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1000 results found for “protease”
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Name :
IDNK E.Coli, ActiveDescription:
Thermosensitive Gluconokinase E.Coli Recombinant, BioActive
Thermosensitive gluconokinase, Gluconate kinase 1, idnK, D-gluconate kinase thermosensitive, D-gluconate kinase, thermosensitive, ECK4261, gntV, JW4225, b4268
Product # :
PKA-122Price :
Quantity :
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Shipped with Ice Packs
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Description
IDNK Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187) and having a molecular mass of 23.4 kDa.IDNK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDNK solution (1 mg/ml) contains 10% Glycerol, 1mM DTT, 0.15M NaCl and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 80unit/mg. One unit will convert 1.0 umole of D-gluconate to 6-phospho-Dgluconate per minute at pH 8.0 at 37˚C.
More Info
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Introduction
D-gluconate kinase or idnk is a thermosensitive protein, consists of 187 a.a and part of the gluconokinase gntK/gntV protein family. Idnk enhances the conversion of ATP + D-gluconate => ADP + 6-phospho-D-gluconate. Idnk has a crucial part in determination of gender, removal of a certain portion of 9p may result in the making of male to female (reversal of sex), that leads to a female that has the genotype of male X, Y.
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Synonyms
Thermosensitive gluconokinase, Gluconate kinase 1, idnK, D-gluconate kinase thermosensitive, D-gluconate kinase, thermosensitive, ECK4261, gntV, JW4225, b4268
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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 MGSMAGESFI LMGVSGSGKT LIGSKVAALL SAKFIDGDDL HPAKNIDKMS QGIPLSDEDR LPWLERLNDA SYSLYKKNET GFIVCSSLKK QYRDILRKGS PHVHFLWLDG DYETILARMQ RRAGHFMPVA LLKSQFEALE RPQADEQDIV RIDINHDIAN VTEQCRQAVL AIRQNRICAK EGSASDQRCE
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 :
Ketohexokinase HumanDescription:
Ketohexokinase Human Recombinant
KHK, Hepatic Fructokinase, Ketohexokinase, Fructokinase.
Product # :
PKA-359Price :
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Shipped with Ice Packs
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Description
Ketohexokinase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids and having a molecular mass of 32.7 kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 1xPBS, pH 7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ketohexokinase catalyzes the phosphorylation of fructose to produce fructose-1-phosphate, resulting in the utilization of ATP and creation of AMP. Ketohexokinase commences initial step in the metabolism of dietary fructose and is a significant regulator of hepatic glucose metabolism. Ketohexokinase is found in liver, renal cortex, and small intestine. Its deficiency causes the benign hereditary metabolic disorder essential fructosuria, leading to fructose being excreted in the urine. Ketohexokinase-dependent metabolism of fructose induces proinflammatory mediators in proximal tubular cells. ketohexokinase plays an unknown physiologic function that remains intact in essential fructosuria. Ketohexokinase expression is reduceed in human clear cell type of renal cell carcinoma.
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Synonyms
KHK, Hepatic Fructokinase, Ketohexokinase, Fructokinase.
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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
MEEKQILCVG LVVLDVISLV DKYPKEDSEI RCLSQRWQRG GNASNSCTIL SLLGAPCAFM GSMAPGHVAD FVLDDLRRYS VDLRYTVFQT TGSVPIATVI INEASGSRTI LYYDRSLPDV SATDFEKVDL TQFKWIHIEG RNASEQVKML QRIDAHNTRQ PPEQKIRVSV EVEKPREELF QLFGYGDVVF VSKDVAKHLG FQSAEEALRG LYGRVRKGAV LVCAWAEEGA DALGPDGKLL HSDAFPPPRV VDTLGAGDTF NASVIFSLSQ GRSVQEALRF GCQVAGKKCG LQGFDGIV.
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 :
MAOA HumanDescription:
Monoamine Oxidase A Human Recombinant
Monoamine Oxidase A, Monoamine Oxidase Type A, EC 1.4.3.4, MAO-A, Amine Oxidase [Flavin-Containing] A, EC 1.4.3, Amine oxidase [flavin-containing] A, Monoamine oxidase type A.
Product # :
ENZ-866Price :
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Shipped with Ice Packs
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Description
MAOA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 520 amino acids (1-497 a.a) and having a molecular mass of 58.8kDa. MAOA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
MAOA protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Monoamine Oxidase A, also known as MAOA catalyzes the oxidative deamination of biogenic as well as xenobiotic amines and has significant functions in the metabolism of neuroactive and vasoactive amines in the central nervous system as well as peripheral tissues. Mutation in MAOA results in Brunner syndrome; in addition MAOA has also been linked with a diversity of other psychiatric disorders, which includes antisocial behavior. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT).
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Synonyms
Monoamine Oxidase A, Monoamine Oxidase Type A, EC 1.4.3.4, MAO-A, Amine Oxidase [Flavin-Containing] A, EC 1.4.3, Amine oxidase [flavin-containing] A, Monoamine oxidase type 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 MGSMENQEKA SIAGHMFDVV VIGGGISGLS AAKLLTEYGV SVLVLEARDR VGGRTYTIRN EHVDYVDVGG AYVGPTQNRI LRLSKELGIE TYKVNVSERL VQYVKGKTYP FRGAFPPVWN PIAYLDYNNL WRTIDNMGKE IPTDAPWEAQ HADKWDKMTM KELIDKICWT KTARRFAYLF VNINVTSEPH EVSALWFLWY VKQCGGTTRI FSVTNGGQER KFVGGSGQVS ERIMDLLGDQ VKLNHPVTHV DQSSDNIIIE TLNHEHYECK YVINAIPPTL TAKIHFRPEL PAERNQLIQR LPMGAVIKCM MYYKEAFWKK KDYCGCMIIE DEDAPISITL DDTKPDGSLP AIMGFILARK ADRLAKLHKE IRKKKICELY AKVLGSQEAL HPVHYEEKNW CEEQYSGGCY TAYFPPGIMT QYGRVIRQPV GRIFFAGTET ATKWSGYMEG AVEAGERAAR EVLNGLGKVT EKDIWVQEPE SKDVPAVEIT HTFWERNLPS.
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 :
GSTT1 HumanDescription:
Glutathione S-Transferase Theta-1 Human Recombinant
Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.
Product # :
ENZ-429Price :
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Shipped with Ice Packs
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Description
GSTT1 Human Recombinant fused with 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 277 amino acids (1-240 a.a.) and having a molecular mass of 31.5kDa.The GSTT1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTT1 solution contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GSTT1 belongs to a superfamily of proteins which catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. GSTT1 is one of the GSTs’ four main classes: alpha, mu, pi and theta (which includes GSTT1 and GSTT2). GSTT1 is involved in activation and detoxification reactions and catalyzes the conjugation of industrial chemicals, such as epoxybutane, ethylene oxides, halomethane with glutathione. GSTT1 is found in erythrocytes, at low levels in the liver as well as in Clara and ciliated cells at the alveolar/bronchiolar junction in the lung.
The GSTT1 gene is deficient in 38% of the population. The GSTTI enzyme deficiency might influence the individual risk for development of acquired aplastic anemia and acute myeloid leukemia. The presence or absence of the GSTT1 gene is concurrent with GSST1+ (the conjugator) and GSTT1- (the non-conjugator) phenotypes correspondingly. The GSTT1+ phenotype is able to catalyze the glutathione conjugation of dichloromethane. GSTT1-null genotypes are seen as having a higher risk of developing leukoplakia. Germline genetic polymorphism in GSTT1 is linked to breast cancer. -
Synonyms
Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMGL ELYLDLLSQP CRAVYIFAKK NDIPFELRIV DLIKGQHLSD ACAQVNPLKK VPALKDGDFT LTESVAILLY LTRKYKVPDY WYPQDLQARA RVDEYLAWQH TTLRRSCLRA LWHKVMFPVF LGEPVSPQTL AATLAELDVT LQLLEDKFLQ NKAFLTGPHI SLADLVAITE LMHPVGAGCQ VFEGRPKLAT WRQRVEAAVG EDLFQEAHEV ILKAKDFPPA DPTIKQKLMP WVLAMIR.
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 :
SERPINA3 HumanDescription:
Alpha-1 AntiChymotrypsin Human
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
Product # :
PRO-378Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Alpha-1 AntiChymotrypsin produced from normal human serum having a molecular mass of 68kDa.
Source
Human Serum.
Formulation
Lyophilized from 0.02M Tris-buffer,pH-7.5 and 0.15M Nacl.
Purity
Greater than 90.0%.
More Info
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Introduction
Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1- ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT. -
Synonyms
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Human SERPINA3 although stable at room temperature for 3 weeks, should be stored between 2-8°C. Do not freeze.
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Solubility
It is recommended to reconstitute the lyophilized human A1ACT in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.
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 :
FKBP1B HumanDescription:
FK506 Binding Protein 1B Human Recombinant
Peptidyl-prolyl cis-trans isomerase FKBP1B, PPIase FKBP1B, 12.6 kDa FK506-binding protein, 12.6 kDa FKBP, FKBP-12.6, FK506-binding protein 1B, FKBP-1B, Immunophilin FKBP12.6, Rotamase, h-FKBP-12, FKBP1B, FKBP12.6, FKBP1L, FKBP9, OTK4.
Product # :
ENZ-194Price :
Quantity :
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Shipped with Ice Packs
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Description
FKBP1B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-108) and having a molecular mass of 14.2kDa.FKBP1B is fused to a 22 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FKBP1B solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE analysis.
Biological Activity
Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
Peptidyl-prolyl cis-trans isomerase FKBP1B (FKBP1B) belongs to the immunophilin protein family which has a role in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP1B is a cis-trans prolyl isomerase which binds the immunosuppressants FK506 and rapamycin. FKBP1B is extremely similar to the FK506-binding protein 1A. The physiological role of FKBP1B is thought to be in excitation-contraction coupling in cardiac muscle.
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Synonyms
Peptidyl-prolyl cis-trans isomerase FKBP1B, PPIase FKBP1B, 12.6 kDa FK506-binding protein, 12.6 kDa FKBP, FKBP-12.6, FK506-binding protein 1B, FKBP-1B, Immunophilin FKBP12.6, Rotamase, h-FKBP-12, FKBP1B, FKBP12.6, FKBP1L, FKBP9, OTK4.
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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 RSMGVEIETI SPGDGRTFPK KGQTCVVHYT GMLQNGKKFD SSRDRNKPFK FRIGKQEVIK GFEEGAAQMS LGQRAKLTCT PDVAYGATGH PGVIPPNATL IFDVELLNLE.
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 :
UBE2D2 HumanDescription:
Ubiquitin Conjugating Enzyme E2D2 Human Recombinant
Ubiquitin-conjugating enzyme E2D 2 (homologous to yeast UBC4/5), UBC4, Ubiquitin carrier protein D2, Ubiquitin-conjugating enzyme E2-17 kDa 2, Ubiquitin-protein ligase D2, UBCH5B, EC 6.3.2.19, E2(17)KB2, PUBC1, UBC4/5, UBC5B, UBCH4.
Product # :
ENZ-1036Price :
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Shipped with Ice Packs
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Description
UBE2D2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 147 amino acids (1-147) and having a molecular mass of 16.7kDa. The UBE2D2 is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The UBE2D2 solution (0.5mg/ml) contains 20mM MES (pH6.0), 50mM NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
UBE2D2 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2D2 takes part in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. UBE2D2 catalyzes ubiquitination of IkB-alpha in a SCFB-TRCP and phosphorylation dependent method.
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Synonyms
Ubiquitin-conjugating enzyme E2D 2 (homologous to yeast UBC4/5), UBC4, Ubiquitin carrier protein D2, Ubiquitin-conjugating enzyme E2-17 kDa 2, Ubiquitin-protein ligase D2, UBCH5B, EC 6.3.2.19, E2(17)KB2, PUBC1, UBC4/5, UBC5B, UBCH4.
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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
MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM.
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 :
TDP2 HumanDescription:
Tyrosyl-DNA Phosphodiesterase 2 Human Recombinant
AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein II.
Product # :
ENZ-698Price :
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Shipped with Ice Packs
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Description
TDP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362) and having a molecular mass of 43.3kDa. TDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TDP2 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.
More Info
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Introduction
Tyrosyl-DNA Phosphodiesterase 2 (TDP2), belongs to the CCR4/nocturin family of divalent cation-dependent phosphodiesterases.TDP2 associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. TDP2 is characterized by similar sequence and structure as APE1 endonuclease, which participates in DNA repair and the activation of transcription factors.
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Synonyms
AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein 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 MGSMELGSCL EGGREAAEEE GEPEVKKRRL LCVEFASVAS CDAAVAQCFL AENDWEMERA LNSYFEPPVE ESALERRPET ISEPKTYVDL TNEETTDSTT SKISPSEDTQ QENGSMFSLI TWNIDGLDLN NLSERARGVC SYLALYSPDV IFLQEVIPPY YSYLKKRSSN YEIITGHEEG YFTAIMLKKS RVKLKSQEII PFPSTKMMRN LLCVHVNVSG NELCLMTSHL ESTRGHAAER MNQLKMVLKK MQEAPESATV IFAGDTNLRD REVTRCGGLP NNIVDVWEFL GKPKHCQYTW DTQMNSNLGI TAACKLRFDR IFFRAAAEEG HIIPRSLDLL GLEKLDCGRF PSDHWGLLCN LDIIL.
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 :
ALDH2 Mouse, ActiveDescription:
Aldehyde Dehydrogenase 2 Mouse Recombinant, Active
Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.
Product # :
ENZ-1093Price :
Quantity :
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Shipped with Ice Packs
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Description
ALDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (20-519) and having a molecular mass of 56.8kDa. ALDH2 Mouse is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDH2 Mouse protein (0.5mg/ml) is formulated in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 180 pmol/min/ug, and was obtained by measuring the increase of NADH in absorbance at 340 nm resulting from the reduction of NAD at pH 8.0 at 25C.
More Info
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Introduction
ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.
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Synonyms
Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.
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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 MGSSAAATSA VPAPNHQPEV FCNQIFINNE WHDAVSRKTF PTVNPSTGEV ICQVAEGNKE DVDKAVKAARAAFQLGSPWR RMDASDRGRL LYRLADLIER DRTYLAALET LDNGKPYVIS YLVDLDMVLK CLRYYAGWAD KYHGKTIPID GDFFSYTRHEPVGVCGQIIP WNFPLLMQAW KLGPALATGN VVVMKVAEQT PLTALYVANL IKEAGFPPGV VNIVPGFGPT AGAAIASHEG VDKVAFTGSTEVGHLIQVAA GSSNLKRVTL ELGGKSPNII MSDADMDWAV EQAHFALFFN QGQCCCAGSR TFVQENVYDE FVERSVARAK SRVVGNPFDSRTEQGPQVDE TQFKKILGYI KSGQQEGAKL LCGGGAAADR GYFIQPTVFG DVKDGMTIAK EEIFGPVMQI LKFKTIEEVV GRANDSKYGLAAAVFTKDLD KANYLSQALQ AGTVWINCYD VFGAQSPFGG YKMSGSGREL GEYGLQAYTE VKTVTVKVPQ KNS.
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 :
UCHL3 MouseDescription:
Ubiquitin Carboxyl-Terminal Esterase L3 Mouse Recombinant
Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.
Product # :
ENZ-978Price :
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Shipped with Ice Packs
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Description
UCHL3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 238 amino acids (1-230) and having a molecular mass of 27.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).UCHL3 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
UCHL3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 9,000 pmol/min/mg, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of ubiquitin-AMC per minute at pH 7.5, at 37°C.More Info
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Introduction
Ubiquitin carboxyl-terminal hydrolase isozyme L3 belongs to a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to produce the ubiquitin monomer. UCHL3 takes part in the regulation of neuronal development and spermatogenesis and is associated to neurodegenerative diseases. UCHL3 has a 54% homology to UCHL1.
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Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.
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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
MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMEPE LLSMVPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERAKFLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGKTSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA LEHHHHHH.
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 :
GAMT HumanDescription:
Guanidinoacetate N-Methyltransferase Human Recombinant
PIG2, TP53I2, GAMT, Guanidinoacetate N-methyltransferase.
Product # :
ENZ-460Price :
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Shipped with Ice Packs
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Description
Recombinant Human GAMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (1-236 a.a) and having a molecular mass of 28.4 kDa. GAMT is fused to a 20 amino acids His-Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The GAMT protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GAMT is a methyltransferase that transfers guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects GAMT gene result in neurologic syndromes and muscular hypotonia, probably due to creatine deficiency and accumulation of guanidinoacetate in the brain of affected individuals. GAMT take parts in the two-step synthesis of creatine from the protein building blocks glycine, arginine, and methionine. GAMT takes part in supplying the energy for muscle contraction, and is in addition a significant player in nervous system functioning. GAMT is active in the liver, pancreas, and kidne.
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Synonyms
PIG2, TP53I2, GAMT, Guanidinoacetate N-methyltransferase.
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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 MSAPSATPIF APGENCSPAW GAAPAAYDAA DTHLRILGKP VMERWETPYM HALAAAASSK GGRVLEVGFG MAIAASKVQE APIDEHWIIE CNDGVFQRLR DWAPRQTHKV IPLKGLWEDV APTLPDGHFD GILYDTYPLS EETWHTHQFN FIKNHAFRLL KPGGVLTYCN LTSWGELMKS KYSDITIMFE ETQVPALLEA GFRRENIRTE VMALVPPADC RYYAFPQMIT PLVTKG.
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 :
ADAT2 HumanDescription:
Adenosine Deaminase, tRNA-specific 2 Human Recombinant
DEADC1, TAD2.
Product # :
ENZ-561Price :
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Description
Recombinant Human ADAT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (1-191 a.a) and having a molecular mass of 23.2 kDa. ADAT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ADAT2 (0.5mg/ml) protein contains 20mM Tris-HCl buffer pH-8, 2mM DTT, 50mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Adenosine Deaminase (ADA), also recognized as ADAT2 is an enzyme that takes part in purine metabolism. ADAT2 is necessary for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. ADAT2 is involved in the deamination of adenosine-34 to inosine in numerous tRNAs. ADAT2 is part of the cytidine and deoxycytidylate deaminase protein family, ADAT2 employs zinc as a cofactor. ADAT2 is a 191 amino acid enzyme that exists as two isoforms formed by alternative splicing events.
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Synonyms
DEADC1, TAD2.
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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 MEAKAAPKPA ASGACSVSAE ETEKWMEEAM HMAKEALENT EVPVGCLMVY NNEVVGKGRN EVNQTKNATR HAEMVAIDQV LDWCRQSGKS PSEVFEHTVL YVTVEPCIMC AAALRLMKIP LVVYGCQNER FGGCGSVLNI ASADLPNTGR PFQCIPGYRA EEAVEMLKTF YKQENPNAPK SKVRKKECQK S.
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 :
PTPN1 HumanDescription:
Protein Tyrosine Phosphatase Non Receptor Type-1 Human Recombinant
Tyrosine-protein phosphatase non-receptor type 1, EC 3.1.3.48, Protein-tyrosine phosphatase 1B, PTP-1B, PTPN1, PTP1B.
Product # :
PKA-219Price :
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Description
Protein Tyrosine Phosphatase Non Receptor Type-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 321 amino acids and having a molecular mass of 37.3 kDa.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 25mM Tris-HCl, pH 7.5, 2mM beta-mercaptoethanol, 1mM EDTA, 1mM DTT and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 10,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37°C.More Info
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Introduction
Protein Tyrosine Phosphatase 1B is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP has been shown to act as a negative regulator of INS signaling by dephosphorylating the phosphotryosine residues of INS receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, and cell response to IFN stimulation.
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Synonyms
Tyrosine-protein phosphatase non-receptor type 1, EC 3.1.3.48, Protein-tyrosine phosphatase 1B, PTP-1B, PTPN1, PTP1B.
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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
MEMEKEFEQI DKSGSWAAIY QDIRHEASDF PCRVAKLPKN KNRNRYRDVS PFDHSRIKLHQEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW EQKSRGVVML NRVMEKGSLKCAQYWPQKEE KEMIFEDTNL KLTLISEDIK SYYTVRQLEL ENLTTQETRE ILHFHYTTWPDFGVPESPAS FLNFLFKVRE SGSLSPEHGP VVVHCSAGIG RSGTFCLADT CLLLMDKRKDPSSVDIKKVL LEMRKFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE PPPEHIPPPPRPPKRILEPHN.
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 :
Protein Cys-A/GDescription:
Protein Cys-A/G Recombinant
Product # :
PRO-1929Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-A/G was lyophilized without any additives.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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.
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Solubility
It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE.
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 :
CEA ProteinDescription:
Carcinoembryonic Antigen Human
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
Product # :
PRO-2801Price :
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Shipped with Ice Packs
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Description
CEA produced from patient source colon carcinoma liver metastatic tissue can be used as general marker in screening and monitoring malignant disease states.
Source
Liver tissue.
Formulation
CEA protein solution contains 0.1M PBS, pH 7.4, 0.09 % NaN3 and 2 % methyl-mannoside.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
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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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Applications
Blood samples from tissue donors were tested and found to be negative for HBsAg, HIV-1 and HIV-2 antibodies and HCV.
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Background
Carcinoembryonic Antigen, commonly known as CEA, is a glycoprotein that was initially identified as a tumor marker. Over the years, research into CEA has unveiled its intricate involvement in various physiological processes, not only in cancer but also in the context of normal development and inflammatory conditions. This research aims to delve into the multifaceted roles of CEA, exploring its structural intricacies, regulatory mechanisms, and its implications in health, disease, and beyond.
Structural Complexity of CEA:
CEA, belonging to the immunoglobulin superfamily, is a complex glycoprotein featuring multiple structural domains. Its diverse forms and glycosylation patterns contribute to its functional versatility. CEA is primarily expressed in fetal tissues, but its presence is often detected in adults under pathological conditions, especially in various types of cancer.
CEA in Cancer Biology:
CEA was first recognized as a biomarker for colorectal cancer, but its overexpression is not limited to this context. Elevated CEA levels have been associated with several other malignancies, including breast, lung, and pancreatic cancers. CEA’s involvement in cancer biology ranges from promoting angiogenesis and metastasis to inhibiting immune responses, making it a critical player in tumor progression and evasion.
Beyond Cancer: CEA in Development and Inflammation:
While CEA’s role in cancer is prominent, recent studies have uncovered its participation in normal physiological processes. During embryonic development, CEA is involved in cell adhesion, contributing to tissue organization and morphogenesis. Additionally, CEA expression can be induced in inflammatory conditions, suggesting its involvement in immune responses and tissue repair mechanisms.
CEA as a Diagnostic and Therapeutic Target:
The diverse expression patterns of CEA in various diseases make it a valuable diagnostic tool. CEA assays are widely used for cancer screening, monitoring disease progression, and assessing treatment efficacy. Moreover, CEA’s presence on the surface of cancer cells has made it a target for immunotherapy, enabling the development of targeted therapies aimed at specifically eradicating CEA-positive tumor cells.
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 :
UBE2N HumanDescription:
Ubiquitin Conjugating Enzyme E2N Human Recombinant
Ubiquitin-conjugating enzyme E2 N, Bendless-like ubiquitin-conjugating enzyme, Ubc13, Ubiquitin carrier protein N, Ubiquitin-protein ligase N, UBE2N, BLU, MGC8489, UbcH-ben, MGC131857.
Product # :
ENZ-104Price :
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Description
UBE2N produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-152a.a.) and having a molecular mass of 19.3kDa.UBE2N is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2N solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
UBE2N belongs to the E2 ubiquitin-conjugating enzyme family. UBE2N catalyzes the ATP-dependent synthesis of non-canonical polyubiquitin chains, a process which doesn’t set in motion proteasomal degradation. UBE2N mediates the transcription of some target genes and is believed to have a role in cell cycle progression; cellular differentiation and DNA repair mechanisms which ensure cell survival after DNA damage.
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Synonyms
Ubiquitin-conjugating enzyme E2 N, Bendless-like ubiquitin-conjugating enzyme, Ubc13, Ubiquitin carrier protein N, Ubiquitin-protein ligase N, UBE2N, BLU, MGC8489, UbcH-ben, MGC131857.
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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 MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI.
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 :
HDAC8 MouseDescription:
Histone Deacetylase 8 Mouse Recombinant
Histone deacetylase 8, HD8, Hdac8.
Product # :
ENZ-1026Price :
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Shipped with Ice Packs
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Description
HDAC8 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 383 amino acids (1-377 a.a.) and having a molecular mass of 42.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).HDAC8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HDAC8 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.
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Synonyms
Histone deacetylase 8, HD8, Hdac8.
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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
MEMPEEPANS GHSLPPVYIY SPEYVSICDS LVKVPKRASM VHSLIEAYAL HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDEDH PDSIEYGLGY DCPATEGIFD YAAAIGGGTI TAAQCLIDGK CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFD RILYVDLDLH HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDMSDVGLG KGRYYSVNVP IQDGIQDEKY YHICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY VLQWQLATLI LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH RIQQILNYIK GNLKHVVHHH HHH.
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 :
CTSD AntibodyDescription:
Cathepsin D, Mouse Anti Human
Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.
Product # :
ANT-324Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.
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Synonyms
Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.
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Physical Appearance
Sterile Filtered colorless solution.
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Immunogen
Anti-human CTSD mAb is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CTSD amino acids 21-412 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
P4G2AT.
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Applications
CTSD antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
CTSD antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
UTI HumanDescription:
Urinary Trypsin Inhibitor-Ulinastatin Human
UTI, Ulinastatin, Urinary Trypsin Inhibitor.
Product # :
PRO-321Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ulinastatin is derived from human urine.
Source
Human Urine.
Formulation
Lyophilized from a (1mg/ml) solution containing no additives.
Biological Activity
Human UTI has an activity of 2350IU/mg.
More Info
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Introduction
Urinary-Trypsin Inhibitor is a glucoprotein proteinase inhibitor which inhibits the activity of trypsin, chymotrypsin, lactate, lipase, hyaluronidase and various pancreatic enzymes. Ulinastatin is effective for acute pancreatitis, chronic recurrent pancreatitis and hemorrhagic, traumatic and endotoxic shocks. Ulinastatin is has strong inhibition effect to various protease, sugar and fat hydrolase. Ulinastatin precursor is proteolytically processed into distinct functioning proteins. Urinary trypsin inhibitor belongs to the superfamily of Kunitz-type protease inhibitors and plays an important role in many physiological and pathological processes. Uristatin gene is located on chromosome 9 in a cluster of lipocalin genes.
High levels of Ulinastatin secretion is an early marker of renal tubular involvement and has radical scavenging activity. Bikunin localizes cell membrane.
Free uristatin and bikunin pass readily into urine and are primarily bound to heavy chains that constitute the proinhibitor form in plasma. UTI has a calculated Mw of approx. 20kDa and 40kDa by SDS-PAGE analysis.
Ulinastatin particularly interacts with ORF3 protein of hepatitis E virus and in charge for enhancing alpha microglobulin export from the hepatocyte. -
Synonyms
UTI, Ulinastatin, Urinary Trypsin Inhibitor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized UTI between 2-8°C, do not freeze. Upon reconstitution UTI 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 UTI in sterile 18MΩ-cm H2O not less than 100µg/ml, 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.
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Name :
CTSZ AntibodyDescription:
Cathepsin-Z, Mouse Anti Human
Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.
Product # :
ANT-528Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
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.
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Synonyms
Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human CTSZ mAb, clone PAT6G11AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CTSZ protein 62-303 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
PAT6G11AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
CTSZ antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
PLA2G1B HumanDescription:
Secreted Phospholipase A2-IB Human Recombinant
Phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IB phospholipase A2, PLA2, PLA2A, PPLA2, sPLA2-IB,MGC119834, MGC119835, PLA2G1B.
Product # :
ENZ-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secreted Phospholipase A2-IB Human Recombinant is manufactured with N-terminal fusionf HisTag. PLA2G1B His-Tagged Fusion Protein is 16 kDa containing 126 amino acid residues of the human secreted phospholipase A2-IB and 16 additional amino acid residues - HisTag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Group IB secretory phospholipase A2 (sPLA2-IB) mediates cell proliferation, cell migration, hormone release and eicosanoid production via its receptor in peripheral tissues. In the CNS, high-affinity binding sites of sPLA2-IB have been documented. sPLA2-IB induced neuronal cell death in a concentrationdependent manner depending on PGD2 metabolites, especially Delta12-PGJ2 that might mediate sPLA2-IB-induced apoptosis. The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of lowmolecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
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Synonyms
Phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IB phospholipase A2, PLA2, PLA2A, PPLA2, sPLA2-IB,MGC119834, MGC119835, PLA2G1B.
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Physical Appearance
Lyophilized (freeze-dried) powder.
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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.
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Solubility
Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MRGSHHHHHH GMASHMAVWQ FRKMIKCVIP GSDPFLEYNN YGCYCGLGGS GTPVDELDKC CQTHDNCYDQ AKKLDSCKFL LDNPYTHTYS YSCSGSAITC SSKNKECEAF ICNCDRNAAI CFSKAPYNKA HKNLDTKKYC QS.
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 :
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 :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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.
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 :
SUOX HumanDescription:
Sulfite Oxidase Human Recombinant
Sulfite Oxidase, EC 1.8.3.1, Sulfite oxidase, mitochondrial.
Product # :
ENZ-887Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SUOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 489 amino acids (80-545 a.a) and having a molecular mass of 53.9kDa. SUOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SUOX protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Sulfite oxidase, also known as SUOX is a homodimeric protein localized to the intermembrane space of mitochondria. Each subunit includes a heme domain as well as a molybdopterin-binding domain. The SUOX enzyme catalyzes the oxidation of sulfite to sulfate, the last reaction in the oxidative degradation of the sulfur amino acids cysteine and methionine. In addition, the deficiency of SUOX results in neurological abnormalities which are often fatal at an early age.
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Synonyms
Sulfite Oxidase, EC 1.8.3.1, Sulfite oxidase, mitochondrial.
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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 MGSESTHIYT KEEVSSHTSP ETGIWVTLGS EVFDVTEFVD LHPGGPSKLM LAAGGPLEPF WALYAVHNQS HVRELLAQYK IGELNPEDKV APTVETSDPY ADDPVRHPAL KVNSQRPFNA EPPPELLTEN YITPNPIFFT RNHLPVPNLD PDTYRLHVVG APGGQSLSLS LDDLHNFPRY EITVTLQCAG NRRSEMTQVK EVKGLEWRTG AISTARWAGA RLCDVLAQAG HQLCETEAHV CFEGLDSDPT GTAYGASIPL ARAMDPEAEV LLAYEMNGQP LPRDHGFPVR VVVPGVVGAR HVKWLGRVSV QPEESYSHWQ RRDYKGFSPS VDWETVDFDS APSIQELPVQ SAITEPRDGE TVESGEVTIK GYAWSGGGRA VIRVDVSLDG GLTWQVAKLD GEEQRPRKAW AWRLWQLKAP VPAGQKELNI VCKAVDDGYN VQPDTVAPIW NLRGVLSNAW HRVHVYVSP.
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 :
AUH HumanDescription:
AU RNA Binding Protein/Enoyl-CoA Hydratase Human Recombinant
Methylglutaconyl-CoA hydratase, mitochondrial, AU-specific RNA-binding enoyl-CoA hydratase, AU-binding protein/enoyl-CoA hydratase, AUH.
Product # :
ENZ-046Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AUH Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 293 amino acids (68-339 a.a.) and having a molecular mass of 31.4kDa. The AUH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AUH solution (1 mg/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.
More Info
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Introduction
Mitochondrial methylglutaconyl-CoA hydratase (AUH) is involved in the amino acid degradation pathway by catalyzing the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA and water. AUH Human is expressed as a single mRNA species of 1.8 kb, and translated as a 40kDa precursor protein which is consequently processed to a 32kDa mature form. AUH has a very low enoyl-CoA hydratase activity. The AUH protein binds to the AU-rich element (ARE), which is a common element found in the 3' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. AU-rich elements are involved in directing RNA to rapid degradation and deadenylation. In addition, AUH is homologous to enol-CoA hydratase, which is an enzyme involved in fatty acid degradation, and has been shown to have intrinsic hydratase enzymatic activity. AUH is therefore a bifunctional chimera between RNA binding and metabolic enzyme activity.
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Synonyms
Methylglutaconyl-CoA hydratase, mitochondrial, AU-specific RNA-binding enoyl-CoA hydratase, AU-binding protein/enoyl-CoA hydratase, AUH.
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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 MSSEMKTEDE LRVRHLEEEN RGIVVLGINR AYGKNSLSKN LIKMLSKAVD ALKSDKKVRT IIIRSEVPGI FCAGADLKER AKMSSSEVGP FVSKIRAVIN DIANLPVPTI AAIDGLALGG GLELALACDI RVAASSAKMG LVETKLAIIP GGGGTQRLPR AIGMSLAKEL IFSARVLDGK EAKAVGLISH VLEQNQEGDA AYRKALDLAR EFLPQGPVAM RVAKLAINQG MEVDLVTGLA IEEACYAQTI PTKDRLEGLL AFKEKRPPRY KGE.
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.