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Search results

1000 results found for “ATP Synthase Mitochondrial”

Name

Description

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  • View Data Sheet

    Name :

    MAX Human

    Description:

    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-811

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    • source
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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

    • 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.

    • 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.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      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.

    Max Human
  • View Data Sheet

    Name :

    AP3S1 Human

    Description:

    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-1280

    Price :

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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

    • 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.

    • 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.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Ap3S1 Human
  • View Data Sheet

    Name :

    FAHD1 Human

    Description:

    Fumarylacetoacetate Hydrolase Domain Containing 1 Human Recombinant

    Fumarylacetoacetate hydrolase domain-containing protein 1, YisK-like protein, FAHD1, C16orf36, YISKL, MGC74876, DKFZp566J2046.

    Product # :

    ENZ-067

    Price :

    Quantity :

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    • description
    • source
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    • More Info
    • Citations

    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

    • 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.

    • Synonyms

      Fumarylacetoacetate hydrolase domain-containing protein 1, YisK-like protein, FAHD1, C16orf36, YISKL, MGC74876, DKFZp566J2046.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Fahd1 Human
  • View Data Sheet

    Name :

    LCAT Human

    Description:

    Lecithin-Cholesterol Acyltransferase Human Recombinant

    Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    Product # :

    ENZ-380

    Price :

    Quantity :

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    • description
    • source
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    • Citations

    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

    • 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.

    • Synonyms

      Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Lcat Human
  • View Data Sheet

    Name :

    UCHL3 Human

    Description:

    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-057

    Price :

    Quantity :

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    • description
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    • biological activity
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    • Citations

    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

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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.

    • Synonyms

      Ubiquitin Carboxyl-Terminal Esterase L3 (ubiquitin thiolesterase), UCH-L3, Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3, EC 3.4.19.12.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Uchl3 Human
  • View Data Sheet

    Name :

    QPRT Human

    Description:

    Quinolinate Phosphoribosyltransferase Human Recombinant

    Quinolinate phosphoribosyltransferase , QPRTase, QAPRTase.

    Product # :

    ENZ-559

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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

    • 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.

    • Synonyms

      Quinolinate phosphoribosyltransferase , QPRTase, QAPRTase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Qprt Human
  • View Data Sheet

    Name :

    SYT11 Human

    Description:

    Synaptotagmin XI Human Recombinant

    Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.

    Product # :

    PRO-2301

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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

    • 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.

    • Synonyms

      Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Syt11 Human
  • View Data Sheet

    Name :

    FUT5 Human

    Description:

    Fucosyltransferase 5 Human Recombinant

    FUT-5

    Product # :

    ENZ-1199

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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

    • Synonyms

      FUT-5

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • 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.

    • 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.

    Fut5 Human
  • View Data Sheet

    Name :

    ACP1 Human

    Description:

    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-408

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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

    • 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.

    • 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.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW VIDSGAVSDW NVGRSPDPRA VSCLRNHGIHTAHKARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH.

    • 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.

    • 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.

    Acp1 Human
  • View Data Sheet

    Name :

    GAPDH Mouse

    Description:

    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-860

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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

    • 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.

    • Synonyms

      Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, Gapdh, Gapd, Glyceraldehyde-3-phosphate dehydrogenase isoform 2, G3PD, GAPD, HEL-S-162eP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Gapdh Mouse
  • View Data Sheet

    Name :

    TrxR Yeast

    Description:

    Thioredoxin Reductase (NADPH) Yeast Recombinant

    Thioredoxin Reductase (NADPH), NTR, TrxR.

    Product # :

    ENZ-278

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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

    • 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.

    • Synonyms

      Thioredoxin Reductase (NADPH), NTR, TrxR.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NTR in sterile 18MΩ-cm H2O.

    • 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.

    Thioredoxin Reductase Yeast
  • View Data Sheet

    Name :

    T4 DNA

    Description:

    T4 DNA Ligase Recombinant

    DNA ligase 4, EC 6.5.1.1, DNA ligase IV, Polydeoxyribonucleotide synthase [ATP] 4.

    Product # :

    ENZ-286

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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

    • Synonyms

      DNA ligase 4, EC 6.5.1.1, DNA ligase IV, Polydeoxyribonucleotide synthase [ATP] 4.

    • Physical Appearance

      400U/ul solution.

    • 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.

    • 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

    • Reaction Conditions

      50mM Tris-HCl, pH7.5 at 25°C, 10mM MgCl2, 10mM DTT and 1mM ATP. Incubate at 16 °C

    • 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.

    • 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.

    T4 Dna Ligase
  • View Data Sheet

    Name :

    HSCB Human

    Description:

    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-1142

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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

    • 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.

    • 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.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Hscb Human
  • View Data Sheet

    Name :

    B3GNT2 Human

    Description:

    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-973

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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

    • 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.

    • 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.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      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.

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    B3Gnt2 Human
  • View Data Sheet

    Name :

    CCDC90B Human

    Description:

    Coiled-Coil Domain Containing 90B Human Recombinant

    MDS011, MDS025, CUA003, Coiled-coil domain-containing protein 90B mitochondrial, CCDC90B.

    Product # :

    PRO-1478

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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

    • 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.

    • Synonyms

      MDS011, MDS025, CUA003, Coiled-coil domain-containing protein 90B mitochondrial, CCDC90B.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Ccdc90B Human
  • View Data Sheet

    Name :

    CKMB1 Human

    Description:

    Creatine Kinase MB Isoenzyme Type-1 Human Recombinant

    Creatine Kinase MB 1, CKMB1

    Product # :

    CKI-269

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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˚C

    Citations

    More Info

    • 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.

    • Synonyms

      Creatine Kinase MB Isoenzyme Type-1, CK MB1

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • 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.

    • 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.

    • 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 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

    • 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.

    Ckmbi Human
  • View Data Sheet

    Name :

    T7 RNAP

    Description:

    T7 RNA Polymerase Recombinant

    T7 RNAP.

    Product # :

    ENZ-1180

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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

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    • 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.

    • Synonyms

      T7 RNAP.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Two years when stored at -20°C, 2 weeks at 4°C. DO NOT STORE AT -70C.

    • Applications

      Synthesis of :

      • ssRNAs.
      • Labeled or unlabeled highly specific RNA probes.
      • Capped mRNA using cap analogues.
    • 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.

    T7 Rnap
  • View Data Sheet

    Name :

    AHCY Mouse

    Description:

    Adenosylhomocysteinase Mouse Recombinant

    EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, Adenosylhomocysteinase.

    Product # :

    ENZ-1054

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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

    • 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.

    • Synonyms

      EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, Adenosylhomocysteinase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage, it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Ahcy Mouse
  • View Data Sheet

    Name :

    HAO1 Mouse

    Description:

    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-1104

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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

    • 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.

    • 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.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Hao1 Mouse
  • View Data Sheet

    Name :

    GLRX5 Human

    Description:

    Glutaredoxin 5 Human Recombinant

    Glutaredoxin-related protein 5 mitochondrial, Monothiol glutaredoxin-5, GLRX5, C14orf87, glutaredoxin 5, GRX5, FLB4739, PR01238, PRO1238, MGC14129.

    Product # :

    ENZ-480

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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

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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).

    • Synonyms

      Glutaredoxin-related protein 5 mitochondrial, Monothiol glutaredoxin-5, GLRX5, C14orf87, glutaredoxin 5, GRX5, FLB4739, PR01238, PRO1238, MGC14129.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Glrx5 Human
  • View Data Sheet

    Name :

    BCOADC-E2 Human

    Description:

    2-Oxo-Acid Dehydrogenase Complex E2 Human Recombinant

    Product # :

    ENZ-084

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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

    • 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.

    • 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.

    • coating concentration

      0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • 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.

    Bcoadc E2 Human
  • View Data Sheet

    Name :

    FBP1 Human, Active

    Description:

    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-1145

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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

    • 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.

    • Synonyms

      Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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

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    Fbp1 Enzyme
  • View Data Sheet

    Name :

    KMT5A Human

    Description:

    Lysine Methyltransferase 5A Human Recombinant

    KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.

    Product # :

    ENZ-1080

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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

    • 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.

    • Synonyms

      KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      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.

    Kmt5A Human
  • View Data Sheet

    Name :

    SRR Human

    Description:

    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-232

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    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    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

    • 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.

    • Synonyms

      Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    Srr Human
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