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1000 results found for “Deaminase”
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Name :
DCN MouseDescription:
Decorin Mouse Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
Product # :
PRO-2234Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Cor a 14.0101Description:
2S albumin Recombinant
Product # :
ALR-022Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant 2S albumin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 14kDa.Cor a 14.0101 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Cor a 14.0101 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Seed storage proteins have been identified as major allergens in several other tree nuts and peanut. 2S albumin Cor a 14.0101 is a seed storage protein in hazelnut. Sensitization to Cor a 14.0101 may cause a severe allergic reaction, mainly in children.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE-type human antibodies.2. Immunodot test with positive/negative samples
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Applications
Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PAP HumanDescription:
Prostate Acid Phosphatase Human
Product # :
ENZ-1171Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Prostate Acid Phosphatase produced in Pooled human seminal fluid having a molecular mass of approximately 100kD.
Source
Pooled human seminal fluid.
Formulation
PAP Human is lyophilized (0.2 µm filtered) from 0.02M NH4HCO3.
Purity
Greater than 96.0% as determined by SDS-PAGE.
More Info
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Introduction
Prostatic acid phosphatase, also known as PAP, is an enzyme produced by the prostate. PAP may be found in increased amounts in men with prostate cancer.
PAP’s physiological function may be associated with the liquefaction process of semen.
The highest levels of PAP are found in metastasized prostate cancer. Diseases of the bone, such as Paget's disease or hyperparathyroidism, diseases of blood cells (sickle-cell disease) or multiple myeloma or lysosomal storage diseases (Gaucher's disease), will show moderately higher levels.
Certain medications can cause temporary changes in PAP levels. Manipulation of the prostate gland through rectal exam, biopsy or massage may increase the level. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
PAP Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized PAP Human in phosphate buffer containing 0.15M NaCl.
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Human Virus Test
Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, Hepatitis C antibodies and Syphilis.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UCK2 HumanDescription:
Uridine-Cytidine Kinase 2 Human Recombinant
UK, UCK 2, Uridine-Cytidine Kinase 2, Uridine Monophosphate Kinase, Cytidine Monophosphokinase 2.
Product # :
PKA-332Price :
Quantity :
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Shipped with Ice Packs
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Description
UCK2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-261a.a.) and having a molecular mass of 30.3kDa.UCK2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UCK2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 2mM DTT, 100mM NaCl, 0.1mM PMSF, 1mM EDTA and 20% glycerol .
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UCK2 is a member of the uridinekinase family. UCK2 catalyzes the phosphorylation of uridine monophosphate to uridine diphosphate and cytidine monophosphate. UCK2 has a part in the production of pyrimidine nucleoside triphosphates essential for RNA and DNA synthesis. Furthermore, an allele of this gene is an important player in mediating nonhumoral immunity to Hemophilus influenzae type B.
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Synonyms
UK, UCK 2, Uridine-Cytidine Kinase 2, Uridine Monophosphate Kinase, Cytidine Monophosphokinase 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD YRQKQVVILS QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELILKTLKE ITEGKTVQIP VYDFVSHSRK EETVTVYPAD VVLFEGILAF YSQEVRDLFQ MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ ILSQYITFVK PAFEEFCLPT KKYADVIIPR GADNLVAINL IVQHIQDILN GGPSKRQTNG CLNGYTPSRK RQASESSSRP HLEHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MMLV RTDescription:
Moloney Murine Leukemia Virus Reverse Trancscriptase Recombinant
Product # :
ENZ-310Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MMLV (Moloney Murine Leukemia Virus) Reverse Transcriptase is a DNA polymerase that synthesizes a complementary DNA strands from single-stranded RNA, DNA, or an RNA-DNA hybrid as a template. This recombinant enzyme was purified from E.coli, which carried a modified MMLV-RT gene. Compared to AMV Reverse Transcriptase, this enzyme has a much weaker 5' - 3' ribonuclease H activity, which allows the syntesis of longer cDNAs (>7kb).
Source
Recombinant E. coli strain.
Formulation
50mM Tris-HCl, 0.1M NaCl, 0.1% Triton X-100, 2mM DTT, 0.1mM EDTA and 50% glycerol.
More Info
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Physical Appearance
Sterile Filtered clear solution (200 U/µl).
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Stability
Stable for 5 days at 10°C, for longer period of time store at -20°C. Please prevent freeze-thaw cycles.
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Unit Definition
One unit is defined as the amount of enzyme required to catalyze the incorporation of 1nmol of deoxyribonucleotide into acid-insoluble forms in 10 minutes at 37oC, using poly(A)-oligo(dT)12-18 as the template-primer. Standard cDNA Synthesis Conditions50mM Tris-HCl (pH8.3), 75mM KCl, 3mM MgCl2, 10mM DTT, 1.0mM each dATP, dGTP, dCTP, and dTTP, 0.2 mg radom hexamer,1-5mg RNA, 200units M-MLV RT. The reaction volume was 20ml and the incubation was 45 min at 42oC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CSNK2A1 Human, HisDescription:
Casein Kinase 2 alpha 1 Human Recombinant, His
Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.
Product # :
PKA-225Price :
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Shipped with Ice Packs
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Description
CK2A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain encoding the sequence of 411 amino acids and having a molecular mass of 47.3 kDa.Casein Kinase 2 alpha subunit is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSNK2A1 is supplied in 20mM Tris pH-8.0 , 500mM NaCl, 1mM DTT and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes.
Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2.
Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm. -
Synonyms
Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQLVRKLGRGKY SEVFEAINIT NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKRWERFVHSENQ HLVSPEALDF LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ 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.
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Name :
KLK15 Human, sf9Description:
Kallikrein-15 Human Recombinant, sf9
Kallikrein Related Peptidase 15, ACO Protease, Kallikrein-Like Serine Protease, Kallikrein 15, Kallikrein-15, Prostinogen, EC 3.4.21.4, EC 3.4.21.-, EC 3.4.21, HSRNASPH, ACO.
Product # :
ENZ-1047Price :
Quantity :
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Shipped with Ice Packs
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Description
KLK15 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 249 amino acids (17-256a.a.) and having a molecular mass of 27.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).KLK15 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK15 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-15 (KLK15) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. KLK15 contains numerous polyadenylation sites and alternative splicing results in multiple transcript variants encoding different isoforms. KLK15 is over expressed in prostate cancer and therefore uses as a diagnostic or prognostic marker for prostate cancer.
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Synonyms
Kallikrein Related Peptidase 15, ACO Protease, Kallikrein-Like Serine Protease, Kallikrein 15, Kallikrein-15, Prostinogen, EC 3.4.21.4, EC 3.4.21.-, EC 3.4.21, HSRNASPH, ACO.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPQDGDKLL EGDECAPHSQ PWQVALYERG RFNCGASLIS PHWVLSAAHC QSRFMRVRLG EHNLRKRDGP EQLRTTSRVI PHPRYEARSH RNDIMLLRLV QPARLNPQVR PAVLPTRCPH PGEACVVSGW GLVSHNEPGT AGSPRSQVSL PDTLHCANIS IISDTSCDKS YPGRLTNTMV CAGAEGRGAE SCEGDSGGPL VCGGILQGIV SWGDVPCDNT TKPGVYTKVC HYLEWIRETM KRNHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Cyclophilin B Human, HisDescription:
Cyclophilin-B Human Recombinant, His Tag
Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.
Product # :
ENZ-808Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cyclophilin-B Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Asp34-Glu216) containing 193 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 22kDa.
Source
Escherichia Coli.
Formulation
Cyclophilin-B was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.
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Synonyms
Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Cyclophilin-B is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS DEKKKGPKVT VKVYFDLRIG DEDVGRVIFG LFGKTVPKTV DNFVALATGE KGFGYKNSKF HRVIKDFMIQ GGDFTRGDGT GGKSIYGERF PDENFKLKHY GPGWVSMANA GKDTNGSQFF ITTVKTAWLD GKHVVFGKVL EGMEVVRKVE STKTDSRDKP LKDVIIADCG KIEVEKPFAI AKE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNCA Delta-NAC HumanDescription:
Alpha Synuclein Delta-NAC Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-161Price :
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Shipped with Ice Packs
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Description
A-Synuclein Delta-NAC Human Recombinant which is a deletion mutant of the a-synuclein that lacks the NAC region (amino acid 61-95), produced in E.Coli is a single, non-glycosylated polypeptide chain of 111 amino acids having a molecular mass of 11.9kDa (molecular size on SDS-PAGE will appear higher), with 6 amino acids added as a linker. The Recombinant Human a-Synuclein Delta-NAC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA Delta-NAC protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK GTEIWMKKDQ LGKNEEGAPQ EGILEDMPVD PDNEAYEMPS EEGYQDYEPE A.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RNMTL1 HumanDescription:
RNA Methyltransferase Like 1 Human Recombinant
RNA Methyltransferase Like 1, 16S RRNA (Guanosine(1370)-2-O)-Methyltransferase, 16S RRNA [Gm1370] 2-O-Methyltransferase, RNA Methyltransferase-Like Protein 1, HC90, MRM3, RRNA Methyltransferase 3, Mitochondrial, Putative RNA Methyltransferase, EC 2.1.1.-, EC 2.1.1, RMTL1, RNMTL1.
Product # :
ENZ-895Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RNMTL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 443 amino acids (1-420 a.a) and having a molecular mass of 49.4kDa.RNMTL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNMTL1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
RNA methyltransferase-like protein 1, also known as RNMTL1 is a member of the RNA methyltransferase TrmH family. RNMTL1 is probable RNA methyltransferase and expressed at an equal level in normal liver and hepatocarcinoma.
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Synonyms
RNA Methyltransferase Like 1, 16S RRNA (Guanosine(1370)-2-O)-Methyltransferase, 16S RRNA [Gm1370] 2-O-Methyltransferase, RNA Methyltransferase-Like Protein 1, HC90, MRM3, RRNA Methyltransferase 3, Mitochondrial, Putative RNA Methyltransferase, EC 2.1.1.-, EC 2.1.1, RMTL1, RNMTL1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAALVRP ARFVVRPLLQ VVQAWDLDAR RWVRALRRSP VKVVFPSGEV VEQKRAPGKQ PRKAPSEASA QEQREKQPLE ESASRAPSTW EESGLRYDKA YPGDRRLSSV MTIVKSRPFR EKQGKILLEG RRLISDALKA GAVPKMFFFS RLEYLKELPV DKLKGVSLIK VKFEDIKDWS DLVTPQGIMG IFAKPDHVKM TYPKTQLQHS LPLLLICDNL RDPGNLGTIL RSAAGAGCSK VLLTKGCVDA WEPKVLRAGM GAHFRMPIIN NLEWETVPNY LPPDTRVYVA DNCGLYAQAE MSNKASDHGW VCDQRVMKFH KYEEEEDVET GASQDWLPHV EVQSYDSDWT EAPAAVVIGG ETYGVSLESL QLAESTGGKR LLIPVVPGVD SLNSAMAASI LLFEGKRQLR GRAEDLSRDR SYH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CAMK4 HumanDescription:
Calcium/Calmodulin-Dependent Protein Kinase IV Human Recombinant
Calcium/calmodulin-dependent protein kinase type IV catalytic chain, CaMK-GR, CaM kinase-GR, CaMK IV, IV, brain Ca(2+)-calmodulin-dependent protein kinase type IV, caMK, CAM kinase IV, EC 2.7.11.17.
Product # :
PKA-021Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CAMK4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 497 amino acids (1-473) and having a molecular mass of 54.5kDa.CAMK4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CAMK4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
CAMK4 is a member of the serine/threonine protein kinase family, and of the Ca(2+)/calmodulin-dependent protein kinase subfamily. CAMK4 is a multifunctional serine/threonine protein kinase with restricted tissue distribution which is associated to transcriptional regulation in lymphocytes, neurons and male germ cells.
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Synonyms
Calcium/calmodulin-dependent protein kinase type IV catalytic chain, CaMK-GR, CaM kinase-GR, CaMK IV, IV, brain Ca(2+)-calmodulin-dependent protein kinase type IV, caMK, CAM kinase IV, EC 2.7.11.17.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLKVTV PSCSASSCSS VTASAAPGTA SLVPDYWIDG SNRDALSDFF EVESELGRGA TSIVYRCKQK GTQKPYALKV LKKTVDKKIV RTEIGVLLRL SHPNIIKLKE IFETPTEISL VLELVTGGEL FDRIVEKGYY SERDAADAVK QILEAVAYLH ENGIVHRDLK PENLLYATPA PDAPLKIADF GLSKIVEHQV LMKTVCGTPG YCAPEILRGC AYGPEVDMWS VGIITYILLC GFEPFYDERG DQFMFRRILN CEYYFISPWW DEVSLNAKDL VRKLIVLDPK KRLTTFQALQ HPWVTGKAAN FVHMDTAQKK LQEFNARRKL KAAVKAVVAS SRLGSASSSH GSIQESHKAS RDPSPIQDGN EDMKAIPEGE KIQGDGAQAA VKGAQAELMK VQALEKVKGA DINAEEAPKM VPKAVEDGIK VADLELEEGL AEEKLKTVEE AAAPREGQGS SAVGFEVPQQ DVILPEY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BD 4 HumanDescription:
Beta Defensin-4 Human Recombinant
HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.
Product # :
CYT-599Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Beta Defensin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 50 amino acids and having a molecular mass of 6 kDa. The BD-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DEFB4 (1mg/ml) was lyophilized with 20mM sodium Phosphate buffer pH-7.4 and 130mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.More Info
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Introduction
Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues. -
Synonyms
HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Beta Defensin-4 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Beta Defensin-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.
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Background
Beta Defensin-4 Human Recombinant: Exploring the Potential of a Novel Antimicrobial Peptide
Abstract:
Beta Defensin-4 (hBD-4) human recombinant is a promising antimicrobial peptide with unique properties and potential therapeutic applications. This research paper provides an in-depth analysis of hBD-4, including its characteristics, mode of action, and potential uses. Furthermore, novel methodologies for the production and optimization of hBD-4 human recombinant are proposed, shedding light on its future implications in the field of infectious disease management.
Introduction:
In the face of increasing drug-resistant infections, alternative therapeutic strategies are crucial. Antimicrobial peptides, such as hBD-4, have gained attention due to their broad-spectrum activity against pathogens. This paper aims to explore the distinctive features of hBD-4 and propose innovative approaches for its production and optimization.
Characteristics and Mode of Action:
hBD-4 is a cationic peptide comprising 50 amino acids and is characterized by a unique structure that contributes to its antimicrobial properties. The mechanism of action involves the disruption of microbial membranes and subsequent cell death. Additionally, hBD-4 exhibits immunomodulatory effects, including the stimulation of chemotaxis and modulation of the inflammatory response.
Production of hBD-4 Human Recombinant:
Efficient production methodologies for hBD-4 human recombinant are essential for its therapeutic applications. Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents advantages and challenges, necessitating careful selection for high yields and protein quality. Optimization strategies, including codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-4 recombinant.
Potential Applications:
hBD-4 human recombinant demonstrates potential therapeutic applications in combating drug-resistant pathogens. Its broad-spectrum antimicrobial activity against bacteria, viruses, and fungi positions it as a promising candidate for infectious disease management. Moreover, hBD-4 shows promise in wound healing and tissue regeneration due to its ability to promote angiogenesis and stimulate cell migration. Exploring its potential in combination with drug delivery systems for targeted therapy is an exciting avenue for future research.
Conclusion:
hBD-4 human recombinant represents a novel antimicrobial peptide with diverse potential applications. Optimizing production methodologies and elucidating its mechanisms of action will further enhance its clinical utility. With its broad-spectrum antimicrobial activity and potential implications in wound healing and targeted therapy, hBD-4 human recombinant holds promise as an innovative therapeutic agent.
What is the molecular weight/Mw of BD4 Protein?
BD4 Protein has a total Mw of 6kDa.
What is the source or expression system of BD4 Protein?
Escherichia Coli.
What is the Purity of BD4 Protein?
BD4 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BD4 Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.
What is the amino acid sequence of BD4 Protein?
EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.
What applications can BD4 Protein be used in?
BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD4 Protein?
The endotoxin level is minimal, BD4 Protein was purified using conventional chromatography techniques.
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 :
Dengue Envelope-3 32kDaDescription:
Dengue Virus Subtype 3 Envelope 32kDa Recombinant
Product # :
DEN-019Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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- More Info
Description
Recombinant Dengue Virus Subtype 3 Envelope 32kDa, produced in E.coli and fused with a 6xHis Tag, containing domains I+II of the dengue envelope.
Source
E.coli.
Formulation
Phosphate buffered saline, pH-7.4.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
-
Introduction
Dengue fever is affected by 1 of 4 closely linked virus serotypes of the genus Flavivirus, family Flaviviridae. One might have dengue fever infected by the different serotype virus after the primary infection. Detection of particular antibodies to dengue viruses is used for the diagnosis in clinic. Recently, lateral flow rapid test products have become a most suitable and known method in the clinical diagnosis. Though, there is difficulty for manufacturers to have the dengue antigens with a whole coverage for Dengue IgG & IgM recognition for all 4 serotype infections as well as with colloid gold binding ability. 8 dengue antigens have been established for the lateral flow products which are well defined for their coverage of dengue IgG & IgM recognition. The researcher can select the products below based on their own specific application.
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Stability
Dengue Envelope-3 32kDa although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Immunoassay.
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Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ARSA Human, SF9Description:
Arylsulfatase A Human Recombinant, Sf9
Arylsulfatase A, Cerebroside-Sulfatase, ASA, Metachromatic Leucodystrophy, MLD, EC 3.1.6.8.
Product # :
ENZ-1087Price :
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Shipped with Ice Packs
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- More Info
Description
ARSA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 498 amino acids (21-509a.a.) and having a molecular mass of 53.0kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). ARSA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ARSA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,500 pmol/min/ug, and defined as the amount of enzyme that hydrolyze 4-Nitrocatechol at pH 5.0 at 37C.
More Info
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Introduction
The enzyme Arylsulfatase A, also known as cerebroside-sulfatase, is responsible to break down sulfatides. The main molecule that Arylsulfatase A breaks down is cerebroside 3-sulfate into cerebroside and sulfate. The enzyme is encoded by the ARSA gene in humans. Phosphate can form a covalent bond with the Arylsulfatase A’s active site 3-oxoalanine, thus, inhibits the protein.
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Synonyms
Arylsulfatase A, Cerebroside-Sulfatase, ASA, Metachromatic Leucodystrophy, MLD, EC 3.1.6.8.
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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.
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Amino Acid Sequence
ADPRPPNIVL IFADDLGYGD LGCYGHPSST TPNLDQLAAG GLRFTDFYVP VSLCTPSRAA LLTGRLPVRM GMYPGVLVPS SRGGLPLEEVTVAEVLAARG YLTGMAGKWH LGVGPEGAFL PPHQGFHRFL GIPYSHDQGP CQNLTCFPPA TPCDGGCDQG LVPIPLLANL SVEAQPPWLP GLEARYMAFA HDLMADAQRQ DRPFFLYYAS HHTHYPQFSG QSFAERSGRG PFGDSLMELD AAVGTLMTAI GDLGLLEETL VIFTADNGPETMRMSRGGCS GLLRCGKGTT YEGGVREPAL AFWPGHIAPG VTHELASSLD LLPTLAALAG APLPNVTLDG FDLSPLLLGT GKSPRQSLFF YPSYPDEVRG VFAVRTGKYK AHFFTQGSAH SDTTADPACH ASSSLTAHEP PLLYDLSKDP GENYNLLGGV AGATPEVLQA LKQLQLLKAQLDAAVTFGPS QVARGEDPAL QICCHPGCTP RPACCHCPDP HAHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2Q2 HumanDescription:
Ubiquitin Conjugating Enzyme E2Q2 Human Recombinant
Ubiquitin-conjugating enzyme E2 Q2, UBE2Q2, E2 ubiquitin-conjugating enzyme Q2, Ubiquitin carrier protein Q2, Ubiquitin-protein ligase Q2, Ubiquitin Conjugating Enzyme E2Q2, Ubiquitin-conjugating enzyme E2 Q2 isoform1.
Product # :
ENZ-885Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
UBE2Q2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-375a.a.) and having a molecular mass of 45.2kDa.UBE2Q2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2Q2 protein solution (0.5mg/ml) containing Phosphate Buffer Saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquitin Conjugating Enzyme E2Q2 (UBE2Q2) is a protein coding gene which receives ubiquitin from the E1 complex and catalyzes its covalent attachment to various proteins. UBE2Q2 which is a part of the ubiquitin-conjugating enzyme family is detected in hypopharyngeal head and neck squamous cell carcinoma and in tumor masses.
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Synonyms
Ubiquitin-conjugating enzyme E2 Q2, UBE2Q2, E2 ubiquitin-conjugating enzyme Q2, Ubiquitin carrier protein Q2, Ubiquitin-protein ligase Q2, Ubiquitin Conjugating Enzyme E2Q2, Ubiquitin-conjugating enzyme E2 Q2 isoform1.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSVSGLK AELKFLASIF DKNHERFRIV SWKLDELHCQ FLVPQQGSPH SLPPPLTLHC NITESYPSSS PIWFVDSEDP NLTSVLERLE DTKNNNLLRQ QLKWLICELC SLYNLPKHLD VEMLDQPLPT GQNGTTEEVT SEEEEEEEEM AEDIEDLDHY EMKEEEPISG KKSEDEGIEK ENLAILEKIR KTQRQDHLNG AVSGSVQASD RLMKELRDIY RSQSYKTGIY SVELINDSLY DWHVKLQKVD PDSPLHSDLQ ILKEKEGIEY ILLNFSFKDN FPFDPPFVRV VLPVLSGGYV LGGGALCMEL LTKQGWSSAY SIESVIMQIN ATLVKGKARV QFGANKNQYN LARAQQSYNS IVQIHEKNGW YTPPKEDG.
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 :
UGT1A1 HumanDescription:
UDP Glucuronosyltransferase 1 Family Polypeptide A1 Human Recombinant
UDP Glucuronosyltransferase 1 Family, Polypeptide A1, UGT1, GNT1, UDP Glycosyltransferase 1 Family, Polypeptide A1, Bilirubin-Specific UDPGT Isozyme 1, UDP-Glucuronosyltransferase 1-A, UDP-Glucuronosyltransferase 1A1, EC 2.4.1.17, UDPGT 1-1, BILIQTL1, HUG-BR1, UGT1-01, UGT-1A, UGT1*1, UGT1.1, UGT1A, Bilirubin UDP-Glucuronosyltransferase Isozyme 1, Bilirubin UDP-Glucuronosyltransferase 1-1, UDP-Glucuronosyltransferase 1-1, UDPGT, UDP-glucuronosyltransferase 1-1.
Product # :
ENZ-864Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UGT1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 488 amino acids (26-490 a.a) and having a molecular mass of 54.7kDa. UGT1A1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UGT1A1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
UDP Glucuronosyltransferase 1 Family Polypeptide A1, also known as UGT1A1 has a main importance in the conjugation as well as subsequent elimination of potentially toxic xenobiotics and endogenous compounds. UGT1A1 is also capable of catalyzing glucuronidation of 17beta, 17alpha, 1-hydroxypyrene, 4-methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone.
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Synonyms
UDP Glucuronosyltransferase 1 Family, Polypeptide A1, UGT1, GNT1, UDP Glycosyltransferase 1 Family, Polypeptide A1, Bilirubin-Specific UDPGT Isozyme 1, UDP-Glucuronosyltransferase 1-A, UDP-Glucuronosyltransferase 1A1, EC 2.4.1.17, UDPGT 1-1, BILIQTL1, HUG-BR1, UGT1-01, UGT-1A, UGT1*1, UGT1.1, UGT1A, Bilirubin UDP-Glucuronosyltransferase Isozyme 1, Bilirubin UDP-Glucuronosyltransferase 1-1, UDP-Glucuronosyltransferase 1-1, UDPGT, UDP-glucuronosyltransferase 1-1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHAGKILL IPVDGSHWLS MLGAIQQLQQ RGHEIVVLAP DASLYIRDGA FYTLKTYPVP FQREDVKESF VSLGHNVFEN DSFLQRVIKT YKKIKKDSAM LLSGCSHLLH NKELMASLAE SSFDVMLTDP FLPCSPIVAQ YLSLPTVFFL HALPCSLEFE ATQCPNPFSY VPRPLSSHSD HMTFLQRVKN MLIAFSQNFL CDVVYSPYAT LASEFLQREV TVQDLLSSAS VWLFRSDFVK DYPRPIMPNM VFVGGINCLH QNPLSQEFEA YINASGEHGI VVFSLGSMVS EIPEKKAMAI ADALGKIPQT VLWRYTGTRP SNLANNTILV KWLPQNDLLG HPMTRAFITH AGSHGVYESI CNGVPMVMMP LFGDQMDNAK RMETKGAGVT LNVLEMTSED LENALKAVIN DKSYKENIMR LSSLHKDRPV EPLDLAVFWV EFVMRHKGAP HLRPAAHDLT WYQYHSLD.
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 :
PLA2G2E HumanDescription:
Secreted Phospholipase A2-IIE Human Recombinant
Group IIE secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIIE, GIIE sPLA2, sPLA(2)-IIE, sPLA2-IIE, PLA2G2E.
Product # :
ENZ-327Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secreted Phospholipase A2-IIE Human Recombinant manufactured with N-terminal His-Tag. PLA2G2E His-Tagged Fusion Protein is 15.8 kDa protein containing 123 amino acid residues of the human secreted phospholipase A2-IIE and 16 additional amino acid residues – His-Tag (underlined).
Source
Escherichia Coli.
Formulation
Sterile filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
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Introduction
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular 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.This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso-PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats. -
Synonyms
Group IIE secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIIE, GIIE sPLA2, sPLA(2)-IIE, sPLA2-IIE, PLA2G2E.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add 0.2 ml of 0.1M Acetate buffer pH-4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10 μg/ml. In higher concentrations the solubility of this antigen is limited.
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Amino Acid Sequence
MRGSHHHHHH GMASHMNLVQ FGVMIEKMTG KSALQYNDYG CYCGIGGSHW PVDQTDWCCH AHDCCYGRLE KLGCEPKLEK YLFSVSERGI FCAGRTTCQR LTCECDKRAA LCFRRNLGTY NRKYAHYPNK LCTGPTPPC
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KLK3, HisDescription:
Kallikrein-3 Human Recombinant, His Tag
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
Product # :
ENZ-620Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLK3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (25-261) and having a molecular mass of 28.8kDa.The KLK3 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KLK3 protein solution (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0) and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-3 (KLK3) belongs to the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 is assumed to act normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.
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Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMIVGGW ECEKHSQPWQ VLVASRGRAV CGGVLVHPQW VLTAAHCIRN KSVILLGRHS LFHPEDTGQV FQVSHSFPHP LYDMSLLKNR FLRPGDDSSH DLMLLRLSEP AELTDAVKVM DLPTQEPALG TTCYASGWGS IEPEEFLTPK KLQCVDLHVI SNDVCAQVHP QKVTKFMLCA GRWTGGKSTC SGDSGGPLVC NGVLQGITSW GSEPCALPER PSLYTKVVHY RKWIKDTIVA NP.
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 :
MGLL HumanDescription:
Monoglyceride Lipase Human Recombinant
Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.
Product # :
ENZ-019Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MGLL 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 333 amino acids (1-313 a.a.) and having a molecular mass of 36.4kDa. The MGLL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MGLL solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
MGLL is a membrane-associated member of the serine hydrolase superfamily. MGLL is expressed in abundance in skeletal muscle and adipose tissue. MGLL functions jointly with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.
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Synonyms
Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH METGPEDPSS MPEESSPRRT PQSIPYQDLP HLVNADGQYL FCRYWKPTGT PKALIFVSHG AGEHSGRYEE LARMLMGLDL LVFAHDHVGH GQSEGERMVV SDFHVFVRDV LQHVDSMQKD YPGLPVFLLG HSMGGAIAIL TAAERPGHFA GMVLISPLVL ANPESATTFK VLAAKVLNLV LPNLSLGPID SSVLSRNKTE VDIYNSDPLI CRAGLKVCFG IQLLNAVSRV ERALPKLTVP FLLLQGSADR LCDSKGAYLL MELAKSQDKT LKIYEGAYHV LHKELPEVTN SVFHEINMWV SQRTATAGTA SPP.
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 :
CS HumanDescription:
Citrate Synthase Human Recombinant
Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, mitochondrial.
Product # :
ENZ-824Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (28-466 a.a) and having a molecular mass of 51.4kDa. CS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CS 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
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Introduction
Citrate synthase also known as CS is a Krebs tricarboxylic acid cycle enzyme which catalyzes the synthesis of citrate from oxaloacetate and acetyl coenzyme A. CS is present in almost all cells capable of oxidative metabolism. CS is nuclear encoded and transported into the mitochondrial matrix, where the mature form is found. The diseases related to CS are: critical illness polyneuropathy and mitochondrial cardiomyopathy.
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Synonyms
Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, mitochondrial.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSASSTNLK DILADLIPKE QARIKTFRQQ HGKTVVGQIT VDMMYGGMRG MKGLVYETSV LDPDEGIRFR GFSIPECQKL LPKAKGGEEP LPEGLFWLLV TGHIPTEEQV SWLSKEWAKR AALPSHVVTM LDNFPTNLHP MSQLSAAVTA LNSESNFARA YAQGISRTKY WELIYEDSMD LIAKLPCVAA KIYRNLYREG SGIGAIDSNL DWSHNFTNML GYTDHQFTEL TRLYLTIHSD HEGGNVSAHT SHLVGSALSD PYLSFAAAMN GLAGPLHGLA NQEVLVWLTQ LQKEVGKDVS DEKLRDYIWN TLNSGRVVPG YGHAVLRKTD PRYTCQREFA LKHLPNDPMF KLVAQLYKIV PNVLLEQGKA KNPWPNVDAH SGVLLQYYGM TEMNYYTVLF GVSRALGVLA QLIWSRALGF PLERPKSMST EGLMKFVDSK SG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ALDOC HumanDescription:
Aldolase C Fructose-Bisphosphate Human Recombinant
Aldolase, Fructose-Bisphosphate C, Aldolase C, Fructose-Bisphosphate, Brain-Type Aldolase, EC 4.1.2.13, ALDC, Fructose-1,6-Biphosphate Triosephosphate Lyase, Fructose-Bisphosphate Aldolase C, Fructoaldolase C, Aldolase 3.
Product # :
ENZ-969Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ALDOC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-364 a.a) and having a molecular mass of 39.4kDa. ALDOC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDOC protein solution (1mg/ml) containing 20mM Tris-Hcl Buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.
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Synonyms
Aldolase, Fructose-Bisphosphate C, Aldolase C, Fructose-Bisphosphate, Brain-Type Aldolase, EC 4.1.2.13, ALDC, Fructose-1,6-Biphosphate Triosephosphate Lyase, Fructose-Bisphosphate Aldolase C, Fructoaldolase C, Aldolase 3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA NHAY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ECH1 HumanDescription:
Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant
peroxisomal, enoyl Coenzyme A hydratase 1.
Product # :
ENZ-562Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ECH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (34-328a.a.) and having a molecular mass of 34.4kDa.ECH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ECH1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 50mM NaCl, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ECH1 is a member of the hydratase/isomerase superfamily. ECH1 demonstrates high sequence similarity to enoyl-coenzyme A (CoA) hydratases of more than a few species, mostly within a conserved domain characteristic of these proteins. ECH1 contains a C-terminal peroxisomal targeting sequence, localizes to both the peroxisome and the mitochondria. peroxisomal takes part in the auxiliary step of the fatty acid beta-oxidation pathway specifically functioning to catalyze the isomerization of 3-trans, 5-cis-dienoyl-CoA to 2-trans, 4-transdienoyl-CoA.
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Synonyms
peroxisomal, enoyl Coenzyme A hydratase 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTGSSAQEAA SGVALGEAPD HSYESLRVTS AQKHVLHVQL NRPNKRNAMN KVFWREMVEC FNKISRDADC RAVVISGAGK MFTAGIDLMD MASDILQPKG DDVARISWYL RDIITRYQET FNVIERCPKP VIAAVHGGCI GGGVDLVTAC DIRYCAQDAF FQVKEVDVGL AADVGTLQRL PKVIGNQSLV NELAFTARKM MADEALGSGL VSRVFPDKEV MLDAALALAA EISSKSPVAV QSTKVNLLYS RDHSVAESLN YVASWNMSML QTQDLVKSVQ ATTENKELKT VTFSKL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
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
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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
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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.
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Synonyms
Fructose-1,6-bisphosphatase isozyme 2, Fructose-1,6-bisphosphatase isozyme 2, FBPase 2, D-fructose-1,6-bisphosphate 1-phosphohydrolase 2, FBP2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH 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.
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Name :
CA12 HumanDescription:
Carbonic Anhydrase XII Human Recombinant
Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.
Product # :
ENZ-886Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CA12 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 283 amino acids (25-301a.a.) and having a molecular mass of 31.94kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).CA12 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CA12 protein solution (0.5mg/ml) containing Phosphate Buffer Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 300 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 7.5 at 37C.More Info
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Introduction
Carbonic anhydrase 12 (CA12) is an enzyme that belongs to the Carbonic anhydrases (CAs) family. This is a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They are involved in various biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA12 is a type I membrane protein which is highly expressed in normal tissues, such as the kidney, colon and pancreas, and is overexpressed in 10% of clear cell renal carcinomas.
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Synonyms
Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
APVNGSKWTY FGPDGENSWS KKYPSCGGLL QSPIDLHSDI LQYDASLTPL EFQGYNLSAN KQFLLTNNGH SVKLNLPSDM HIQGLQSRYS ATQLHLHWGN PNDPHGSEHT VSGQHFAAEL HIVHYNSDLY PDASTASNKS EGLAVLAVLI EMGSFNPSYD KIFSHLQHVK YKGQEAFVPG FNIEELLPER TAEYYRYRGS LTTPPCNPTV LWTVFRNPVQ ISQEQLLALE TALYCTHMDD PSPREMINNF RQVQKFDERL VYTSFSQVQV CTAAGLSHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.