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Search results

1000 results found for “Enterokinase”

Name

Description

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  • View Data Sheet

    Name :

    GLSA1 E.Coli

    Description:

    Glutaminase 1 E.Coli Recombinant

    Glutaminase 1, ybaS.

    Product # :

    ENZ-133

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    Description

    GLSA1 E.Coli Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310a.a.) and having a molecular mass of 35.0kDa. The GLSA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GLSA1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GlsA1 is a member of the great superfamily of serine-dependent beta-lactamases and penicillin-binding proteins which exist almost in every bacteria and eukaryotes and catalyze the hydrolytic deamidation of l-glutamine to l-glutamate and free NH4+.

    • Synonyms

      Glutaminase 1, ybaS.

    • 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 MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA KQLGYNVFKG

    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.

    Glsa1 Ecoli
  • View Data Sheet

    Name :

    KLK2 Human, sf9

    Description:

    Kallikrein-2 Human Recombinant, sf9

    hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.

    Product # :

    ENZ-971

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    Description

    KLK2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 246 amino acids (25-261 aa) and having a molecular mass of 27.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).KLK2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK2 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.

    More Info

    • Introduction

      KLK2 is a part of the grandular kallikrein protein family whose Members are engaged in a diverse array of biological functions. Kallikreins are a subgroup of serine proteases which are clustered on chromosome 19. KLK2 is a highly active trypsin-like serine protease which selectively cleaves at arginine remains. KLK2 is mostly expressed in prostatic tissue and is accountable for cleaving pro-prostate-specific antigen into its enzymatically active form. KLK2 is greatly expressed in prostate tumor cells and may possibly be a prognostic maker for prostate cancer risk.

    • Synonyms

      hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.

    • 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

      ADPIVGGWEC EKHSQPWQVA VYSHGWAHCG GVLVHPQWVL TAAHCLKKNS QVWLGRHNLF EPEDTGQRVP VSHSFPHPLY NMSLLKHQSL RPDEDSSHDL MLLRLSEPAK ITDVVKVLGL PTQEPALGTT CYASGWGSIE PEEFLRPRSL QCVSLHLLSN DMCARAYSEK VTEFMLCAGL WTGGKDTCGG DSGGPLVCNG VLQGITSWGP EPCALPEKPA VYTKVVHYRK WIKDTIAANP HHHHHH

    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.

    Klk2 Human Sf9
  • View Data Sheet

    Name :

    ST6GAL1 Human, sf9

    Description:

    ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, sf9 Human Recombinant

    ST6 Beta-Galactoside Alpha-2,6-Sialyltransferase 1, ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, ST6Gal I, CMP-N-Acetylneuraminate-Beta-Galactosamide-Alpha-2,6-Sialyltransferase 1,B-Cell Antigen CD75, Alpha 2,6-ST 1, EC 2.4.99.1, ST6GalI, SIAT1, CMP-N-Acetylneuraminate Beta-Galactosamide Alpha-2,6-Sialyltransferase, Sialyltransferase 1 (Beta-Galactoside Alpha-2,6-Sialyltransferase) , ST6 N-Acetylgalactosaminide Alpha-2,6-Sialyltransferase 1, Sialyltransferase 1, ST6N.

    Product # :

    ENZ-950

    Price :

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    • More Info

    Description

    ST6GAL1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 389 amino acids (27-406 a.a.) and having a molecular mass of 44.6kDa. ST6GAL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ST6GAL1 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.

    More Info

    • Introduction

      ST6GAL1 also known as ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, is part of the glycosyltransferase family 29. ST6GAL1 is a type II membrane protein which catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. Furthermore, ST6GAL1 is normally found in the Golgi however it can be proteolytically processed to a soluble form, ST6GAL1 is also involved in the generation of the cell-surface carbohydrate determinants as well differentiation antigens HB-6, CD75, and CD76.

    • Synonyms

      ST6 Beta-Galactoside Alpha-2,6-Sialyltransferase 1, ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, ST6Gal I, CMP-N-Acetylneuraminate-Beta-Galactosamide-Alpha-2,6-Sialyltransferase 1,B-Cell Antigen CD75, Alpha 2,6-ST 1, EC 2.4.99.1, ST6GalI, SIAT1, CMP-N-Acetylneuraminate Beta-Galactosamide Alpha-2,6-Sialyltransferase, Sialyltransferase 1 (Beta-Galactoside Alpha-2,6-Sialyltransferase) , ST6 N-Acetylgalactosaminide Alpha-2,6-Sialyltransferase 1, Sialyltransferase 1, ST6N.

    • 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

      ADPKEKKKGS YYDSFKLQTK EFQVLKSLGK LAMGSDSQSV SSSSTQDPHR GRQTLGSLRG LAKAKPEASF QVWNKDSSSK NLIPRLQKIW KNYLSMNKYK VSYKGPGPGI KFSAEALRCH LRDHVNVSMV EVTDFPFNTS EWEGYLPKES IRTKAGPWGR CAVVSSAGSL KSSQLGREID DHDAVLRFNG APTANFQQDV GTKTTIRLMN SQLVTTEKRF LKDSLYNEGI LIVWDPSVYH SDIPKWYQNP DYNFFNNYKT YRKLHPNQPF YILKPQMPWE LWDILQEISP EEIQPNPPSS GMLGIIIMMT LCDQVDIYEF LPSKRKTDVC YYYQKFFDSA CTMGAYHPLL YEKNLVKHLN QGTDEDIYLL GKATLPGFRT IHCHHHHHH.

    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.

    St6Gal1 Human Sf9
  • View Data Sheet

    Name :

    GST S. Japonicum

    Description:

    Glutathione S-Transferase Schistosoma Japonicum Recombinant

    Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase.

    Product # :

    ENZ-1147

    Price :

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    • description
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    • biological activity
    • More Info

    Description

    GST S. Japonicum Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-218) and having a molecular mass of 25.4 kDa.

    Source

    Escherichia Coli.

    Formulation

    GST S. Japonicum protein solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 30unit/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

    More Info

    • Introduction

      Glutathione S-transferase, also known as GST, is an antioxidant enzyme. It is the primary defense mechanism from reactive oxygen in the cell. The enzyme GST reduces hydroperoxides of lipids via a Se-independent glutathione peroxidase actions. GST detoxifies peroxidation of lipids bi-products, for example 4-hydroxynonenal.

    • Synonyms

      Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase.

    • 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

      MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK

    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.

    Gst Japonicum
  • View Data Sheet

    Name :

    NEU1 Human

    Description:

    Sialidase 1 Human Recombinant

    Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

    Product # :

    ENZ-645

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    Description

    NEU1 Human Recombinant produced in E. coli is a single polypeptide chain containing 393 amino acids (48-415) and having a molecular mass of 42.9 kDa.NEU1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NEU1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sialidase 1 (NEU1) is a lysosomal enzyme which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, the NEU1 enzyme is part of a heterotrimeric complex in cooperation with beta-galactosidase and cathepsin A. NEU1 gene mutations may lead to sialidosis, a lysosomal storage disease that can be the type 1 (cherry red -myoclonus syndrome or normosomatic type), which is late-onset, or the type 2 (the dysmorphic type), which takes place at an earlier age with increased acuteness.

    • Synonyms

      Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

    • 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 MGSHMENDFG LVQPLVTMEQ LLWVSGRQIG SVDTFRIPLI TATPRGTLLA FAEARKMSSS DEGAKFIALR RSMDQGSTWS PTAFIVNDGD VPDGLNLGAV VSDVETGVVF LFYSLCAHKA GCQVASTMLV WSKDDGVSWS TPRNLSLDIG TEVFAPGPGS GIQKQREPRK GRLIVCGHGT LERDGVFCLL SDDHGASWRY GSGVSGIPYG QPKQENDFNP DECQPYELPD GSVVINARNQ NNYHCHCRIV LRSYDACDTL RPRDVTFDPE LVDPVVAAGA VVTSSGIVFF SNPAHPEFRV NLTLRWSFSN GTSWRKETVQ LWPGPSGYSS LATLEGSMDG EEQAPQLYVL YEKGRNHYTE SISVAKISVY GTL

    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.

    Neu1 Human
  • View Data Sheet

    Name :

    SPINK1 Human

    Description:

    Serine Peptidase Inhibitor Kazal Type 1 Human Recombinant

    Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.

    Product # :

    ENZ-724

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    Description

    SPINK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 79 amino acids (24-79) and having a molecular mass of 8.6kDa.SPINK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPINK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Trypsin inhibitor SPINK1 is secreted from pancreatic acinar cells into pancreatic fluid. SPINK1 has a role in inhibition of trypsin-catalyzed premature initiation of zymogens in the pancreas and the pancreatic duct. Alterations in SPINK1 gene are the cause for tropical calcific and pancreatitis hereditary pancreatitis.

    • Synonyms

      Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.

    • 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 MGSDSLGREA KCYNELNGCT KIYDPVCGTD GNTYPNECVL CFENRKRQTS ILIQKSGPC.

    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.

    Spink1 Human
  • View Data Sheet

    Name :

    Lysozyme Human

    Description:

    Lysozyme Human Recombinant

    EC 3.2.1.17, LYZ, Lysozyme.

    Product # :

    ENZ-1159

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    Description

    Recombinant Human Lysozyme produced in Plant is a non-glycosylated, polypeptide chain containing 130 amino acids and having a molecular mass of 14.7kDa. The Recombinant Human Lysozyme is purified by proprietary chromatographic techniques.

    Source

    Oryza sativa (rice).

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Purity as determined by SDS-PAGE is greater than 90%.

    Biological Activity

    1.6x105 U/mg.

    More Info

    • Introduction

      Lysozymeis an antimicrobial enzyme produced by animals that are part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.Lysozymes have primarily a bacteriolytic function - those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

    • Synonyms

      EC 3.2.1.17, LYZ, Lysozyme.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) off white powder.

    • Stability

      Store the lyophilized Lysozyme between 2-8°C, do not freeze. Upon reconstitution Lysozyme should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 1mg/ml in PBS.

    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.

    Lysozyme Human
  • View Data Sheet

    Name :

    HK1 Human

    Description:

    Hexokinase-1 Human Recombinant

    Hexokinase-1, EC 2.7.1.1, Hexokinase type I, HK I, Brain form hexokinase, HK1-ta, HK1-tb, HXK1, HK1.

    Product # :

    PKA-226

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    Description

    HK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain fused to a 20 amino acids His tag at the N-terminal encoding the sequence of 937 amino acids and having a molecular mass of 104.6 kDa. HXK1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >2 units/ml obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. In the coupled mode, one unit will produce 1.0 umole of NADPH per minute as glucose is phosphorylated by ATP at pH 7.4 at 25C.

    More Info

    • Introduction

      Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase1 encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of HXK1 results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein.

    • Synonyms

      Hexokinase-1, EC 2.7.1.1, Hexokinase type I, HK I, Brain form hexokinase, HK1-ta, HK1-tb, HXK1, HK1.

    • 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). Please avoid freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG LSRDFNPTAT VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVHMESE VYDTPENIVH GSGSQLFDHV AECLGDFMEK RKIKDKKLPV GFTFSFPCQQ SKIDEAILIT WTKRFKASGV EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH NAKEILTRLG VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKTH PQYSRRFHKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLAHFHLT KDMLLEVKKR MRAEMELGLR KQTHNNAVVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV LLVKIRSGKK RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF TFSFPCQQTS LDAGILITWT KGFKATDCVG HDVVTLLRDA IKRREEFDLD VVAVVNDTVG TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ GQMCINMEWG AFGDNGCLDD IRTHYDRLVD EYSLNAGKQR YEKMISGMYL GEIVRNILID FTKKGFLFRG QISETLKTRG IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA VVDKIRENRG LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG AALITAVGVR LRTEASS.

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    Hk1 Human
  • View Data Sheet

    Name :

    TNAA E.Coli

    Description:

    Tryptophanase E.Coli Recombinant

    Tryptophanase/L-cysteine desulfhydrase, PLP-dependent, Tryptophanase, TNAA, L-tryptophan indole-lyase, TNase, tnaA, ind.

    Product # :

    ENZ-852

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    Description

    TNAA Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 494 amino acids (1-471) and having a molecular mass of 55.2kDa.TNAA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TNAA solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tryptophanase, also known as tnaA, catalyzes chemical reaction using 2 substrates which are L-tryptophan and H2O. tnaA protein's three products are indole, pyruvate, and NH3.

    • Synonyms

      Tryptophanase/L-cysteine desulfhydrase, PLP-dependent, Tryptophanase, TNAA, L-tryptophan indole-lyase, TNase, tnaA, ind.

    • 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 MGSMENFKHL PEPFRIRVIE PVKRTTRAYR EEAIIKSGMN PFLLDSEDVF IDLLTDSGTG AVTQSMQAAM MRGDEAYSGS RSYYALAESV KNIFGYQYTI PTHQGRGAEQ IYIPVLIKKR EQEKGLDRSK MVAFSNYFFD TTQGHSQING CTVRNVYIKE AFDTGVRYDF KGNFDLEGLE RGIEEVGPNN VPYIVATITS NSAGGQPVSL ANLKAMYSIA KKYDIPVVMD SARFAENAYF IKQREAEYKD WTIEQITRET YKYADMLAMS AKKDAMVPMG GLLCMKDDSF FDVYTECRTL CVVQEGFPTY GGLEGGAMER LAVGLYDGMN LDWLAYRIAQ VQYLVDGLEE IGVVCQQAGG HAAFVDAGKL LPHIPADQFP AQALACELYK VAGIRAVEIG SFLLGRDPKT GKQLPCPAEL LRLTIPRATY TQTHMDFIIE AFKHVKENAA NIKGLTFTYE PKVLRHFTAK LKEV.

    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.

    Tnaa Ecoli
  • View Data Sheet

    Name :

    phrB E.Coli

    Description:

    Deoxyribodipyrimidine photo-lyase E.Coli Recombinant

    800x600 ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    ENZ-362

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    Description

    800x600 800x600 phrB E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 495 amino acids (1-472) and having a molecular mass of 56.1kDa.phrB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The phrB solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Deoxyribodipyrimidine photo-lyase (phrB) is a member of the DNA photolyase class-1 family. phrB takes part in repair of UV radiation-inducedDNA damage. phrB catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidinedimers (in cis-syn configuration), which are formed between closest bases on the same DNA strand uponexposure to ultraviolet radiation.

    • Synonyms

      ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708.

    • 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 MGSMTTHLVW FRQDLRLHDN LALAAACRNS SARVLALYIA TPRQWATHNM SPRQAELINA QLNGLQIALA EKGIPLLFRE VDDFVASVEI VKQVCAENSV THLFYNYQYE VNERARDVEV ERALRNVVCE GFDDSVILPP GAVMTGNHEM YKVFTPFKNA WLKRLREGMP ECVAAPKVRS SGSIEPSPSI TLNYPRQSFD TAHFPVEEKA AIAQLRQFCQ NGAGEYEQQR DFPAVEGTSR LSASLATGGL SPRQCLHRLL AEQPQALDGG AGSVWLNELI WREFYRHLIT YHPSLCKHRP FIAWTDRVQW QSNPAHLQAW QEGKTGYPIV DAAMRQLNST GWMHNRLRMI TASFLVKDLL IDWREGERYF MSQLIDGDLA ANNGGWQWAA STGTDAAPYF RIFNPTTQGE KFDHEGEFIR QWLPELRDVP GKVVHEPWKW AQKAGVTLDY PQPIVEHKEA RVQTLAAYEA ARKGK.

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    Phrb Ecoli
  • View Data Sheet

    Name :

    Lysostaphin

    Description:

    Lysostaphin Recombinant

    Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    Product # :

    ENZ-269

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    Description

    Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized without any additives.

    Purity

    98% as determined by RP-HPLC.

    Biological Activity

    Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C.  Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.

    More Info

    • Introduction

      Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.

    • Synonyms

      Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Lyophilized Lysostaphin although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution Lysostaphin can be stored at 4°C up to 3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.

    • Protein content

      Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.

    • Specific Activity

      Determined to be 3,540 units/mg.

    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.

    Lysostaphin
  • View Data Sheet

    Name :

    ACO1 Human

    Description:

    Aconitase-1 Human Recombinant

    Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.

    Product # :

    ENZ-056

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    Description

    ACO1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 912 amino acids (1-889a.a.) and having a molecular mass of 100.8kDa.ACO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACO1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    2mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACO1 has a part in an iron sensor. ACO1 catalyzes the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process.

    • Synonyms

      Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.

    • 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 MGSMSNPFAH LAEPLDPVQP GKKFFNLNKL EDSRYGRLPF SIRVLLEAAI RNCDEFLVKK QDIENILHWN VTQHKNIEVP FKPARVILQD FTGVPAVVDF AAMRDAVKKL GGDPEKINPV CPADLVIDHS IQVDFNRRAD SLQKNQDLEF ERNRERFEFL KWGSQAFHNM RIIPPGSGII HQVNLEYLAR VVFDQDGYYY PDSLVGTDSH TTMIDGLGIL GWGVGGIEAE AVMLGQPISM VLPQVIGYRL MGKPHPLVTS TDIVLTITKH LRQVGVVGKF VEFFGPGVAQ LSIADRATIA NMCPEYGATA AFFPVDEVSI TYLVQTGRDE EKLKYIKKYL QAVGMFRDFN DPSQDPDFTQ VVELDLKTVV PCCSGPKRPQ DKVAVSDMKK DFESCLGAKQ GFKGFQVAPE HHNDHKTFIY DNTEFTLAHG SVVIAAITSC TNTSNPSVML GAGLLAKKAV DAGLNVMPYI KTSLSPGSGV VTYYLQESGV MPYLSQLGFD VVGYGCMTCI GNSGPLPEPV VEAITQGDLV AVGVLSGNRN FEGRVHPNTR ANYLASPPLV IAYAIAGTIR IDFEKEPLGV NAKGQQVFLK DIWPTRDEIQ AVERQYVIPG MFKEVYQKIE TVNESWNALA TPSDKLFFWN SKSTYIKSPP FFENLTLDLQ PPKSIVDAYV LLNLGDSVTT DHISPAGNIA RNSPAARYLT NRGLTPREFN SYGSRRGNDA VMARGTFANI RLLNRFLNKQ APQTIHLPSG EILDVFDAAE RYQQAGLPLI VLAGKEYGAG SSRDWAAKGP FLLGIKAVLA ESYERIHRSN LVGMGVIPLE YLPGENADAL GLTGQERYTI IIPENLKPQM KVQVKLDTGK TFQAVMRFDT DVELTYFLNG GILNYMIRKM AK

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    Aco1 Human
  • View Data Sheet

    Name :

    ENO2 Human, His

    Description:

    Enolase-2 Human Recombinant, His Tag

    Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    Product # :

    ENZ-298

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    Description

    Neuron Specific Enolase Human Recombinant is expressed in E. coli containing 433 amino acids 2-434 fused to an amino terminal hexahistidine tag.The NSE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Enolase 2 is supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    More Info

    • Introduction

      NSE is the ?? isoform of the glycolytic enzyme enolase and is expressed primarily in neurons, in normal and neoplastic neuroendocrine cells. NSE is a highly soluble cytoplasmic protein that is readily secreted into the CSF and serum following tissue damage. NSE shows neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons and binds in a calcium-dependent manner to cultured neocortical neurons promoting cell survival.

    • Synonyms

      Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles.

    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.

    Eno2 Human His
  • View Data Sheet

    Name :

    ENO1 Human

    Description:

    Enolase-1 Human Recombinant

    NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    Product # :

    ENZ-452

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    Description

    The ENO1 Human Recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 47.1kDa and containing 434 amino acids (1-434 a.a.).

    Source

    Escherichia Coli.

    Formulation

    The ENO1 protein solution (1mg/ml) is formulated in 20mM Tris-HCl pH-7.5 1mM MgSO4 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20,000pmol/min/ug, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.

    More Info

    • Introduction

      ENO1 is a homodimeric soluble protein that encodes a smaller monomeric structural lens protein, tau-crystallin. ENO1 is a glycolytic enzyme expressed in mainly all tissues. ENO1 isoenzyme full length protein is found in the cytoplasm. The shorter protein is formed from another translation start that is restricted to the nucleus, and binds to a component in the c-myc promoter. ENO1 is involved in anaerobic metabolism under hypoxic conditions and plays a role as a cell surface plasminogen receptor during tissue invasion. Irregular expression of Enolase-1 is linked with tumor progression in several cases of breast and lung cancer. Enolase-1 is as an auto antigen associated with Hashimoto's encephalopathy and severe asthma. ENO1 is the target protein of serum anti-endothelial antibody in Behcet's disease.

    • Synonyms

      NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    • 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

      MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK AKFAGRNFRN PLAK.

    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.

    Eno1 Human
  • View Data Sheet

    Name :

    GKN1 Human

    Description:

    Gastrokine 1 Human Recombinant

    BRICHOS domain containing 1, 18 kDa antrum mucosa protein, gastrokine 1, Protein CA11, AMP-18, BRICD1, foveolin, FOV.

    Product # :

    PRO-1206

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    Description

    GKN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 223 amino acids (1-199) and having a molecular mass of 24.5 kDa.GKN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GKN1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gastrokine-1 (GKN1) is a member of the gastrokine family. GKN1 has mitogenic activity and is involved in preserving the integrity of the gastric mucosal epithelium. GKN1 is down-regulated in human gastric cancer tissue in comparison to normal gastric mucosa. GKN1 is expressed in the stomach; however no expression is detected in cancer tissue or gastric cancer cell lines.

    • Synonyms

      BRICHOS domain containing 1, 18 kDa antrum mucosa protein, gastrokine 1, Protein CA11, AMP-18, BRICD1, foveolin, FOV.

    • 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 MGSH MLAYSS VHCFREDKMK FTIVFAGLLG VFLAPALANY NINVNDDNNN AGSGQQSVSV NNEHNVANVD NNNGWDSWNS IWDYGNGFAA TRLFQKKTCI VHKMNKEVMP SIQSLDALVK EKKLQGKGPG GPPPKGLMYS VNPNKVDDLS KFGKNIANMC RGIPTYMAEE MQEASLFFYS GTCYTTSVLW IVDISFCGDT VEN.

    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.

    Gkn1 Human
  • View Data Sheet

    Name :

    GLU-C S.aureus

    Description:

    Glutamyl endopeptidase Staphylococcal Recombinant

    Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.

    Product # :

    ENZ-955

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    Description

    Recombinant Staphylococcal GLU-C produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 267 amino acids and having a molecular mass of 28.9kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamyl endopeptidase (GLU-C) is an enzyme which cleaves peptide bonds on the carboxyl-terminal side of glutamic acid and, less frequently, aspartic acid (for example: Glu-|-Xaa, Asp-|-Xaa). GLU-C is a pathogenic factor involved in the adherence and colonization of human tissue. GLU-C preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. GLU-C is required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. GLU-C is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. Furthermore, GLU-C protects bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. GLU-C may also be involved in the stability of secreted lipases.

    • Synonyms

      Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Lyophilized GLU-C although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLU-C should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized GLU-C in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLPNNDRHQI TDTTNGHYAP VTYIQVEAPT GTFIASGVVV GKDTLLTNKH VVDATHGDPH ALKAFPSAIN QDNYPNGGFT AEQITKYSGE GDLAIVKFSP NEQNKHIGEV VKPATMSNNA ETQVNQNITV TGYPGDKPVA TMWESKGKIT YLKGEAMQYD LSTTGGNSGS PVFNEKNEVI GIHWGGVPNE FNGAVFINEN VRNFLKQNIE DIHFANDDQP NNPDNPDNPN NPDNPNNPDE PNNPDNPNNP DNPDNGDNNN SDNPDAA.

    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.

    Glu C Saureus
  • View Data Sheet

    Name :

    UMOD Porcine

    Description:

    Uromodulin Porcine

    Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    Product # :

    ENZ-733

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    Description

    Porcine Uromodulin is a 97kDa glycoprotein which is produced in the thick ascending limb of Henle´s loop and early distal convoluted tubules of the nephron.

    Source

    Porcine Urine.

    Formulation

    The UMOD protein was lyophilized from 0.4µm filtered solution at a concentration of 0.5mg/ml containing deionized water.

    More Info

    • Introduction

      Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

    • Synonyms

      Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add 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 in the cell culture.

    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.

    Umod Porcine
  • View Data Sheet

    Name :

    MMP-2 Human, HEK

    Description:

    Matrix Metalloproteinase-2 Human Recombinant, HEK

    72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    Product # :

    ENZ-100

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    • sds-page

    Description

    MMP-2 Human Recombinant produced in HEK293 cells is a proform of the Human MMP-2 (Ala30-Cys660) and fused with a ployhistide tag at the C-terminus, having an Mw of 71kDa. MMP-2 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The MMP-2 is supplied as a 0.2µm filtered solution in 20mM Tris-HCl, 150mM NaCl and 0.05% Brij 35, pH 7.4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The activity was measured by its ability to cleave fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (RND,Catalog # ES001)., The specific activity is > 1,000 pmoles/min/µg.
    Recombinant Human MMP-2 protein pro form needs to be activated with p-aminophenylmercuric acetate (APMA).
    Activation Protocol:
    1. Dilute MMP2 to 100µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
    2. Activate MMP2 by adding APMA to a final concentration of 1mM. (Sigma, Catalog # A9563) and 100mM stock in DMSO.
    3. Incubate at 37°C for 1 hour.

    sds-page

    mmp-2 human hek sds-page - Product image 1

    More Info

    • Introduction

      Matrix metalloproteinase-2 (MMP-2) is a type IV collagenase, which is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).

    • Synonyms

      72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    • Physical Appearance

      The MMP-2 is supplied as a sterile Filtered colorless solution.

    • Stability

      Store MMP-2 at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time.Avoid multiple freeze-thaw cycles.

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

    Mmp 2 Human
  • View Data Sheet

    Name :

    Alkaline Phosphatase Bovine

    Description:

    Alkaline Phosphatase Bovine Intestinal

    EC 3.1.3.1, IAP, AP, ALPI, Intestinal-type alkaline phosphatase, Intestinal alkaline phosphatase.

    Product # :

    ENZ-322

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    Description

    The Alkaline Phosphatase is purified by affinity chromatography, which results in an enzyme of high specific activity and purity. Alkaline Phosphatase is Dimeric protein having a molecular weight of 140 kDa, one Zn++ ion is tightly bound to each subunit, and another less tightly bound is involved in the catalytic reaction. Mg++ stimulates the catalysis. The binding site for Mg++ is different to that of Zn++, but will be occupied by excess Zn++ followed by loss of enzyme activity.

    Source

    Calf Intestine.

    Formulation

    50% glycerol, 5mM MgCl2, 0.1mM ZnCl2 and 5mM TRIS, pH 7.0.

    Purity

    95% pure by Gel Filtration.

    Biological Activity

    >1500 U/mg (pH 9.6), 25°C and 0.025M glycin, 10% glycerol as buffer.

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    • Synonyms

      EC 3.1.3.1, IAP, AP, ALPI, Intestinal-type alkaline phosphatase, Intestinal alkaline phosphatase.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

      AP should be stored at 4°C. Please Do-Not freeze.

    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.

    Alkaline Phosphatase
  • View Data Sheet

    Name :

    CA1 E.Coli

    Description:

    Carbonic Anhydrase-1 E.Coli Recombinant

    Carbonate dehydratase, CAN, ECK0125, JW0122, yadF, CA 1, CA I, CA1, CAI, Car 1, Car1, Carbonate dehydratase I, Carbonic anhydrase 1, Carbonic anhydrase B.

    Product # :

    ENZ-1138

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    Description

    CA1 E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-220) and having a molecular mass of 27.0 kDa. CA1 E.Coli is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CA1 E.Coli protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CA, also known as carbonic anhydrase is an enzyme that functions around the involvement of CO2 + H2O to HCO3- + H+ (conversion of CO2 to bicarbonate & protons). This enzyme holds a Zn ion as part of its active site. The central function of CA is to preserve the acid-base homeostasis within the blood and various organs. carbonic anhydrase assists Carbonic Anhydrase I to move CO2 to and from tissues.

    • Synonyms

      Carbonate dehydratase, CAN, ECK0125, JW0122, yadF, CA 1, CA I, CA1, CAI, Car 1, Car1, Carbonate dehydratase I, Carbonic anhydrase 1, Carbonic anhydrase B.

    • 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 MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL LHIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK.

    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.

    Ca1 Protein
  • View Data Sheet

    Name :

    ENO2 Human

    Description:

    Enolase-2 Human Recombinant

    Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    Product # :

    ENZ-324

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    • sds-page

    Description

    ENO2 Human Recombinant expressed in E. coli contains 434 amino acids and its Mw is 47 kDa. The Enolase-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ENO2 is supplied in 20mM Tris pH-7.5, 0.1M KCl, 5mM MgSO4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    > 25,000 pmol/min/ug, determined by the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37C.

    sds-page

    ENO2 Human sds-page - Product image 1

    More Info

    • Introduction

      Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.

    • Synonyms

      Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE ARFAGHNFRN PSVL.

    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.

    Eno2 Human Recombinant
  • View Data Sheet

    Name :

    KLK11 Human

    Description:

    Kallikrein-11 Human Recombinant

    Kallikrein-11, hK11, Hippostasin, Serine protease 20, Trypsin-like protease, Kallikrein-11 inactive chain 1, Kallikrein-11 inactive chain 2, KLK11, PRSS20, TLSP, UNQ649/PRO1279, Kallikrein 11.

    Product # :

    ENZ-816

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    Description

    KLK11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (54-278 a.a) and having a molecular mass of 24.8kDa.

    Source

    Escherichia Coli.

    Formulation

    KLK11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.

    • Synonyms

      Kallikrein-11, hK11, Hippostasin, Serine protease 20, Trypsin-like protease, Kallikrein-11 inactive chain 1, Kallikrein-11 inactive chain 2, KLK11, PRSS20, TLSP, UNQ649/PRO1279, Kallikrein 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

      MIIKGFECKP HSQPWQAALF EKTRLLCGAT LIAPRWLLTA AHCLKPRYIV HLGQHNLQKE EGCEQTRTAT ESFPHPGFNN SLPNKDHRND IMLVKMASPV SITWAVRPLT LSSRCVTAGT SCLISGWGST SSPQLRLPHT LRCANITIIE HQKCENAYPG NITDTMVCAS VQEGGKDSC GDSGGPLVCN QSLQGIISWG QDPCAITRKP GVYTKVCKYV DWIQET.

    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.

    Klk11 Human
  • View Data Sheet

    Name :

    NDK E.Coli

    Description:

    Nucleoside Diphosphate Kinase E.Coli Recombinant

    Nucleoside diphosphate kinase, NDK, NDP kinase, Nucleoside-2-P kinase, b2518, JW2502.

    Product # :

    PKA-034

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    Description

    NDK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-143 a.a.) and having a molecular mass of 18kDa.NDK is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleoside diphosphate kinase (Ndk) is an enzyme which catalyzes the exchange of phosphate groups between different nucleoside diphosphates. Ndk’s activity sustains equilibrium between the concentrations of various nucleoside triphosphates for example, when GTP is produced in the citric acid (Krebs) cycle is converted to ATP. Ndk has a key role in the synthesis of nucleoside triphosphates other than ATP.

    • Synonyms

      Nucleoside diphosphate kinase, NDK, NDP kinase, Nucleoside-2-P kinase, b2518, JW2502.

    • 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 MGSHMAIERT FSIIKPNAVA KNVIGNIFAR FEAAGFKIVG TKMLHLTVEQ ARGFYAEHDG KPFFDGLVEF MTSGPIVVSV LEGENAVQRH RDLLGATNPA NALAGTLRAD YADSLTENGT HGSDSVESAA REIAYFFGEG EVCPRTR.

    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.

    Ndk Ecoli
  • View Data Sheet

    Name :

    HERC5 Human

    Description:

    HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 Human Recombinant

    HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.

    Product # :

    ENZ-797

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    HERC5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (681-1024 a.a.) and having a molecular mass of 43kDa. HERC5 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    HERC5 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 (HERC5) is a member of the HERC family of ubiquitin ligases, found in a cluster of HERC family genes on chromosome 4. HERC5 is a protein with a HECT domain and 5 RCC1 repeats. The HERC5 protein localizes to the cytoplasm and perinuclear region and serves as an INF-induced E3 protein ligase that mediates ISGylation of protein targets. HERC5 exhibits antiviral activity towards HIV-1, influenza A virus and human papillomavirus. HERC5 is a major E3 ligase for ISG15 conjugation. HERC5 also serves as a positive regulator of innate antiviral response in cells induced by INF. Pro-inflammatory cytokines upregulate HERC5 in endothelial cells. HERC5 is physically connected with polyribosomes, broadly modifies recently synthesized proteins in a cotranslational fashion.

    • Synonyms

      HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSFDLTVRR NHLIEDVLNQ LSQFENEDLR KELWVSFSGE IGYDLGGVKK EFFYCLFAEM IQPEYGMFMY PEGASCMWFP VKPKFEKKRY FFFGVLCGLS LFNCNVANLP FPLALFKKLL DQMPSLEDLK ELSPDLGKNL QTLLDDEGDN FEEVFYIHFN VHWDRNDTNL IPNGSSITVN QTNKRDYVSK YINYIFNDSV KAVYEEFRRG FYKMCDEDII KLFHPEELKD VIVGNTDYDW KTFEKNARYE PGYNSSHPTI VMFWKAFHKL TLEEKKKFLV FLTGTDRLQM KDLNNMKITF CCPESWNERD PIRALTCFSV LFLPKYSTME TVEEALQEAI NNNRGFG.

    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.

    Herc5 Human
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