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1000 results found for “nuclease”
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Name :
Urokinase HumanDescription:
Urokinase Human
Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.
Product # :
ENZ-264Price :
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Shipped at Room temp
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Description
Urokinase is a two-chain glycoprotein containing 411 amino acids with 12 disulfide bonds. Its molecular weight is 54,000 Dalton.
Source
Human urine.
Formulation
The Urokinase was lyophilized from a concentrated (1mg/ml) solution containing phosphate buffer.
Purity
Greater than 90.0%.
Citations
More Info
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Introduction
Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
It can be obtained from human urine or kidney cell culture. -
Synonyms
Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Urokinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Urokinase should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Urokinase in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Contaminants
Free of: Hepatitis B surface antigen, Hepatitis C antibody and HIV I and II.
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Specific Activity
187,973IU/mg.
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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Name :
AMPD2 HumanDescription:
AMPD2 Human Recombinant
(Isoform L), EC 3.5.4.6, SPG63, AMP Deaminase Isoform L, AMP Deaminase 2, AMPD Isoform L, AMPD, PCH9, AMP deaminase 2.
Product # :
ENZ-835Price :
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Description
AMPD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 667 amino acids (236-879 a.a) and having a molecular mass of 77.0kDa. AMPD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AMPD2 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 85% as determined by Analysis by SDS-PAGE.
Citations
More Info
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Introduction
AMPD2 is significant in purine metabolism by converting AMP to IMP. AMPD2 which functions as a homotetramer, is one of the three AMP deaminases shown in mammals. More than a few transcript variants encoding differentisoforms have been discovered for AMPD2.
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Synonyms
(Isoform L), EC 3.5.4.6, SPG63, AMP Deaminase Isoform L, AMP Deaminase 2, AMPD Isoform L, AMPD, PCH9, AMP deaminase 2.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDLLDAAK SVVRALFIRE KYMALSLQSF CPTTRRYLQQ LAEKPLETRT YEQGPDTPVS ADAPVHPPAL EQHPYEHCEP STMPGDLGLG LRMVRGVVHV YTRREPDEHC SEVELPYPDL QEFVADVNVL MALIINGPIK SFCYRRLQYL SSKFQMHVLL NEMKELAAQK KVPHRDFYNI RKVDTHIHAS SCMNQKHLLR FIKRAMKRHL EEIVHVEQGR EQTLREVFES MNLTAYDLSV DTLDVHADRN TFHRFDKFNA KYNPIGESVL REIFIKTDNR VSGKYFAHII KEVMSDLEES KYQNAELRLS IYGRSRDEWD KLARWAVMHR VHSPNVRWLV QVPRLFDVYR TKGQLANFQE MLENIFLPLF EATVHPASHP ELHLFLEHVD GFDSVDDESK PENHVFNLES PLPEAWVEED NPPYAYYLYY TFANMAMLNH LRRQRGFHTF VLRPHCGEAG PIHHLVSAFM LAENISHGLL LRKAPVLQYL YYLAQIGIAM SPLSNNSLFL SYHRNPLPEY LSRGLMVSLS TDDPLQFHFT KEPLMEEYSI ATQVWKLSSC DMCELARNSV LMSGFSHKVK SHWLGPNYTK EGPEGNDIRR TNVPDIRVGY RYETLCQELA LITQAVQSEM LETIPEEAGI TMSPGPQ.
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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Name :
MMP2 HumanDescription:
Matrix Metalloproteinase-2 Human Recombinant
kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
Product # :
ENZ-769Price :
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Description
MMP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 576 amino acids (110-660a.a) and having a molecular mass of 64.7kDa. MMP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Matrix metalloproteinase-2 (MMP-2) is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).
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Synonyms
kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFYNFFP RKPKWDKNQI TYRIIGYTPD LDPETVDDAF ARAFQVWSDV TPLRFSRIHD GEADIMINFG RWEHGDGYPF DGKDGLLAHA FAPGTGVGGD SHFDDDELWT LGEGQVVRVK YGNADGEYCK FPFLFNGKEY NSCTDTGRSD GFLWCSTTYN FEKDGKYGFC PHEALFTMGG NAEGQPCKFP FRFQGTSYDS CTTEGRTDGY RWCGTTEDYD RDKKYGFCPE TAMSTVGGNS EGAPCVFPFT FLGNKYESCT SAGRSDGKMW CATTANYDDD RKWGFCPDQG YSLFLVAAHE FGHAMGLEHS QDPGALMAPI YTYTKNFRLS QDDIKGIQEL YGASPDIDLG TGPTPTLGPV TPEICKQDIV FDGIAQIRGE IFFFKDRFIW RTVTPRDKPM GPLLVATFWP ELPEKIDAVY EAPQEEKAVF FAGNEYWIYS ASTLERGYPK PLTSLGLPPD VQRVDAAFNW SKNKKTYIFA GDKFWRYNEV KKKMDPGFPK LIADAWNAIP DNLDAVVDLQ GGGHSYFFKG AYYLKLENQS LKSVKFGSIK SDWLGC.
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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Name :
Pfu DNA PolymeraseDescription:
Pfu-DNA Polymerase Recombinant
DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.
Product # :
ENZ-265Price :
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Description
Pfu DNA Polymerase is a thermo-stable enzyme having a Mw of about 90kDa. Pfu DNA Polymerase is derived from E. coli that and cloned from Pyrococcus furiosus strain Vc1 DSM3638. Pfu DNA Polymerase replicates DNA at 75°C, catalyzing the polymerization of nucleotides into duplex DNA in the 5´ to 3´ direction in the existence of magnesium. Pfu DNA Polymerase possesses 3´ to 5´ exonuclease (proofreading) activity. Base misinsertions that take place during polymerization are swiftly removed by the proofreading activity of the polymerase. Therefore, Pfu DNA Polymerase is suggested for use in PCR and primer extension reactions that require high-fidelity synthesis. Pfu DNA Polymerase-generated PCR fragments are blunt-ended.
Source
Escherichia Coli.
Formulation
50mM Tris-HCl, pH 8.2, 1mM DTT, 0.1mM EDTA, 0.05% CHAPS and 50% glycerol.
Citations
More Info
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Introduction
Pfu DNA polymeraseenzyme is found in the hyperthermophilic archaeonPyrococcus furiosus, where it functions in vivoto replicate the organism's DNA. In vitro, Pfu is used to swiftly amplify DNAin the Polymerase Chain Reaction, where the enzyme serves the central function of copying a new strand of DNA during each extension step. Pfu DNA polymerase has superior thermostability and 'proofreading' properties compared to other thermostable polymerases. Unlike Taq DNA polymerase, Pfu DNA polymerase possesses 3' to 5' exonuclease proof reading activity, meaning that it works its way along the DNA from the 5' endto the 3' endand corrects nucleotidemisin corporation errors. Pfu DNA polymerase-generated PCRfragments will have fewer errors than Taq-generated PCR inserts. As a result, Pfu is more commonly used for molecular cloning of PCR fragments than the historically popular Taq. Pfu DNA polymerase is superior for techniques that require high-fidelity DNA synthesis, but can also be used in conjunction with Taq polymerase to obtain the fidelity of Pfu with the speed of Taq polymerase activity.
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Synonyms
DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.
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Physical Appearance
Sterile liquid formulation.
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Stability
Pfu DNA Polymerase although stable at 10°C for 5 days, should be stored below -18°C.Please prevent freeze-thaw cycles.
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Applications
1. Ideal for high-fidelity amplification.
2. 3'-5' exonuclease activity provides a low error rate.
3. One of the most thermostable DNA polymerases known.
4. Lack of extendase activity means no unwanted 3’ overhangs.
5. Optimal for blunt-end PCR cloning.
6. Optimum temperature near 75°C.
7. 95% active after 1-hour incubation at 98°C. -
PCR Protocol
Add the following components to amplify 1kb DNA template: 0.2µl Pfu-DNA Polymerase.4µl 2.5mM dNTPs.5µl 10x buffer with MgSO4. 1µl Primers mix (10µM each).1µl Template.38µl ddH2O. Amplify using the following cycling parameters: Heat Soak: 1 cycle at 94°C/4 min.Denaturation: 30 cycles at 94°C/30 sec.Annealing: 30 cycles at 55°C /30 sec.Extension: 30 cycles at 72°C /90 sec. Final: 1 cycle at 72°C /5 min.
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Unit Definition
1U of enzyme catalyzes the incorporation of 10nmol of dNTP into acid-insoluble product in 30 minutes at 75°C.
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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Name :
CES2E MouseDescription:
Carboxylesterase 2E Mouse Recombinant
9030624L02Rik, Ces5, Ces2e.
Product # :
ENZ-1141Price :
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Description
CES2E Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids ( 27-559 aa) and having a molecular mass of 60.5kDa.CES2E is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CES2E solution (0.25 mg/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 > 30unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0 umole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 25C˚.
Citations
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Introduction
Carboxylesterase 2E or CES2E is an enzyme that hydrolyzes various carboxylic acid esters. This enzyme can be found mainly in mammalian liver cells. CES2E is taking part in chemical reactions, especially in carboxylic ester and water catalyzation to alcohol & carboxylate.
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Synonyms
9030624L02Rik, Ces5, Ces2e.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
QDSASPIRNT HTGQVRGSLV HVKDTDIAVH TFLGIPFAKP PVGPLRFAPP EAPEPWSGVR DGTSHPNMCL QNDNLMGSED LKMMNLILPP ISMSEDCLYL NIYVPAHAHE GSNLPVMVWI HGGALTVGMA SMYDGSMLAA TEDVVVVAIQ YRLGVLGFFS TGDQHAKGNW GYLDQVAALR WVQQNIVHFG GNPDRVTIFG ESAGGTSVSS HVVSPMSQGL FHGAIMESGV AVLPDLISSS
SEMVHRIVAN LSGCAAVNSE TLMCCLRGKN EAEMLAINKV FKIIPGVVDG EFLPKHPQEL MASKDFHPVP SIIGINNDEY GWILPTIMDP AQKIEEITRK TLPAVLKSTA LKMMLPPECG DLLMEEYMGD TEDPETLQAQ FREMKGDFMF VIPALQVAHF QRSHAPVYFY EFQHRPSFFK DFRPPYVKAD HGDEIFLVFG YQFGNIKLPY TEEEEQLSRR IMKYWANFAR HGNPNSEGLP YWPVMDHDEQ YLQLDIQPSV GRALKARRLQ FWTKTLPQKI QELKGSQERH KELLEHHHHH H
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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Name :
POLR3F HumanDescription:
Polymerase III Polypeptide F Human Recombinant
DNA-directed RNA polymerase III subunit RPC6, RNA polymerase III subunit C6, DNA-directed RNA polymerase III subunit F, RNA polymerase III 39 kDa subunit, RPC39, POLR3F, RPC6.
Product # :
ENZ-650Price :
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Description
POLR3F Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-316) and having a molecular mass of 38.1kDa.POLR3F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The POLR3F solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Polymerase III Polypeptide F (POLR3F) is a member of the eukaryotic RPC34/RPC39 RNA polymerase subunit family. POLR3F is DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. POLR3F is one of many subunits forming eukaryotic RNA polymerase III (RNA Pol III), which transcribes 5S ribosomal RNA and tRNA genes. POLR3F binds both TFIIIB90 and TBP, 2 subunits of RNA polymerase III transcription initiation factor IIIB (TFIIIB).
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Synonyms
DNA-directed RNA polymerase III subunit RPC6, RNA polymerase III subunit C6, DNA-directed RNA polymerase III subunit F, RNA polymerase III 39 kDa subunit, RPC39, POLR3F, RPC6.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAEVKVK VQPPDADPVE IENRIIELCH QFPHGITDQV IQNEMPHIEA QQRAVAINRL LSMGQLDLLR SNTGLLYRIK DSQNAGKMKG SDNQEKLVYQ IIEDAGNKGI WSRDIRYKSN LPLTEINKIL KNLESKKLIK AVKSVAASKK KVYMLYNLQP DRSVTGGAWY SDQDFESEFV EVLNQQCFKF LQSKAETARE SKQNPMIQRN SSFASSHEVW KYICELGISK VELSMEDIET ILNTLIYDGK VEMTIIAAKE GTVGSVDGHM KLYRAVNPII PPTGLVRAPC GLCPVFDDCH EGGEISPSNC IYMTEWLEF.
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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Name :
GOT1 MouseDescription:
Glutamic-Oxaloacetic Transaminase 1 Mouse Recombinant
Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.
Product # :
ENZ-872Price :
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Description
GOT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (1-413a.a) and having a molecular mass of 48.6kDa.GOT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GOT1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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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.
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Synonyms
Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPPSVF AQVPQAPPVL VFKLTADFRD DPDPRKVNLG VGAYRTDESQ PWVLPVVRKV EQKIANDNSL NHEYLPILGL AEFRSCASRL VLGDNSPAIR ENRVGGVQSL GGTGALRIGA DFLGRWYNGT DNKNTPIYVS SPTWENHNAV FSAAGFKDIR PYCYWDAEKR GLDLQGFLND LENAPEFSIF VLHACAHNPT GTDPTPEQWK QIAAVMQRRF LFPFFDSAYQ GFASGDLEKD AWAIRYFVSE GFELFCAQSF SKNFGLYNER VGNLTVVGKE SDSVLRVLSQ MEKIVRITWS NPPAQGARIV AATLSDPELF KEWKGNVKTM ADRILTMRSE LRARLEALKT PGTWSHITEQ IGMFSFTGLN PKQVEYLVNE KHIYLLPSGR INMCGLTTKN LDYVATSIHE AVTKIQ.
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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Name :
UMPS HumanDescription:
Uridine Monophosphate Synthetase Human Recombinant
OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.
Product # :
ENZ-663Price :
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Description
UMPS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 500 amino acids (1-480 a.a) and having a molecular mass of 54.3kDa.UMPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UMPS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Uridine 5'-monophosphate synthase (UMPS), is a bifunctional enzyme that catalyzes the ultimate two steps of the de novo pyrimidine biosynthetic pathway. UMPS in eukaryotes links the orotate phosphoribosyltransferase and the orotidine-5’-monophosphate (OMP) decarboxylase activities into a single protein. The harmony of these 2 enzymes is assumed to be stabilized the catalytic centers as a result of the low molar concentration of the protein in mammalian cells.mutations in this gene are the reason of inherited orotic aciduria disease.
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Synonyms
OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV.
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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Name :
MMP9 MouseDescription:
Matrix Metalloproteinase-9 Mouse Recombinant
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Product # :
ENZ-1177Price :
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Description
MMP9 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 717 amino acids (20-730 a.a.) and having a molecular mass of 79.3 kDa. MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MMP9 Mouse protein solution (0.25mg/ml) contains 20mM Tris-HCl pH-7.5, 10mM CaCl2, 100mM NaCl, 0.05% Brij35 and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Biological Activity
Defined as the amount of enzyme that cleaves 1pmol of Mca-PLGLDpa-AR-NH2 per minute at pH 7.5 at 25C. Specific activity is > 500 pmol/min/ug.
Citations
More Info
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Introduction
MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.
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Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
APYQRQPTFV VFPKDLKTSN LTDTQLAEAY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS QTLKAIRTPR CGVPDVGRFQ TFKGLKWDHH NITYWIQNYS EDLPRDMIDD AFARAFAVWG EVAPLTFTRV YGPEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGAGVQ GDAHFDDDEL WSLGKGVVIP TYYGNSNGAP CHFPFTFEGR SYSACTTDGR NDGTPWCSTT ADYDKDGKFG FCPSERLYTE HGNGEGKPCV FPFIFEGRSY SACTTKGRSD GYRWCATTAN YDQDKLYGFC PTRVDATVVG GNSAGELCVF PFVFLGKQYS SCTSDGRRDG RLWCATTSNF DTDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPLYSYLEGF PLNKDDIDGI QYLYGRGSKP DPRPPATTTT EPQPTAPPTM CPTIPPTAYP TVGPTVGPTG APSPGPTSSP SPGPTGAPSP GPTAPPTAGS SEASTESLSP ADNPCNVDVF DAIAEIQGAL HFFKDGWYWK FLNHRGSPLQ GPFLTARTWP ALPATLDSAF EDPQTKRVFF FSGRQMWVYT GKTVLGPRSL DKLGLGPEVT HVSGLLPRRL GKALLFSKGR VWRFDLKSQK VDPQSVIRVD KEFSGVPWNS HDIFQYQDKA YFCHGKFFWR VSFQNEVNKV DHEVNQVDDV GYVTYDLLQC P-HHHHHH
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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Name :
MMP9 MouseDescription:
Matrix Metalloproteinase-9 Mouse Recombinant
AW743869, Matrix metalloproteinase-9, 92 kDa type IV collagenase, Gelatinase B, GELB, Mmp9, MANDP2, B/MMP, B/MMP9, Clg4, Clg4b, Gel B, MMP-9, pro-MMP-9, 92 kDa gelatinase.
Product # :
ENZ-1191Price :
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Description
MMP9 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-730 a.a) containing a total of 717 amino acids, having a molecular mass of 79.3kDa. MMP9 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
MMP9 protein solution (1mg/ml) containing 10% glycerol, 20mM Tris-HCl (pH 7.5), 1mM CaCl2 and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is greater than 1,500 pmol/min/ug and is defined by the amount of enzyme that cleaves 1pmole of Mca-PLGLDpa-AR-NH2 per minute at pH 7.5 at 37˚C.
Citations
More Info
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Synonyms
AW743869, Matrix metalloproteinase-9, 92 kDa type IV collagenase, Gelatinase B, GELB, Mmp9, MANDP2, B/MMP, B/MMP9, Clg4, Clg4b, Gel B, MMP-9, pro-MMP-9, 92 kDa gelatinase.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
APYQRQPTFV VFPKDLKTSN LTDTQLAEAY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS QTLKAIRTPR CGVPDVGRFQ TFKGLKWDHH NITYWIQNYS EDLPRDMIDD AFARAFAVWG EVAPLTFTRV YGPEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGAGVQ GDAHFDDDEL WSLGKGVVIP TYYGNSNGAP CHFPFTFEGR SYSACTTDGR NDGTPWCSTT ADYDKDGKFG FCPSERLYTE HGNGEGKPCV FPFIFEGRSY SACTTKGRSD GYRWCATTAN YDQDKLYGFC PTRVDATVVG GNSAGELCVF PFVFLGKQYS SCTSDGRRDG RLWCATTSNF DTDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPLYSYLEGF PLNKDDIDGI QYLYGRGSKP DPRPPATTTT EPQPTAPPTM CPTIPPTAYP TVGPTVGPTG APSPGPTSSP SPGPTGAPSP GPTAPPTAGS SEASTESLSP ADNPCNVDVF DAIAEIQGAL HFFKDGWYWK FLNHRGSPLQ GPFLTARTWP ALPATLDSAF EDPQTKRVFF FSGRQMWVYT GKTVLGPRSL DKLGLGPEVT HVSGLLPRRL GKALLFSKGR VWRFDLKSQK VDPQSVIRVD KEFSGVPWNS HDIFQYQDKA YFCHGKFFWR VSFQNEVNKV DHEVNQVDDV GYVTYDLLQC PHHHHHH.
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Background
The MMP9 mouse recombinant, a variant of the matrix metalloproteinase 9 enzyme, has emerged as a crucial focus of biomedical research due to its diverse biological functions and potential implications in various physiological and pathological processes. Matrix metalloproteinase 9 (MMP9) is a key enzyme involved in extracellular matrix remodeling, cell migration, and tissue homeostasis. The MMP9 mouse recombinant, generated through recombinant DNA technology, offers a valuable tool for investigating the molecular characteristics and biological roles of this enzyme.
Understanding the molecular characteristics of MMP9 is vital to unravel its functional significance. MMP9 belongs to the matrix metalloproteinase family, characterized by their ability to degrade various components of the extracellular matrix. MMP9 exhibits unique structural features, including a catalytic domain, a hemopexin-like domain, and a prodomain that regulates its activation. These characteristics contribute to the complexity of MMP9 and its involvement in multiple physiological and pathological processes.
MMP9 plays diverse roles in different biological contexts. It is involved in tissue remodeling processes, such as embryogenesis, wound healing, and tissue repair. Additionally, MMP9 participates in inflammatory responses, immune cell recruitment, and angiogenesis. The precise mechanisms underlying these functions are still being elucidated, highlighting the need for further investigation.
The MMP9 mouse recombinant offers exciting prospects for research and therapeutic applications. By utilizing this recombinant protein, scientists can investigate the role of MMP9 in disease progression, explore its interactions with other molecules, and potentially develop targeted therapies. MMP9 has been implicated in various diseases, including cancer metastasis, cardiovascular disorders, and neurodegenerative conditions, making it a promising candidate for therapeutic interventions.
This research aims to provide a comprehensive analysis of the MMP9 mouse recombinant, focusing on its molecular characteristics, biological roles, and potential therapeutic implications. By shedding light on the intricate nature of MMP9, we aim to contribute to a deeper understanding of its functional significance and pave the way for future research and therapeutic advancements.
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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Name :
ENO2 MouseDescription:
Enolase-2 Mouse Recombinant
AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.
Product # :
ENZ-1028Price :
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Description
ENO2 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (1-434) and having a molecular mass of 49.7kDa.ENO2 is fused to a 23 amino acid His-tag at N-terminus& purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ENO2 solution (1mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 10,000 pmol/min/µg, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.Citations
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Introduction
Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.
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Synonyms
AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.
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Physical Appearance
Sterile Filtered clear colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSIEKIW AREILDSRGN PTVEVDLYTA KGLFRAAVPS GASTGIYEAL ELRDGDKQRY LGKGVLKAVD HINSRIAPAL ISSGISVVEQ EKLDNLMLEL DGTENKSKFG ANAILGVSLA VCKAGAAERD LPLYRHIAQL AGNSDLILPV PAFNVINGGS HAGNKLAMQE FMILPVGAES FRDAMRLGAE VYHTLKGVIK DKYGKDATNV GDEGGFAPNI LENSEALELV KEAIDKAGYT EKMVIGMDVA ASEFYRDGKY DLDFKSPADP SRYITGDQLG ALYQDFVRNY PVVSIEDPFD QDDWAAWSKF TANVGIQIVG DDLTVTNPKR IERAVEEKAC NCLLLKVNQI GSVTEAIQAC KLAQENGWGV MVSHRSGETE DTFIADLVVG LCTGQIKTGA PCRSERLAKY NQLMRIEEEL GDEARFAGHN FRNPSVL.
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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Name :
PREP HumanDescription:
Prolyl Endopeptidase Human Recombinant
Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.
Product # :
ENZ-828Price :
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Description
PREP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 733 amino acids (1-710 a.a) and having a molecular mass of 83.1kDa. PREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PREP protein solution (0.25mg/ml) containing PBS buffer (pH 7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prolyl Endopeptidase , also known as PREP is a cytosolic prolyl endopeptidase which cleaves peptide bonds on the C-terminal side of prolyl residues within peptides which are up to about 30 a.a long. In addition, Prolyl endopeptidases have been shown to be implicated in the maturation and degradation of peptide hormones and neuropeptides.
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Synonyms
Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLSLQYP DVYRDETAVQ DYHGHKICDP YAWLEDPDSE QTKAFVEAQN KITVPFLEQC PIRGLYKERM TELYDYPKYS CHFKKGKRYF YFYNTGLQNQ RVLYVQDSLE GEARVFLDPN ILSDDGTVAL RGYAFSEDGE YFAYGLSASG SDWVTIKFMK VDGAKELPDV LERVKFSCMA WTHDGKGMFY NSYPQQDGKS DGTETSTNLH QKLYYHVLGT DQSEDILCAE FPDEPKWMGG AELSDDGRYV LLSIREGCDP VNRLWYCDLQ QESSGIAGIL KWVKLIDNFE GEYDYVTNEG TVFTFKTNRQ SPNYRVINID FRDPEESKWK VLVPEHEKDV LEWIACVRSN FLVLCYLHDV KNILQLHDLT TGALLKTFPL DVGSIVGYSG QKKDTEIFYQ FTSFLSPGII YHCDLTKEEL EPRVFREVTV KGIDASDYQT VQIFYPSKDG TKIPMFIVHK KGIKLDGSHP AFLYGYGGFN ISITPNYSVS RLIFVRHMGG ILAVANIRGG GEYGETWHKG GILANKQNCF DDFQCAAEYL IKEGYTSPKR LTINGGSNGG LLVAACANQR PDLFGCVIAQ VGVMDMLKFH KYTIGHAWTT DYGCSDSKQH FEWLVKYSPL HNVKLPEADD IQYPSMLLLT ADHDDRVVPL HSLKFIATLQ YIVGRSRKQS NPLLIHVDTK AGHGAGKPTA KVIEEVSDMF AFIARCLNVD WIP.
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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Name :
QTRT1 HumanDescription:
Queuine TRNA-Ribosyltransferase 1 Human Recombinant
Queuine TRNA-Ribosyltransferase 1, TRNA-Guanine Transglycosylase, TGT, Guanine Insertion Enzyme, EC 2.4.2.29, TGUT, Queuine TRNA-Ribosyltransferase, TGT, Catalytic Subunit, TGT, 43-KD Subunit, FP3235, Queuine tRNA-ribosyltransferase.
Product # :
ENZ-877Price :
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Description
QTRT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-403 a.a) and having a molecular mass of 46.7kDa. QTRT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
QTRT1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Queuine TRNA-Ribosyltransferase 1 also known as QTRT1 is a member of the queuine tRNA-ribosyltransferase family. QTRT1 interacts with QTRTD1 to form an active queuine tRNA-ribosyltransferase. Furthermore, QTRT1 exchanges queuine for the guanine at the wobble position of tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr), in this manner forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
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Synonyms
Queuine TRNA-Ribosyltransferase 1, TRNA-Guanine Transglycosylase, TGT, Guanine Insertion Enzyme, EC 2.4.2.29, TGUT, Queuine TRNA-Ribosyltransferase, TGT, Catalytic Subunit, TGT, 43-KD Subunit, FP3235, Queuine tRNA-ribosyltransferase.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMAGAA TQASLESAPR IMRLVAECSR SRARAGELWL PHGTVATPVF MPVGTQATMK GITTEQLDAL GCRICLGNTY HLGLRPGPEL IQKANGLHGF MNWPHNLLTD SGGFQMVSLV SLSEVTEEGV RFRSPYDGNE TLLSPEKSVQ IQNALGSDII MQLDDVVSST VTGPRVEEAM YRSIRWLDRC IAAHQRPDKQ NLFAIIQGGL DADLRATCLE EMTKRDVPGF AIGGLSGGES KSQFWRMVAL STSRLPKDKP RYLMGVGYAT DLVVCVALGC DMFDCVFPTR TARFGSALVP TGNLQLRKKV FEKDFGPIDP ECTCPTCQKH SRAFLHALLH SDNTAALHHL TVHNIAYQLQ LMSAVRTSIV EKRFPDFVRD FMGAMYGDPT LCPTWATDAL ASVGITLG.
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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Name :
AARS HumanDescription:
Alanyl-tRNA Synthetase Human Recombinant
Alanyl-tRNA synthetase cytoplasmic, EC 6.1.1.7, Alanine-tRNA ligase, AlaRS, Renal carcinoma antigen NY-REN-42, PL-12, AARS.
Product # :
ENZ-305Price :
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Description
Alanyl-tRNA synthetase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 110 kDa. PL-12 is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
AARS is supplied in 20mM HEPES buffer pH-8, 250mM sodium chloride, and 20% glycerol.
Purity
AARS purity is greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alanyl-tRNA synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge tRNA molecules with the respective amino acids. This 108 kDa protein is an autoantigen recognized by PL-12 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that epitope spreading occurs in the autoimmune PL-12 response such that even antibodies to an isolated alanyl-tRNA molecule can develop.
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Synonyms
Alanyl-tRNA synthetase cytoplasmic, EC 6.1.1.7, Alanine-tRNA ligase, AlaRS, Renal carcinoma antigen NY-REN-42, PL-12, AARS.
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Physical Appearance
Sterile Filtered clear solution.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sampels).
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coating concentration
0.3-0.8 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for labeling of functional groups.
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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Name :
BACE1 HumanDescription:
Beta-Secretase 1 Human Recombinant
Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.
Product # :
ENZ-1119Price :
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Description
BACE1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 442 amino acids (22-457 a.a.) and having a molecular mass of 49.2kDa. BACE1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
BACE1 protein solution containing Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 5 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.
Citations
More Info
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Introduction
Beta-secretase 1 or BACE1 or beta-site amyloid precursor protein cleaving enzyme 1, is a protein that is encoded by the BACE1 gene in humans. Expression of BACE1 is seen primarily in neurons as it is crucial for the creation of myelin sheats in the peripheric nervous system. Beta-secretase 1 is a proteas that is located in the cell membrane (transmembrane). The enzyme consists of 2 active sites (aspartate residues) in the extracellular domain that can act as a dimer.
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Synonyms
Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
TQHGIRLPLR SGLGGAPLGL RLPRETDEEP EEPGRRGSFV EMVDNLRGKS GQGYYVEMTV GSPPQTLNIL VDTGSSNFAV GAAPHPFLHR YYQRQLSSTY RDLRKGVYVP YTQGKWEGEL GTDLVSIPHG PNVTVRANIA AITESDKFFI NGSNWEGILG LAYAEIARPD DSLEPFFDSL VKQTHVPNLF SLQLCGAGFP LNQSEVLASV GGSMIIGGID HSLYTGSLWY TPIRREWYYE VIIVRVEING QDLKMDCKEY NYDKSIVDSG TTNLRLPKKV FEAAVKSIKA ASSTEKFPDG FWLGEQLVCW QAGTTPWNIF PVISLYLMGE VTNQSFRITI LPQQYLRPVE DVATSQDDCY KFAISQSSTG TVMGAVIMEG FYVVFDRARK RIGFAVSACH VHDEFRTAAV EGPFVTLDME DCGYNIPQTD ESTLMTHHHH 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.
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Name :
phrB E.ColiDescription:
Deoxyribodipyrimidine photo-lyase E.Coli Recombinant
800x600 ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}
Product # :
ENZ-362Price :
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Description
800x600 800x600 phrB E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 495 amino acids (1-472) and having a molecular mass of 56.1kDa.phrB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The phrB solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Deoxyribodipyrimidine photo-lyase (phrB) is a member of the DNA photolyase class-1 family. phrB takes part in repair of UV radiation-inducedDNA damage. phrB catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidinedimers (in cis-syn configuration), which are formed between closest bases on the same DNA strand uponexposure to ultraviolet radiation.
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Synonyms
ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708.
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Physical Appearance
Sterile Filtered clear solution.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTTHLVW FRQDLRLHDN LALAAACRNS SARVLALYIA TPRQWATHNM SPRQAELINA QLNGLQIALA EKGIPLLFRE VDDFVASVEI VKQVCAENSV THLFYNYQYE VNERARDVEV ERALRNVVCE GFDDSVILPP GAVMTGNHEM YKVFTPFKNA WLKRLREGMP ECVAAPKVRS SGSIEPSPSI TLNYPRQSFD TAHFPVEEKA AIAQLRQFCQ NGAGEYEQQR DFPAVEGTSR LSASLATGGL SPRQCLHRLL AEQPQALDGG AGSVWLNELI WREFYRHLIT YHPSLCKHRP FIAWTDRVQW QSNPAHLQAW QEGKTGYPIV DAAMRQLNST GWMHNRLRMI TASFLVKDLL IDWREGERYF MSQLIDGDLA ANNGGWQWAA STGTDAAPYF RIFNPTTQGE KFDHEGEFIR QWLPELRDVP GKVVHEPWKW AQKAGVTLDY PQPIVEHKEA RVQTLAAYEA ARKGK.
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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Name :
GOT2 MouseDescription:
Glutamic-Oxaloacetic Transaminase 2 Mouse Recombinant
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV,Kynurenine Aminotransferase 4.
Product # :
ENZ-1095Price :
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Description
GOT2 Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (30-430 a.a.) and having a molecular mass of 46.8kDa. Mouse GOT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GOT2 solution (0.5mg/ml) contains PBS, pH 7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Activity is greater than 20 units/mg, and is defined as the amount of enzyme that converts 1umole of alpha-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25℃.
Citations
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Introduction
GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 takes part in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.
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Synonyms
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV,Kynurenine Aminotransferase 4.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSWWTHVEM GPPDPILGVT EAFKRDTNSK KMNLGVGAYR DDNGKPYVLP SVRKAEAQIA AKNLDKEYLP IGGLAEFCKA SAELALGENN EVLKSGRFVT VQTISGTGAL RVGASFLQRF FKFSRDVFLP KPSWGNHTPI FRDAGMQLQG YRYYDPKTCG FDFSGALEDI SKIPEQSVLL LHACAHNPTG VDPRPEQWKE IASVVKKKNL FAFFDMAYQG FASGDGDKDA WAVRHFIEQG INVCLCQSYA KNMGLYGERV GAFTVVCKDA EEAKRVESQL KILIRPLYSN PPLNGARIAA TILTSPDLRK QWLQEVKGMA DRIISMRTQL VSNLKKEGSS HNWQHITDQI GMFCFTGLKP EQVERLTKEF SVYMTKDGRI SVAGVTSGNV GYLAHAIHQV.
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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Name :
TEVDescription:
Tobacco Etch Virus Protease Recombinant
rTEV, TEV, P1 protease.
Product # :
PRO-585Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant TEV Protease (rTEV) is a site-specific protease purified from E. coli. The protease can be used for the removal of affinity tags from fusion proteins. The seven-amino-acid recognition site for rTEV is Glu-Asn-Leu-Tyr-Phe-Gln-Gly with cleavage occurring between Gln and Gly. The optimal temperature for cleavage is 30°C; however, the enzyme can be used at temperatures as low as 4°C. The rTEV contains His tag.The rTEV is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The rTEV contains 25mM Tris, Ph 8.0, 75mM NaCl, 5mM EDTA, 10mM GSH, 50% Glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
TEV protease is the common name for the 27 kDa catalytic domain of the Nuclear Inclusion a (NIa) protein encoded by the tobacco etch virus (TEV). Because its sequence specificity is far more stringent than that of factor Xa, thrombin, or enterokinase, TEV protease is a very useful reagent for cleaving fusion proteins. TEV protease recognizes a linear epitope of the general form E-Xaa-Xaa-Y -Xaa-Q-(G/S), with cleavage occurring between Q and G or Q and S. The most commonly used sequence is ENLYFQG.
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Synonyms
rTEV, TEV, P1 protease.
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Physical Appearance
Sterile liquid formulation.
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Stability
rTEV although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Cleavage Conditions
A number of variables can be changed to optimize the cleavage of any specific protein. The amount of rTEV, the temperature of the incubation, and the time needed for cleavage may be examined. If the protein of interest is heat-labile, then 4°C incubations are recommended. Reactions at 4°C will require longer incubation times and/or more rTEV.
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Unit Definition
One unit is defined as the amount of enzyme needed to cleave 3 ug of fusion protein in 1 hour to 85 % completion at 30°C in a buffer containing 50 mM Tris-HCl, pH 8.0, 0.5 mM EDTA, and 1 mM DTT.
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.
- View Data Sheet
Name :
MMP 3 Human, GSTDescription:
Matrix Metalloproteinase-3 Human Recombinant, GST Tag
Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.
Product # :
ENZ-455Price :
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Description
MMP-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain fused to a GST tag containing 228 amino acids (251-478) and having a total molecular mass of 51kDa. MMP-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MMP-3 is supplied in 50mM Tris-Acetate, pH-7.5, 1mM EDTA and 20% Glycerol.
Citations
More Info
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Introduction
MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.
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Synonyms
Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.
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Physical Appearance
Sterile Filtered clear solution.
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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. Please avoid freeze thaw cycles.
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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Name :
Nucleosome BovineDescription:
Bovine Nucleosome
Product # :
PRO-2557Price :
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Description
Nucleosome Bovine shows multiple bands between 14-18kDa and is purified from bovine tissues by proprietary protein-chemical techniques.
Source
Bovine tissues.
Formulation
Nucleosome Bovine is supplied in 20mM HEPES buffer pH-7.5, 500mM NaCl, 1mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Nucleosome core proteins are a group of proteins which are necessary for DNA packaging in eukaryotes. Every core contains an octamer with 2 copies of each histone 2A, 2B, 3 and 4 around which an approx. 140 bp section of DNA is wound twice.
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Physical Appearance
Sterile Filtered clear solution.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG type human auto antibodies.2. Checkerboard analysis of positive/negative samples.
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coating concentration
0.2-0.5 μg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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.
- View Data Sheet
Name :
MUG E.ColiDescription:
G/U Mismatch-Specific DNA Glycosylase E.Coli Recombinant
xanthine DNA glycosylase, dug, ECK3058, JW3040, ygjF, G/U mismatch-specific DNA glycosylase, Double-strand-specific uracil glycosylase, Mismatch-specific uracil DNA-glycosylase, mug.
Product # :
ENZ-703Price :
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Description
MUG Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (1-168) and having a molecular mass of 21.1kDa. MUG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MUG solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
G/U mismatch-specific DNA glycosylase (mug) is a part of the TDG/mug DNA glycosylase family. Mug is necessary for DNA damage lesion repair in stationary-phase cells. Mug protein removes three N4-ethenocytosine and takes away s the uracil base from mismatches in the order of U:G>U:A. The enzyme Uracil-N-Glycosylase removes uracil from the DNA leaving an AP position. Mug is also able to hydrolyzing the carbon-nitrogen bond among the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine plays a role in substrate recognition.
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Synonyms
xanthine DNA glycosylase, dug, ECK3058, JW3040, ygjF, G/U mismatch-specific DNA glycosylase, Double-strand-specific uracil glycosylase, Mismatch-specific uracil DNA-glycosylase, mug.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVEDILA PGLRVVFCGI NPGLSSAGTG FPFAHPANRF WKVIYQAGFT DRQLKPQEAQ HLLDYRCGVT KLVDRPTVQA NEVSKQELHA GGRKLIEKIE DYQPQALAIL GKQAYEQGFS QRGAQWGKQT LTIGSTQIWV LPNPSGLSRV SLEKLVEAYR ELDQALVVRG R.
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.
- View Data Sheet
Name :
TOP1 70kDa HumanDescription:
DNA Topoisomerase-I 70kDa Recombinant Human
DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.
Product # :
ENZ-073Price :
Quantity :
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Description
Recombinant TOP1 70kDa protein is an enzyme fragment having a molecular mass of 72KDa (pH 9.4). TOP1 70kDa protein is fused to a hexa-histidine purification tag.
Source
Sf9 insect cells.
Formulation
TOP1 70kDa is supplied in 20mM HEPES buffer pH-8.0, 500mM NaCl, and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TOP1 is an important nuclear enzyme that interconverts supercoiled DNA to the necessary topological conformations for standard DNA replication and transcription. TOP1 is the target antigen for TOP1 autoantibodies. TOP1 antibodies are a specific marker in scleroderma patients (specificity 98-100%) and are related with the existence of diffuse skin involvement and pulmonary fibrosis. In human tissues top1 enzyme is primarily synthesized as a protein with a molecular weight of 100-kDa. Most of this precursor is then proteolytically processed to a 70-kDa size, from which the TOP1 antigen has derived its name.
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Synonyms
DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative samples) and immunodot test with positive/negative samples.
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coating concentration
0.5-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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Applications
Western blot with anti TOP1 70kDa autoantibody positive sample or monoclonal anti-hexa-His-tag antibody.
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.
- View Data Sheet
Name :
NDUFS4 HumanDescription:
Histidine NADH Dehydrogenase Fe-S Protein 4 Human Recombinant
AQDQ, NDUFS4, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 mitochondrial, NADH-ubiquinone oxidoreductase 18 kDa subunit, Complex I-18 kDa, CI-18 kDa, Complex I-AQDQ, CI-AQDQ.
Product # :
ENZ-421Price :
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Description
NDUFS4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (43-175 a.a.) and having a molecular mass of 15.5 kDa.The NDUFS4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFS4 solution contains 20mM Tris pH-8 & 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NDUFS4 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), the primary multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I is involved in cellular ATP production, the main source of energy for numerous vital processes in living cells. NDUFS4 removes electrons from NADH and passes them by a series of diverse protein-coupled redox centers to the electron acceptor ubiquinone. NDUFS4 presents a hotspot of mutations in the genetic apparatus of oxidative phosphorylation and the correct assembly of the subunit it encodes is essential for completion of the assembly of complex I.
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Synonyms
AQDQ, NDUFS4, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 mitochondrial, NADH-ubiquinone oxidoreductase 18 kDa subunit, Complex I-18 kDa, CI-18 kDa, Complex I-AQDQ, CI-AQDQ.
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Physical Appearance
Sterile Filtered colorless solution.
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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).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MAQDQTQDTQ LITVDEKLDI TTLTGVPEEH IKTRKVRIFV PARNNMQSGV NNTKKWKMEF DTRERWENPL MGWASTADPL SNMVLTFSTK EDAVSFAEKN GWSYDIEERK VPKPKSKSYG ANFSWNKRTR VSTK.
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.
- View Data Sheet
Name :
DsbCDescription:
Disulfide-Bond Isomerase Recombinant
Disulfide-bond isomerase C, dsbC, xprA, Disulfide-bond isomerase (DsbC) E.Coli, Thiol:disulfide interchange protein dsbC, Disulfide-bond isomerase C Thiol:disulfide interchange protein dsbC .
Product # :
ENZ-291Price :
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Shipped with Ice Packs
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Description
Disulfide-Bond Isomerase Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids (21-236) and having a molecular mass of 23.6 kDa.DsbC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 20mM Tris-HCl buffer pH 7.5 and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. DsbC is periplasmic enzyme known as a disulfide isomerase and can convert aberrant disulfide bonds to correct ones.
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Synonyms
Disulfide-bond isomerase C, dsbC, xprA, Disulfide-bond isomerase (DsbC) E.Coli, Thiol:disulfide interchange protein dsbC, Disulfide-bond isomerase C Thiol:disulfide interchange protein dsbC .
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MDDAAIQQTL AKMGIKSSDI QPAPVAGMKT VLTNSGVLYI TDDGKHIIQG PMYDVSGTAP VNVTNKMLLK QLNALEKEMI VYKAPQEKHV ITVFTDITCG YCHKLHEQMA DYNALGITVR YLAFPRQGLD SDAEKEMKAI WCAKDKNKAF DDVMAGKSVA PASCDVDIAD HYALGVQLGV SGTPAVVLSN GTLVPGYQPP KEMKEFLDEH QKMTSGK.
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.