGDHNV VCPVAQLAGR LAAQGARVYA YVFEHRASTL SWPLWMGVPH GYEIEFIFGI PLDPSRNYTA EEKIFAQRLM RYWANFARTG DPNEPRDPKA PQWPPYTAGA QQYVSLDLRP LEVRRGLRAQ ACAFWNRFLP KLLSATDTLD EAERQWKAEF HRWSSYMVHW KNQFDHYSKQ DRCSDLHHHH HH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

N-Acetylgalactosaminidase Alpha Human Recombinant

Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.

Product # :

ENZ-963

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Description

NAGA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 400 amino acids (18-411) and having a molecular mass of 45.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NAGA is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NAGA protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
N-Acetylgalactosaminidase Alpha (NAGA) is a lysosomal exoglycosidase which removes terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids. NAGA is necessary for the breakdown of glycolipids.
Synonyms
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
LDNGLLQTPP MGWLAWERFR CNINCDEDPK NCISEQLFME MADRMAQDGW RDMGYTYLNI DDCWIGGRDA SGRLMPDPKR FPHGIPFLAD YVHSLGLKLG IYADMGNFTC MGYPGTTLDK VVQDAQTFAE WKVDMLKLDG CFSTPEERAQ GYPKMAAALN ATGRPIAFSC SWPAYEGGLP PRVNYSLLAD ICNLWRNYDD IQDSWWSVLS ILNWFVEHQD ILQPVAGPGH WNDPDMLLIG NFGLSLEQSR AQMALWTVLA APLLMSTDLR TISAQNMDIL QNPLMIKINQ DPLGIQGRRI HKEKSLIEVY MRPLSNKASA LVFFSCRTDM PYRYHSSLGQ LNFTGSVIYE AQDVYSGDII SGLRDETNFT VIINPSGVVM WYLYPIKNLE MSQQHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Coagulation Factor-VIII Human Recombinant

Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.

Product # :

PRO-318

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Description

Antihemophilic Facor Human Recombinant produced in CHO is a glycosylated polypeptide chain having 2332 amino acids. The Factor-VIII is purified by proprietary chromatographic techniques.

Source

CHO cells (Chinese Hamster Ovarian Cells).

Formulation

Each 250IU vial was lyophilized from a solution containing 8mg Tween-80, 112mM NaCl, 40mg Mannitol, 10mg Trehalose, 1ng VWF and 4.2mM CaCl2.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The specific activity was found to be 7,058 IU/mg.

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Introduction
Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
Synonyms
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Factor-VIII although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-VIII should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute 250IU lyophilized Factor-VIII in 5ml sterile 18M-cm H2O, which can then be further diluted to other aqueous solutions.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Isocitrate Dehydrogenase-1 Human Recombinant

Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

Product # :

ENZ-193

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Description

IDH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 434 amino acids (1-414) and having a molecular mass of 48.8 kDa.IDH1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The IDH1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl,
1mM DTT, 0.1mM PMSF and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

The Specific activity is > 0.7 units/ml. One unit will convert 1.0 umole of isocitrate to alpha-ketoglutarate per minute at pH7.5 at 25C.

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Introduction
Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.
Synonyms
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKHNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPSD GTQKVTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK ELAFFANALE EVSIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKIKLA QAKL

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

DBH Human Recombinant

EC 1.14.17.1, DBM, DBH.

Product # :

ENZ-891

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Description

DBH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 599 amino acids (40-617 a.a) and having a molecular mass of 67.2kDa.DBH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DBH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
DBH catalyzes the chemical reaction. DBH is an oxidoreductase which belongs to the copper type II, ascorbate-dependent monooxygenase family, in particular those performing on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated can not be derived from O2 with reduced ascorbate as one donor, as well as incorporation of one ato of oxygen into the other donor.
Synonyms
EC 1.14.17.1, DBM, DBH.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSAPRESPLP YHIPLDPEGS LELSWNVSYT QEAIHFQLLV RRLKAGVLFG MSDRGELENA DLVVLWTDGD TAYFADAWSD QKGQIHLDPQ QDYQLLQVQR TPEGLTLLFK RPFGTCDPKD YLIEDGTVHL VYGILEEPFR SLEAINGSGL QMGLQRVQLL KPNIPEPELP SDACTMEVQA PNIQIPSQET TYWCYIKELP KGFSRHHIIK YEPIVTKGNE ALVHHMEVFQ CAPEMDSVPH FSGPCDSKMK PDRLNYCRHV LAAWALGAKA FYYPEEAGLA FGGPGSSRYL RLEVHYHNPL VIEGRNDSSG IRLYYTAKLR RFNAGIMELG LVYTPVMAIP PRETAFILTG YCTDKCTQLA LPPSGIHIFA SQLHTHLTGR KVVTVLVRDG REWEIVNQDN HYSPHFQEIR MLKKVVSVHP GDVLITSCTY NTEDRELATV GGFGILEEMC VNYVHYYPQT QLELCKSAVD AGFLQKYFHL INRFNNEDVC TCPQASVSQQ FTSVPWNSFN RDVLKALYSF APISMHCNKS SAVRFQGEWN LQPLPKVIST LEEPTPQCPT SQGRSPAGPT VVSIGGGKG

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Branched Chain Amino-Acid Transaminase 2 Human Recombinant

Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.

Product # :

ENZ-606

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Description

BCAT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (28-392) and having a molecular mass of 43.9kDa.BCAT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The BCAT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 10% glycerol, 0.2M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Branched Chain Amino-Acid Transaminase 2 (BCAT2) is a member of the class-IV pyridoxal-phosphate-dependent aminotransferase family. BCAT2 is a branched chain aminotransferase found in mitochondria. BCAT2 forms a dimer which catalyzes the first step in the production of the branched chain amino acids leucine, isoleucine, and valine. In addition, BCAT2 may actn as a transporter of branched chain alpha-keto acids.
Synonyms
Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMASSSF KAADLQLEMT QKPHKKPGPG EPLVFGKTFT DHMLMVEWND KGWGQPRIQP FQNLTLHPAS SSLHYSLQLF EGMKAFKGKD QQVRLFRPWL NMDRMLRSAM RLCLPSFDKL ELLECIRRLI EVDKDWVPDA AGTSLYVRPV LIGNEPSLGV SQPTRALLFV ILCPVGAYFP GGSVTPVSLL ADPAFIRAWV GGVGNYKLGG NYGPTVLVQQ EALKRGCEQV LWLYGPDHQL TEVGTMNIFV YWTHEDGVLE LVTPPLNGVI LPGVVRQSLL DMAQTWGEFR VVERTITMKQ LLRALEEGRV REVFGSGTAC QVCPVHRILY KDRNLHIPTM ENGPELILRF QKELKEIQYG IRAHEWMFPV.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Xylosyltransferase 2 Human Recombinant

Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.

Product # :

ENZ-1086

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

XYLT2 Human Recombinant is a single, glycosylated polypeptide chain containing 839 amino acids (Gly37-Arg865, luminal domain, isoform 1, natural variant with Thr305) and having a molecular mass of 94.0kDa. XYLT2 is fused to an N-terminal linker (2 extra a.a), C-terminal linker (2 extra a.a) and C-terminal His-tag (6 extra a.a).

Source

HEK293 Cells.

Formulation

XYLT2 filtered (0.4 µm) and lyophilized in 0.05 M PBS and 0.075 M NaCl, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
XYLT2 or Xylosyltransferase 2 is an enzyme which is expressed in ubiquitous and is part of the glycosyltransfe-rases family. XYLT2 promotes proteoglycans formation by attaching GAG chains to the substrate protein via transfer of xylose molecule from the donor (nucleoside diphosphate) to the protein’s serine residues. XYLT2 is present in the ER and the cis part of the Golgi, furthermore the protein is released to the extracellular matrix.
Synonyms
Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. XYLT2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
ASGLEEDEAG EKGRQRKPRP LDPGEGSKDT DSSAGRRGST GRRHGRWRGR AESPGVPVAK VVRAVTSRQR ASRRVPPAPP PEAPGRQNLS GAAAGEALVG AAGFPPHGDT GSVEGAPQPT DNGFTPKCEI VGKDALSALA RASTKQCQQE IANVVCLHQA GSLMPKAVPR HCQLTGKMSP GIQWDESQAQ QPMDGPPVRI AYMLVVHGRA IRQLKRLLKA VYHEQHFFYI HVDKRSDYLH REVVELAQGY DNVRVTPWRM VTIWGGASLL TMYLRSMRDL LEVPGWAWDF FINLSATDYP TRTNEELVAF LSKNRDKNFL KSHGRDNSRF IKKQGLDRLF HECDSHMWRL GERQIPAGIV VDGGSDWFVL TRSFVEYVVY TDDPLVAQLR QFYTYTLLPA ESFFHTVLEN SLACETLVDN NLRVTNWNRK LGCKCQYKHI VDWCGCSPND FKPQDFLRLQ QVSRPTFFAR KFESTVNQEV LEILDFHLYG SYPPGTPALK AYWENTYDAA DGPSGLSDVM LTAYTAFARL SLHHAATAAP PMGTPLCRFE PRGLPSSVHL YFYDDHFQGY LVTQAVQPSA QGPAETLEMW LMPQGSLKLL GRSDQASRLQ SLEVGTDWDP KERLFRNFGG LLGPLDEPVA VQRWARGPNL TATVVWIDPT YVVATSYDIT VDTETEVTQY KPPLSRPLRP GPWTVRLLQF WEPLGETRFL VLPLTFNRKL PLRKDDASWL HAGPPHNEYM EQSFQGLSSI LNLPQPELAE EAAQRHTQLT GPALEAWTDR ELSSFWSVAG LCAIGPSPCP SLEPCRLTSW SSLSPDPKSE LGPVKADGRL RKLHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Thiamine Triphosphatase Human Recombinant

MGC2652, THTP, THTPASE.

Product # :

ENZ-249

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
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Description

Recombinant Human THTPA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230 a.a.) and having a molecular mass of 27.7 kDa. THTPA is fused to a 20 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

The THTPA 1mg/ml protein solution contains 20mM Tris-HCL buffer, pH-8, 1mM DTT and 10% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
THTPA enzyme is part of the THTPase family. THTPA is localized to the cytoplasm and expressed at small quantities in a variety of tissues, including testis, uterus, prostate, bladder, lung and kidney. THTPA is a hydrolase that catalyzes the H2O-dependent hydrolysis of thiamine triphosphate (THTP) to thiamine diphosphate (THDP), the main form of thiamine within the cell. THTPA occurs as a monomer and is activated at an optimal pH of 8.5.
Synonyms
MGC2652, THTP, THTPASE.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store THTPA at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA DHWLRRREDS GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG LGAGDVAAVL GPLGLQEVAS FVTKRSAWKL VLLGADEEEP QLRVDLDTAD FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Nei Endonuclease VIII-Like 1 Human Recombinant

Endonuclease 8-like 1, DNA glycosylase/AP lyase Neil1, DNA-(apurinic or apyrimidinic site) lyase Neil1, Endonuclease VIII-like 1, FPG1, Nei homolog 1, NEH1, Nei-like protein 1, NEIL1, NEI1, hFPG1.

Product # :

ENZ-220

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
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Description

NEIL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (1-390) and having a molecular mass of 45.8kDa.NEIL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NEIL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
NEIL1 is a member of a class of DNA glycosylases homologous to the bacterial Fpg/Nei family. These glycosylases initiate the first step in base excision repair by cleaving bases damaged by reactive oxygen species and introducing a DNA strand break via the associated lyase reaction. NEIL1 participates in the DNA repair pathway by initiating base excision repair by removing damaged bases, primarily oxidized pyrimidines.
Synonyms
Endonuclease 8-like 1, DNA glycosylase/AP lyase Neil1, DNA-(apurinic or apyrimidinic site) lyase Neil1, Endonuclease VIII-like 1, FPG1, Nei homolog 1, NEH1, Nei-like protein 1, NEIL1, NEI1, hFPG1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPEGPELHLA SQFVNEACRA LVFGGCVEKS SVSRNPEVPF ESSAYRISAS ARGKELRLIL SPLPGAQPQQ EPLALVFRFG MSGSFQLVPR EELPRHAHLR FYTAPPGPRL ALCFVDIRRF GRWDLGGKWQ PGRGPCVLQE YQQFRENVLR NLADKAFDRP ICEALLDQRF FNGIGNYLRA EILYRLKIPP FEKARSVLEA LQQHRPSPEL TLSQKIRTKL QNPDLLELCH SVPKEVVQLG GKGYGSESGE EDFAAFRAWL RCYGMPGMSS LQDRHGRTIW FQGDPGPLAP KGRKSRKKKS KATQLSPEDR VEDALPPSKA PSRTRRAKRD LPKRTATQRP EGTSLQQDPE APTVPKKGRR KGRQAASGHC RPRKVKADIP SLEPEGTSAS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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