Search results
1000 results found for “Glycosylase”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
UCK1 HumanDescription:
Uridine-Cytidine Kinase 1 Human Recombinant
Uridine-cytidine kinase 1, UCK 1, Cytidine monophosphokinase 1, UCK1 Uridine monophosphokinase 1, URK1, FLJ12255, RP11-334J6.5, Uridine-cytidine kinase 1 isoform a.
Product # :
PKA-317Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
UCK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (143-273a.a) and having a molecular mass of 17.5kDa.UCK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UCK1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
UCK1 is a uridine-cytidine kinase which catalyzes the phosphorylation of uridine and cytidine to uridine monophosphate and cytidine monophosphate. UCK1 does not phosphorylate deoxyribonucleosides or purine ribonucleosides. UCK1 is also phosphorylates uridine and cytidine analogs and uses ATP and GTP as a phosphate donor.
-
Synonyms
Uridine-cytidine kinase 1, UCK 1, Cytidine monophosphokinase 1, UCK1 Uridine monophosphokinase 1, URK1, FLJ12255, RP11-334J6.5, Uridine-cytidine kinase 1 isoform a.
-
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 MFYSQEIRDM FHLRLFVDTD SDVRLSRRVL RDVRRGRDLE QILTQYTTFV KPAFEEFCLP TKKYADVIIP RGVDNMVAIN LIVQHIQDIL NGDICKWHRG GSNGRSYKRT FSEPGDHPGM LTSGKRSHLE SS.
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 :
LDHBDescription:
Lactate Dehydrogenase B Recombinant
Lactate Dehydrogenase, EC 1.1.1.27, LDH.
Product # :
ENZ-279Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
The DNA encoding chicken LDH-B is cloned from cDNA library of chicken heart.
Source
Escherichia Coli.
Formulation
The protein (1 mg/ml) was lyophilized with 0.1mg potassium phosphate.
Purity
Greater than 95.0% as determined by:(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity was found to be 258 U/mg protein.More Info
-
Introduction
Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist. -
Synonyms
Lactate Dehydrogenase, EC 1.1.1.27, LDH.
-
Physical Appearance
Sterile lyophilized powder.
-
Stability
Lyophilized Lactate Dehydrogenase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LDH should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized LDH in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Unit Definition
One unit is defined as 1umol of NAD+ production per minute under the assay conditions (25°C, pH 7.0). Both transaminase activities include a-hydroxyglutarate dehydrogenase activity.
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 :
RNASE3 Human, Sf9Description:
Ribonuclease 3 Human Recombinant, Sf9
ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.
Product # :
ENZ-1024Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RNASE3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (28-160 a.a.) and having a molecular mass of 16.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).RNASE3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
RNASE3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ribonuclease 3 (RNASE3) is cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. RNASE3 possesses a broad diversity of biological activities. RNASE3 protein has shown antibacterial activity such as cytoplasmic membrane depolarization of preferentially Gram-negative and Gram-positive strains and promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.
-
Synonyms
ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.
-
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
ADPRPPQFTR AQWFAIQHIS LNPPRCTIAM RAINNYRWRC KNQNTFLRTT FANVVNVCGN QSIRCPHNRT LNNCHRSRFR VPLLHCDLIN PGAQNISNCR YADRPGRRFY VVACDNRDPR DSPRYPVVPV HLDTTIHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ALDH2 MouseDescription:
Aldehyde Dehydrogenase 2 Mouse Recombinant
Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.
Product # :
ENZ-879Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ALDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (20-519 a.a) and having a molecular mass of 56.8kDa. ALDH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDH2 protein e solution (0.5mg/ml) containing Phosphate buffered salin(pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
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 DVDKAVKAAR AAFQLGSPWR RMDASDRGRL LYRLADLIER DRTYLAALET LDNGKPYVIS YLVDLDMVLK CLRYYAGWAD KYHGKTIPID GDFFSYTRHE PVGVCGQIIP WNFPLLMQAW KLGPALATGN VVVMKVAEQT PLTALYVANL IKEAGFPPGV VNIVPGFGPT AGAAIASHEG VDKVAFTGST EVGHLIQVAA GSSNLKRVTL ELGGKSPNII MSDADMDWAV EQAHFALFFN QGQCCCAGSR TFVQENVYDE FVERSVARAK SRVVGNPFDS RTEQGPQVDE TQFKKILGYI KSGQQEGAKL LCGGGAAADR GYFIQPTVFG DVKDGMTIAK EEIFGPVMQI LKFKTIEEVV GRANDSKYGL AAAVFTKDLD 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 :
WARS HumanDescription:
Tryptophanyl-tRNA Synthetase Human Recombinant
GAMMA-2, IFI53, IFP53, WRS, WARS, TrpRS, hWRS, EC=6.1.1.2, Tryptophanyl-tRNA synthetase, INF-induced protein 53, Tryptophan--tRNA ligase, GAMMA-2.
Product # :
ENZ-545Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
WARS Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 491 amino acids (1-471 a.a.) and having a molecular mass of 55.3 kDa. The WARS is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl, 1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
WARS is part of the class I tRNA synthetase family. 2 types of tryptophanyl tRNA synthetase exist, a cytoplasmic form, called WARS, and a mitochondrial form, called WARS2. WARS catalyzes the aminoacylation of tRNA(trp) with tryptophan and is induced by INF. WARS controls ERK, Akt, and eNOS activation pathways that are related with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression.
-
Synonyms
GAMMA-2, IFI53, IFP53, WRS, WARS, TrpRS, hWRS, EC=6.1.1.2, Tryptophanyl-tRNA synthetase, INF-induced protein 53, Tryptophan--tRNA ligase, GAMMA-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 MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY KAAAGEDYKA DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY DKLIVRFGSS KIDKELINRI ERATGQRPHH FLRRGIFFSH RDMNQVLDAY ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT KWLQDVFNVP LVIQMTDDEK YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY MGMSSGFYKN VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM SASDPNSSIF LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF MYLTFFLEDD DKLEQIRKDY TSGAMLTGEL KKALIEVLQP LIAEHQARRK EVTDEIVKEF MTPRKLSFDF Q.
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 :
REV1 HumanDescription:
REV1 Polymerase Human Recombinant
REV1 Polymerase (DNA Directed), REV1L, Alpha Integrin-Binding Protein 80, Rev1-Like Terminal Deoxycytidyl Transferase, AIBP80, REV1 (Yeast Homolog)- Like, REV1 Homolog (S. Cerevisiae) , REV1-Like (Yeast) , DNA Repair Protein REV1, REV1 Homolog, REV1- Like, EC 2.7.7.-.
Product # :
ENZ-796Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
REV1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (51-256) and having a molecular mass of 25.2kDa.REV1 is fused to a 21 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The REV1 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
-
Introduction
REV1 Polymerase (REV1) contains a BRCT domain, which is imperative in protein-protein interactions. REV1 is a deoxycytidyl transferase involved in DNA repair. REV1 assists in the 1st step in the bypass of abasic lesions by the incorporation of a nucleotide opposite the lesion. REV1 is essential for normal generation of mutations by physical and chemical agents. REV1 transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. A role for the human Rev1-like protein has been suggested as a scaffold which recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA.
-
Synonyms
REV1 Polymerase (DNA Directed), REV1L, Alpha Integrin-Binding Protein 80, Rev1-Like Terminal Deoxycytidyl Transferase, AIBP80, REV1 (Yeast Homolog)- Like, REV1 Homolog (S. Cerevisiae) , REV1-Like (Yeast) , DNA Repair Protein REV1, REV1 Homolog, REV1- Like, EC 2.7.7.-.
-
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 MGVAIYVNGY TDPSAEELRK LMMLHGGQYH VYYSRSKTTH IIATNLPNAK IKELKGEKVI RPEWIVESIK AGRLLSYIPY QLYTKQSSVQ KGLSFNPVCR PEDPLPGPSN IAKQLNNRVN HIVKKIETEN EVKVNGMNSW NEEDENNDFS FVDLEQTSPG RKQNGIPHPR GSTAIFNGHT PSSNGALKTQ DCLVPMVNSV ASRLSPA.
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 :
PDXP HumanDescription:
Pyridoxal Phosphatase Human Recombinant
CIN, PLP, PLPP, EC 3.1.3.74.
Product # :
ENZ-551Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PDXP Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296 a.a.) and having a molecular mass of 33.8 kDa. The PDXP is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
PDXP is the active form of vitamin B6 that functions as a coenzyme in preserving biochemical homeostasis. The desired degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP. PDXP shows activity to pyridoxal 5''-phosphate (PLP), pyridoxine 5''-phosphate (PMP) and Pyridoxine 5''-phosphate (PNP), with a highest activity with PLP followed by PNP.
-
Synonyms
CIN, PLP, PLPP, EC 3.1.3.74.
-
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 MARCERLRGA ALRDVLGRAQ GVLFDCDGVL WNGERAVPGA PELLERLARA GKAALFVSNN SRRARPELAL RFARLGFGGL RAEQLFSSAL CAARLLRQRL PGPPDAPGAV FVLGGEGLRA ELRAAGLRLA GDPSAGDGAA PRVRAVLVGY DEHFSFAKLR EACAHLRDPE CLLVATDRDP WHPLSDGSRT PGTGSLAAAV ETASGRQALV VGKPSPYMFE CITENFSIDP ARTLMVGDRL ETDILFGHRC GMTTVLTLTG VSRLEEAQAY LAAGQHDLVP HYYVESIADL TEGLED.
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 :
A2LD1 HumanDescription:
AIG2-Like Domain 1 Human Recombinant
Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.
Product # :
PRO-172Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
A2LD1 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 173 amino acids (1-153 a.a.) and having a molecular mass of 19.4kDa. The A2LD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The A2LD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Gamma-glutamylaminecyclotransferase (A2LD1) is an enzyme which converts gamma-glutamylamines to free amines and 5-oxoproline. A2LD1 demonstrates high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. A2LD1 assists in the proteolytic degradation of crosslinked fibrin by breaking down isodipeptide L-gamma-glutamyl-L-epsilon-lysine, which is a byproduct of fibrin degradation. The reaction catalyzed by the A2LD1 produces 5-oxo-L-proline and a free alkylamine.
-
Synonyms
Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.
-
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 MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI PWLLHLPGSG RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED RAPGAEEPPA PTAVQCFVYS RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR ENR.
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 :
PLA2G1B HumanDescription:
Secreted Phospholipase A2-IB Human Recombinant
Phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IB phospholipase A2, PLA2, PLA2A, PPLA2, sPLA2-IB,MGC119834, MGC119835, PLA2G1B.
Product # :
ENZ-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Secreted Phospholipase A2-IB Human Recombinant is manufactured with N-terminal fusionf HisTag. PLA2G1B His-Tagged Fusion Protein is 16 kDa containing 126 amino acid residues of the human secreted phospholipase A2-IB and 16 additional amino acid residues - HisTag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Group IB secretory phospholipase A2 (sPLA2-IB) mediates cell proliferation, cell migration, hormone release and eicosanoid production via its receptor in peripheral tissues. In the CNS, high-affinity binding sites of sPLA2-IB have been documented. sPLA2-IB induced neuronal cell death in a concentrationdependent manner depending on PGD2 metabolites, especially Delta12-PGJ2 that might mediate sPLA2-IB-induced apoptosis. The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of lowmolecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
-
Synonyms
Phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IB phospholipase A2, PLA2, PLA2A, PPLA2, sPLA2-IB,MGC119834, MGC119835, PLA2G1B.
-
Physical Appearance
Lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MRGSHHHHHH GMASHMAVWQ FRKMIKCVIP GSDPFLEYNN YGCYCGLGGS GTPVDELDKC CQTHDNCYDQ AKKLDSCKFL LDNPYTHTYS YSCSGSAITC SSKNKECEAF ICNCDRNAAI CFSKAPYNKA HKNLDTKKYC QS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
THTPA HumanDescription:
Thiamine Triphosphatase Human Recombinant
MGC2652, THTP, THTPASE.
Product # :
ENZ-249Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human THTPA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230 a.a.) and having a molecular mass of 27.7 kDa. THTPA is fused to a 20 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The THTPA 1mg/ml protein solution contains 20mM Tris-HCL buffer, pH-8, 1mM DTT and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
THTPA enzyme is part of the THTPase family. THTPA is localized to the cytoplasm and expressed at small quantities in a variety of tissues, including testis, uterus, prostate, bladder, lung and kidney. THTPA is a hydrolase that catalyzes the H2O-dependent hydrolysis of thiamine triphosphate (THTP) to thiamine diphosphate (THDP), the main form of thiamine within the cell. THTPA occurs as a monomer and is activated at an optimal pH of 8.5.
-
Synonyms
MGC2652, THTP, THTPASE.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store THTPA at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA DHWLRRREDS GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG LGAGDVAAVL GPLGLQEVAS FVTKRSAWKL VLLGADEEEP QLRVDLDTAD FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SGCD HumanDescription:
Sarcoglycan Delta Human Recombinant
35DAG, CMD1L, DAGD, SG-delta, SGCDP, SGD, Delta-sarcoglycan, 35 kDa dystrophin-associated glycoprotein.
Product # :
PRO-1373Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SGCD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 257 amino acids (57-289a.a) and having a molecular mass of 28kDa. SGCD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SGCD 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
Sarcoglycan Delta (SGCD) is one of the four known components of the sarcoglycan complex, which is a subcomplex of the dystrophin-glycoprotein complex (DGC) and is expressed mainly in skeletal and cardiac muscle. DGC forms a link between the F-actin cytoskeleton and the extracellular matrix. SGCD protein’s mutations have been associated with autosomal recessive limb-girdle muscular dystrophy and dilated cardiomyopathy. SGCD gene expression is regulated by MITF In melanocytic cells.
-
Synonyms
35DAG, CMD1L, DAGD, SG-delta, SGCDP, SGD, Delta-sarcoglycan, 35 kDa dystrophin-associated glycoprotein.
-
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 RSHMKVMNFT IDGMGNLRIT EKGLKLEGDS EFLQPLYAKE IQSRPGNALY FKSARNVTVN ILNDQTKVLT QLITGPKAVE AYGKKFEVKT VSGKLLFSAD NNEVVVGAER LRVLGAEGTV FPKSIETPNV RADPFKELRL ESPTRSLVME APKGVEINAE AGNMEATCRT ELRLESKDGE IKLDAAKIRL PRLPHGSYTP TGTRQKVFEI CVCANGRLFL SQAGAGSTCQ INTSVCL.
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 :
ADK HumanDescription:
Adenosine Kinase Human Recombinant
Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK.
Product # :
PKA-367Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Adenosine Kinase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 362 amino acids (22-362a.a.) and having a molecular mass of 40.5 kDa. Adenosine Kinase protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
ADK protein solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 1mM EDTA, 50mM NaCl & 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.
-
Synonyms
Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK.
-
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 MRENILFGMG NPLLDISAVV DKDFLDKYSL KPNDQILAED KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA ATFFGCIGID KFGEILKRKA AEAHVDAHYY EQNEQPTGTC AACITGDNRS LIANLAAANC YKKEKHLDLE KNWMLVEKAR VCYIAGFFLT VSPESVLKVA HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN ETEAATFARE QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR TGCTFPEKPD FH.
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 :
MPO HumanDescription:
Myeloperoxidase Human
Myeloperoxidase, EC 1.11.1.7, MPO.
Product # :
ENZ-074Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MPO is a natural protein having a molecular mass of 150kDa containing 2 subunits each of a heavy chain with 64kDa and a light chain with 13kDa. MPO is isolated from human peripheral blood polymorphonuclear leukocytes.
Source
Human peripheral blood polymorphonuclear leukocytes.
Formulation
MPO solution is supplied in 20mM HEPES buffer pH-7.5, 200mM NaCl and 20% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
-
Introduction
Myeloperoxidase is an important enzyme used by granulocytes during phagocytic lysis of foreign particles engulfed. In normal tissues and in a variety of myeloproliferative disorders myeloid cells of both neutrophilic and eosinophilic types, at all stages of maturation, exhibit strong cytoplasmic reactivity for MPO. Erythroid precursors, megakaryocytes, lymphoid cells, mast cells, and plasma cells are nonreactive. MPO is not observed in the neoplastic cells of a wide variety of epithelial tumors and sarcomas. MPO is useful in differentiating between myeloid and lymphoid leukemias.
-
Synonyms
Myeloperoxidase, EC 1.11.1.7, MPO.
-
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. Avoid multiple 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 :
IDNK E.Coli, ActiveDescription:
Thermosensitive Gluconokinase E.Coli Recombinant, BioActive
Thermosensitive gluconokinase, Gluconate kinase 1, idnK, D-gluconate kinase thermosensitive, D-gluconate kinase, thermosensitive, ECK4261, gntV, JW4225, b4268
Product # :
PKA-122Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IDNK Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187) and having a molecular mass of 23.4 kDa.IDNK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDNK solution (1 mg/ml) contains 10% Glycerol, 1mM DTT, 0.15M NaCl and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 80unit/mg. One unit will convert 1.0 umole of D-gluconate to 6-phospho-Dgluconate per minute at pH 8.0 at 37˚C.
More Info
-
Introduction
D-gluconate kinase or idnk is a thermosensitive protein, consists of 187 a.a and part of the gluconokinase gntK/gntV protein family. Idnk enhances the conversion of ATP + D-gluconate => ADP + 6-phospho-D-gluconate. Idnk has a crucial part in determination of gender, removal of a certain portion of 9p may result in the making of male to female (reversal of sex), that leads to a female that has the genotype of male X, Y.
-
Synonyms
Thermosensitive gluconokinase, Gluconate kinase 1, idnK, D-gluconate kinase thermosensitive, D-gluconate kinase, thermosensitive, ECK4261, gntV, JW4225, b4268
-
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 MGSMAGESFI LMGVSGSGKT LIGSKVAALL SAKFIDGDDL HPAKNIDKMS QGIPLSDEDR LPWLERLNDA SYSLYKKNET GFIVCSSLKK QYRDILRKGS PHVHFLWLDG DYETILARMQ RRAGHFMPVA LLKSQFEALE RPQADEQDIV RIDINHDIAN VTEQCRQAVL AIRQNRICAK EGSASDQRCE
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
AK2 MouseDescription:
Adenylate Kinase 2 Mouse Recombinant
Adenylate kinase 2 mitochondrial isoform a, Ak-2, D4Ertd220e, mitochondrial, ATP-AMP transphosphorylase 2, ATP:AMP phosphotransferas, Adenylate monophosphate kinase.
Product # :
PKA-107Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
AK2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-239 a.a) and having a molecular mass of 29kDa.AK2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AK2 protein solution (0.5mg/ml) containing 20mM Tris-Hcl buffer (pH8.5), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 40 units/mg. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 37C.
More Info
-
Introduction
Adenylate kinases play a role in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. There are 3 types of adenylate kinase isozymes, AK1, AK2, and AK3 in vertebrates. Expression of these isozymes are tissue-specific and developmentally regulated. AK2 is localized in the mitochondrial intermembrane space and is involved in apoptosis. AK2 is mutated in individuals with reticular dysgenesis.
-
Synonyms
Adenylate kinase 2 mitochondrial isoform a, Ak-2, D4Ertd220e, mitochondrial, ATP-AMP transphosphorylase 2, ATP:AMP phosphotransferas, Adenylate monophosphate kinase.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
AK2 Mouse Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAPNVL ASEPEIPKGI RAVLLGPPGA GKGTQAPKLA ENFCVCHLAT GDMLRAMVAS GSEL TMDAGKLVSD EMVVELIEKN LETPSCKNGF LLDGFPRTVR QAEMLDDLME KRKEKLDSVI EFSIQDSLLI RRITGRLIHP KSGRS
NPPKEPMKDD ITGEPLIRRS DDNEKALKTR LEAYHTQTTP LVEYYRKRGI HCAIDASQTP DIVFASILAA FSKATCKDLV MFI
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 :
UBE2F HumanDescription:
Ubiquitin-Conjugating Enzyme E2F Human Recombinant
Ubiquitin-conjugating enzyme E2F (putative), NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, NEDD8-conjugating enzyme UBE2F, NCE2, EC 6.3.2.-.
Product # :
ENZ-625Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
UBE2F Human Recombinant produced in E. coli is a single polypeptide chain containing 209 amino acids (1-185) and having a molecular mass of 23.7 kDa.UBE2F is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The UBE2F solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Ubiquitin-conjugating enzyme E2 F (UBE2F) is a member of the ubiquitin-conjugating enzyme family and UBE2F subfamily. Ubiquitin-conjugating enzymes or sometimes as ubiquitin-carrier enzymes, run the second step in the ubiquitination reaction which targets a protein for degradation using the proteasome. The UBE2F receives the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins.
RBX2-UBE2F complex neddylates specific target proteins, for example CUL5 as can be seen from the specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1. -
Synonyms
Ubiquitin-conjugating enzyme E2F (putative), NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, NEDD8-conjugating enzyme UBE2F, NCE2, 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 MGSHMLTLAS KLKRDDGLKG SRTAATASDS TRRVSVRDKL LVKEVAELEA NLPCTCKVHF PDPNKLHCFQ LTVTPDEGYY QGGKFQFETE VPDAYNMVPP KVKCLTKIWH PNITETGEIC LSLLREHSID GTGWAPTRTL KDVVWGLNSL FTDLLNFDDP LNIEAAEHHL RDKEDFRNKV DDYIKRYAR
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
Description:
Ornithine Aminotransferase Human Recombinant
DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.
Product # :
ENZ-472Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Ornithine Aminotransferase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (33-439 a.a.) and having a molecular wieght of 45.2kDa.The Ornithine Aminotransferase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ornithine Aminotransferase protein solution contains 20mM Tris, pH-8, and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ornithine Aminotransferase is a mitochondrial enzyme which is an important factor that converts arginine and ornithine into the major excitatory and inhibitory neurotransmitters glutamate and GABA. Ornithine Aminotransferase mutations result in a deficiency that cause the autosomal recessive eye disease Gyrate Atrophy.
-
Synonyms
DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.
-
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
MTVQGPPTSD DIFEREYKYG AHNYHPLPVA LERGKGIYLW DVEGRKYFDF LSSYSAVNQG HCHPKIVNAL KSQVDKLTLT SRAFYNNVLG EYEEYITKLF NYHKVLPMNT GVEAGETACK LARKWGYTVK GIQKYKAKIV AAGNFWGRT LSAISSSTDP TSYDGFGPFM PGFDIIPYND LPALERALQD PNVAAFMVEP IQGEAGVVVP DPGYLMGVRE LCTRHQVLFI ADEIQTGLAR TGRWLAVDYE NVRPDIVLLG KALSGGLYPV SAVLCDDDIM LTIKPGEHGS TYGGNPLGCR VAIAALEVLE EENLAENADK LGIILRNELM KLPSDVVTAV RGKGLLNAIV IKETKDWDAW KVCLRLRDNG LLAKPTHGDI IRFAPPLVIK EDELRESIEI INKTILSF.
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 :
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 :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
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
-
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).
-
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.
-
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 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.
- View Data Sheet
Name :
CKBB Human, ActiveDescription:
Creatine Kinase Brain Human Recombinant, Active
Creatine kinase B-type, EC 2.7.3.2, Creatine kinase B chain, B-CK, CKB, CKBB, CKBBI.
Product # :
CKI-268Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CKBB Human Recombinant produced in Pichia Pastoris is a dimeric glycosylated full length polypeptide chain comprised of 2 identical B subunits and having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and having a Mw of 47kDa The CKBB is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
CKBB Human contains 10Mm Bis-Tris-HCl pH-6.0, 50% glycerol, 0.5mM EDTA and 0.5mM DTT.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity of CKBB was measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 854 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 1,171ng/ml.More Info
-
Introduction
Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.
-
Synonyms
Creatine kinase B-type, EC 2.7.3.2, Creatine kinase B chain, B-CK, CKB, CKBB, CKBBI.
-
Physical Appearance
Sterile Filtered colourless liquid formulation.
-
Stability
CKBB should be stored below -18°C. 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 :
ALPP HumanDescription:
Alkaline Phosphatase Placental Human Recombinant
ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
Product # :
ENZ-333Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- More Info
Description
Placental Alkaline Phosphatase Human Recombinant encoding 154-287 amino acids expressed in E.coli, shows a 41kDa band on SDS-PAGE (including GST tag).PLAP Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PLAP in 50mM Tris-Acetate, pH7.5, 1mM EDTA and 20% Glycerol.
More Info
-
Introduction
Placental alkaline phosphatase (PLAP) is a membrane-associated siaglycoprotein enzyme normally present at high concentration in syncytiotrophoblasts within the placenta during the third trimester of gestation. The expression of PLAP was originally thought to be restricted to term placenta but a human PLAP-like variant has been described which shares more than 85% homology with PLAP itself. PLAP is expressed only in normal term placenta, endocervix and fallopian tube and also in ovarian and proximal gastrointestinal tumors. It is also commonly expressed in germ cell tumors and more recently described in seminomas.
-
Synonyms
ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
-
Physical Appearance
Sterile filtered liquid.
-
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. 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 :
CTSZ HumanDescription:
Cathepsin-Z Human Recombinant
Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.
Product # :
ENZ-748Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CTSZ Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (62-303) and having a molecular mass of 29.5kDa.CTSZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTSZ solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.
-
Synonyms
Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLPKSWDW RNVDGVNYAS ITRNQHIPQY CGSCWAHAST SAMADRINIK RKGAWPSTLL SVQNVIDCGN AGSCEGGNDL SVWDYAHQHG IPDETCNNYQ AKDQECDKFN QCGTCNEFKE CHAIRNYTLW RVGDYGSLSG REKMMAEIYA NGPISCGIMA TERLANYTGG IYAEYQDTTY INHVVSVAGW GISDGTEYWI VRNSWGEPWG ERGWLRIVTS TYKDGKGARY NLAIEEHCTF GDPIV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Welqut ProteaseDescription:
Welqut Protease Staphylococcus aureus Recombinant
Product # :
ENZ-1113Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Welqut Protease Recombinant is a single, non-glycosylated polypeptide chain containing 204 amino acids and having a molecular mass of 22kDa. The Welqut Protease is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Welqut Protease contains 10 mM Na2HPO4, 50% glycerol, 1.8 mM KH2PO4, pH 7.3, 140 mM NaCl and 2.7 mM KCl.
Purity
Greater than 97.0% as determined by SDS-PAGE.
More Info
-
Introduction
WELQut Protease is an extremely specific and recombinant serine protease from Staphylococcus aureus. The WELQut Protease identifies and accurately cleaves recombinant proteins that has a recognition sequence added to them, with the amino acid sequence Trp, Glu, Leu, Gln, X (any amino acid). WELQut Protease cut externally from the recognition sequence, therefor doesn’t leave extra amino acids bound to the target protein. The protease isn’t temperature sensitive (works in 4-30°C) or pH sensitive (pH 6.5-9.0), also, there is no need in any particular buffers.
-
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.
-
Unit Definition
Each unit is defined as the amount of enzyme required to cleave ≥99% of 100μg of a control protein in 16 h at 20°C. Enzyme activity is assayed in 100μl 100 mM Tris-HCl (pH 8.0).
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 :
Benzonase Nuclease, 90%Description:
Benzonase Nuclease Serratia Marcescens Recombinant, 90%
Product # :
ENZ-1150Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Benzonase Nuclease Serratia Marcescens Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 30kDa with 2 essential disulfide bonds. Benzonase Nuclease is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Benzonase Nuclease solution contains 50% glycerol, 50 mM Tris-HCl pH 8.0, 20 mM NaCl and 2 mM MgCl2.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Serratia marcescens secretes an endonuclease that has exceptionally high specific activity to the medium that surrounds it. The Benzonase Nuclease is mainly used for elimination of nucleic acid contamination from purified proteins, downstream processing, reduction of viscosity etc. Nucleic acid contaminants are caused by nuclease released to the medium. The DNA is being destroyed by the release of the S. marcescens nuclease and it acts as the killer gene for the auto destruction of microorganisms.
-
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.
-
Specificity
Unspecific (DNA, RNA) attacks all nucleic acids (single strand, double strand, circular, supercoiled) with no apparent sequence preference. Final reaction product: 5’-mono-phosphate terminated oligonucleotides (3-5 bases). Protease Activity: Not detectable
-
Unit Definition
1U Benzonase Nuclease is defined as the amount of enzyme that causes a ΔA260 of 1 in 30 min, which corresponds to complete digestion of 37μg DNA. Standard reaction conditions are 1mg/ml sonicated DNA substrate in 50mM Tris-HCl pH 8.0, 0.1mg/ml BSA, 1mM MgCl2, incubated at 37°C.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SETD7 HumanDescription:
Set7/9 Histone Methyltransferase Human Recombinant
Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7, EC 2.1.1.43, Histone H3-K4 methyltransferase, H3-K4-HMTase, SET domain-containing protein 7, Set9, SET7/9, SETD7.
Product # :
ENZ-314Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SETD7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids & having a molecular mass of 40.7 kDa. The SETD7 purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein containing 50mM Tris-HCl buffer (pH7.5), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Set 7/9 is a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet). The methylation of lysine residues of histones plays a critical role in the regulation of chromatin structure and gene expression.
Acetylation, phosphorylation and methylation of the amino-terminal tails of histone are thought to be involved in the regulation of chromatin structure and function. The enzymes identified in the methylation of specific lysine residue on histones belong to the SET family with just one exception. Set7/9, unlike most other SET proteins, is exclusively a mono-methylase. -
Synonyms
Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7, EC 2.1.1.43, Histone H3-K4 methyltransferase, H3-K4-HMTase, SET domain-containing protein 7, Set9, SET7/9, SETD7.
-
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.
-
Amino Acid Sequence
MDSDDEMVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK FFFFDGSTLE GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDT DGRLIFKGQY KDNIRHGVCW IYYPDGGSLV GEVNEDGEMT GEKIAYVYPD ERTALYGKFI DGEMIEGKLA TLMSTEEGRP HFELMPGNSV YHFDKSTSSC ISTNALLPDP YESERVYVAE SLISSAGEGL FSKVAVGPNT VMSFYNGVRI THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT PNCIYDMFVH PRFGPIKCIR TLRAVEADEE LTVAYGYDHS PPGKSGPEAP EWYQVELKAF QATQQK
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.