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Search results

1000 results found for “nuclease”

Name

Description

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  • View Data Sheet

    Name :

    PNP Human

    Description:

    Purine Nucleoside Phosphorylase Human Recombinant

    Purine nucleoside phosphorylase, Inosine phosphorylase, NP, PUNP, PRO1837, FLJ94043, FLJ97288, FLJ97312, MGC117396, MGC125915, MGC125916, PNP.

    Product # :

    ENZ-025

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    Description

    PNP 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 309 amino acids (1-289 a.a.) and having a molecular mass of 34.2kDa. The PNP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PNP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PNP is a member of the PNP/MTAP phosphorylase family of proteins. PNP catalyzes the reversible phosphorolysis of ribonucleosides and 2’-deoxyribonucleosides with specificity for guanine, hypoxanthine and their analogs. PNP deficiency is a rare autosomal recessive genetic disease linked to a severe defect in T-lymphocyte function and neurologic disorder in children, comprising four percent of combined immunodeficiency cases.

    • Synonyms

      Purine nucleoside phosphorylase, Inosine phosphorylase, NP, PUNP, PRO1837, FLJ94043, FLJ97288, FLJ97312, MGC117396, MGC125915, MGC125916, PNP.

    • 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 MENGYTYEDY KNTAEWLLSH TKHRPQVAII CGSGLGGLTD KLTQAQIFDY GEIPNFPRST VPGHAGRLVF GFLNGRACVM MQGRFHMYEG YPLWKVTFPV RVFHLLGVDT LVVTNAAGGL NPKFEVGDIM LIRDHINLPG FSGQNPLRGP NDERFGDRFP AMSDAYDRTM RQRALSTWKQ MGEQRELQEG TYVMVAGPSF ETVAECRVLQ KLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVIMDYE SLEKANHEEV LAAGKQAAQK LEQFVSILMA SIPLPDKAS.

    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.

    Pnp Human
  • View Data Sheet

    Name :

    ALPL Mouse

    Description:

    Alkaline Phosphatase Liver/Bone/Kidney Mouse Recombinant

    Alpl, Akp-2, Akp2, ALP, APTNAP, TNAP, TNSALP, HOPS, AP-TNAP, Alkaline phosphatase 2.

    Product # :

    ENZ-1008

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    Description

    ALPL produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 493 amino acids (19-503 a.a.) and having a molecular mass of 54.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). ALPL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ALPL protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 46,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of 4-Methylumbelliferyl phosphate to phosphate and 4-Methylumbelliferone per minute at pH 8.8 at 25C.

    Citations

    More Info

    • Introduction

      Alkaline Phosphatase Liver/Bone/Kidney (Alpl) is a part of the alkaline phosphatases family which comprises 4 related alkaline phosphatases. Alpl is a membrane-bound glycosylated enzyme which is not expressed in any particular tissue. Alpl takes part in skeletal mineralization.

    • Synonyms

      Alpl, Akp-2, Akp2, ALP, APTNAP, TNAP, TNSALP, HOPS, AP-TNAP, Alkaline phosphatase 2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      VPEKERDPSY WRQQAQETLK NALKLQKLNT NVAKNVIMFL GDGMGVSTVT AARILKGQLH HNTGEETRLE MDKFPFVALS KTYNTNAQVP DSAGTATAYL CGVKANEGTV GVSAATERTR CNTTQGNEVT SILRWAKDAG KSVGIVTTTR VNHATPSAAY AHSADRDWYS DNEMPPEALS QGCKDIAYQL MHNIKDIDVI MGGGRKYMYP KNRTDVEYEL DEKARGTRLD GLDLISIWKS FKPRHKHSHY VWNRTELLAL DPSRVDYLLG LFEPGDMQYE LNRNNLTDPS LSEMVEVALR ILTKNLKGFF LLVEGGRIDH GHHEGKAKQA LHEAVEMDQA IGKAGAMTSQ KDTLTVVTAD HSHVFTFGGY TPRGNSIFGL APMVSDTDKK PFTAILYGNG PGYKVVDGER ENVSMVDYAH NNYQAQSAVP LRHETHGGED VAVFAKGPMA HLLHGVHEQN YIPHVMAYAS CIGANLDHCA WAGSGLEHHH HHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Alpl Mouse
  • View Data Sheet

    Name :

    ALPP Human, Active

    Description:

    Alkaline Phosphatase Placental Human Recombinant, BioActive

    3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.

    Product # :

    ENZ-1133

    Price :

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    • Citations

    Description

    ALPP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 494 amino acids (23-506 a.a.) and having a molecular mass of 53.9kDa. ALPP is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ALPP protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      Placental alkaline phosphatase also known as PLAP is a membranal siaglycoprotein enzyme typicallyfoundin high concentration in syncytiotrophoblasts in the placenta amid the 3th trimester of gestation. The expression of PLAP was at firstconsidered to be onlyin the term placenta, though, a human PLAP-like variant has been found,thathas more than 85% homology with PLAP itself. PLAP is expressed strictly in normal term placenta, endocervix & fallopian tube and in ovarian and proximal gastrointestinal tumors. It is also widely expressed in germ cell tumors and more recently found in seminomas.

    • Synonyms

      3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.

    • 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

      ADLMIIPVEE ENPDFWNREA AEALGAAKKL QPAQTAAKNL IIFLGDGMGV STVTAARILK GQKKDKLGPE LPLAMDRFPY VALSKTYNVD KHVPDSGATA TAYLCGVKGN FQTIGLSAAA RFNQCNTTRG NEVISVMNRA KKAGKSVGVV TTTRVQHASP AGTYAHTVNR NWYSDADVPA SARQEGCQDI ATQLISNMDI DVILGGGRKY MFRMGTPDPE YPDDYSQGGT RLDGKNLVQE WLAKRQGARY VWNRTELMQA SLDPSVTHLM GLFEPGDMKY EIHRDSTLDP SLMEMTEAAL RLLSRNPRGF FLFVEGGRID HGHHESRAYR ALTETIMFDD AIERAGQLTS EEDTLSLVTA DHSHVFSFGG YPLRGSSIFG LAPGKARDRK AYTVLLYGNG PGYVLKDGAR PDVTESESGS PEYRQQSAVP LDEETHAGED VAVFARGPQA HLVHGVQEQT FIAHVMAFAA CLEPYTACDL APPAGTTDHH HHHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Alpp Human
  • View Data Sheet

    Name :

    UCHL3 Mouse

    Description:

    Ubiquitin Carboxyl-Terminal Esterase L3 Mouse Recombinant

    Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.

    Product # :

    ENZ-978

    Price :

    Quantity :

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    • Citations

    Description

    UCHL3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 238 amino acids (1-230) and having a molecular mass of 27.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).UCHL3 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    UCHL3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 9,000 pmol/min/mg, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of ubiquitin-AMC per minute at pH 7.5, at 37°C.

    Citations

    More Info

    • 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 hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.

    • 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

      MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMEPE LLSMVPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERAKFLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGKTSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA 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.

    Uchl3 Mouse
  • View Data Sheet

    Name :

    GUSB Human

    Description:

    Glucuronidase Beta Human Recombinant

    GUSB, BG, MPS7, Glucuronidase Beta, EC 3.2.1.31, Beta-G1, Beta-D-Glucuronidase, Glucuronidase, Beta, Beta-Glucuronidasem.

    Product # :

    ENZ-1018

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    Description

    GUSB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 635 amino acids (23-651a.a) and having a molecular mass of 73.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GUSB is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GUSB protein solution (0.25mg/ml) 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 > 1600 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-Methylumbelliferone to 4- Methylum-belliferyl-β-D-glucosiduronic acid per minute at 37C and pH6.0.

    Citations

    More Info

    • Introduction

      Glucuronidase Beta (GUSB) is a lysosomal hydrolase which is taking part in the stepwise degradation of glucuronic acid-containing glycosaminoglycans and plays a significant role in the degradation of dermatan and keratin sulfates. GUSB is comprised of heparin sulfate, chondroitin sulfate and hyaluronan.

    • Synonyms

      GUSB, BG, MPS7, Glucuronidase Beta, EC 3.2.1.31, Beta-G1, Beta-D-Glucuronidase, Glucuronidase, Beta, Beta-Glucuronidasem.

    • 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

      LQGGMLYPQE SPSRECKELD GLWSFRADFS DNRRRGFEEQ WYRRPLWESG PTVDMPVPSS FNDISQDWRL RHFVGWVWYE REVILPERWT QDLRTRVVLR IGSAHSYAIV WVNGVDTLEH EGGYLPFEAD ISNLVQVGPL PSRLRITIAI NNTLTPTTLP PGTIQYLTDT SKYPKGYFVQ NTYFDFFNYA GLQRSVLLYT TPTTYIDDIT VTTSVEQDSG LVNYQISVKG SNLFKLEVRL LDAENKVVAN GTGTQGQLKV PGVSLWWPYL MHERPAYLYS LEVQLTAQTS LGPVSDFYTL PVGIRTVAVT KSQFLINGKP FYFHGVNKHE DADIRGKGFD WPLLVKDFNL LRWLGANAFR TSHYPYAEEV MQMCDRYGIV VIDECPGVGL ALPQFFNNVS LHHHMQVMEE VVRRDKNHPA VVMWSVANEP ASHLESAGYY LKMVIAHTKS LDPSRPVTFV SNSNYAADKG APYVDVICLN SYYSWYHDYG HLELIQLQLA TQFENWYKKY QKPIIQSEYG AETIAGFHQD PPLMFTEEYQ KSLLEQYHLG LDQKRRKYVV GELIWNFADF MTEQSPTRVL GNKKGIFTRQ RQPKSAAFLL RERYWKIANE TRYPHSVAKS QCLENSLFTH 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.

    Gusb Human
  • View Data Sheet

    Name :

    ACE2 Rat

    Description:

    Angiotensin Converting Enzyme 2 Rat Recombinant

    ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.

    Product # :

    ENZ-1124

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    Description

    ACE2 Rat produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 731 amino acids (18-740 aa) and having a molecular mass of 84.7kDa. ACE2 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The ACE2 solution contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of McaYVADAPK(Dnp)-OH per minute at pH 7.5, at 25C.

    Citations

    More Info

    • Introduction

      Angiotensin converting enzyme 2 or ACE-2 is an enzyme that is located in the cell membranes in different organs such as kidney, intestines, lungs, heart & arteries. ACE2 acts as an entry receptor of SARS coronaviruses & SARS-CoV-2.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen bound to the external envelope of the virion that has a role in a crucial part in viral infection by identifying host cell receptors and starting fusion of the viral and cellular membranes. Couple of main domains in coronavirus S1 have been identified, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains acts as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 has a signal peptide, a transmembrane domain & a single metalloproteinase active site holds an HEXXH zinc-binding domain. ACE-2 takes part as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

    • Synonyms

      ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.

    • 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

      QSLIEEKAES FLNKFNQEAE DLSYQSSLAS WNYNTNITEE NAQKMNEAAA KWSAFYEEQS KIAQNFSLQE IQNATIKRQL KALQQSGSSA LSPDKNKQLN TILNTMSTIY STGKVCNSMN PQECFLLEPG LDEIMATSTD YNRRLWAWEG WRAEVGKQLR PLYEEYVVLK NEMARANNYE DYGDYWRGDY EAEGVEGYNY NRNQLIEDVE NTFKEIKPLY EQLHAYVRTK LMEVYPSYIS PTGCLPAHLL GDMWGRFWTN LYPLTTPFLQ KPNIDVTDAM VNQSWDAERI FKEAEKFFVS VGLPQMTPGF WTNSMLTEPG DDRKVVCHPT AWDLGHGDFR IKMCTKVTMD NFLTAHHEMG HIQYDMAYAK QPFLLRNGAN EGFHEAVGEI MSLSAATPKH LKSIGLLPSN FQEDNETEIN FLLKQALTIV GTLPFTYMLE KWRWMVFQDK IPREQWTKKW WEMKREIVGV VEPLPHDETY CDPASLFHVS NDYSFIRYYT RTIYQFQFQE ALCQAAKHDG PLHKCDISNS TEAGQKLLNM LSLGNSGPWT LALENVVGSR NMDVKPLLNY FQPLFVWLKE QNRNSTVGWS TDWSPYADQS IKVRISLKSA LGKNAYEWTD NEMYLFRSSV AYAMREYFSR EKNQTVPFGE ADVWVSDLKP RVSFNFFVTS PKNVSDIIPR SEVEEAIRMS RGRINDIFGL NDNSLEFLGI YPTLKPPYEP PVTLEHHHHH H.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ace2 Rat
  • View Data Sheet

    Name :

    POLR2J2 Human

    Description:

    Polymerase II Polypeptide J2 Human Recombinant

    HRPB11B, RPB11b1, POLR2J2, DNA-directed RNA polymerase II subunit RPB11-b1.

    Product # :

    ENZ-689

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    Description

    POLR2J2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115) and having a molecular mass of 15.5kDa. POLR2J2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The POLR2J2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT and 250mM Imidazole.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      POLR2J2 belongs to the RNA polymerase II subunit 11 gene family, that includes 3 genes in a cluster on chromosome 7q22.1 and a pseudogene on chromosome 7p13. DNA directed RNA polymerase II polypeptide J family encodes a subunit of RNA polymerase II, the polymerase which is responsible for synthesizing messenger RNA in eukaryotes. This locus produces multiple, otherwise spliced transcripts which express isoforms with distinct C-termini compared to DNA directed RNA polymerase II polypeptide J. Most or all variants are spliced to include additional non-coding exons at the 3' end that makes them candidates for nonsense-mediated decay (NMD). Therefore, it is unknown if this locus expresses a protein or proteins in vivo.

    • Synonyms

      HRPB11B, RPB11b1, POLR2J2, DNA-directed RNA polymerase II subunit RPB11-b1.

    • 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 MGSMNAPPAF ESFLLFEGEK ITINKDTKVP KACLFTINKE DHTLGNIIKS QLLKDPQVLF AGYKVPHPLE HKIIIRVQTT PDYSPQEAFT NAITDLISEL SLLEERFRTC LLPLRLLP.

    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.

    Polr2J2 Human
  • View Data Sheet

    Name :

    UBA5 Human

    Description:

    Ubiquitin-Like Modifier Activating Enzyme 5 Human Recombinant

    Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.

    Product # :

    ENZ-602

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    Description

    UBA5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-404) and having a molecular mass of 47.4kDa.UBA5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBA5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ubiquitin-like modifier activating enzyme 5 (UBA5) is a member of the ubiquitin-activating E1 family and UBA5 subfamily. Ubiquitin and ubiquitin-like proteins are recognized as covalently conjugated to various cellular substrates by a three-step enzymatic pathway. The ubiquitin-activating enzyme (E1) has a vital role in the first step of ubiquitination pathway to activate ubiquitin or ubiquitin-like proteins. UBA5 activates an ubiquitin-like protein, ubiquitin-fold modifier 1 (Ufm1), by forming a high-energy thioester bond. UBA5 is located primarily in cytoplasm, while it generally localizes to the nucleus in presence of SUMO2.

    • Synonyms

      Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.

    • 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 MGSHMAESVE RLQQRVQELE RELAQERSLQ VPRSGDGGGG RVRIEKMSSE VVDSNPYSRL MALKRMGIVS DYEKIRTFAV AIVGVGGVGS VTAEMLTRCG IGKLLLFDYD KVELANMNRL FFQPHQAGLS KVQAAEHTLR NINPDVLFEV HNYNITTVEN
      FQHFMDRISN GGLEEGKPVD LVLSCVDNFE ARMTINTACN ELGQTWMESG VSENAVSGHI QLIIPGESAC FACAPPLVVA ANIDEKTLKR EGVCAASLPT TMGVVAGILV QNVLKFLLNF GTVSFYLGYN AMQDFFPTMS MKPNPQCDDR NCRKQQEEYK KKVAALPKQE VIQEEEEIIH
      EDNEWGIELV SEVSEEELKN FSGPVPDLPE GITVAYTIPK KQEDSVTELT VEDSGESLED LMAKMKNM.

    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.

    Uba5 Human
  • View Data Sheet

    Name :

    PRSS22 Mouse

    Description:

    Protease Serine 22 Mouse Recombinant

    Brain-specific serine protease 4, Prss22, 4733401N09Rik, BSSP-4, SP001LA, Serine protease 22, Serine protease 26, Tryptase epsilon, Bssp4, Prss26.

    Product # :

    ENZ-964

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    Description

    PRSS22 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 283 amino acids (33-307) and having a molecular mass of 31.1kDa.PRSS22 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PRSS22 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Protease Serine 22 also known as Prss22 is identified brain-specific expression gene which is expressed mainly in epitheliumrich tissues such as the lung and eye. Prss22 encodes to a serine protease which called BSSP-4 or BSP-2.

    • Synonyms

      Brain-specific serine protease 4, Prss22, 4733401N09Rik, BSSP-4, SP001LA, Serine protease 22, Serine protease 26, Tryptase epsilon, Bssp4, Prss26.

    • 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

      ATIRVSPDCG KPQQLNRIVG GEDSMDAQWP WIVSILKNGS HHCAGSLLTN RWVVTAAHCF KSNMDKPSLF SVLLGAWKLG SPGPRSQKVG IAWVLPHPRY SWKEGTHADI ALVRLEHSIQ FSERILPICL PDSSVRLPPK TDCWIAGWGS IQDGVPLPHP QTLQKLKVPI IDSELCKSLY WRGAGQEAIT EGMLCAGYLE GERDACLGDS GGPLMCQVDD HWLLTGIISW GEGCAERNRP GVYTSLLAHR SWVQRIVQGV QLRGYLADSG DTGSSLEHHH HHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Prss22 Mouse
  • View Data Sheet

    Name :

    Aminopeptidase

    Description:

    Aminopeptidase Aeromonas Recombinant

    Bacterial leucyl aminopeptidase, EC 3.4.11.10.

    Product # :

    ENZ-275

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    Description

    The 29 kDa Aeromonas Aminopeptidase is produced by genetic engineering and can be used for physical & structural investigations, sequence and amino-terminal determinations. This exopeptidase recognizes a specific stop sign at –X- Pro and requires a free a-amino group in the L-configuration. It is therefore suitable for the removal of the redundant N-terminal methionine often added to engineered recombinant proteins.

    Source

    Aeromonas Proteolytica.

    Formulation

    Buffered solution containing 10mM Tris-HCl, 100mM NaCl and 5µM ZnSO4, pH 8.0.

    Purity

    Greater than 95.0% as determined by SEC-HPLC.

    Biological Activity

    Recombinant Aeromonas Aminopeptidase was found to have an activity of 108 Units/mg protein.

    Citations

    More Info

    • Synonyms

      Bacterial leucyl aminopeptidase, EC 3.4.11.10.

    • Physical Appearance

      Sterile filtered liquid formulation.

    • Stability

      Two years when stored at -20°C, 2 weeks at 4°C.

    • Unit Definition

      One unit of aminopeptidase activity is defined as the amount of enzyme that releases 1 μmole p-nitroaniline at 25°C in 1 minute.

    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.

    Aminopeptidase
  • View Data Sheet

    Name :

    ARSG Human

    Description:

    Arylsulfatase G Human Recombinant

    Arylsulfatase G, ASG, ARSG, KIAA1001, UNQ839/PRO1777.

    Product # :

    ENZ-677

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    Description

    ARSG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 532 amino acids (17-525) and having a molecular mass of 57kDa.ARSG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARSG solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Arylsulfatase G (ARSG) is a member of the sulfatase enzyme family. Sulfatases are enzymes which hydrolyze sulfate esters from sulfated steroids, carbohydrates, proteoglycans, and glycolipids. Sulfatases are involved in hormone biosynthesis, modulation of cell signaling, and degradation of macromolecules. The ARSG protein exhibits arylsulfatase activity at acidic pH, as is characteristic of lysosomal sulfatases. The Arylsulfatase G enzyme localizes in the lysosomes. ARSG is inhibited by phosphate, which forms a covalent bond with the active site 3-oxoalanine. Arylsulfatase G is widely expressed, having very low expression in the brain, lung, heart and skeletal muscle.

    • Synonyms

      Arylsulfatase G, ASG, ARSG, KIAA1001, UNQ839/PRO1777.

    • 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 MGSGFLYPLV DFCISGKTRG QKPNFVIILA DDMGWGDLGA NWAETKDTAN LDKMASEGMR FVDFHAAAST CSPSRASLLT GRLGLRNGVT RNFAVTSVGG LPLNETTLAE VLQQAGYVTG IIGKWHLGHH GSYHPNFRGF DYYFGIPYSH DMGCTDTPGY NHPPCPACPQ GDGPSRNLQR DCYTDVALPL YENLNIVEQP VNLSSLAQKY AEKATQFIQR ASTSGRPFLL YVALAHMHVP LPVTQLPAAP RGRSLYGAGL WEMDSLVGQI KDKVDHTVKE NTFLWFTGDN GPWAQKCELA GSVGPFTGFW QTRQGGSPAK QTTWEGGHRV PALAYWPGRV PVNVTSTALL SVLDIFPTVV ALAQASLPQG RRFDGVDVSE VLFGRSQPGH RVLFHPNSGA AGEFGALQTV RLERYKAFYI TGGARACDGS TGPELQHKFP LIFNLEDDTA EAVPLERGGA EYQAVLPEVR KVLADVLQDI ANDNISSADY TQDPSVTPCC NPYQIACRCQ AA.

    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.

    Arsg Human
  • View Data Sheet

    Name :

    ASPA Human, His

    Description:

    Aspartoacylase Human Recombinant, His Tag

    Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP.

    Product # :

    ENZ-572

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    Description

    ASPA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313) and having a molecular mass of 38.1kDa.ASPA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ASPA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 1mM DTT, 0.1M NaCl and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Aspartoacylase is a homodimer which catalyzes the deacetylation of N-acetylaspartic acid (NAA) (a protein whose hydrolysis is crucial to maintenance of intact white matter) to generate acetate and L-aspartate. Aspartoacylase (ASPA) is expressed in the liver, lung and kidney tissue, as well as in the skeletal muscle and in cerebral white matter. NAA is ample in the brain where hydrolysis by aspartoacylase is believed to aid maintain white matter. In other tissues ASPA functions as a scavenger of NAA from body fluids. ASPA gene mutations cause Canavan disease (CAND or spongy degeneration of the brain).

    • Synonyms

      Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP.

    • 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 MGSMTSCHIA EEHIQKVAIF GGTHGNELTG VFLVKHWLEN GAEIQRTGLE VKPFITNPRA VKKCTRYIDC DLNRIFDLEN LGKKMSEDLP YEVRRAQEIN HLFGPKDSED SYDIIFDLHN TTSNMGCTLI LEDSRNNFLI QMFHYIKTSL APLPCYVYLI
      EHPSLKYATT RSIAKYPVGI EVGPQPQGVL RADILDQMRK MIKHALDFIH HFNEGKEFPP CAIEVYKIIE KVDYPRDENG EIAAIIHPNL QDQDWKPLHP GDPMFLTLDG KTIPLGGDCT VYPVFVNEAA YYEKKEAFAK TTKLTLNAKS IRCCLH.

    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.

    Aspa Human
  • View Data Sheet

    Name :

    NMT1 Human

    Description:

    N-Myristoyltransferase 1 Human Recombinant

    N-Myristoyltransferase 1, NMT, Myristoyl-CoA:Protein N-Myristoyltransferase 1, Type I N-Myristoyltransferase, EC 2.3.1.97, Myristoyl-CoA:Protein,N- Myristoyltransferase, Glycylpeptide N-Tetradecanoyltransferase 1,Peptide N-Myristoyltransferase 1,Alternative, Short Form NMT-S, Short Form NMT-S,Long Form, NMT-L, Alternative, Long Form, NMT-L, NMT 1.

    Product # :

    ENZ-842

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    Description

    NMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 59.2kDa.NMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMT1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Myristate, a rare 14-carbon saturated fatty acid, is co-translationally attached by an amide linkage to the N-terminal glycine residue of cellular & viral proteins with various functions. N-Myristoyltransferase 1, also known as NMT1 catalyzes the transfer of myristate from CoA to proteins. NMT1 seems to be irreversible and is essential for full expression of the biologic activities of several N-myristoylated proteins, as well as the alpha subunit of the signal-transducing guanine nucleotide-binding protein, G protein.

    • Synonyms

      N-Myristoyltransferase 1, NMT, Myristoyl-CoA:Protein N-Myristoyltransferase 1, Type I N-Myristoyltransferase, EC 2.3.1.97, Myristoyl-CoA:Protein,N- Myristoyltransferase, Glycylpeptide N-Tetradecanoyltransferase 1,Peptide N-Myristoyltransferase 1,Alternative, Short Form NMT-S, Short Form NMT-S,Long Form, NMT-L, Alternative, Long Form, NMT-L, NMT 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMADESET AVKPPAPPLP QMMEGNGNGH EHCSDCENEE DNSYNRGGLS PANDTGAKKK KKKQKKKKEK GSETDSAQDQ PVKMNSLPAE RIQEIQKAIE LFSVGQGPAK TMEEASKRSY QFWDTQPVPK LGEVVNTHGP VEPDKDNIRQ EPYTLPQGFT WDALDLGDRG VLKELYTLLN ENYVEDDDNM FRFDYSPEFL LWALRPPGWL PQWHCGVRVV SSRKLVGFIS AIPANIHIYD TEKKMVEINF LCVHKKLRSK RVAPVLIREI TRRVHLEGIF QAVYTAGVVL PKPVGTCRYW HRSLNPRKLI EVKFSHLSRN MTMQRTMKLY RLPETPKTAG LRPMETKDIP VVHQLLTRYL KQFHLTPVMS QEEVEHWFYP QENIIDTFVV ENANGEVTDF LSFYTLPSTI MNHPTHKSLK AAYSFYNVHT QTPLLDLMSD ALVLAKMKGF DVFNALDLME NKTFLEKLKF GIGDGNLQYY LYNWKCPSMG AEKVGLVLQ.

    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.

    Nmt1 Human
  • View Data Sheet

    Name :

    PIN4 Human

    Description:

    Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 4 Human Recombinant

    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.

    Product # :

    ENZ-106

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    Description

    PIN4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (1-156 a.a.) and having a molecular mass of 18.8kDa.PIN4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PIN4 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-HCl pH8.0 using chymotrypsin.

    Citations

    More Info

    • Introduction

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (PIN4) is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and is vital for cell cycle regulation. PIN4 has 2 different isoforms: PAR14 and PAR17. Furthermore, Pin4 protein binds to double-stranded DNA under physiological salt conditions.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.

    • 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 MPMAGLLKGL VRQLERFSVQ QQASKMPPKG KSGSGKAGKG GAASGSDSAD KKAQGPKGGG NAVKVRHILC EKHGKIMEAM EKLKSGMRFN EVAAQYSEDK ARQGGDLGWM TRGSMVGPFQ EAAFALPVSG MDKPVFTDPP VKTKFGYHII MVEGRK.

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    Pin4 Human
  • View Data Sheet

    Name :

    MAP E.coli

    Description:

    Methionine Aminopeptidase E.Coli Recombinant

    Methionine aminopeptidase, MAP, Peptidase M, map, b0168, JW0163.

    Product # :

    ENZ-123

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    Description

    MAP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-264 a.a.) and having a molecular mass of 31.5kDa.MAP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAP protein solution (1mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Methionine aminopeptidases and designated peptidase M proteins belong to the M24 family of proteins. MAP protein removes the amino-terminal methionine residue from nascent polypeptides. The active site of MAP contains 2 adjacent divalent metal ions connected by a water molecule or hydroxide ion.

    • Synonyms

      Methionine aminopeptidase, MAP, Peptidase M, map, b0168, JW0163.

    • 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 MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL RKDDTIPAII SHDE.

    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.

    Map Ecoli
  • View Data Sheet

    Name :

    CTSA Mouse

    Description:

    Cathepsin-A Mouse Recombinant

    Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.

    Product # :

    ENZ-945

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    Description

    CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect cells.

    Formulation

    CTSA protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.

    • Synonyms

      Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.

    • 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

      APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.

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    Ctsa Mouse
  • View Data Sheet

    Name :

    TRDMT1 Human

    Description:

    tRNA Aspartic Acid Methyltransferase 1 Human Recombinant

    tRNA (cytosine(38)-C(5))-methyltransferase, DNA (cytosine-5)-methyltransferase-like protein 2, Dnmt2, DNA methyltransferase homolog HsaIIP, DNA MTase homolog HsaIIP, M.HsaIIP, PuMet, TRDMT1, DNMT2, DMNT2, RNMT1, MHSAIIP.

    Product # :

    ENZ-599

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    Description

    TRDMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (1-391) and having a molecular mass of 47.2kDa.TRDMT1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TRDMT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      tRNA aspartic acid methyltransferase 1 (TRDMT1) is a member of the C5-methyltransferase family. TRDMT1 specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). TRDMT1 is a protein responsible for the methylation of aspartic acid transfer RNA, particularly at the cytosine-38 residue in the anticodon loop. In addition, the TRDMT1 enzyme has residual DNA-(cytosine-C5) methyltransferase activity. TRDMT1 is expressed ubiquitously; however it has a higher expression in the testis, ovary and thymus and at much lower levels in the spleen, prostate, colon, small intestine, and peripheral blood leukocytes. Though similar in sequence and structure to DNA cytosine methyltransferases, the TRDMT1 gene is distinctive and extremely conserved in its function between taxa.

    • Synonyms

      tRNA (cytosine(38)-C(5))-methyltransferase, DNA (cytosine-5)-methyltransferase-like protein 2, Dnmt2, DNA methyltransferase homolog HsaIIP, DNA MTase homolog HsaIIP, M.HsaIIP, PuMet, TRDMT1, DNMT2, DMNT2, RNMT1, MHSAIIP.

    • 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 MGSHMEPLRV LELYSGVGGM HHALRESCIP AQVVAAIDVN TVANEVYKYN FPHTQLLAKT IEGITLEEFD RLSFDMILMS PPCQPFTRIG RQGDMTDSRT NSFLYILDIL PRLQKLPKYI LLENVKGFEV SSTRDLLIQT IENCGFQYQE FLLSPTSLGI PNSRLRYFLI AKLQSEPLPF QAPGQVLMEF PKIESVHPQK YAMDVENKIQ EKNVEPNISF DGSIQCSGKD AILFKLETAE EIHRKNQQDS DLSVKMLKDF LEDDTDVNQY LLPPKSLLRY ALLLDIVQPT CRRSVCFTKG YGSYIEGTGS VLQTAEDVQV ENIYKSLTNL SQEEQITKLL ILKLRYFTPK EIANLLGFPP EFGFPEKITV KQRYRLLGNS LNVHVVAKLI KILYE.

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    Trdmt1 Human
  • View Data Sheet

    Name :

    ProMatrilysin

    Description:

    ProMatrix Metalloproteinase-7 Recombinant

    Product # :

    ENZ-272

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    Description

    Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

    Source

    Escherichia Coli.

    Formulation

    The protein contains the following additives 25mM Tris-HCl (pH 7.5),150mM NaCl, 5mM CaCl2, 0.01% Brij-35 and 0.02% NaN3.

    Purity

    Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 1400 IU/mg.

    Citations

    More Info

    • Physical Appearance

      Sterile clear liquid solution.

    • Stability

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

    • Unit Definition

      One unit is defined as the digestion of 1 µg Azocoll/min at 37°C.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Promatrilysin
  • View Data Sheet

    Name :

    TDP2 Human

    Description:

    Tyrosyl-DNA Phosphodiesterase 2 Human Recombinant

    AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein II.

    Product # :

    ENZ-698

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    Description

    TDP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362) and having a molecular mass of 43.3kDa. TDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TDP2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tyrosyl-DNA Phosphodiesterase 2 (TDP2), belongs to the CCR4/nocturin family of divalent cation-dependent phosphodiesterases.TDP2 associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. TDP2 is characterized by similar sequence and structure as APE1 endonuclease, which participates in DNA repair and the activation of transcription factors.

    • Synonyms

      AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein II.

    • 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 MGSMELGSCL EGGREAAEEE GEPEVKKRRL LCVEFASVAS CDAAVAQCFL AENDWEMERA LNSYFEPPVE ESALERRPET ISEPKTYVDL TNEETTDSTT SKISPSEDTQ QENGSMFSLI TWNIDGLDLN NLSERARGVC SYLALYSPDV IFLQEVIPPY YSYLKKRSSN YEIITGHEEG YFTAIMLKKS RVKLKSQEII PFPSTKMMRN LLCVHVNVSG NELCLMTSHL ESTRGHAAER MNQLKMVLKK MQEAPESATV IFAGDTNLRD REVTRCGGLP NNIVDVWEFL GKPKHCQYTW DTQMNSNLGI TAACKLRFDR IFFRAAAEEG HIIPRSLDLL GLEKLDCGRF PSDHWGLLCN LDIIL.

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    Tdp2 Human
  • View Data Sheet

    Name :

    Pfu-sso7d DNA Polymerase

    Description:

    Pfu-sso7d DNA Polymerase Recombinant

    DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.

    Product # :

    ENZ-1202

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    Description

    Pfu-sso7d DNA Polymerase is derived from E. coli, having a molecular mass of 100 kDa. The Pfu-sso7d DNA Polymerase possesses the following activities: 5´→3´ DNA polymerase activity and 3´→5´ exonuclease activity. It generates blunt ends in the amplification products. The Pfu-ssod7 DNA Polymerase brings together a Pyrococcus furiosus DNA polymerase with a proc+essivity-enhancing domain Ssod7.

    Source

    Escherichia Coli.

    Formulation

    20mM Tris-HCl (pH 8.0), 50% glycerol, 0.1mM EDTA, 100mM KCl, 1mM DTT, 0.1% Tween20 and 0.1% NP-40.

    Purity

    Greater than 95 % as determined by SDS-PAGE analyses

    Citations

    More Info

    • Synonyms

      DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.

    • Physical Appearance

      Sterile liquid formulation.

    • Stability

      Store Pfu-sso7d DNA Polymerase 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

      It is applicable for amplification reaction of genomic DNA, cDNA, dU-containing DNA and crude samples as templates.

    • Background

      The Pfu-sso7d DNA Polymerase preforms very well for all major PCR applications. The Pfu-sso7d DNA Polymerase generates long amplicons with accuracy and speed. The high fidelity makes the Pfu-sso7d DNA Polymerase a great choice for cloning. The error rate of Pfu-sso7d DNA Polymerase is approximately 50 fold lower than that of the Thermus aquaticus DNA polymerase. It generates blunt ends in the amplification products.

    • Unit Definition

      1U of enzyme catalyzes the incorporation of 10nmol of dNTP into polynucleotide fraction in 30 minutes at 74°C.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Pfu Sso7D Dna Polymerase
  • View Data Sheet

    Name :

    AICDA Human

    Description:

    Activation-Induced Cytidine Deaminase Human Recombinant

    Single-stranded DNA cytosine deaminase, Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.

    Product # :

    ENZ-651

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    Description

    AICDA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-198) and having a molecular mass of 26.1kDa.AICDA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AICDA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Activation-Induced Cytidine Deaminase (AICDA) belongs to the the cytidine deaminase family. AICDA is involved in somatic hypermutation, gene conversion, and class-switch recombination in B-lymphocytes. AICDA is necessary for a number of crucial steps of B-cell terminal differentiation needed for efficient antibody responses. AICDA has a role in the epigenetic regulation of gene expression by participating in DNA demethylation. AICDA is strongly expressed in the lymph nodes and tonsils.

    • Synonyms

      Single-stranded DNA cytosine deaminase, Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.

    • 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 MDSLLMNRRK FLYQFKNVRW AKGRRETYLC YVVKRRDSAT SFSLDFGYLR NKNGCHVELL FLRYISDWDL DPGRCYRVTW FTSWSPCYDC ARHVADFLRG NPNLSLRIFT ARLYFCEDRK AEPEGLRRLH RAGVQIAIMT FKDYFYCWNT FVENHERTFK
      AWEGLHENSV RLSRQLRRIL LPLYEVDDLR DAFRTLGL.

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    Aicda Human
  • View Data Sheet

    Name :

    HPSE Human

    Description:

    Heparanase-1 Human Recombinant

    Heparanase, HPA, HSE1, HPA1, HPR1, HPSE1, heparanase-1, EC 3.2.1.166, Endo-glucoronidase, HEP, Heparanase-1, Hpa1.

    Product # :

    ENZ-778

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    Description

    HPSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (36-543 a.a) and having a molecular mass of 60kDa.HPSE is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    HPSE protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HPSE also known as Heparanase-1 is an enzyme which cleaves heparan sulfate proteoglycans to allow cell movement through changing the extracellular matrix. In fact, the Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. HPSE is significant for the overall degradation of proteins in lysosomes.

    • Synonyms

      Heparanase, HPA, HSE1, HPA1, HPR1, HPSE1, heparanase-1, EC 3.2.1.166, Endo-glucoronidase, HEP, Heparanase-1, Hpa1.

    • 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 MGSQDVVDLD FFTQEPLHLV SPSFLSVTID ANLATDPRFL ILLGSPKLRT LARGLSPAYL RFGGTKTDFL IFDPKKESTF EERSYWQSQV NQDICKYGSI PPDVEEKLRL EWPYQEQLLL REHYQKKFKN STYSRSSVDV LYTFANCSGL DLIFGLNALL RTADLQWNSS NAQLLLDYCS SKGYNISWEL GNEPNSFLKK ADIFINGSQL GEDFIQLHKL LRKSTFKNAK LYGPDVGQPR RKTAKMLKSF LKAGGEVIDS VTWHHYYLNG RTATKEDFLN PDVLDIFISS VQKVFQVVES TRPGKKVWLG ETSSAYGGGA PLLSDTFAAG FMWLDKLGLS ARMGIEVVMR QVFFGAGNYH LVDENFDPLP DYWLSLLFKK LVGTKVLMAS VQGSKRRKLR VYLHCTNTDN PRYKEGDLTL YAINLHNVTK YLRLPYPFSN KQVDKYLLRP LGPHGLLSKS VQLNGLTLKM VDDQTLPPLM EKPLRPGSSL GLPAFSYSFF VIRNAKVAAC I.

    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.

    Hpse Human
  • View Data Sheet

    Name :

    OLA1 Human

    Description:

    Obg-Like ATPase 1 Human Recombinant

    Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.

    Product # :

    ENZ-637

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    • source
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    • Citations

    Description

    OLA1 Human Recombinant produced in E. coli is a single polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 47.3kDa.OLA1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OLA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Obg-like ATPase 1 (OLA1) acts as a negative regulator of the cellular antioxidant response independent of transcriptional processes. OLA1 curbs the antioxidant response via nontranscriptional mechanisms. OLA1 hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. OLA1 is clearly down-regulated by DNA damage-inducing agents. OLA1 is expressed in all tissues; however it is more abundant in the testis, liver, lung, and brain. OLA1 is overexpressed in a number of malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.

    • Synonyms

      Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.

    • 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 MGSHMPPKKG GDGIKPPPII GRFGTSLKIG IVGLPNVGKS TFFNVLTNSQ ASAENFPFCT IDPNESRVPV PDERFDFLCQ YHKPASKIPA FLNVVDIAGL VKGAHNGQGL GNAFLSHISA CDGIFHLTRA FEDDDITHVE GSVDPIRDIE IIHEELQLKD EEMIGPIIDK LEKVAVRGGD KKLKPEYDIM CKVKSWVIDQ KKPVRFYHDW NDKEIEVLNK HLFLTSKPMV YLVNLSEKDY IRKKNKWLIK IKEWVDKYDP GALVIPFSGA LELKLQELSA EERQKYLEAN MTQSALPKII KAGFAALQLE YFFTAGPDEV RAWTIRKGTK APQAAGKIHT DFEKGFIMAE VMKYEDFKEE GSENAVKAAG KYRQQGRNYI VEDGDIIFFK FNTPQQPKKK.

    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.

    Ola1 Human
  • View Data Sheet

    Name :

    FUCA2 Human

    Description:

    Fucosidase Alpha-L- 2 Plasma Human Recombinant

    Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

    Product # :

    ENZ-840

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    Description

    FUCA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (29-467 a.a) and having a molecular mass of 53.3kDa.FUCA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FUCA2 protein solution (1mg/ml) containing 20mM phosphate (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fucosidase Alpha-L- 2 Plasma (FUCA2) is a plasma alpha-L-fucosidase, which represents 10-20% of the total cellular fucosidase activity. FUCA2 protein belongs to the glycosyl hydrolase 29 family, and catalyzes the hydrolysis of the alpha-1,6-linked fucose fused to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. FUCA2 is crucial for Helicobacter pylori adhesion to human gastric cancer cells.

    • Synonyms

      Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

    • 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 MGSHSATRFD PTWESLDARQ LPAWFDQAKF GIFIHWGVFS VPSFGSEWFW WYWQKEKIPK YVEFMKDNYP PSFKYEDFGP LFTAKFFNAN QWADIFQASG AKYIVLTSKH HEGFTLWGSE YSWNWNAIDE GPKRDIVKEL EVAIRNRTDL RFGLYYSLFE WFHPLFLEDE SSSFHKRQFP VSKTLPELYE LVNNYQPEVL WSDGDGGAPD QYWNSTGFLA WLYNESPVRG TVVTNDRWGA GSICKHGGFY TCSDRYNPGH LLPHKWENCM TIDKLSWGYR REAGISDYLT IEELVKQLVE TVSCGGNLLM NIGPTLDGTI SVVFEERLRQ MGSWLKVNGE AIYETHTWRS QNDTVTPDVW YTSKPKEKLV YAIFLKWPTS GQLFLGHPKA ILGATEVKLL GHGQPLNWIS LEQNGIMVEL PQLTIHQMPC KWGWALALTN VI.

    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.

    Fuca2 Human
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