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1000 results found for “ATP Synthase Mitochondrial”
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Name :
MAX HumanDescription:
MYC Associated Factor X Human Recombinant
bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.
Product # :
PRO-811Price :
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Shipped with Ice Packs
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Description
MAX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-160 a.a.) and having a molecular mass of 19.3kDa. MAX protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
MAX Human solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MAX protein is part of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. MAX forms homodimers and heterodimers with Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms offers a complex system of transcriptional regulation. In contrast to Myc, which is exceedingly regulated throughout progression during the cell cycle, Max is very stable and is much more abundant than Myc.
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Synonyms
bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.
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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
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS LEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AP3S1 HumanDescription:
Assembly Protein Complex 3 Subunit-1 Human Recombinant
CLAPS3, Sigma3A ,AP-3 complex subunit sigma-1, AP-3 complex subunit sigma-3A, Adapter-related protein complex 3 sigma-1 subunit, Clathrin-associated/assembly/adapter protein, small 3, Sigma-3A-adaptin, Sigma-adaptin 3a.
Product # :
PRO-1280Price :
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Description
AP3S1 Human Recombinant produced in E. coli is a single polypeptide chain containing 213 amino acids (1-193) and having a molecular mass of 23.8 kDa. AP3S1 is fused to 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The AP3S1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
AP-3 complex subunit sigma-1 (AP3S1) belongs to the AP-3 complex, an adapter-related complex which is not clathrin-associated. AP3S1 is linkd with the Golgi region in addition to more peripheral structures. AP3S1 facilitates the budding of vesicles from the Golgi membrane and involved in trafficking to lysosomes.
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Synonyms
CLAPS3, Sigma3A ,AP-3 complex subunit sigma-1, AP-3 complex subunit sigma-3A, Adapter-related protein complex 3 sigma-1 subunit, Clathrin-associated/assembly/adapter protein, small 3, Sigma-3A-adaptin, Sigma-adaptin 3a.
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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 MIKAILIFNN HGKPRLSKFY QPYSEDTQQQ IIRETFHLVS RDENVCNFL EGGLLIGGSD NKLIYRHYAT LYFVFCVDSS ESELGILDLI QVFVETLDKC ENVCELDLI FHVDKVHNIL AEMVMGGMVL ETNMNEIVTQ IDAQNKLEKS EAGLAGAPAR AVSAVKNMNL PEIPRNINIG DISIKVPNLP SFK.
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 :
FAHD1 HumanDescription:
Fumarylacetoacetate Hydrolase Domain Containing 1 Human Recombinant
Fumarylacetoacetate hydrolase domain-containing protein 1, YisK-like protein, FAHD1, C16orf36, YISKL, MGC74876, DKFZp566J2046.
Product # :
ENZ-067Price :
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Description
FAHD1 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 244 amino acids (1-224 a.a.) and having a molecular mass of 27kDa. The FAHD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FAHD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) is a member of the FAH family. FAHD1 is considered to have hydrolase activity and it uses Magnesium and Calcium as cofactors. It seems quite likely that the metal binding sites are involved in an enzymatic activity connected to the catabolism of aromatic amino acids.
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Synonyms
Fumarylacetoacetate hydrolase domain-containing protein 1, YisK-like protein, FAHD1, C16orf36, YISKL, MGC74876, DKFZp566J2046.
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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 MGIMAASRPL SRFWEWGKNI VCVGRNYADH VREMRSAVLS EPVLFLKPST AYAPEGSPIL MPAYTRNLHH ELELGVVMGK RCRAVPEAAA MDYVGGYALC LDMTARDVQD ECKKKGLPWT LAKSFTASCP VSAFVPKEKI PDPHKLKLWL KVNGELRQEG ETSSMIFSIP YIISYVSKII TLEEGDIILT GTPKGVGPVK ENDEIEAGIH GLVSMTFKVE KPEY.
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 :
LCAT HumanDescription:
Lecithin-Cholesterol Acyltransferase Human Recombinant
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Product # :
ENZ-380Price :
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Description
LCAT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 441 amino acids (25-440) which includes a 25 amino acid His Tag fused at N-terminus and having a total molecular mass of 49.8 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCAT protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
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Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
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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 MGSHMFWLLN VLFPPHTTPK AELSNHTRPV ILVPGCLGNQ LEAKLDKPDV VNWMCYRKTE DFFTIWLDLN MFLPLGVDCW IDNTRVVYNR SSGLVSNAPG VQIRVPGFGK TYSVEYLDSS KLAGYLHTLV QNLVNNGYVR DETVRAAPYD WRLEPGQQEE YYRKLAGLVE EMHAAYGKPV FLIGHSLGCL HLLYFLLRQP QAWKDRFIDG FISLGAPWGG SIKPMLVLAS GDNQGIPIMS SIKLKEEQRI TTTSPWMFPS RMAWPEDHVF ISTPSFNYTG RDFQRFFADL HFEEGWYMWL QSRDLLAGLP APGVEVYCLY GVGLPTPRTY IYDHGFPYTD PVGVLYEDGD DTVATRSTEL CGLWQGRQPQ PVHLLPLHGI QHLNMVFSNL TLEHINAILL GAYRQGPPAS PTASPEPPPP E.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UCHL3 HumanDescription:
Ubiquitin Carboxyl-Terminal Esterase L3 Human Recombinant
Ubiquitin Carboxyl-Terminal Esterase L3 (ubiquitin thiolesterase), UCH-L3, Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3, EC 3.4.19.12.
Product # :
ENZ-057Price :
Quantity :
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Shipped with Ice Packs
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Description
UCHL3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230a.a.) and having a molecular mass of 28.3kDa.UCHL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UCHL3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT and 10% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity: >3,000 pmole/min/ug. Measured by the hydrolysis of Ubiquitin-AMC at pH 8.0, at 37C.Citations
More Info
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Introduction
Ubiquitin carboxyl-terminal hydrolase isozyme L3 belongs to a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to produce the ubiquitin monomer. UCHL3 takes part in the regulation of neuronal development and spermatogenesis and is associated to neurodegenerative diseases. UCHL3 has a 54% homology to UCHL1.
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Synonyms
Ubiquitin Carboxyl-Terminal Esterase L3 (ubiquitin thiolesterase), UCH-L3, Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3, EC 3.4.19.12.
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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). Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERARYLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGETSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA
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 :
QPRT HumanDescription:
Quinolinate Phosphoribosyltransferase Human Recombinant
Quinolinate phosphoribosyltransferase , QPRTase, QAPRTase.
Product # :
ENZ-559Price :
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Shipped with Ice Packs
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Description
QPRT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 317 amino acids (1-297 a.a.) and having a molecular mass of 32.9 kDa. The QPRT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The QPRT solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
QPRT is a key enzyme in the catabolism of quinolinate. QPRT is in between the tryptophannicotinamide adenine dinucleotide (NAD) pathway, resulting in the production of nicotinic acid, carbon dioxide and pyrophosphate. Rise of QPRT levels in the brain is related to the pathogenesis of neurodegenerative disorders such as epilepsy, Alzheimer's disease, and Huntington's disease.
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Synonyms
Quinolinate phosphoribosyltransferase , QPRTase, QAPRTase.
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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 MDAEGLALLL PPVTLAALVD SWLREDCPGL NYAALVSGAG PSQAALWAKS PGVLAGQPFF DAIFTQLNCQ VSWFLPEGSK LVPVARVAEV RGPAHCLLLG ERVALNTLAR CSGIASAAAA AVEAARGAGW TGHVAGTRKT TPGFRLVEKY GLLVGGAASH RYDLGGLVMV KDNHVVAAGG VEKAVRAARQ AADFALKVEV ECSSLQEAVQ AAEAGADLVL LDNFKPEELH PTATVLKAQF PSVAVEASGG ITLDNLPQFC GPHIDVISMG MLTQAAPALD FSLKLFAKEV APVPKIH.
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 :
SYT11 HumanDescription:
Synaptotagmin XI Human Recombinant
Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.
Product # :
PRO-2301Price :
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Shipped with Ice Packs
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Description
SYT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (37-431 a.a) and having a molecular mass of 47kDa. SYT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SYT11 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 50% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Synaptotagmin-11 (SYT11) protein may be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may function as Ca2+ sensors in the process of vesicular trafficking and exocytosis.
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Synonyms
Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.
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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 MGSWSCCHQQ AEKKQKNPPY KFIHMLKGIS IYPETLSNKK KIIKVRRDKD GPGREGGRRN LLVDAAEAGL LSRDKDPRGP SSGSCIDQLP IKMDYGEELR SPITSLTPGE SKTTSPSSPE EDVMLGSLTF SVDYNFPKKA LVVTIQEAHG LPVMDDQTQG SDPYIKMTIL PDKRHRVKTR VLRKTLDPVF DETFTFYGIP YSQLQDLVLH FLVLSFDRFS RDDVIGEVMV PLAGVDPSTG KVQLTRDIIK RNIQKCISRG ELQVSLSYQP VAQRMTVVVL KARHLPKMDI TGLSGNPYVK VNVYYGRKRI AKKKTHVKKC TLNPIFNESF IYDIPTDLLP DISIEFLVID FDRTTKNEVV GRLILGAHSV TASGAEHWRE VCESPRKPVA KWHSLSEY.
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 :
FUT5 HumanDescription:
Fucosyltransferase 5 Human Recombinant
FUT-5
Product # :
ENZ-1199Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The FUT5 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FUT5 His-Tagged Fusion Protein produced in E. coli, is a 30kDa protein containing 172 amino acid residues of the FUT5 Human, 203-374 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
FUT-5
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized FUT5 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Fucosyltransferase 5 also known as FUT5 is a glycosyltransferase which takes part in the biosynthesis of glycolipids and glycoproteins. FUT5 mainly catalyzes the transfer of fucose (a monosaccharide) to the type 2 chain of oligosaccharides (Galβ1-4GlcNAc). FUT5 takes an important part in various biological processes which include regulation of inflammation, cell-cell interactions and immune response modulation. FUT5 is expressed mainly in tissues such as the pancreas, liver and various immune cells.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ACP1 HumanDescription:
Acid Phosphatase-1 Human Recombinant
HAAP, MGC3499, MGC111030, ACP1, Low molecular weight phosphotyrosine protein phosphatase, LMW-PTPase, LMW-PTP, Low molecular weight cytosolic acid phosphatase, Red cell acid phosphatase 1, Adipocyte acid phosphatase.
Product # :
ENZ-408Price :
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Shipped with Ice Packs
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Description
Recombinant Human ACP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (1-158 a.a.) and having a molecular mass of 20.1 kDa. ACP1 is fused to a 20 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The ACP1 protein solution contains 20mM MES, pH-6, 0.1mM PMSF, 2mM EDTA and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ACP1 is part of the phosphotyrosine protein. ACP1 functions as an acid phosphatase and a protein tyrosine phosphatase (PTPase) existing in all human tissues, including adipocytes. ACP1 enzyme hydrolyzes protein tyrosine phosphate to protein tyrosine and orthophosphate, and also orthophosphoric monoesters to alcohol and orthophosphate. ACP1 is present in adipocytes, thus playing a specific role in the regulation of adipose tissue. High levels of the ACP1 negatively regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. High significant differences in birth weight-placental weight relationships were observed among acid phosphatase locus 1 phenotypes.
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Synonyms
HAAP, MGC3499, MGC111030, ACP1, Low molecular weight phosphotyrosine protein phosphatase, LMW-PTPase, LMW-PTP, Low molecular weight cytosolic acid phosphatase, Red cell acid phosphatase 1, Adipocyte acid phosphatase.
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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 MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW VIDSGAVSDW NVGRSPDPRA VSCLRNHGIHTAHKARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH.
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Unit Definition
One unit is defined as the amount of enzyme that will hydrolyze 1nmole of p-nitrophenyl phosphate per minute at 37°C in MES pH5.0 using 10mM of substrate.
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Specific Activity
> 15,000 Units per 1mg protein.
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 :
GAPDH MouseDescription:
GAPDH Mouse Recombinant
Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, Gapdh, Gapd, Glyceraldehyde-3-phosphate dehydrogenase isoform 2, G3PD, GAPD, HEL-S-162eP.
Product # :
ENZ-860Price :
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Shipped with Ice Packs
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Description
GAPDH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 356 amino acids (1-333a.a.) and having a molecular mass of 38.2kDa.GAPDH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
GAPDH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GAPDH is a catalytic enzyme normally known to play a role in glycolysis. GAPDH exists as a tetramer composed of 36-kDa subunits and has a range of intracellular functions. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Besides functioning as a glycolytic enzyme in cytoplasm, GAPDH has function in intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and DNA repair. GAPDH catalyzes a vital energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains.
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Synonyms
Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, Gapdh, Gapd, Glyceraldehyde-3-phosphate dehydrogenase isoform 2, G3PD, GAPD, HEL-S-162eP.
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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 MGSMVKVGVN GFGRIGRLVT RAAICSGKVE IVAINDPFID LNYMVYMFQY DSTHGKFNGT VKAENGKLVI NGKPITIFQE RDPTNIKWGE AGAEYVVEST GVFTTMEKAG AHLKGGAKRV IISAPSADAP MFVMGVNHEK YDNSLKIVSN ASCTTNCLAP LAKVIHDNFG IVEGLMTTVH AITATQKTVD GPSGKLWRDG RGAAQNIIPA STGAAKAVGK VIPELNGKLT GMAFRVPTPN VSVVDLTCRL EKPAKYDDIK KVVKQASEGP LKGILGYTED QVVSCDFNSN SHSSTFDAGA GIALNDNFVK LISWYDNEYG YSNRVVDLMA YMASKE.
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 :
TrxR YeastDescription:
Thioredoxin Reductase (NADPH) Yeast Recombinant
Thioredoxin Reductase (NADPH), NTR, TrxR.
Product # :
ENZ-278Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of protein contains 20mM phosphate buffer pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be 5.8 IU/mg.
Citations
More Info
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Introduction
Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.
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Synonyms
Thioredoxin Reductase (NADPH), NTR, TrxR.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized NTR in sterile 18MΩ-cm H2O.
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Unit Definition
One unit equals the change in absorbance at 412 nm per minute at 25°C using 0.2mM NADPH containing 5mM DTNB (pH 7.0).
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.
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Name :
T4 DNADescription:
T4 DNA Ligase Recombinant
DNA ligase 4, EC 6.5.1.1, DNA ligase IV, Polydeoxyribonucleotide synthase [ATP] 4.
Product # :
ENZ-286Price :
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Description
T4 DNA Ligase 55.3kDa protein catalyzes the formation of a phosphodiester bond between juxtaposed 5' -phosphate and 3' -hydroxyl termini in duplex DNA or RNA. This enzyme will join blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA, RNA or DNA/RNA hybrids.
Source
E.Coli, cloned gene-30, bacteriophage T4.
Formulation
50% glycerol, 20mM Tris-HCl (pH-7.5), 50mM KCl, 1mM DTT and 0.1mM EDTA.
Citations
More Info
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Synonyms
DNA ligase 4, EC 6.5.1.1, DNA ligase IV, Polydeoxyribonucleotide synthase [ATP] 4.
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Physical Appearance
400U/ul solution.
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Stability
Store T4 DNA Ligase at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Applications
Cloning of restriction enzyme generated DNA fragments.
Cloning of PCR products.
Joining of double-stranded oligonucleotide linkers or adaptors to DNA.
Site-directed mutagenesis.
Amplified fragment length polymorphism (AFLP).
Ligase-mediated RNA detection.
Nick repair in duplex DNA, RNA or DNA/RNA hybrids.
Self-circularization of linear DNA
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Reaction Conditions
50mM Tris-HCl, pH7.5 at 25°C, 10mM MgCl2, 10mM DTT and 1mM ATP. Incubate at 16 °C
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Inactivation
T4 DNA Ligase can be inhibited by NaCl/KCl at a concentrations >than 200mM or by heating at 65 °C for 10 min or at 70 °C for 5 min.
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Unit Definition
1U is the amount of T4 DNA Ligase required to ligate > than 50% DNA fragments in a 20μl ligation reaction system, 6μg of λDNA-Hind III decomposition product reacts at 16°C for 30 minutes.
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 :
HSCB HumanDescription:
HscB Iron-Sulfur Cluster Co-Chaperone Human Recombinant
HscB iron-sulfur cluster co-chaperone homolog (E. coli), DnaJ homolog (Hsp40) subfamily C member 20, iron-sulfur cluster co-chaperone protein HscB mitochondrial, J-type co-chaperone HSC20, DNAJC20, HSC20, dJ366L4.2, JAC1.
Product # :
PRO-1142Price :
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Description
HSCB Human Recombinant produced in E. coli is a single polypeptide chain containing 231 amino acids (30-235) and having a molecular mass of 26.7 kDa.HSCB is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The HSCB solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HscB Iron-Sulfur Cluster Co-Chaperone (HSCB) is a member of the hscB family and contains 1 J domain. HSCB is expressed in the lung, brain, stomach, spleen, ovary, testis, liver, muscle and heart and localized to mitochondria and cytoplasm. HSCB may function as a co-chaperone in iron-sulfur cluster assembly in mitochondria, it also interacts with ISCU and HSPA9.
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Synonyms
HscB iron-sulfur cluster co-chaperone homolog (E. coli), DnaJ homolog (Hsp40) subfamily C member 20, iron-sulfur cluster co-chaperone protein HscB mitochondrial, J-type co-chaperone HSC20, DNAJC20, HSC20, dJ366L4.2, JAC1.
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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 MGSHMAASQA GSNYPRCWNC GGPWGPGRED RFFCPQCRAL QAPDPTRDYF SLMDCNRSFR VDTAKLQHRY QQLQRLVHPD FFSQRSQTEK DFSEKHSTLV NDAYKTLLAP LSRGLYLLKL HGIEIPERTD YEMDRQFLIE IMEINEKLAE AESEAAMKEI ESIVKAKQKE FTDNVSSAFE QDDFEEAKEI LTKMRYFSNI EEKIKLKKIP L
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 :
B3GNT2 HumanDescription:
Beta-1,3-N-Acetylglucosaminyltransferase 2 Human Recombinant
B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.
Product # :
ENZ-973Price :
Quantity :
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Description
B3GNT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 375 amino acids (29-397a.a.) and having a molecular mass of 43.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). B3GNT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
B3GNT2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Beta-1,3-N-Acetylglucosaminyltransferase 2 (B3GNT2) is a part of the beta-1,3-N-acetylglucosaminyltransferase family which takes part in the synthesis of poly-N-acetyllactosamine. B3GNT2 is a type II transmembrane protein which prefers the substrate of lacto-N-neotetraose. B3GNT2 catalyzes the initiation and elongation of poly-N-acetyllactosamine chains and comprises the main polylactosamine synthase.
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Synonyms
B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.
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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
ADPKSSSQEK NGKGEVIIPK EKFWKISTPP EAYWNREQEK LNRQYNPILS MLTNQTGEAG RLSNISHLNY CEPDLRVTSV VTGFNNLPDR FKDFLLYLRC RNYSLLIDQP DKCAKKPFLL LAIKSLTPHF ARRQAIRESW GQESNAGNQT VVRVFLLGQT PPEDNHPDLS DMLKFESEKH QDILMWNYRD TFFNLSLKEV LFLRWVSTSC PDTEFVFKGD DDVFVNTHHI LNYLNSLSKT KAKDLFIGDV IHNAGPHRDK KLKYYIPEVV YSGLYPPYAG GGGFLYSGHL ALRLYHITDQ VHLYPIDDVY TGMCLQKLGL VPEKHKGFRT FDIEEKNKNN ICSYVDLMLV HSRKPQEMID IWSQLQSAHL KCHHHHHH.
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 :
CCDC90B HumanDescription:
Coiled-Coil Domain Containing 90B Human Recombinant
MDS011, MDS025, CUA003, Coiled-coil domain-containing protein 90B mitochondrial, CCDC90B.
Product # :
PRO-1478Price :
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Description
CCDC90B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (43-230 a.a) and having a molecular mass of 24.1kDa.CCDC90B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CCDC90B protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Coiled-Coil Domain Containing 90B (CCDC90B) is a member of the CCDC90 family. The CCDC90B protein is distinguished by the presence of a domain of unknown function, DUF1640. The DUF1640 domain is a characteristic of the entire protein with excluding of the first 23 amino acid residues which are a mitochondrial targeting site and the cleaved CCDC90B is expected to be a mitochondrial protein with no transmembrane spans or segments. CCDC90B is predicted to contain at least 3 specific phospohorylation sites.
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Synonyms
MDS011, MDS025, CUA003, Coiled-coil domain-containing protein 90B mitochondrial, CCDC90B.
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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 MGSGYDRRPV DITPLEQRKL TFDTHALVQD LETHGFDKTQ AETIVSALTA LSNVSLDTIY KEMVTQAQQE ITVQQLMAHL DAIRKDMVIL EKSEFANLRA ENEKMKIELD QVKQQLMHET SRIRADNKLD INLERSRVTD MFTDQEKQLM ETTTEFTKKD TQTKSIISET SNKIDAEIAS LKTLMESNKL E.
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 :
CKMB1 HumanDescription:
Creatine Kinase MB Isoenzyme Type-1 Human Recombinant
Creatine Kinase MB 1, CKMB1
Product # :
CKI-269Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CKMB1 Human Recombinant produced in E.Coli is a non covalently linked heterodimer that consists of 381 a.a. and having a total Mw of ~85.6kDa. The CKMB1 is purified by proprietary chromatographic techniques.
Source
E.Coli
Formulation
CKMB1 was lyophilized a concentrated solution containing 20mM Tris, 150mM NaCl, pH-8 and 5% Trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
CKMB1 activity was measured kinetically by the CK-NAC assay at 37°C which was found to be between 500-600 units/mg. 1U converts 1µmole of creatine phosphate to creatine/min at 37˚CCitations
More Info
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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
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Synonyms
Creatine Kinase MB Isoenzyme Type-1, CK MB1
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized CKMB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 CKMB1 in sterile 18MΩ-cm H2O at 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CKM1
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQCKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K
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Background
What is the molecular weight / Mw of CKMB1 Protein?
CKMB1 Protein is a non covalently heterodimer having a total Mw of 85.6
What is the source or expression system of CKMB1 Protein?
Escherichia Coli.
What is the Purity of CKMB1 Protein?
CKMB1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CKMB1 Protein?
The activity was determined kinetically by the CK-NAC assay at 37°C which ranges between 500-600 U/mg.
What is the amino acid sequence of CKMB1 Protein?
CKM1
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ
CKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K
What applications can CKMB1 Protein be used in?
CKMB1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CKMB1 Protein?
The endotoxin level is minimal, CKMB1 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 :
T7 RNAPDescription:
T7 RNA Polymerase Recombinant
T7 RNAP.
Product # :
ENZ-1180Price :
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Description
T7 RNA polymerase Recombinant protein is produced by bacteriophage T7 DNA which is expressed in recombinant E. coli bacterial system T7 RNA Polymerase is a DNA-dependent 5'→ 3' RNA polymerase which specifically recognizes T7 promoter sequences.
Source
T7 Bacteriophage RNA Polymerase gene
Formulation
Transcription Buffer 40mM Tris-HCl (25°C, pH-8), 20mM MgCl2, 2.5mM TCEP & 2mM spermidine.
Purity
Greater than 95% as visualized by SDS-PAGE
Citations
More Info
-
Introduction
T7 RNA polymerase active enzyme synthesizes RNA at an increasing degree of that of E. coli RNA polymerase and it terminates transcription often. T7 RNA polymerase is very selective for initiation at its own promoter sequences and is resistant to antibiotics that inhibit E. coli RNA polymerase. In-vitro transcription of mRNA is achieved via bacteriophage T7 RNA polymerase using its ability to produce full-length RNA transcripts with high reliability, thoughT7 RNAP can manufacture as well immunostimulatory by products for example dsRNA which affect protein expression.
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Synonyms
T7 RNAP.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Two years when stored at -20°C, 2 weeks at 4°C. DO NOT STORE AT -70C.
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Applications
Synthesis of :
- ssRNAs.
- Labeled or unlabeled highly specific RNA probes.
- Capped mRNA using cap analogues.
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Unit Definition
1U is defined as the amount of enzyme required to incorporate 1nmol of [3H] ATP into acid-insoluble precipitates within 1 hour at 37℃, pH-8.
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 :
AHCY MouseDescription:
Adenosylhomocysteinase Mouse Recombinant
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, Adenosylhomocysteinase.
Product # :
ENZ-1054Price :
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Shipped with Ice Packs
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Description
AHCY Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 456 amino acids (1-432 a.a) and having a molecular mass of 50.2kDa.AHCY is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AHCY protein solution (0.25mg/ml) containing 20mM Tris-Hcl buffer (pH8.0) containing 40% glycerol 0.2M NaCl, 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.
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Synonyms
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, Adenosylhomocysteinase.
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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 MGSHMSDKLP YKVADIGLAA WGRKALDIAE NEMPGLMRMR EMYSASKPLK GARIAGCLHM TVETAVLIET LVALGAEVRW SSCNIFSTQD HAAAAIAKAG IPVFAWKGET DEEYLWCIEQ TLHFKDGPLN MILDDGGDLT NLIHTKYPQL LSGIRGISEE TTTGVHNLYK MMSNGILKVP AINVNDSVTK SKFDNLYGCR ESLIDGIKRA TDVMIAGKVA VVAGYGDVGK GCAQALRGFG ARVIITEIDP INALQAAMEG YEVTTMDEAC KEGNIFVTTT GCVDIILGRH FEQMKDDAIV CNIGHFDVEI DVKWLNENAV EKVNIKPQVD RYWLKNGRRI ILLAEGRLVN LGCAMGHPSF VMSNSFTNQV MAQIELWTHP DKYPVGVHFL PKKLDEAVAE AHLGKLNVKL TKLTEKQAQY LGMPINGPFK PDHYRY.
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 :
HAO1 MouseDescription:
Hydroxyacid Oxidase 1 Mouse Recombinant
(S)-2-hydroxy-acid oxidase; EC 1.1.3.15, Glycolate oxidase, GOX, GOX1MGC142227;GOXMGC142225, HAO1, HAO-1, HAOX1, hydroxyacid oxidase (glycolate oxidase) 1, hydroxyacid oxidase 1, Hydroxyacid Oxidase1, Hydroxyacid Oxidase-1.
Product # :
ENZ-1104Price :
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Shipped with Ice Packs
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Description
HAO1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-370) and having a molecular mass of 43.4 kDa.HAO1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HAO1 protein (1mg/ml) is containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,000 pmol/min/ug, and defined as the amount of enzyme that oxidize glyoxylate at pH 8.0 at 25C.
Citations
More Info
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Introduction
Hydroxyacid Oxidase 1 (HAO1) is a part of the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyses the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate by reducing oxygen to hydrogen peroxide. HAO1 is expressed mainly in the liver and pancreas and is most active on twocarbon substrates such as glycolate. HAO1 isthe main cause of hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.
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Synonyms
(S)-2-hydroxy-acid oxidase; EC 1.1.3.15, Glycolate oxidase, GOX, GOX1MGC142227;
GOXMGC142225, HAO1, HAO-1, HAOX1, hydroxyacid oxidase (glycolate oxidase) 1, hydroxyacid oxidase 1, Hydroxyacid Oxidase1, Hydroxyacid Oxidase-1. -
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 MGSMLPRLVC ISDYEQHVRS VLQKSVYDYY RSGANDQETL ADNIQAFSRW KLYPRMLRNV ADIDLSTSVL GQRVSMPICV GATAMQCMAH VDGELATVRA CQTMGTGMML SSWATSSIEE VAEAGPEALR WMQLYIYKDR EISRQIVKRA EKQGYKAIFV TVDTPYLGNR IDDVRNRFKL PPQLRMKNFE TNDLAFSPKG NFGDNSGLAE YVAQAIDPSL SWDDITWLRR LTSLPIVVKG ILRGDDAKEA VKHGVDGILV SNHGARQLDG VPATIDVLPE IVEAVEGKVE VFLDGGVRKG TDVLKALALG AKAVFVGRPI IWGLAFQGEK GVQDVLEILK EEFRLAMALS GCQNVKVIDK TLVRKNPLAV SKI.
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 :
GLRX5 HumanDescription:
Glutaredoxin 5 Human Recombinant
Glutaredoxin-related protein 5 mitochondrial, Monothiol glutaredoxin-5, GLRX5, C14orf87, glutaredoxin 5, GRX5, FLB4739, PR01238, PRO1238, MGC14129.
Product # :
ENZ-480Price :
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Shipping Method :
Shipped with Ice Packs
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Description
GLRX5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-157 a.a.) and having a molecular mass of 18.8 kDa. GRX5 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLRX5 solution containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GLRX5 is small redox enzyme of approximately 100 amino acids which uses glutathione as a cofactor. GLRX5 is a mitochondrial protein, which is evolutionarily conserved. GLRX5 is oxidized by substrates, and reduced non-enzymatically by glutathione. GLRX5 is involved in the biogenesis of iron-sulfur clusters that are required for normal iron homeostasis. GLRX5 is necessary for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1. Defects in the GLRX5 gene are a cause of anemia sideroblastic pyridoxine-refractory autosomal recessive (PRARSA).
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Synonyms
Glutaredoxin-related protein 5 mitochondrial, Monothiol glutaredoxin-5, GLRX5, C14orf87, glutaredoxin 5, GRX5, FLB4739, PR01238, PRO1238, MGC14129.
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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 MSGSLGRAAA ALLRWGRGAG GGGLWGPGVR AAGSGAGGGG SAEQLDALVK KDKVVVFLKG TPEQPQCGFS NAVVQILRLH GVRDYAAYNV LDDPELRQGI KDYSNWPTIP QVYLNGEFVG GCDILLQMHQ NGDLVEELKK LGIHSALLDE KKDQDSK.
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 :
BCOADC-E2 HumanDescription:
2-Oxo-Acid Dehydrogenase Complex E2 Human Recombinant
Product # :
ENZ-084Price :
Quantity :
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Shipped with Ice Packs
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Description
BCOADC-E2 is a Full-length cDNA coding for the mature form of the human BCOADC-E2 protein having a molecular mass of 47,321 Dalton(pH 6.5). BCOADC-E2 protein is fused to a hexa-histidine purification tag.
Source
Sf9 insect cells.
Formulation
DLST (0.91mg/ml) is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 75% as determined by SDS-PAGE.
Citations
More Info
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.
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coating concentration
0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.
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Applications
Western blot with anti-M2-Antigen autoantibody-positive patient sera or monoclonal
anti-hexa-His-tag antibody.
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 :
FBP1 Human, ActiveDescription:
Fructose-1,6-Bisphosphatase 1, BioActive Human Recombinant
Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.
Product # :
ENZ-1145Price :
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Shipped with Ice Packs
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Description
FBP1 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-338) and having a molecular mass of 39.0 kDa.FBP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FBP1 protein solution (1mg/ml) contains 1mM DTT, 10% glycerol and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 7,000pmol/min/ug, and is determined by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. 1 unit oxidizes 1.0pmole of fructose 1,6 diphosphate to fructose 6- phosphate and inorganic phosphate per minute at pH 9.5 at 37˚C.
Citations
More Info
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Introduction
FBP1 or Fructose-1, 6-bisphosphatase 1 is an enzyme, catalyzing the formation of fructose 6-phosphate & inorganic phosphate from fructose 1, 6-bisphosphate. FBP1 is part of the gluconeogenesis regulatory enzymes. Mutations in the enzyme gene can result in metabolic acidosis & hypoglycemia.
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Synonyms
Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.
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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 MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ
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 :
KMT5A HumanDescription:
Lysine Methyltransferase 5A Human Recombinant
KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.
Product # :
ENZ-1080Price :
Quantity :
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Shipped with Ice Packs
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Description
KMT5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 165 amino acids (195-352 a.a.) and having a molecular mass of 18.9kDa (Migrates at 18-28 kDa on SDS-PAGE under reducing conditions).KMT5A is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KMT5A protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 5mM DTT, 0.2M NaCl, 1mM EDTA and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Lysine Methyltransferase 5A (KMT5A) is an enzyme which catalyzes both histones and non-histone proteins. KMT5A contributes to the maintenance of proper higher-order structure of DNA during mitosis. KMT5A takes part in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. KMT5A plays a role as a barrier to prevent cellular senescence through chromatinmediated regulation of senescence-associated metabolic remodeling. KMT5A mediates monomethylation of p53/TP53 at 'Lys-382', which leads to repress p53/TP53-target genes. The loss of KMT5A simultaneously stimulate nucleolar function and retinoblastoma protein-mediated mitochondrial metabolism.
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Synonyms
KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.
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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
MKAELQSEER KRIDELIESG KEEGMKIDLI DGKGRGVIAT KQFSRGDFVV EYHGDLIEIT DAKKREALYA QDPSTGCYMY YFQYLSKTYC VDATRETNRL GRLINHSKCG NCQTKLHDID GVPHLILIAS RDIAAGEELL YDYGDRSKAS IEAHPWLKHH HHHHH.
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 :
SRR HumanDescription:
Serine Racemase Human Recombinant
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
Product # :
ENZ-232Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SRR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-340) and having a molecular mass of 39.1kDa.SRR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Serine racemase (SRR) is an enzyme which generates D-serine from L-serine. D-serine functions as a neuronal signaling molecule by activating NMDA receptors in the brain. Mammalian SRR is a pyridoxal 5'-phosphate dependent enzyme which catalyzes both the racemization of L-serine to D-serine and also the elimination of water from L-serine, producing pyruvate and ammonia. The SRR enzyme is physiologically stimulated by divalent cations (e.g., magnesium) and is allosterically activated by the magnesium/ATP complex.
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Synonyms
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMCAQYC ISFADVEKAH INIRDSIHLT PVLTSSILNQ LTGRNLFFKC ELFQKTGSFK IRGALNAVRS LVPDALERKP KAVVTHSSGN HGQALTYAAK LEGIPAYIVV PQTAPDCKKL AIQAYGASIV YCEPSDESRE NVAKRVTEET EGIMVHPNQE PAVIAGQGTI ALEVLNQVPL VDALVVPVGG GGMLAGIAIT VKALKPSVKV YAAEPSNADD CYQSKLKGKL MPNLYPPETI ADGVKSSIGL NTWPIIRDLV DDIFTVTEDE IKCATQLVWE RMKLLIEPTA GVGVAAVLSQ HFQTVSPEVK NICIVLSGGN VDLTSSITWV KQAERPASYQ SVSV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.