Search results
1000 results found for “Epimerase”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
GPT HumanDescription:
Glutamic-Pyruvate Transaminase Human Recombinant
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
Product # :
ENZ-192Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPT solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.
-
Synonyms
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS
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 :
NMNAT1 HumanDescription:
Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant
NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.
Product # :
ENZ-384Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NMNAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-279 a.a.) and having a molecular mass of 36 kDa. The NMNAT1 is fused to a 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NMNAT1 Human solution containing 20mM Tris pH-8, 0.1M NaCl, 1mM DTT, 1mM EDTA & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.
-
Synonyms
NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMENS EKTEVVLLAC GSFNPITNMH LRLFELAKDY MNGTGRYTVV KGIISPVGDA YKKKGLIPAY HRVIMAELAT KNSKWVEVDT WESLQKEWKE TLKVLRHHQE KLEASDCDHQ QNSPTLERPG RKRKWTETQD SSQKKSLEPK TKAVPKVKLL CGADLLESFA VPNLWKSEDI TQIVANYGLI CVTRAGNDAQ KFIYESDVLW KHRSNIHVVN EWIANDISST KIRRALRRGQSIRYLVPDLV QEYIEKHNLY SSESEDRNAG VILAPLQRNT AEAKT.
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 :
GYG1 HumanDescription:
Glycogenin-1 Human Recombinant
Glycogenin-1, GYG1, GYG.
Product # :
ENZ-431Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GYG1 Human Recombinant fused with a 32 amino acid His-T7 tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 365 amino acids (1-333 a.a.) and having a molecular mass of 41.2kDa.The GYG1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GYG1 solution contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Glycogenin-1 (GYG1) is an enzyme involved in glycogen biosynthesis. GYG1 is the chief enzyme involved in glycogen polymerisation. Glycogenin-1 is vital for the function of self-glucosylates, using an inter-subunit mechanism, to form an oligosaccharide primer which acts as substrate for glycogen synthase. In addition, GYG1 has a role in regulating glycogen metabolism and the achievement of maximal glycogen levels in skeletal muscle. GYG1 mRNA and protein content and activity increase in the muscle during recovery from prolonged and exhaustive exercise. GYG1 is inactivated with glycogen catabolism which concurs with an increase in glycogenin gene expression as exercise and glycogenolysis advance. Glycogenin will remain covalently attached to the reducing end of the glycogen molecule.
-
Synonyms
Glycogenin-1, GYG1, GYG.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MHHHHHHMAS MTGGQQMGRD LYDDDDKDRW GSMTDQAFVT LTTNDAYAKG ALVLGSSLKQ HRTTRRLVVL ATPQVSDSMR KVLETVFDEV IMVDVLDSGD SAHLTLMKRP ELGVTLTKLH CWSLTQYSKC VFMDADTLVL ANIDDLFDRE ELSAAPDPGW PDCFNSGVFV YQPSVETYNQ LLHLASEQGS FDGGDQGILN TFFSSWATTD IRKHLPFIYN LSSISIYSYL PAFKVFGASA KVVHFLGRVK PWNYTYDPKT KSVKSEAHDP NMTHPEFLIL WWNIFTTNVL PLLQQFGLVK DTCSYVNVED VSGAISHLSL GEIPAMAQPF VSSEERKERW EQGQADYMGA DSFDNIKRKL DTYLQ.
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 :
GCK HumanDescription:
Glucokinase/Hexokinase-4 Human Recombinant
Glucokinase, EC 2.7.1.2, Hexokinase-4, Hexokinase type IV, HK IV, HK4, Hexokinase-D, GCK, GK, GLK, HHF3, HKIV, HXKP, MODY2.
Product # :
PKA-236Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Glucokinase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-465) fused to a 20aa His tag at the N-terminal encoding the sequence of 485 amino acids and having a molecular mass of 54.3 kDa.HK4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl pH-8.0 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Alternative splicing of Glucokinase results in three tissue-specific forms of glucokinase, one found in pancreatic islet beta cells and two found in liver. The protein localizes to the outer membrane of mitochondria. In contrast to other forms of hexokinase, HK4 is not inhibited by its product glucose-6-phosphate but remains active while glucose is abundant. Mutations in this gene have been associated with non-insulin dependent diabetes mellitus (NIDDM), maturity onset diabetes of the young, type 2 (MODY2) and persistent hyperinsulinemic hypoglycemia of infancy (PHHI).
-
Synonyms
Glucokinase, EC 2.7.1.2, Hexokinase-4, Hexokinase type IV, HK IV, HK4, Hexokinase-D, GCK, GK, GLK, HHF3, HKIV, HXKP, MODY2.
-
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). Please avoid freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH EEASVKMLPT YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS VKTKHQMYSI PEDAMTGTAE MLFDYISECI SDFLDKHQMK HKKLPLGFTF SFPVRHEDID KGILLNWTKG FKASGAEGNN VVGLLRDAIK RRGDFEMDVV AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN VELVEGDEGR MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGQQLYE KLIGGKYMGE LVRLVLLRLV DENLLFHGEA SEQLRTRGAF ETRFVSQVES DTGDRKQIYN ILSTLGLRPS TTDCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED VMRITVGVDG SVYKLHPSFK ERFHASVRRL TPSCEITFIE SEEGSGRGAA LVSAVACKKA CMLGQ.
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 :
TIMP2 Human HEKDescription:
Tissue Inhibitor of Metalloprotease 2 Human Recombinant, HEK
TIMP metallopeptidase inhibitor 2, CSC-21K, tissue inhibitor of metalloproteinase 2, TIMP-2, metalloproteinase inhibitor 2.
Product # :
ENZ-120Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TIMP2 Human Recombinant produced in HEK-293 cells is a secreted protein with the sequence of Human TIMP-2 (amino acids Cys27-Pro220) and is fused to a polyhistidine tag at the C-terminus.
Source
HEK293 Cells.
Formulation
The TIMP2 protein was lyophilized after extensive dialysis against PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The IC50 of 3 nM is measured by its ability to inhibit recombinant human MMP-2 cleavage of the colorimetric peptide substrate, Mca-PLGL-DpaAR-NH2.More Info
-
Introduction
TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMPfamily members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.
-
Synonyms
TIMP metallopeptidase inhibitor 2, CSC-21K, tissue inhibitor of metalloproteinase 2, TIMP-2, metalloproteinase inhibitor 2.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TIMP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TIMP2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized TIMP2 in sterile assay buffer (50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% Brij-35, PH 7.5) not less than 100µg/ml.
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 :
FBP2 HumanDescription:
Fructose-1,6-Bisphosphatase 2 Human Recombinant
Fructose-1,6-bisphosphatase isozyme 2, Fructose-1,6-bisphosphatase isozyme 2, FBPase 2, D-fructose-1,6-bisphosphate 1-phosphohydrolase 2, FBP2.
Product # :
ENZ-667Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
FBP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (1-339) and having a molecular mass of 39kDa. FBP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FBP2 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
-
Introduction
Fructose-1,6-bisphosphatase isozyme 2 (FBP2) is a part of the FBPase class 1 family. FBP2 is a gluconeogenesis regulatory enzyme Which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate.
-
Synonyms
Fructose-1,6-bisphosphatase isozyme 2, Fructose-1,6-bisphosphatase isozyme 2, FBPase 2, D-fructose-1,6-bisphosphate 1-phosphohydrolase 2, FBP2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTDRSPF ETDMLTLTRY VMEKGRQAKG TGELTQLLNS MLTAIKAISS AVRKAGLAHL YGIAGSVNVT GDEVKKLDVL SNSLVINMVQ SSYSTCVLVS EENKDAIITA KEKRGKYVVC FDPLDGSSNI DCLASIGTIF AIYRKTSEDE PSEKDALQCG RNIVAAGYAL YGSATLVALS TGQGVDLFML DPALGEFVLV EKDVKIKKKG KIYSLNEGYA KYFDAATTEY VQKKKFPEDG SAPYGARYVG SMVADVHRTL VYGGIFLYPA NQKSPKGKLR LLYECNPVAY IIEQAGGLAT TGTQPVLDVK PEAIHQRVPL ILGSPEDVQE YLTCVQKNQA GS.
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 :
TaqDNADescription:
Taq DNA Polymerase Recombinant
DNA polymerase I thermostable, EC 2.7.7.7, Taq polymerase 1.
Product # :
ENZ-308Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Taq DNA Polymerase(a) is a thermostable enzyme of approximately 95 kDa isolated from Thermus aquaticus. This unmodified enzyme replicates DNA at 74°C and exhibits a half-life of 40 minutes at 95°C. The enzyme catalyzes the polymerization of nucleotides into duplex DNA in the 5´~3´ direction in the presence of magnesium and also possesses a 5´~3´ exonuclease activity. Taq DNA Polymerase is recommended for use in PCR but is not recommended for use in DNA sequencing reactions.
Source
Recombinant e.coli contains Thermus aquaticus polymerase gene.
Formulation
Taq DNA Polymerase solution in 20mM Tris-HCl, pH 8.0, 100mM KCl, 0.1mM EDTA, 1mM DTT, 50% Glycerol, 0.5% NP40, 0.5% Tween 20.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Synonyms
DNA polymerase I thermostable, EC 2.7.7.7, Taq polymerase 1.
-
Stability
Stable for 5 days at 10°C, for longer period of time store at -20°C.
-
Specify Your Own Reaction Conditions
Choose either Taq with Mg-free 10X Reaction Buffer and separate 25mM MgCl2 or Taq with 10X Reaction Buffer containing 15mM MgCl2.
-
Storage Buffer
Compatibility with Reaction Buffers: Taq DNA Polymerase in Storage Buffer. Use of other reaction buffers that do not contain Triton X-100 (final concentration of 0.1%) will result in inactivation of the enzyme. 50mM Tris-HCl (pH 8.0), 100mM NaCl, 0.1mM EDTA, 1mM DTT, 50% glycerol and 1% Triton X-100.
-
Unit Definition
One unit is defined as the amount of enzyme required to catalyze the incorporation of 10nmol of dNTP into acid-insoluble material in 30 minutes at 74°C. The reaction conditions are: 50mM Tris-HCl (pH 9.0 at 25°C), 50mM NaCl, 5mM MgCl2, 200µm each of dATP, dCTP, dGTP, dTTP (a mix of unlabeled and [3H]dTTP), 10µg activated calf thymus DNA and 0.1mg/ml BSA in a final volume of 50ul.
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 :
NDUFS3 HumanDescription:
Histidine NADH Dehydrogenase Fe-S Protein 3 Human Recombinant
CI-30, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondria, Complex I-30kD, CI-30kD, NADH-ubiquinone oxidoreductase 30 kDa subunit.
Product # :
ENZ-662Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human NDUFS3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 249amino acids (37-264 a.a.) and having a molecular mass of 28.7 kDa. NDUFS3 is fused to a 21 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The NDUFS3 protein solution (0.25mg/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
-
Introduction
NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 (NDUFS3) is a member of the complex I 30 kDa subunit family. NDUFS3 is one of the iron-sulfur protein (IP) components of mitochondrial NADH:ubiquinone oxidoreductase (complex I). This complex is the first enzyme complex in the electron transport chain of mitochondria. The iron-sulfur protein (IP) fraction of complex I consists of seven subunits. NDUFS3 gene mutations are linked with Leigh syndrome resulting from mitochondrial complex indefficiency.
-
Synonyms
CI-30, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondria, Complex I-30kD, CI-30kD, NADH-ubiquinone oxidoreductase 30 kDa subunit.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MESAGADTRP TVRPRNDVAH KQLSAFGEYV AEILPKYVQQ VQVSCFNELE VCIHPDGVIP VLTFLRDHTN AQFKSLVDLT AVDVPTRQNR FEIVYNLLSL RFNSRIRVKT YTDELTPIES AVSVFKAANW YEREIWDMFG VFFANHPDLR RILTDYGFEG HPFRKDFPLS GYVELRYDDE VKRVVAEPVE LAQEFRKFDL NSPWEAFPVY RQPPESLKLE AGDKKPDAK
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 :
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
More Info
- description
- source
- formulation
- purity
- More Info
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
-
Introduction
Uridine phosphorylase from Salmonella typhimurium (StUP) catalyzes the reversible phosphorolysis of uridine with the formation of ribose-1-phosphate and uracil.
-
Synonyms
Uridine phosphorylase, EC 2.4.2.3, UrdPase, UPase, StUP.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
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.
-
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.
-
Enzymatic Activity
30 U/mg protein.
-
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.
- View Data Sheet
Name :
ENO2 Human, HisDescription:
Enolase-2 Human Recombinant, His Tag
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
Product # :
ENZ-298Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Neuron Specific Enolase Human Recombinant is expressed in E. coli containing 433 amino acids 2-434 fused to an amino terminal hexahistidine tag.The NSE is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Enolase 2 is supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.More Info
-
Introduction
NSE is the ?? isoform of the glycolytic enzyme enolase and is expressed primarily in neurons, in normal and neoplastic neuroendocrine cells. NSE is a highly soluble cytoplasmic protein that is readily secreted into the CSF and serum following tissue damage. NSE shows neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons and binds in a calcium-dependent manner to cultured neocortical neurons promoting cell survival.
-
Synonyms
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CES1 HumanDescription:
Carboxylesterase 1 Human Recombinant
Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.
Product # :
ENZ-1099Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CES1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 559 amino acids (19-568 a.a.) and having a molecular mass of 61.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CES1 protein solution (0.5mg/ml) contains 25mM Sodium Acetate (pH 4.0), 10% glycerol, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
CES1 is a part of the alpha/beta fold hydrolase familyand participates in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. CES1hydrolyzes aromatic and aliphatic esters, although it has no catalytic activity toward amides or a fatty acyl-CoA ester. CES1hydrolyzes the methyl ester group of cocaine to form benzoylecgonine and catalyzes the transesterification of cocaine to form cocaethylene. CES1also plays a role in detoxification in the lung and protection of the central nervous system from ester or amide compounds.CES1 is found in most tissues, mainly in the liver.
-
Synonyms
Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADLGHPSSPP VVDTVHGKVL GKFVSLEGFA QPVAIFLGIP FAKPPLGPLR FTPPQPAEPW
SFVKNATSYP PMCTQDPKAG QLLSELFTNR KENIPLKLSE DCLYLNIYTP ADLTKKNRLP
VMVWIHGGGL MVGAASTYDG LALAAHENVV VVTIQYRLGI WGFFSTGDEH SRGNWGHLDQ
VAALRWVQDN IASFGGNPGS VTIFGESAGG ESVSVLVLSP LAKNLFHRAI SESGVALTSV
LVKKGDVKPL AEQIAITAGC KTTTSAVMVH CLRQKTEEEL LETTLKMKFL SLDLQGDPRE
SQPLLGTVID GMLLLKTPEE LQAERNFHTV PYMVGINKQE FGWLIPMQLM SYPLSEGQLD
QKTAMSLLWK SYPLVCIAKE LIPEATEKYL GGTDDTVKKK DLFLDLIADV MFGVPSVIVA
RNHRDAGAPT YMYEFQYRPS FSSDMKPKTV IGDHGDELFS VFGAPFLKEG ASEEEIRLSK
MVMKFWANFA RNGNPNGEGL PHWPEYNQKE GYLQIGANTQ AAQKLKDKEV AFWTNLFAKK AVEKPPQTEH IELHHHHHH.
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 :
GPT Human, His ActiveDescription:
Glutamic-Pyruvate Transaminase, His Tag Active Human Recombinant
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
Product # :
ENZ-1000Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPT solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.
More Info
-
Introduction
GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.
-
Synonyms
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS
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 :
UGP2 HumanDescription:
UDP-Glucose Pyrophosphorylase 2 Human Recombinant
UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.
Product # :
ENZ-832Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
UGP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (1-508 a.a) and having a molecular mass of 59.3kDa.UGP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UGP2 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
UDP-Glucose Pyrophosphorylase 2, also known as UGP2 is an essential intermediary in mammalian carbohydrate inter conversions. UGP2 transfers a glucose moiety from glucose-1-phosphate to MgUTP and forms UDP-glucose and MgPPi. UDP-glucose is a direct precursor of glycogen in the liver and muscle tissue, moreover in lactating mammary gland it is converted to UDP-galactose which is next converted to lactose.
-
Synonyms
UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSRFVQD LSKAMSQDGA SQFQEVIRQE LELSVKKELE KILTTASSHE FEHTKKDLDG FRKLFHRFLQ EKGPSVDWGK IQRPPEDSIQ PYEKIKARGL PDNISSVLNK LVVVKLNGGL GTSMGCKGPK SLIGVRNENT FLDLTVQQIE HLNKTYNTDV PLVLMNSFNT DEDTKKILQK YNHCRVKIYT FNQSRYPRIN KESLLPVAKD VSYSGENTEA WYPPGHGDIY ASFYNSGLLD TFIGEGKEYI FVSNIDNLGA TVDLYILNHL MNPPNGKRCE FVMEVTNKTR ADVKGGTLTQ YEGKLRLVEI AQVPKAHVDE FKSVSKFKIF NTNNLWISLA AVKRLQEQNA IDMEIIVNAK TLDGGLNVIQ LETAVGAAIK SFENSLGINV PRSRFLPVKT TSDLLLVMSN LYSLNAGSLT MSEKREFPTV PLVKLGSSFT KVQDYLRRFE SIPDMLELDH LTVSGDVTFG KNVSLKGTVI IIANHGDRID IPPGAVLENK IVSGNLRILD H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PYCR1 HumanDescription:
Pyrroline-5-Carboxylate Reductase 1 Human Recombinant
P5C, PRO3, P5CR 1, Pyrroline-5-Carboxylate Reductase 1 mitochondrial, ARCL2B, PYCR, PIG45, PP222, Proliferation-Inducing Protein 45.
Product # :
ENZ-035Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PYCR1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-319a.a.) and having a molecular mass of 35.5kDa.PYCR1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PYCR1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl Buffer (pH 8.5) and 10% Glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
PYCR1 is a universal housekeeping enzyme which catalyzes the NAD(P)H-dependent conversion of pyrroline-5-carboxylate to proline. PYCR1 enzyme also takes a physiologic part in the generation of NADP(+) in certain cell types. PYCR1 forms a homopolymer and localizes to the mitochondrion. Mutations in PYCR1 are the source of cutis laxa autosomal recessive type 2B (ARCL2B).
-
Synonyms
P5C, PRO3, P5CR 1, Pyrroline-5-Carboxylate Reductase 1 mitochondrial, ARCL2B, PYCR, PIG45, PP222, Proliferation-Inducing Protein 45.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV KLTPHNKETV QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT ISSIEKKLSA FRPAPRVIRC MTNTPVVVRE GATVYATGTH AQVEDGRLME QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH ALHVLESGGF RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL SPSGHTKLLP RSLAPAGKD
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ENPP1 MouseDescription:
Ectonucleotide Pyrophosphatase Mouse Recombinant
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, E-NPP 1, Membrane component chromosome 6 surface marker 1, Phosphodiesterase I/nucleotide pyrophosphatase 1, Plasma-cell membrane glycoprotein PC-1, ENPP1, M6S1, NPPS, PC1, PDNP1, NPP1, PC-1, PCA1, ARHR2, COLED.
Product # :
ENZ-1193Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
ENPP1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing 828 amino acids (Lys85-Glu906) and having a molecular mass of 95.2kDa. ENPP1 Mouse is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
The filtered (0.4µm) concentrated protein solution was lyophilized with PBS, PH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Synonyms
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, E-NPP 1, Membrane component chromosome 6 surface marker 1, Phosphodiesterase I/nucleotide pyrophosphatase 1, Plasma-cell membrane glycoprotein PC-1, ENPP1, M6S1, NPPS, PC1, PDNP1, NPP1, PC-1, PCA1, ARHR2, COLED.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
-
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
-
Amino Acid Sequence
KEVKSCKGRC FERTFSNCRC DAACVSLGNC CLDFQETCVE PTHIWTCNKF RCGEKRLSRF VCSCADDCKT HNDCCINYSS VCQDKKSWVE ETCESIDTPE CPAEFESPPT LLFSLDGFRA EYLHTWGGLL PVISKLKNCG TYTKNMRPMY PTKTFPNHYS IVTGLYPESH GIIDNKMYDP KMNASFSLKS KEKFNPLWYK GQPIWVTANH QEVKSGTYFW PGSDVEIDGI LPDIYKVYNG SVPFEERILA VLEWLQLPSH ERPHFYTLYL EEPDSSGHSH GPVSSEVIKA LQKVDRLVGM LMDGLKDLGL DKCLNLILIS DHGMEQGSCK KYVYLNKYLG DVNNVKVVYG PAARLRPTDV PETYYSFNYE ALAKNLSCRE PNQHFRPYLK PFLPKRLHFA KSDRIEPLTF YLDPQWQLAL NPSERKYCGS GFHGSDNLFS NMQALFIGYG PAFKHGAEVD SFENIEVYNL MCDLLGLIPA PNNGSHGSLN HLLKKPIYNP SHPKEEGFLS QCPIKSTSND LGCTCDPWIV PIKDFEKQLN LTTEDVDDIY HMTVPYGRPR ILLKQHHVCL LQQQQFLTGY SLDLLMPLWA SYTFLRNDQF SRDDFSNCLY QDLRIPLSPV HKCSYYKSNS KLSYGFLTPP RLNRVSNHIY SEALLTSNIV PMYQSFQVIW HYLHDTLLQR YAHERNGINV VSGPVFDFDY DGRYDSLEIL KQNSRVIRSQ EILIPTHFFI VLTSCKQLSE TPLECSALES SAYILPHRPD NIESCTHGKR ESSWVEELLT LHRARVTDVE LITGLSFYQD RQESVSELLR LKTHLPIFSQ EDHHHHHH.
-
Background
Ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1) is an enzyme with multifaceted roles in cellular metabolism, bone mineralization, and insulin signaling. Research utilizing mouse models has been pivotal in elucidating the complex biology of ENPP1 and its implications for various physiological processes and disease states. This study aims to provide a comprehensive exploration of ENPP1 in mouse physiology, shedding light on its diverse functions and potential applications in understanding metabolic health and disease mechanisms.
The primary objective of this research is to elucidate the impact of ENPP1 in mouse models on metabolic health. In vivo experiments using genetically modified mice with altered ENPP1 expression or activity will be conducted to investigate how ENPP1 influences glucose homeostasis, insulin sensitivity, and lipid metabolism. Understanding these mechanisms is fundamental for deciphering the role of ENPP1 in metabolic diseases such as diabetes and obesity.
The second objective is to assess the clinical relevance of ENPP1 in mouse models of bone health. Mouse models of skeletal disorders will be employed to explore how ENPP1 affects bone mineralization, density, and remodeling. These investigations may provide valuable insights into potential therapeutic strategies targeting ENPP1 in bone-related diseases.
The third objective is to explore the broader implications of ENPP1 in mouse physiology, including its effects on vascular health, inflammation, and tissue repair. Research will investigate its roles in vascular calcification, inflammation resolution, and tissue regeneration. Understanding the multifaceted properties of ENPP1 in mouse models may open new avenues for therapeutic interventions in various metabolic and chronic disease contexts.
By delving into the diverse functions of ENPP1 in mouse physiology, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for metabolic diseases, bone disorders, and other conditions influenced by ENPP1.
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 :
B3GAT3 HumanDescription:
Beta-1,3-Glucuronyltransferase 3 Human Recombinant
Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.
Product # :
ENZ-711Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
B3GAT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (29-335 a.a) and having a molecular mass of 36.4kDa. B3GAT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
B3GAT3 protein solution (1mg/ml) containing 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
-
Introduction
Beta-1,3-glucuronyltransferase 3 (B3GAT3) is involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. B3GAT3 has a part in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. B3GAT3 shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc.
-
Synonyms
Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQPCDCLP PLRAAAEQLR QKDLRISQLQ AELRRPPPAP AQPPEPEALP TIYVVTPTYA RLVQKAELVR LSQTLSLVPR LHWLLVEDAE GPTPLVSGLL AASGLLFTHL VVLTPKAQRL REGEPGWVHP RGVEQRNKAL DWLRGRGGAV GGEKDPPPPG TQGVVYFADD DNTYSRELFE EMRWTRGVSV WPVGLVGGLR FEGPQVQDGR VVGFHTAWEP SRPFPVDMAG FAVALPLLLD KPNAQFDSTA PRGHLESSLL SHLVDPKDLE PRAANCTRVL VWHTRTEKPK MKQEEQLQRQ GRGSDPAIEV.
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 :
BCAT2 HumanDescription:
Branched Chain Amino-Acid Transaminase 2 Human Recombinant
Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.
Product # :
ENZ-606Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
BCAT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (28-392) and having a molecular mass of 43.9kDa.BCAT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCAT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 10% glycerol, 0.2M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Branched Chain Amino-Acid Transaminase 2 (BCAT2) is a member of the class-IV pyridoxal-phosphate-dependent aminotransferase family. BCAT2 is a branched chain aminotransferase found in mitochondria. BCAT2 forms a dimer which catalyzes the first step in the production of the branched chain amino acids leucine, isoleucine, and valine. In addition, BCAT2 may actn as a transporter of branched chain alpha-keto acids.
-
Synonyms
Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMASSSF KAADLQLEMT QKPHKKPGPG EPLVFGKTFT DHMLMVEWND KGWGQPRIQP FQNLTLHPAS SSLHYSLQLF EGMKAFKGKD QQVRLFRPWL NMDRMLRSAM RLCLPSFDKL ELLECIRRLI EVDKDWVPDA AGTSLYVRPV LIGNEPSLGV SQPTRALLFV ILCPVGAYFP GGSVTPVSLL ADPAFIRAWV GGVGNYKLGG NYGPTVLVQQ EALKRGCEQV LWLYGPDHQL TEVGTMNIFV YWTHEDGVLE LVTPPLNGVI LPGVVRQSLL DMAQTWGEFR VVERTITMKQ LLRALEEGRV REVFGSGTAC QVCPVHRILY KDRNLHIPTM ENGPELILRF QKELKEIQYG IRAHEWMFPV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ACPP MouseDescription:
Acid Phosphatase Prostate Mouse Recombinant
acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.
Product # :
ENZ-1157Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
ACPP Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (32-381 aa) and having a molecular mass of 41.3kDa.ACPP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The ACPP solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >80,000 unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37C.
More Info
-
Introduction
Prostatic Acid Phosphatase or ACPP is part of a family of proteins called histidine acid phosphatase. ACPP enhances the hydrolyzation of many phosphate monoesters and proteins that are phosphorylated. In order to function best, ACPP needs a range of range of 4-6 pH, furthermore, L(+)-tartrate inhibits ACPP’s catalyzation. This enzyme can act as a lipid phosphatase as well and can inhibit lysophosphatidic acid in seminal plasma.
-
Synonyms
acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
KELKFVTLVF RHGDRGPIET FPTDPITESS WPQGFGQLTQ WGMEQHYELG SYIRKRYGRF LNDTYKHDQI YIRSTDVDRT LMSAMTNLAA LFPPEGISIW NPRLLWQPIP VHTVSLSEDR LLYLPFRDCP RFEELKSETL ESEEFLKRLH PYKSFLDTLS SLSGFDDQDL FGIWSKVYDP LFCESVHNFT LPSWATEDAM IKLKELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILKNMK LATQPQKYKK LVMYSAHDTT VSGLQMALDV YNGVLPPYAS CHMMELYHDK GGHFVEMYYR NETQNEPYPL TLPGCTHSCP LEKFAELLDP VISQDWATEC MATSSHQGRN HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PTPS HumanDescription:
6-Pyruvoyltetrahydropterin Synthase Human Recombinant
PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.
Product # :
ENZ-471Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
6-PyruvoylTetrahydropterin Synthase Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145) and having a molecular mass of 18.5kDa. 6-PyruvoylTetrahydropterin Synthase is fused to a 20 amino acid His Tag at N-terminus and purified using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
6-PyruvoylTetrahydropterin Synthase is formulated in 20mM Tris-HCl buffer pH-8, 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
-
Introduction
6-PyruvoylTetrahydropterin Synthase is part of the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. 6-PyruvoylTetrahydropterin Synthase catalyzes the elimination of inorganic triphosphate from dihydroneopterin triphosphate, which is the second and irreversible step in the biosynthesis of tetrahydrobiopterin from GTP. Tetrahydrobiopterin, is a necessary cofactor and regulator of a range of enzyme activities, including enzymes involved in serotonin biosynthesis and NO synthase activity. Mutations in 6-PyruvoylTetrahydropterin Synthase gene result in hyperphenylalaninemia.
-
Synonyms
PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSTEGGGRRC QAQVSRRISF SASHRLYSKF LSDEENLKLF GKCNNPNGHG HNYKVVVTVH GEIDPATGMV MNLADLKKYM EEAIMQPLDH KNLDMDVPYF ADVVSTTENV AVYIWDNLQK VLPVGVLYKV KVYETDNNIV VYKGE.
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 :
CAS9 S. PyogenesDescription:
CRISPR-Associated Protein-9 Nuclease S. Pyogenes Recombinant
CRISPR-associated endonuclease Cas9/Csn1, SpyCas9, cas9, csn1.
Product # :
ENZ-901Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Cas9-NLS produced in E.coli, comprises the entire Cas9 protein sequence (1368 amino acids) joined to a proprietary nuclear localization sequence (NLS) and a 6xHis tag at the C-terminus, having a total of 1414 amino acids. The protein has an apparent molecular weight of 163kDa.
Source
Escherichia Coli.
Formulation
The CAS9 solution contains 10mM Tris-HCl, 300mM NaCl, 0.1mM EDTA, 50% glycerol and 1mM DTT pH 7.5.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Cas9 (CRISPR associated protein 9) is an RNA-guided DNA endonuclease enzyme associated with the CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) adaptive immunity system in Streptococcus pyogenes, among other bacteria. S. Pyogenes utilizes Cas9 to remember and later probe and cleave foreign DNA, such as invading bacteriophage DNA or plasmid DNA. In case that the DNA substrate is complementary to the guide RNA, Cas9 cleaves the invading DNA. In addition to its original role in bacterial immunity, the Cas9 protein has been heavily employed as a genome engineering tool to induce site-directed double strand breaks in DNA. These disruptions may lead to gene inactivation or the presentation of heterologous genes via non-homologous end joining and homologous recombination respectively in many laboratory model organisms.
-
Synonyms
CRISPR-associated endonuclease Cas9/Csn1, SpyCas9, cas9, csn1.
-
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.
-
Non-specific DNAse activity
The incubation of 20pmol of CAS9 protein with 1µg of lambda DNA at 37°C for 4 hours is free of detectable DNA degradation, as visualized on agarose gel.
-
Enzymatic Activity
97% of PCR product digestion after 30 minutes at 37°C.
-
Endonuclease Activity
The incubation of 20pmol of CAS9 protein with 1µg pUC19 supercoiled vector at 37°C for 4 hours leads to formation of less than 10% open circular pUC19 form as determined by gel electrophoresis.
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 :
UGT8 HumanDescription:
UDP Glycosyltransferase 8 Human Recombinant
UDP Glycosyltransferase 8, CGT, UDP-Galactose Ceramide Galactosyltransferase, 2-Hydroxyacylsphingosine 1-Beta-Galactosyltransferase, Ceramide UDP-Galactosyltransferase, Cerebroside Synthase, UGT4, UDP-Galactose-Ceramide Galactosyltransferase, Uridine Diphosphate Glycosyltransferase 8, EC 2.4.1.45, EC 2.4.1.
Product # :
ENZ-754Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
UGT8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 544 amino acids (21-541 a.a) and having a molecular mass of 61.6kDa.UGT8 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
UGT8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
UDP Glycosyltransferase 8 (UGT8) is a member of the UDP-glycosyltransferase family. UGT8 catalyzes the transfer of galactose to ceramide, a crucial enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.
-
Synonyms
UDP Glycosyltransferase 8, CGT, UDP-Galactose Ceramide Galactosyltransferase, 2-Hydroxyacylsphingosine 1-Beta-Galactosyltransferase, Ceramide UDP-Galactosyltransferase, Cerebroside Synthase, UGT4, UDP-Galactose-Ceramide Galactosyltransferase, Uridine Diphosphate Glycosyltransferase 8, EC 2.4.1.45, EC 2.4.1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAKIIIVP PIMFESHMYI FKTLASALHE RGHHTVFLLS EGRDIAPSNH YSLQRYPGIF NSTTSDAFLQ SKMRNIFSGR LTAIELFDIL DHYTKNCDLM VGNHALIQGL KKEKFDLLLV DPNDMCGFVI AHLLGVKYAV FSTGLWYPAE VGAPAPLAYV PEFNSLLTDR MNLLQRMKNT GVYLISRLGV SFLVLPKYER IMQKYNLLPE KSMYDLVHGS SLWMLCTDVA LEFPRPTLPN VVYVGGILTK PASPLPEDLQ RWVNGANEHG FVLVSFGAGV KYLSEDIANK LAGALGRLPQ KVIWRFSGPK PKNLGNNTKL IEWLPQNDLL GHSKIKAFLS HGGLNSIFET MYHGVPVVGI PLFGDHYDTM TRVQAKGMGI LLEWKTVTEK ELYEALVKVI NNPSYRQRAQ KLSEIHKDQP GHPVNRTIYW IDYIIRHNGA HHLRAAVHQI SFCQYFLLDI AFVLLLGAAL LYFLLSWVTK FIYRKIKSLW SRNKHSTVNG HYHNGILNGK YKRNGHIKHE KKVK.
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 :
AOC3 HumanDescription:
Amine Oxidase Copper Containing 3 Human Recombinant
VAP-1, AOC3, HPAO, VAP1, Membrane primary amine oxidase, Copper amine oxidase, HPAO, Semicarbazidesensitive amine oxidase, SSAO, Vascular adhesion protein 1.
Product # :
ENZ-1152Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
AOC3 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 746 amino acids (27-763 aa) and having a molecular mass of 82.8kDa.AOC3 is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The AOC3 solution (0.25 mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Amine Oxidase Copper Containing 3 , also referred to AOC3, a copper amine oxidase with a topaquinone cofactor.
AOC3 is a cell adhesion protein which participates in recirculation & extravasation of lymphocyte by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin independent fashion.
Amine Oxidase Copper Containing 3 acts in adipogenesis.
The protein catalyzes the oxidative deamination of small primary amines such as methylamine, benzylamine & aminoacetone in a reaction that produces an aldehyde, ammonia and H2O2. -
Synonyms
VAP-1, AOC3, HPAO, VAP1, Membrane primary amine oxidase, Copper amine oxidase, HPAO, Semicarbazidesensitive amine oxidase, SSAO, Vascular adhesion protein 1.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADPGRGGDGG EPSQLPHCPS VSPSAQPWTH PGQSQLFADL SREELTAVMR FLTQRLGPGL VDAAQARPSD NCVFSVELQL PPKAAALAHL DRGSPPPARE ALAIVFFGRQ PQPNVSELVV GPLPHPSYMR DVTVERHGGP LPYHRRPVLF QEYLDIDQMI FNRELPQASG LLHHCCFYKH RGRNLVTMTT APRGLQSGDR ATWFGLYYNI SGAGFFLHHV GLELLVNHKA LDPARWTIQK VFYQGRYYDS LAQLEAQFEA GLVNVVLIPD NGTGGSWSLK SPVPPGPAPP LQFYPQGPRF SVQGSRVASS LWTFSFGLGA FSGPRIFDVR FQGERLVYEI SLQEALAIYG GNSPAAMTTR YVDGGFGMGK YTTPLTRGVD CPYLATYVDW HFLLESQAPK TIRDAFCVFE QNQGLPLRRH HSDLYSHYFG GLAETVLVVR SMSTLLNYDY VWDTVFHPSG AIEIRFYATG YISSAFLFGA TGKYGNQVSE HTLGTVHTHS AHFKVDLDVA GLENWVWAED MVFVPMAVPW SPEHQLQRLQ VTRKLLEMEE QAAFLVGSAT PRYLYLASNH SNKWGHPRGY RIQMLSFAGE PLPQNSSMAR GFSWERYQLA VTQRKEEEPS SSSVFNQNDP WAPTVDFSDF INNETIAGKD LVAWVTAGFL HIPHAEDIPN TVTVGNGVGF FLRPYNFFDE DPSFYSADSI YFRGDQDAGA CEVNPLACLP QAAACAPDLP AFSHGGFSHN HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
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 :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
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
-
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.
-
Synonyms
Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH 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.
- View Data Sheet
Name :
HERC5 HumanDescription:
HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 Human Recombinant
HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.
Product # :
ENZ-797Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HERC5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (681-1024 a.a.) and having a molecular mass of 43kDa. HERC5 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
HERC5 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 (HERC5) is a member of the HERC family of ubiquitin ligases, found in a cluster of HERC family genes on chromosome 4. HERC5 is a protein with a HECT domain and 5 RCC1 repeats. The HERC5 protein localizes to the cytoplasm and perinuclear region and serves as an INF-induced E3 protein ligase that mediates ISGylation of protein targets. HERC5 exhibits antiviral activity towards HIV-1, influenza A virus and human papillomavirus. HERC5 is a major E3 ligase for ISG15 conjugation. HERC5 also serves as a positive regulator of innate antiviral response in cells induced by INF. Pro-inflammatory cytokines upregulate HERC5 in endothelial cells. HERC5 is physically connected with polyribosomes, broadly modifies recently synthesized proteins in a cotranslational fashion.
-
Synonyms
HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFDLTVRR NHLIEDVLNQ LSQFENEDLR KELWVSFSGE IGYDLGGVKK EFFYCLFAEM IQPEYGMFMY PEGASCMWFP VKPKFEKKRY FFFGVLCGLS LFNCNVANLP FPLALFKKLL DQMPSLEDLK ELSPDLGKNL QTLLDDEGDN FEEVFYIHFN VHWDRNDTNL IPNGSSITVN QTNKRDYVSK YINYIFNDSV KAVYEEFRRG FYKMCDEDII KLFHPEELKD VIVGNTDYDW KTFEKNARYE PGYNSSHPTI VMFWKAFHKL TLEEKKKFLV FLTGTDRLQM KDLNNMKITF CCPESWNERD PIRALTCFSV LFLPKYSTME TVEEALQEAI NNNRGFG.
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.