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1000 results found for “creatine kinases”
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Name :
IMPA2 HumanDescription:
Inositol Monophosphatase 2 Human Recombinant
Inositol monophosphatase 2, IMP 2, IMPase 2, Inositol-1(or 4)-monophosphatase 2, Myo-inositol monophosphatase A2, IMPA2, IMP.18P.
Product # :
ENZ-070Price :
Quantity :
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Shipped with Ice Packs
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Description
IMPA2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 308 amino acids (1-288 a.a.) and having a molecular mass of 33.5kDa. The IMPA2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IMPA2 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
IMPA2 is a member of the inositol monophosphatase family. IMPA2 catalyzes the dephosphoylration of inositol monophosphate and has a significant role in phosphatidylinositol signaling. IMPA2 can use the myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. IMPA2 is a pharmacological target for lithium Li(+) action in brain. IMPA2 is considered to have a role in schizophrenia and bipolar disorder.
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Synonyms
Inositol monophosphatase 2, IMP 2, IMPase 2, Inositol-1(or 4)-monophosphatase 2, Myo-inositol monophosphatase A2, IMPA2, IMP.18P.
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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 MKPSGEDQAA LAAGPWEECF QAAVQLALRA GQIIRKALTE EKRVSTKTSA ADLVTETDHL VEDLIISELR ERFPSHRFIA EEAAASGAKC VLTHSPTWII DPIDGTCNFV HRFPTVAVSI GFAVRQELEF GVIYHCTEER LYTGRRGRGA FCNGQRLRVS GETDLSKALV LTEIGPKRDP ATLKLFLSNM ERLLHAKAHG VRVIGSSTLA LCHLASGAAD AYYQFGLHCW DLAAATVIIR EAGGIVIDTS GGPLDLMACR VVAASTREMA MLIAQALQTI NYGRDDEK.
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 :
GNMT Human, ActiveDescription:
Glycine N-Methyltransferase Human Recombinant , Active
Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP.
Product # :
ENZ-1059Price :
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Description
GNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295 a.a) and having a molecular mass of 34.9kDa.GNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GNMT protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37C.
More Info
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Introduction
GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine and sarcosine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine (sarcosine) with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.
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Synonyms
Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20
Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP. -
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 MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD.
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 :
TPA (36-310) HumanDescription:
Tissue Plasminogen Activator (36-310 a.a.) Human Recombinant
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA, Alteplase, Reteplase, Plasminogen Activator, Tissue, Plasminogen/Activator Kringle.
Product # :
ENZ-1050Price :
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Description
TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 284 amino acids (36-310a.a.) and having a molecular mass of 32.0kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).TPA is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TPA protein solution (0.25mg/ml) contains 50mM MES(pH5.5),10% glycerol, 100mM NaCl and 5mM CaCl2.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism. -
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA, Alteplase, Reteplase, Plasminogen Activator, Tissue, Plasminogen/Activator Kringle.
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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
ADPSYQVICR DEKTQMIYQQ HQSWLRPVLR SNRVEYCWCN SGRAQCHSVP VKSCSEPRCF NGGTCQQALY FSDFVCQCPE GFAGKCCEID TRATCYEDQG ISYRGTWSTA ESGAECTNWN SSALAQKPYS GRRPDAIRLG LGNHNYCRNP DRDSKPWCYV FKAGKYSSEF CSTPACSEGN SDCYFGNGSA YRGTHSLTES GASCLPWNSM ILIGKVYTAQ NPSAQALGLG KHNYCRNPDG DAKPWCHVLK NRRLTWEYCD VPSCSTCGLR QYSQPQFRHH HHHH.
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 :
UPP1 SalmonellaDescription:
Uridine Phosphorylase Salmonella Typhimurium Recombinant
Uridine phosphorylase, EC 2.4.2.3, UrdPase, UPase, StUP.
Product # :
ENZ-348Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Uridine phosphorylase Salmonella typhimurium Recombinantproduced in E.Coli is a non-glycosylated, polypeptide having a total molecular mass of 163068 Dalton.
Source
Escherichia Coli.
Formulation
The UPase was lyophilized from 1mg/ml solution containing 25mM Tris-HCl, pH 8.0, 0.15M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Uridine phosphorylase from Salmonella typhimurium (StUP) catalyzes the reversible phosphorolysis of uridine with the formation of ribose-1-phosphate and uracil.
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Synonyms
Uridine phosphorylase, EC 2.4.2.3, UrdPase, UPase, StUP.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized UPase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UPase 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 UPase in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Enzymatic Activity
30 U/mg protein.
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Unit Definition
One unit phosphorylates 1μm of uridine within 1 min at pH 7.3.
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 :
CYB5R1 HumanDescription:
Cytochrome B5 Reductase 1 Human Recombinant
B5R.1, B5R1, B5R2, humb5R2, NQO3A2, NADH-cytochrome b5 reductase 1, CYB5R1, NAD (P) H: quinone oxidoreductase type 3 polypeptide A2.
Product # :
ENZ-727Price :
Quantity :
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Shipped with Ice Packs
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Description
CYB5R1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 300 amino acids (29-305) and having a molecular mass of 33.8kDa. CYB5R1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CYB5R1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cytochrome b5 reductase 1 (CYB5R1) is a part of the flavoprotein pyridine nucleotide cytochrome reductase family. CYB5R1 is engaged in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin decrease.
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Synonyms
B5R.1, B5R1, B5R2, humb5R2, NQO3A2, NADH-cytochrome b5 reductase 1, CYB5R1, NAD (P) H: quinone oxidoreductase type 3 polypeptide A2.
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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 MGSLVRRSRR PQVTLLDPNE KYLLRLLDKT TVSHNTKRFR FALPTAHHTL GLPVGKHIYL STRIDGSLVI RPYTPVTSDE DQGYVDLVIK VYLKGVHPKF PEGGKMSQYL DSLKVGDVVE FRGPSGLLTY TGKGHFNIQP NKKSPPEPRV AKKLGMIAGG TGITPMLQLI RAILKVPEDP TQCFLLFANQ TEKDIILRED LEELQARYPN RFKLWFTLDH PPKDWAYSKG FVTADMIREH LPAPGDDVLV LLCGPPPMVQ LACHPNLDKL GYSQKMRFTY.
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 :
PRDX1 HumanDescription:
Peroxiredoxin-1 Human Recombinant
Peroxiredoxin-1, EC 1.11.1.15, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Proliferation-associated gene protein, Natural killer cell-enhancing factor A, NKEF-A, PRDX1, TDPX2, PRDX-1, PAG, PAGA, PRX1, PAGB, PRXI, MSP23, NKEFA.
Product # :
ENZ-372Price :
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Shipped with Ice Packs
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Description
Peroxiredoxin Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain (1-199) containing 219 amino acids and having a molecular mass of 24 kDa. The Peroxiredoxin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Peroxiredoxin solution (1mg/ml) contains 20mM Tris-HCl pH-7.5 & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Enzymatic activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for minute. Specific activity is >2,000pmol/min/ug.
More Info
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Introduction
PRDX1 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX1 is an important protector of red blood cells against reactive oxygen species and in tumor prevention.
PRDX1 is antioxidant protective in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX1 has a proliferative effect and is involved in cancer development or progression.
Peroxiredoxin-1 is plays a role in redox regulation of the cell. Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. Peroxiredoxin is involved in eliminating peroxides generated during metabolism. Peroxiredoxin participates in the signaling cascades of growth factors and TNF-alpha by regulating the intracellular concentrations of h(2)o(2). -
Synonyms
Peroxiredoxin-1, EC 1.11.1.15, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Proliferation-associated gene protein, Natural killer cell-enhancing factor A, NKEF-A, PRDX1, TDPX2, PRDX-1, PAG, PAGA, PRX1, PAGB, PRXI, MSP23, NKEFA.
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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 MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS DRAEEFKKLN CQVIGASVDS HFCHLAWVNT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITVNDLPVG RSVDETLRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVQK SKEYFSKQK.
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 :
LYN HumanDescription:
v-yes-1 Yamaguchi Sarcoma Viral Related Oncogene Human Recombinant
Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.
Product # :
PRO-136Price :
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Shipped with Ice Packs
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Description
LYN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 535 amino acids (1-512) and having a molecular mass of 61.0kDa. LYN is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The LYN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) ,0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Tyrosine-protein kinase Lyn (LYN) belongs to the src family of non-receptor protein tyrosine kinases, which is primarily expressed in haematopoietic tissues. LYN protein is involved in induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. LYN protein stimulates SAPK by a MKK7- and MEKK1-dependent mechanism. The LYN - MEKK1 - MKK7 - SAPK pathway is efficient in the induction of apoptosis by genotoxic agents.
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Synonyms
Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.
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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 MGSMGCIKSK GKDSLSDDGV DLKTQPVRNT ERTIYVRDPT SNKQQRPVPE SQLLPGQRFQ TKDPEEQGDI VVALYPYDGI HPDDLSFKKG EKMKVLEEHG EWWKAKSLLT KKEGFIPSNY VAKLNTLETE EWFFKDITRK DAERQLLAPG NSAGAFLIRE SETLKGSFSL SVRDFDPVHG DVIKHYKIRS LDNGGYYISP RITFPCISDM IKHYQKQADG LCRRLEKACI SPKPQKPWDK DAWEIPRESI KLVKRLGAGQ FGEVWMGYYN NSTKVAVKTL KPGTMSVQAF LEEANLMKTL QHDKLVRLYA VVTREEPIYI ITEYMAKGSL LDFLKSDEGG KVLLPKLIDF SAQIAEGMAY IERKNYIHRD LRAANVLVSE SLMCKIADFG LARVIEDNEY TAREGAKFPI KWTAPEAINF GCFTIKSDVW SFGILLYEIV TYGKIPYPGR TNADVMTALS QGYRMPRVEN CPDELYDIMK MCWKEKAEER PTFDYLQSVL DDFYTATEGQ YQQQP.
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 :
GKN1 HumanDescription:
Gastrokine 1 Human Recombinant
BRICHOS domain containing 1, 18 kDa antrum mucosa protein, gastrokine 1, Protein CA11, AMP-18, BRICD1, foveolin, FOV.
Product # :
PRO-1206Price :
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Description
GKN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 223 amino acids (1-199) and having a molecular mass of 24.5 kDa.GKN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GKN1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Gastrokine-1 (GKN1) is a member of the gastrokine family. GKN1 has mitogenic activity and is involved in preserving the integrity of the gastric mucosal epithelium. GKN1 is down-regulated in human gastric cancer tissue in comparison to normal gastric mucosa. GKN1 is expressed in the stomach; however no expression is detected in cancer tissue or gastric cancer cell lines.
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Synonyms
BRICHOS domain containing 1, 18 kDa antrum mucosa protein, gastrokine 1, Protein CA11, AMP-18, BRICD1, foveolin, FOV.
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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 MGSH MLAYSS VHCFREDKMK FTIVFAGLLG VFLAPALANY NINVNDDNNN AGSGQQSVSV NNEHNVANVD NNNGWDSWNS IWDYGNGFAA TRLFQKKTCI VHKMNKEVMP SIQSLDALVK EKKLQGKGPG GPPPKGLMYS VNPNKVDDLS KFGKNIANMC RGIPTYMAEE MQEASLFFYS GTCYTTSVLW IVDISFCGDT VEN.
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 :
Lysozyme HumanDescription:
Lysozyme Human Recombinant
EC 3.2.1.17, LYZ, Lysozyme.
Product # :
ENZ-1159Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Lysozyme produced in Plant is a non-glycosylated, polypeptide chain containing 130 amino acids and having a molecular mass of 14.7kDa. The Recombinant Human Lysozyme is purified by proprietary chromatographic techniques.
Source
Oryza sativa (rice).
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Purity as determined by SDS-PAGE is greater than 90%.
Biological Activity
1.6x105 U/mg.
More Info
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Introduction
Lysozymeis an antimicrobial enzyme produced by animals that are part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.Lysozymes have primarily a bacteriolytic function - those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
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Synonyms
EC 3.2.1.17, LYZ, Lysozyme.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) off white powder.
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Stability
Store the lyophilized Lysozyme between 2-8°C, do not freeze. Upon reconstitution Lysozyme 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
Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 1mg/ml in PBS.
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 :
GGPS1 HumanDescription:
Geranylgeranyl Diphosphate Synthase 1 Human Recombinant
GGPPS, GGPPS1, GGPP synthetase.
Product # :
ENZ-555Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GGPS1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-300 a.a.) and having a molecular mass of 37 kDa. The GGPS1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GGPS1 Human recombinant (1mg/ml) protein solution contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GGPS1 is PART of the prenyltransferase family. GGPS1 is widely expressed in testis, heart and skeletal muscle, GGPS1 is localized in the cytoplasm and catalyzes the formation of geranylgeranyl pyrophosphate, a precursor of geranylgeranylated proteins and carotenoids. GGPS1 is a significant enzyme that is responsible for the C20-prenylation of proteins and for the regulation of a nuclear hormone receptor.
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Synonyms
GGPPS, GGPPS1, GGPP synthetase.
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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 MEKTQETVQR ILLEPYKYLL QLPGKQVRTK LSQAFNHWLK VPEDKLQIII EVTEMLHNAS LLIDDIEDNS KLRRGFPVAH SIYGIPSVIN SANYVYFLGL EKVLTLDHPD AVKLFTRQLL ELHQGQGLDI YWRDNYTCPT EEEYKAMVLQ KTGGLFGLAV
GLMQLFSDYK EDLKPLLNTL GLFFQIRDDY ANLHSKEYSE NKSFCEDLTE GKFSFPTIHA IWSRPESTQV QNILRQRTEN IDIKKYCVHY LEDVGSFEYT RNTLKELEAK AYKQIDARGG NPELVALVKH LSKMFKEENE.
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 Human, ActiveDescription:
Glutamic-Oxaloacetic Transaminase 2 Human Recombinant, Active
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
Product # :
ENZ-998Price :
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Shipped with Ice Packs
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Description
GOT2 Recombinant Human 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 47kDa. The GOT2 fused to a 23 amino acid his tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GOT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 60 units/mg, and is defined as the amount of enzyme that convert 1umole of α-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C.More Info
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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 is invloved in amino acid metabolism and the urea and tricarboxylic acid cycles. The 2 enzymes are homodimeric and demonstrate close homology.
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Synonyms
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSSWWTHV EMGPPDPILG VTEAFKRDTN SKKMNLGVGA YRDDNGKPYV LPSVRKAEAQ IAAKNLDKEY LPIGGLAEFC KASAELALGE NSEVLKSGRF VTVQTISGTG ALRIGASFLQ RFFKFSRDVF LPKPTWGNHT PIFRDAGMQL QGYRYYDPKT CGFDFTGAVE DISKIPEQSV LLLHACAHNP TGVDPRPEQW KEIATVVKKR NLFAFFDMAY QGFASGDGDK DAWAVRHFIE QGINVCLCQS YAKNMGLYGE RVGAFTMVCK DADEAKRVES QLKILIRPMY SNPPLNGARI AAAILNTPDL RKQWLQEVKV MADRIIGMRT QLVSNLKKEG STHNWQHITD QIGMFCFTGL KPEQVERLIK EFSIYMTKDG RISVAGVTSS NVGYLAHAIH QVTK.
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 :
CYSH E.ColiDescription:
Phosphoadenosine phosphosulfate reductase E.Coli Recombinant
Phosphoadenosine phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, PAPS reductase, thioredoxin dependent, PAPS sulfotransferase, PAdoPS reductase, cysH, b2762, JW2732.
Product # :
ENZ-131Price :
Quantity :
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Description
CYSH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-244 a.a.) and having a molecular mass of 30.1kDa.CYSH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CYSH protein solution (0.5mg/ml) conteins 20% Glycerol, Phosphate-Buffered Saline (pH 7.4) and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
CysH (Phosphoadenosine phosphosulfate reductase) is a member of the PAPS reductase family, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The 3 substrates of the CysH enzyme are adenosine 3',5'-bisphosphate, sulfite, and thioredoxin disulfide, whereas its two products are 3'-phosphoadenylyl sulfate and thioredoxin.
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Synonyms
Phosphoadenosine phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, PAPS reductase, thioredoxin dependent, PAPS sulfotransferase, PAdoPS reductase, cysH, b2762, JW2732.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
CYSH E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG LHEG.
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 :
UBE2K HumanDescription:
Ubiquitin-Conjugating Enzyme E2K Human Recombinant
HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.
Product # :
ENZ-339Price :
Quantity :
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Description
UBE2K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-200a.a.) and having a molecular mass of 26.5kDa.UBE2K is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 50mM NaCl, and 10% glycerol.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
UBE2K belongs to the ubiquitin-conjugating enzymes family which take part in many cellular processes such as selective protein degradation, DNA repair, cell cycle control, and sporulation. In this mechanism, the ATP-coupled activation and subsequent ligation of ubiquitin are catalyzed by separate enzymes functionally linked by ubiquitin carrier protein UBC1. In addition, UBE2K is involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with amyloid-?, huntingtin, and MHC-heavy chain proteins.
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Synonyms
HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMANI AVQRIKREFK EVLKSEETSK NQIKVDLVDE NFTELRGEIA GPPDTPYEGG RYQLEIKIPE TYPFNPPKVR FITKIWHPNI SSVTGAICLD ILKDQWAAAM TLRTVLLSLQ ALLAAAEPDD PQDAVVANQY KQNPEMFKQT ARLWAHVYAG APVSSPEYTK KIENLCAMGF DRNAVIVALS SKSWDVETAT ELLLSN.
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 :
SRR HumanDescription:
Serine Racemase Human Recombinant
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
Product # :
ENZ-232Price :
Quantity :
Shipping Method :
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Description
SRR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-340) and having a molecular mass of 39.1kDa.SRR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Serine racemase (SRR) is an enzyme which generates D-serine from L-serine. D-serine functions as a neuronal signaling molecule by activating NMDA receptors in the brain. Mammalian SRR is a pyridoxal 5'-phosphate dependent enzyme which catalyzes both the racemization of L-serine to D-serine and also the elimination of water from L-serine, producing pyruvate and ammonia. The SRR enzyme is physiologically stimulated by divalent cations (e.g., magnesium) and is allosterically activated by the magnesium/ATP complex.
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Synonyms
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
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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 MGSHMCAQYC ISFADVEKAH INIRDSIHLT PVLTSSILNQ LTGRNLFFKC ELFQKTGSFK IRGALNAVRS LVPDALERKP KAVVTHSSGN HGQALTYAAK LEGIPAYIVV PQTAPDCKKL AIQAYGASIV YCEPSDESRE NVAKRVTEET EGIMVHPNQE PAVIAGQGTI ALEVLNQVPL VDALVVPVGG GGMLAGIAIT VKALKPSVKV YAAEPSNADD CYQSKLKGKL MPNLYPPETI ADGVKSSIGL NTWPIIRDLV DDIFTVTEDE IKCATQLVWE RMKLLIEPTA GVGVAAVLSQ HFQTVSPEVK NICIVLSGGN VDLTSSITWV KQAERPASYQ SVSV.
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 :
NMT2 HumanDescription:
N-Myristoyltransferase 2 Human Recombinant
Glycylpeptide N-tetradecanoyltransferase 2, Myristoyl-CoA:protein N-myristoyltransferase 2, NMT 2, Peptide N-myristoyltransferase 2, Type II N-myristoyltransferase, NMT2.
Product # :
ENZ-068Price :
Quantity :
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Description
NMT2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 518 amino acids (1-498 a.a.) and having a molecular mass of 59.1kDa. The NMT2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NMT2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycylpeptide N-tetradecan-oyltransferases 2 (NMT2) is a cytoplasmic protein which is a member of the NMT family of proteins. The proteins in the NMT family catalyze the addition of a myristoyl group to the N-terminal glycine residue of eukaryotic, fungal and viral proteins. These proteins are mostly detected in the heart, gut, kidney, liver and placenta. NMT catalyzes the reaction of N-terminal myristoylation of various signaling proteins. NMT transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. There are several distinct NMTs which vary in the molecular weight and /or subcellular distribution.
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Synonyms
Glycylpeptide N-tetradecanoyltransferase 2, Myristoyl-CoA:protein N-myristoyltransferase 2, NMT 2, Peptide N-myristoyltransferase 2, Type II N-myristoyltransferase, NMT2.
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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
MGSSHHHHHH SSGLVPRGSH MAEDSESAAS QQSLELDDQD TCGIDGDNEE ETEHAKGSPG GYLGAKKKKK KQKRKKEKPN SGGTKSDSAS DSQEIKIQQP SKNPSVPMQK LQDIQRAMEL LSACQGPARN IDEAAKHRYQ FWDTQPVPKL DEVITSHGAI EPDKDNVRQE PYSLPQGFMW DTLDLSDAEV LKELYTLLNE NYVEDDDNMF RFDYSPEFLL WALRPPGWLL QWHCGVRVSS NKKLVGFISA IPANIRIYDS VKKMVEINFL CVHKKLRSKR VAPVLIREIT RRVNLEGIFQ AVYTAGVVLP KPIATCRYWH RSLNPKKLVE VKFSHLSRNM TLQRTMKLYR LPDVTKTSGL RPMEPKDIKS VRELINTYLK QFHLAPVMDE EEVAHWFLPR EHIIDTFVVE SPNGKLTDFL SFYTLPSTVM HHPAHKSLKA AYSFYNIHTE TPLLDLMSDA LILAKSKGFD VFNALDLMEN KTFLEKLKFG IGDGNLQYYL YNWRCPGTDS EKVGLVLQ.
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 :
CDA HumanDescription:
Cytidine Deaminase Human Recombinant
Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.
Product # :
ENZ-007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDA Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids (1-146 a.a.) and having a molecular mass of 18.3kDa. The CDA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDA solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 1mM DTT, 2mM EDTA, 100mM NaCl and 40% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 10,000pmol/min/ug, and is defined as the amount of required to deaminate 1.0pmole of cytidine per min at pH 7.5 at 25C.
More Info
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Introduction
Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. CDA is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as Ara-C and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function. CDA can form homotetramers and is generally expressed in granulocytes. Mutations in the CDA gene are linked to decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.
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Synonyms
Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.
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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 MAQKRPACTL KPECVQQLLV CSQEAKQSAY CPYSHFPVGA ALLTQEGRIF KGCNIENACY PLGICAERTA IQKAVSEGYK DFRAIAIASD MQDDFISPCG ACRQVMREFG TNWPVYMTKP DGTYIVMTVQ ELLPSSFGPE DLQKTQ.
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 :
ALPP Human, ActiveDescription:
Alkaline Phosphatase Placental Human Recombinant, BioActive
3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
Product # :
ENZ-1133Price :
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Description
ALPP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 494 amino acids (23-506 a.a.) and having a molecular mass of 53.9kDa. ALPP is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ALPP protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,500unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.
More Info
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Introduction
Placental alkaline phosphatase also known as PLAP is a membranal siaglycoprotein enzyme typicallyfoundin high concentration in syncytiotrophoblasts in the placenta amid the 3th trimester of gestation. The expression of PLAP was at firstconsidered to be onlyin the term placenta, though, a human PLAP-like variant has been found,thathas more than 85% homology with PLAP itself. PLAP is expressed strictly in normal term placenta, endocervix & fallopian tube and in ovarian and proximal gastrointestinal tumors. It is also widely expressed in germ cell tumors and more recently found in seminomas.
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Synonyms
3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADLMIIPVEE ENPDFWNREA AEALGAAKKL QPAQTAAKNL IIFLGDGMGV STVTAARILK GQKKDKLGPE LPLAMDRFPY VALSKTYNVD KHVPDSGATA TAYLCGVKGN FQTIGLSAAA RFNQCNTTRG NEVISVMNRA KKAGKSVGVV TTTRVQHASP AGTYAHTVNR NWYSDADVPA SARQEGCQDI ATQLISNMDI DVILGGGRKY MFRMGTPDPE YPDDYSQGGT RLDGKNLVQE WLAKRQGARY VWNRTELMQA SLDPSVTHLM GLFEPGDMKY EIHRDSTLDP SLMEMTEAAL RLLSRNPRGF FLFVEGGRID HGHHESRAYR ALTETIMFDD AIERAGQLTS EEDTLSLVTA DHSHVFSFGG YPLRGSSIFG LAPGKARDRK AYTVLLYGNG PGYVLKDGAR PDVTESESGS PEYRQQSAVP LDEETHAGED VAVFARGPQA HLVHGVQEQT FIAHVMAFAA CLEPYTACDL APPAGTTDHH HHHH.
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 :
GPBB HumanDescription:
Glycogen Phosphorylase Human Recombinant
Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.
Product # :
ENZ-282Price :
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Description
Glycogen Phosphorylase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain. The Human GPBB mature chain: 2 - 843 aa; that is a total of 842 aa having a molecular mass of 96695.96 Dalton. The theoretical pI is 6.40.The GPBB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of protein contains 50% glycerol.
Purity
Greater than 85.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Glycogen phosphorylase is one of the phosphorylaseenzymes(EC2.4.1.1). It breaks up glycogeninto glucosesubunits. Glycogenis left with one less glucosemolecule, and the free glucosemolecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphateby the enzyme phosphoglucomutase.
Glycogen phosphorylase can only act on linearchainsof glycogen(a 1-4 glycosidic linkage). Its work will immediately come to a halt four residues away from a 1-6 branch(which are exceedingly common in glycogen). In these situations, a debranching enzymeis necessary, which will straighten out the chain in that area. Additionally, an alpha 1-6 glucosidaseenzymeis required to break the remaining 1-6 residue that remains in the new linear chain. After all this is done, glycogen phosphorylase can continue.
An insulinstimulated enzyme known as phosphoprotein phosphatase(PP-1) inactivates glycogen phosphorylase to prevent glycogen break up.
GPBB - a sensitive marker for the AMI diagnosis within 4 hours after the onset of chest pain. It has also been shown that GPBB is increased in a considerable proportion of AMI patients within 2-3 hours from chest pain onset. GPBB is increased early in patients with unstable angina. GPBB can also be a sensitive marker for the detection of peri-operative myocardial ischaemia and infarction in patients undergoing coronary artery bypass grafting. -
Synonyms
Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.
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Physical Appearance
Sterile Filtered colourless liquid formualtion.
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Stability
GPBB although stable at 10°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.
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Applications
Immunoassays and western blot.
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 :
POFUT1 HumanDescription:
Protein O-Fucosyltransferase 1 Human Recombinant
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
Product # :
ENZ-679Price :
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Description
POFUT1 Human Recombinant produced in E. coli is a single polypeptide chain containing 385 amino acids (27-388) and having a molecular mass of 43.7 kDa. POFUT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The POFUT1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
GDP-fucose protein O-fucosyltransferase 1 (POUFUT1), belongs to the glycosyltransferase O-Fuc family. POUFUT1 encodes a member of the glycosyltransferase O-Fuc family and Expressed mainly in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle.POUFUT1 adds O-fucose through an O-glycosidic linkage to Preserve serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and emitted proteins. POUFUT1 is involved in ligand-induced receptor signaling. Alternative splicing of this gene results in 2 transcript variants encoding different isoforms.POFUT1 participates in Notch signaling, as Notch ligands can use as POFUT1 substrates.
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Synonyms
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGSWDPAG YLLYCPCMGR FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA PTHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YREQWSQRFS PKEHPVLALP GAPAQFPVLE EHRPLQKYMV WSDEMVKTGE AQIHAHLVRP YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TAAPLTMTMC LPDLKEIQRA VKLWVRSLDA QSVYVATDSE SYVPELQQLF KGKVKVVSLK PEVAQVDLYI LGQADHFIGN CVSSFTAFVK RERDLQGRPS SFFGMDRPPK LRDEF.
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 :
MAT2B HumanDescription:
Methionine Adenosyltransferase II Beta Human Recombinant
MAT2-beta, MAT-2B, MAT2-B, DTDP-4-keto-6-deoxy-D-glucose 4-reductase, MAT-II, MATIIbeta, MAT II beta, Methionine adenosyltransferase 2 subunit beta, Methionine adenosyltransferase II beta, MGC12237, MSTP045, Nbla02999, SDR23E1, TGR, UNQ2435/PRO4995, MAT2B.
Product # :
ENZ-461Price :
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Description
Recombinant Human MAT2B produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-323 a.a) and having a molecular mass of 36.4 kDa. MAT2B is is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The MAT2B protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT, 1mM EDTA and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MAT2B is part of the methionine adenosyltransferase family. MAT2B catalyzes the biosynthesis of S-adenosylmethionine from methionine and ATP. MAT2B is the regulatory beta subunit of MAT. MAT2B expression in hepatoma cell lines increases DNA synthesis and thus take part in cell proliferation.
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Synonyms
MAT2-beta, MAT-2B, MAT2-B, DTDP-4-keto-6-deoxy-D-glucose 4-reductase, MAT-II, MATIIbeta, MAT II beta, Methionine adenosyltransferase 2 subunit beta, Methionine adenosyltransferase II beta, MGC12237, MSTP045, Nbla02999, SDR23E1, TGR, UNQ2435/PRO4995, MAT2B.
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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
MPEMPEDMEQ EEVNIPNRRV LVTGATGLLG RAVHKEFQQN NWHAVGCGFR RARPKFEQVN LLDSNAVHHI IHDFQPHVIV HCAAERRPDV VENQPDAASQ LNVDASGNLA KEAAAVGAFL IYISSDYVFD GTNPPYREED IPAPLNLYGK TKLDGEKAVL ENNLGAAVLR IPILYGEVEK LEESAVTVMF DKVQFSNKSA NMDHWQQRFP THVKDVATVC RQLAEKRMLD PSIKGTFHWS GNEQMTKYEM ACAIADAFNL PSSHLRPITD SPVLGAQRPR NTQLDCSKLE TLGIGQRTPF RIGIKESLWP FLIDKRWRQT VFH.
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 :
YARS HumanDescription:
Tyrosyl-tRNA Synthetase Human Recombinant
Tyrosyl-tRNA synthetase cytoplasmic, Tyrosyl--tRNA ligase, TyrRS, YARS, YRS, YTS, CMTDIC.
Product # :
ENZ-134Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
YARS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 548 amino acids (1-528 a.a.) and having a molecular mass of 61.3kDa.YARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
YARS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Tyrosyl-tRNA synthetase (YARS) is a member of the class I tRNA synthetase family. YARS is a vital enzyme which catalyzes the aminoacylation of tRNATrp with tryptophan, a critical function of the cell’s protein synthesis machinery. Expression of YARS is highly stimulated in human cells by the addition of IFN-gamma.
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Synonyms
Tyrosyl-tRNA synthetase cytoplasmic, Tyrosyl--tRNA ligase, TyrRS, YARS, YRS, YTS, CMTDIC.
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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 MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKIYW GTATTGKPHV AYFVPMSKIA DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVSYYENV IKAMLESIGV PLEKLKFIKG TDYQLSKEYT LDVYRLSSVV TQHDSKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD AQFGGIDQRK IFTFAEKYLP ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED VKKKLKKAFC EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT AYVDLEKDFA AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPM AKGPAKNSEP EEVIPSRLDI RVGKIITVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV VVLCNLKPQK MRGVESQGML LCASIEGINR QVEPLDPPAG SAPGEHVFVK GYEKGQPDEE LKPKKKVFEK LQADFKISEE CIAQWKQTNF MTKLGSISCK SLKGGNIS.
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 :
CYB5R2 HumanDescription:
Cytochrome B5 Reductase 2 Human Recombinant
CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.
Product # :
ENZ-799Price :
Quantity :
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Shipped with Ice Packs
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Description
CYB5R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a.) and having a molecular mass of 33.8kDa. CYB5R2 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
CYB5R2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytochrome b5 reductase 2 (CYB5R2) is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. CYB5R2 is responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).
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Synonyms
CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.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 MGSMNSRRRE PITLQDPEAK YPLPLIEKEK ISHNTRRFRF GLPSPDHVLG LPVGNYVQLL AKIDNELVVR AYTPVSSDDD RGFVDLIIKI YFKNVHPQYP EGGKMTQYLE NMKIGETIFF RGPRGRLFYH GPGNLGIRPD QTSEPKKTLA DHLGMIAGGT GITPMLQLIR HITKDPSDRT RMSLIFANQT EEDILVRKEL EEIARTHPDQ FNLWYTLDRP PIGWKYSSGF VTADMIKEHL PPPAKSTLIL VCGPPPLIQT AAHPNLEKLG YTQDMIFTY.
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 :
NDUFV3 HumanDescription:
NADH Dehydrogenase Flavoprotein 3 Human Recombinant
NADH Dehydrogenase (Ubiquinone) Flavoprotein 3 10kDa, Renal Carcinoma Antigen NY-REN-4, NADH-Ubiquinone Oxidoreductase 9 KDa Subunit, EC 1.6.5.311, CI-10k, Complex I 10kDa
Product # :
ENZ-749Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NDUFV3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (35-108) and having a molecular mass of 10.8kDa.NDUFV3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFV3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
NDUFV3 is one of no less than 41 subunits which form the NADH-ubiquinone oxidoreductase complex that is involved in the mitochondrial respiratory chain and assists in catalyzing the rotenone-sensitive oxidation of NADH and the reduction of ubiquinone. NDUFV3 is 1 of 3 proteins found in the flavoprotein fraction of the complex but it exact function is unknown. Two transcript variants encoding altered isoforms are known for this gene.
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Synonyms
NADH Dehydrogenase (Ubiquinone) Flavoprotein 3 10kDa, Renal Carcinoma Antigen NY-REN-4, NADH-Ubiquinone Oxidoreductase 9 KDa Subunit, EC 1.6.5.311, CI-10k, Complex I 10kDa
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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 MGSSAESGKS EKGQPQNSKK QSPPKKPAPV PAEPFDNTTY KNLQHHDYST YTFLDLNLEL SKFRMPQPSS GRESPRH
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 :
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 :
Quantity :
Shipping Method :
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.
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.