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Search results

1000 results found for “placental lactogen”

Name

Description

Product #

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  • View Data Sheet

    Name :

    HMGCL Human

    Description:

    3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant

    Hydroxymethylglutaryl-CoA lyase mitochondrial, HL, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase, HMGCL.

    Product # :

    ENZ-218

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    Description

    HMGCL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (28-325) and having a molecular mass of 34.2kDa.HMGCL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HMGCL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hydroxymethylglutaryl-CoA lyase (HMGCL) is a mitochondrial matrix protein which is a member of the HMG-CoA lyase family. HMGCL is a homodimer and participates in leucine catabolism and ketogenesis, the hepatic synthesis of ketone bodies which, during fasting, provides a major source of energy for the heart, brain and kidney. More precisely, HMGCL catalyzes the final step of these processes, the cleavage of 3-hydroxy-3-methylglutaryl-CoA to acetoacetic acid and acetyl-CoA.

    • Synonyms

      Hydroxymethylglutaryl-CoA lyase mitochondrial, HL, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase, HMGCL.

    • 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 MGSHMTLPKR VKIVEVGPRD GLQNEKNIVS TPVKIKLIDM LSEAGLSVIE TTSFVSPKWV PQMGDHTEVL KGIQKFPGIN YPVLTPNLKG FEAAVAAGAK EVVIFGAASE LFTKKNINCS IEESFQRFDA ILKAAQSANI SVRGYVSCAL GCPYEGKISP AKVAEVTKKF YSMGCYEISL GDTIGVGTPG IMKDMLSAVM QEVPLAALAV HCHDTYGQAL ANTLMALQMG VSVVDSSVAG LGGCPYAQGA SGNLATEDLV YMLEGLGIHT GVNLQKLLEA GNFICQALNR KTSSKVAQAT CKL.

    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.

    Hmgcl Human
  • View Data Sheet

    Name :

    GATC Human

    Description:

    Glutamyl-TRNA Amidotransferase, Subunit C Human Recombinant

    Glutamyl-TRNA(Gln) Amidotransferase Subunit C, Glu-AdT Subunit C, 15E1.2, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog (Bacterial), Glutamyl-TRNA(Gln) Amidotransferase Subunit C Mitochondrial, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog, EC 6.3.5, Protein 15E1.2.

    Product # :

    ENZ-722

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    Description

    GATC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (1-136 a.a) and having a molecular mass of 17.5kDa (Molecular size on SDS-PAGE will appear higher).GATC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GATC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamyl-TRNA Amidotransferase, Subunit C also known as GATC allows the formation of properly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction occurs in the attendance of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). In addition, GATC is subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (PET112) and C (GATC) subunits.

    • Synonyms

      Glutamyl-TRNA(Gln) Amidotransferase Subunit C, Glu-AdT Subunit C, 15E1.2, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog (Bacterial), Glutamyl-TRNA(Gln) Amidotransferase Subunit C Mitochondrial, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog, EC 6.3.5, Protein 15E1.2.

    • 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 MGSMWSRLVW LGLRAPLGGR QGFTSKADPQ GSGRITAAVI EHLERLALVD FGSREAVARL EKAIAFADRL RAVDTDGVEP MESVLEDRCL YLRSDNVVEG NCADELLQNS HRVVEEYFVA PPGNISLPKL DEQEPFPHS

    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.

    Gatc Human
  • View Data Sheet

    Name :

    PREP Human

    Description:

    Prolyl Endopeptidase Human Recombinant

    Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.

    Product # :

    ENZ-828

    Price :

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    • formulation
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    Description

    PREP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 733 amino acids (1-710 a.a) and having a molecular mass of 83.1kDa. PREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PREP protein solution (0.25mg/ml) containing PBS buffer (pH 7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prolyl Endopeptidase , also known as PREP is a cytosolic prolyl endopeptidase which cleaves peptide bonds on the C-terminal side of prolyl residues within peptides which are up to about 30 a.a long. In addition, Prolyl endopeptidases have been shown to be implicated in the maturation and degradation of peptide hormones and neuropeptides.

    • Synonyms

      Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.

    • 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 MGSMLSLQYP DVYRDETAVQ DYHGHKICDP YAWLEDPDSE QTKAFVEAQN KITVPFLEQC PIRGLYKERM TELYDYPKYS CHFKKGKRYF YFYNTGLQNQ RVLYVQDSLE GEARVFLDPN ILSDDGTVAL RGYAFSEDGE YFAYGLSASG SDWVTIKFMK VDGAKELPDV LERVKFSCMA WTHDGKGMFY NSYPQQDGKS DGTETSTNLH QKLYYHVLGT DQSEDILCAE FPDEPKWMGG AELSDDGRYV LLSIREGCDP VNRLWYCDLQ QESSGIAGIL KWVKLIDNFE GEYDYVTNEG TVFTFKTNRQ SPNYRVINID FRDPEESKWK VLVPEHEKDV LEWIACVRSN FLVLCYLHDV KNILQLHDLT TGALLKTFPL DVGSIVGYSG QKKDTEIFYQ FTSFLSPGII YHCDLTKEEL EPRVFREVTV KGIDASDYQT VQIFYPSKDG TKIPMFIVHK KGIKLDGSHP AFLYGYGGFN ISITPNYSVS RLIFVRHMGG ILAVANIRGG GEYGETWHKG GILANKQNCF DDFQCAAEYL IKEGYTSPKR LTINGGSNGG LLVAACANQR PDLFGCVIAQ VGVMDMLKFH KYTIGHAWTT DYGCSDSKQH FEWLVKYSPL HNVKLPEADD IQYPSMLLLT ADHDDRVVPL HSLKFIATLQ YIVGRSRKQS NPLLIHVDTK AGHGAGKPTA KVIEEVSDMF AFIARCLNVD WIP.

    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.

    Prep Human
  • View Data Sheet

    Name :

    CTSZ Mouse, Active

    Description:

    Cathepsin-Z, Active Mouse Recombinant

    Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    Product # :

    ENZ-1108

    Price :

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    • description
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    • biological activity
    • More Info

    Description

    CTSZ Mouse Recombinant produced in Baculovirus is a single, glycosylated, polypeptide chain containing 292 amino acids (23-306 aa) and having a molecular mass of 32.8kDa.CTSZ is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CTSZ solution (0.5 mg/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 > 3,000 pmol/min/ug. One unit will convert 1 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25°C.

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    • 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

      ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT
      RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV
      WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE
      KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV
      RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH HH

    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.

    Cathepsin Z Mouse
  • 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.

    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.

    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.

    Pin4 Human
  • View Data Sheet

    Name :

    B3GAT3 Human

    Description:

    Beta-1,3-Glucuronyltransferase 3 Human Recombinant

    Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.

    Product # :

    ENZ-711

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    Description

    B3GAT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (29-335 a.a) and having a molecular mass of 36.4kDa. B3GAT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    B3GAT3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Beta-1,3-glucuronyltransferase 3 (B3GAT3) is involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. B3GAT3 has a part in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. B3GAT3 shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc.

    • Synonyms

      Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.

    • 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 MGSQPCDCLP PLRAAAEQLR QKDLRISQLQ AELRRPPPAP AQPPEPEALP TIYVVTPTYA RLVQKAELVR LSQTLSLVPR LHWLLVEDAE GPTPLVSGLL AASGLLFTHL VVLTPKAQRL REGEPGWVHP RGVEQRNKAL DWLRGRGGAV GGEKDPPPPG TQGVVYFADD DNTYSRELFE EMRWTRGVSV WPVGLVGGLR FEGPQVQDGR VVGFHTAWEP SRPFPVDMAG FAVALPLLLD KPNAQFDSTA PRGHLESSLL SHLVDPKDLE PRAANCTRVL VWHTRTEKPK MKQEEQLQRQ GRGSDPAIEV.

    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.

    B3Gat3 Human
  • View Data Sheet

    Name :

    PPIL1 Human

    Description:

    Peptidylprolyl Isomerase (Cyclophilin)-Like 1 Human Recombinant

    Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIL-1, CYPL1, hCyPX, MGC678, PPIase, CGI-124, PPIL1.

    Product # :

    ENZ-388

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    • sds-page

    Description

    PPIL1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-166) and having a molecular mass of 19.3 kDa. PPIL1 is fused to 8 amino acid His Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPIL1 solution containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol

    Purity

    Greater than 95.0% 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.

    sds-page

    PPIL1 Human SDS-PAGE - Product image 1

    More Info

    • Introduction

      PPIL1 belongs to the cyclophilin family of peptidylprolyl isomerases (PPIases).
      The cyclophilins are a well conserved, ubiquitous family, members of which take an significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 protein increases the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. PPIL1 is a novel molecular target for colon-cancer therapy.

    • Synonyms

      Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIL-1, CYPL1, hCyPX, MGC678, PPIase, CGI-124, PPIL1.

    • 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

      MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLEHH HHHH.

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    Ppil1 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.

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    Tnaa Ecoli
  • View Data Sheet

    Name :

    KRT19 Human

    Description:

    Cytokeratin 19 Human Recombinant

    Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.

    Product # :

    PRO-350

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    Description

    Cytokeratin 19 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 44,098 Dalton. The KRT19 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized after from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTK-19 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. Unlike its related family members, this smallest known acidic cytokeratin is not paired with a basic cytokeratin in epithelial cells. It is specifically expressed in the periderm, the transiently superficial layer that envelopes the developing epidermis. The type I cytokeratins are clustered in a region of chromosome 17q12-q21.

    • Synonyms

      Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KRT19 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT19 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 KRT19 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Reconstitution to filaments

      Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5 M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4 M urea and then to low salt condition (50 mM NaCl, 2 mM dithiothreitol, 10 mM Tris-HCl, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's 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.

    Krt19 Human
  • View Data Sheet

    Name :

    CKMBITII Human

    Description:

    Creatine Kinase MB Isoenzyme Type-II Human Recombinant

    Creatine Kinase MB Isoenzyme Type-II, CKMBITII, CKMBI, CKMB.

    Product # :

    CKI-270

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    Description

    CKMBITII Human Recombinant produced in Pichia Pastoris reacts with polyclonal antibodies to MB Isoenzyme in ELISA.

    Source

    Pichia Pastoris.

    Formulation

    Each mg of protein contains 10mM Tris-HCl, pH-6.8, 0.5mM EDTA and 0.5mM DTT, 50% (v/v) glycerol.

    Biological Activity

    The enzyme activity measured by kinetic assay at 340nm was 650 IU/mg at 37 degrees.

    More Info

    • Introduction

      CK-MB Type II possesses the naturally occurring carboxy-terminal amino acid lysine.
      This occurs during a myocardial infarct (MI or heart attack) when CK-MB Type II is released from damaged heart muscle, and the C-terminal lysine is cleaved in the blood stream, thus creating CK-MB Type I. This difference can be exploited in diagnosis of an MI.

    • Synonyms

      Creatine Kinase MB Isoenzyme Type-II, CKMBITII, CKMBI, CKMB.

    • Physical Appearance

      Sterile Filtered colourless liquid formulation.

    • Stability

      CKMBITII although stable at 15°C for 7 days, should be stored below -18°C. 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.

    Ckmbitii Human
  • View Data Sheet

    Name :

    PI3Ka Bovine

    Description:

    Phosphoinositide 3-kinase alpha p110a/p85a Bovine Recombinant

    Phosphoinositide 3-kinase alpha p110a/p85a, PI3Ka, 2.7.1.137, Phosphatidylinositol 3-kinase, 1-phosphatidylinositol 3-kinase, PI3-kinase, PtdIns-3-kinase, Type I phosphatidylinositol kinase, Type III phosphoinositide 3-kinase.

    Product # :

    PKA-327

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    Description

    The PI3Ka catalytic and regulatory subunits are coexpressed in Sf9 insect cells. Phosphoinositide 3-kinase alpha Bovine Recombinant is a glycosilated protein having a molecular weight as follows: p85a chain 83.5 kDa, p110 chain 124.3 kDa.

    Source

    Sf9 insect cells.

    Formulation

    PI3Ka solution in 25mM HEPES, pH 8.0, 25mM NaCl, 2.5mM MgCl2 and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PI3Ka plays a specific role in apoptosis in human colon cancer cells. Injection of neutralizing antibodies specific to PI3Ka into adenocarcinoma cells induced apoptosis, a response that was reverted by treating cells with caspase inhibitor. It was also shown that PI3Ka mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
      PI3Ka is a key regulator of the initiation of keratinocyte differentiation. A decrease in PI3Ka activity results in a loss of keratinocyte adhesion to the extracellular membrane and the initiation of early phase differentiation.

    • Synonyms

      Phosphoinositide 3-kinase alpha p110a/p85a, PI3Ka, 2.7.1.137, Phosphatidylinositol 3-kinase, 1-phosphatidylinositol 3-kinase, PI3-kinase, PtdIns-3-kinase, Type I phosphatidylinositol kinase, Type III phosphoinositide 3-kinase.

    • Physical Appearance

      Sterile filtered liquid formualtion.

    • 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

      1 unit is defined as 1 picomole phosphate transferred to PIP2 per minute.

    • Specific Activity

      1,000 U/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.

    Pi3Ka Bovine
  • View Data Sheet

    Name :

    FUT7 Human

    Description:

    Fucosyltransferase 7 Human Recombinant

    Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.

    Product # :

    ENZ-784

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    Description

    FUT7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (37-342) and having a molecular mass of 37.9kDa.FUT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FUT7 solution (0.25mg/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.

    More Info

    • Introduction

      Fucosyltransferase 7 (FUT7) is a golgi stack membrane protein which is involved in the creation of sialyl-Lewis X antigens. The FUT7 protein leads the synthesis of the E-selectin-binding sialyl-Lewis X moiety. FUT7 catalyzes alpha-1,3 glycosidic linkages involved in the expression of sialyl Lewis X antigens.

    • Synonyms

      Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.

    • 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 MGSPRGTPAP QPTITILVWH WPFTDQPPEL PSDTCTRYGI ARCHLSANRS LLASADAVVF HHRELQTRRS HLPLAQRPRG QPWVWASMES PSHTHGLSHL RGIFNWVLSY RRDSDIFVPY GRLEPHWGPS PPLPAKSRVA AWVVSNFQER QLRARLYRQL APHLRVDVFG RANGRPLCAS CLVPTVAQYR FYLSFENSQH RDYITEKFWR NALVAGTVPV VLGPPRATYE AFVPADAFVH VDDFGSAREL AAFLTGMNES RYQRFFAWRD RLRVRLFTDW RERFCAICDR YPHLPRSQVY EDLEGWFQA.

    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.

    Fut7 Human
  • View Data Sheet

    Name :

    PGRN Human

    Description:

    Progranulin Human Recombinant

    GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.

    Product # :

    CYT-524

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    Description

    Progranulin Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 1-593 amino acids and having a molecular mass of 74kDa. The Progranulin is purified by standard chromatographic techniques.

    Source

    HEK 293 cells.

    Formulation

    The protein contains 1xPBS.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Activates phospho-ERK1/2 in neuronal mouse P19 cells and regulates food intake and body weight.

    More Info

    • Introduction

      A 88-kDa progranulin, also called proepithelin and PC cell-derived growth factor, is a single precursor protein of granulins which are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin/epithelin motif. Granulins are a variety of active, 6 kDa peptides and named granulin A (epithelin 1), granulin B (epithelin 2), granulin C, etc. Both the peptides and intact progranulin protein regulate cell growth. However, different members of the granulin protein family may act as inhibitors, stimulators, or have dual actions on cell growth. Granulin family members are important in normal development, wound healing, and tumorigenesis.

    • Synonyms

      GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Progranulin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PGRN should be stored at 4C between 2-7 days and for future use below -18C. 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 Progranulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Progranulin Human
  • View Data Sheet

    Name :

    FUCA1 Human

    Description:

    Fucosidase Alpha-L- 1 Plasma Human Recombinant

    Fucosidase, Alpha-L- 1, Tissue, Alpha-L-Fucoside Fucohydrolase 1, Alpha-L-Fucosidase 1, Alpha-L-Fucosidase I, EC 3.2.1.51, Tissue Alpha-L-Fucosidase, EC 3.2.1, FUCA, Tissue alpha-L-fucosidase.

    Product # :

    ENZ-921

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    Description

    FUCA1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 445 amino acids (28-466a.a.) and having a molecular mass of 51.7kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). FUCA1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    FUCA1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fucosidase Alpha-L- 1 Plasma, also known as FUCA1 is a member of the glycosyl hydrolase 29 family which is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Fucosidosis is an autosomal recessive lysosomal storage disease caused by the absence of alpha-L-fucosidase activity.

    • Synonyms

      Fucosidase, Alpha-L- 1, Tissue, Alpha-L-Fucoside Fucohydrolase 1, Alpha-L-Fucosidase 1, Alpha-L-Fucosidase I, EC 3.2.1.51, Tissue Alpha-L-Fucosidase, EC 3.2.1, FUCA, Tissue alpha-L-fucosidase.

    • 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

      VRRAQPPRRY TPDWPSLDSR PLPAWFDEAK FGVFIHWGVF SVPAWGSEWF WWHWQGEGRP QYQRFMRDNY PPGFSYADFG PQFTARFFHP EEWADLFQAA GAKYVVLTTK HHEGFTNWPS PVSWNWNSKD VGPHRDLVGE LGTALRKRNI RYGLYHSLLE WFHPLYLLDK KNGFKTQHFV SAKTMPELYD LVNSYKPDLI WSDGEWECPD TYWNSTNFLS WLYNDSPVKD EVVVNDRWGQ NCSCHHGGYY NCEDKFKPQS LPDHKWEMCT SIDKFSWGYR RDMALSDVTE ESEIISELVQ TVSLGGNYLL NIGPTKDGLI VPIFQERLLA VGKWLSINGE AIYASKPWRV QWEKNTTSVW YTSKGSAVYA IFLHWPENGV LNLESPITTS TTKITMLGIQ GDLKWSTDPD KGLFISLPQL PPSAVPAEFA WTIKLTGVKH 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.

    Fuca1 Human
  • View Data Sheet

    Name :

    Betacellulin Bovine

    Description:

    Betacellulin Bovine Recombinant

    Product # :

    CYT-406

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    Description

    Betacellulin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9003 Dalton. Betacellulin Bovine Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Betacellulin Bovine Recombinant was lyophilized after extensive dialysis against 50mM acetic acid.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Betacellulin Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Bovine 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 BTC Bovine in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Gly-Asn-Ser-Thr.

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 9kDa.

      What is the source or expression system of BETACELLULIN Protein?
      Escherichia Coli.

      What is the Purity of BETACELLULIN Protein?
      BETACELLULIN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BETACELLULIN Protein?
      The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

      What is the amino acid sequence of BETACELLULIN Protein?
      BETACELLULIN Protein is composed from 80 amino acids.

      What applications can BETACELLULIN Protein be used in?
      BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BETACELLULIN Protein?
      The endotoxin level is minimal, BETACELLULIN Protein was purified using conventional chromatography techniques.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.59 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 by RP-HPLC, using a calibrated solution of BTC as a Reference Standard.

    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.

    Betacellulin Bovine
  • 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.

    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 :

    ADPRH Human

    Description:

    ADP-Ribosylarginine Hydrolase Human Recombinant

    [Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.

    Product # :

    ENZ-631

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    Description

    ADPRH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 42.1kDa.ADPRH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADPRH solution (0.5mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-ribosylarginine hydrolase (ADPRH) is a member of the ADP-ribosylglycohydrolase family. ADPRH catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. The human ADPRH enzyme is DTT-independent as opposed to the rat and mouse enzymes, which require DTT for maximal activity.

    • Synonyms

      [Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.

    • 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 MGSHMEKYVA AMVLSAAGDA LGYYNGKWEF LQDGEKIHRQ LAQLGGLDAL DVGRWRVSDD TVMHLATAEA LVEAGKAPKL TQLYYLLAKH YQDCMEDMDG RAPGGASVHN AMQLKPGKPN GWRIPFNSHE GGCGAAMRAM CIGLRFPHHS QLDTLIQVSI ESGRMTHHHP TGYLGALASA LFTAYAVNSR PPLQWGKGLM ELLPEAKKYI VQSGYFVEEN LQHWSYFQTK WENYLKLRGI LDGESAPTFP ESFGVKERDQ FYTSLSYSGW GGSSGHDAPM IAYDAVLAAG DSWKELAHRA FFHGGDSDST AAIAGCWWGV MYGFKGVSPS NYEKLEYRNR
      LEETARALYS LGSKEDTVIS L.

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    Adprh Human
  • View Data Sheet

    Name :

    LPL Human

    Description:

    Lipoprotein Lipase Human Recombinant

    Lipoprotein lipase, LPL, LIPD, HDLCQ11.

    Product # :

    ENZ-086

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    Description

    The Recombinant Human LPL produced in E.coli has a molecular mass of 51.61kDa containing 458 amino acid residues of the human LPL and fused to a 10 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    LPL was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 50mM Acetate buffer, pH=4.

    More Info

    • Introduction

      LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.

    • Synonyms

      Lipoprotein lipase, LPL, LIPD, HDLCQ11.

    • 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

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA QEHYPVSAGY TKLVGQDVAR FINWMEEEFN YPLDNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCSSKEAF EKGLCLSCRK NRCNNLGYEI SKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESETH TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLIYTEV DIGELLMLKL KWKSDSYFSW SDWWSSPGFA IQKIRVKAGE TQKKVIFCSR EKVSHLQKGK APAVFVKCHD KSLNKKSG.

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    Lpl Human
  • View Data Sheet

    Name :

    IHH Human

    Description:

    Indian Hedgehog Human Recombinant

    Indian hedgehog protein, IHH, HHG-2, BDA1.

    Product # :

    CYT-195

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    Description

    IHH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.

    More Info

    • Introduction

      IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.

    • Synonyms

      Indian hedgehog protein, IHH, HHG-2, BDA1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IHH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IHH 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 IHH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.

    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.

    Ihh Human
  • View Data Sheet

    Name :

    IHH Mouse

    Description:

    Indian Hedgehog Mouse Recombinant

    Indian hedgehog protein, IHH, HHG-2, BDA1.

    Product # :

    CYT-398

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    Description

    IHH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0μg/ml corresponding to a specific activity of 100-334units/mg.

    More Info

    • Introduction

      IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.

    • Synonyms

      Indian hedgehog protein, IHH, HHG-2, BDA1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IHH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IHH 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 IHH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.

    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.

    Ihh Mouse
  • View Data Sheet

    Name :

    OTOR Human, His

    Description:

    Otoraplin Human Recombinant, His Tag

    Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.

    Product # :

    CYT-884

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    Description

    OTOR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (26-128 a.a) and having a molecular mass of 14.3kDa. OTOR is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OTOR protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
      Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness.

    • Synonyms

      Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.

    • 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 MGSHMLASKK LCADDECVYT ISLASAQEDY NAPDCRFINV KKGQQIYVYS KLVKENGAGE FWAGSVYGDG QDEMGVVGYF PRNLVKEQRV YQEATKEVPT TDIDFFCE.

    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.

    Otor Human His
  • View Data Sheet

    Name :

    BST1 Human

    Description:

    Bone Marrow Stromal Cell Antigen 1 Human Recombinant

    Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

    Product # :

    CYT-1071

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    Description

    BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.

    • Synonyms

      Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 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

      RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

    • Background

      The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine

      Introduction

      In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.

      BST-1: A Versatile Player

      BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.

      Engineering a Cellular Conductor

      With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.

      Entering the Biological Stage

      Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.

      An Enthusiastic Applause for Results

      Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.

      Conclusion

      The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.

      What is the molecular weight/Mw of BST1 Protein?
      BST1 Protein has a total Mw of 30.5kDa.

      What is the source or expression system of BST1 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of BST1 Protein?
      BST1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BST1 Protein?
      The biological functionality of BST1 Protein will be determined in the future.

      What is the amino acid sequence of BST1 Protein?
      RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

      What applications can BST1 Protein be used in?
      BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BST1 Protein?
      The endotoxin level is minimal, BST1 Protein was purified using conventional chromatography techniques.

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

    Bst1 Human
  • View Data Sheet

    Name :

    TBCEL Human

    Description:

    Tubulin Folding Cofactor E-Like Human Recombinant

    Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    Product # :

    PRO-030

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    Description

    TBCEL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. The TBCEL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.

    • Synonyms

      Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    • 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 MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.

    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.

    Tbcel Human
  • View Data Sheet

    Name :

    PNOC Human

    Description:

    Prepronociceptin Human Recombinant

    Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.

    Product # :

    PRO-1442

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    Description

    PNOC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (20-176) and having a molecular mass of 20.6kDa. PNOC is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    PNOC protein solution (1mg/ml) containing 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

      Prepronociceptin (PNOC) is the ligand of the opioid receptor-like receptor (OPRL1). PNOC functions as a transmitter in the brain by modulating nociceptive and locomotor behavior. The PNOC protein may also be involved in neuronal differentiation and development.

    • Synonyms

      Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.

    • 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 MGSSCQRDCL TCQEKLHPAL DSFDLEVCIL ECEEKVFPSP LWTPCTKVMA RSSWQLSPAA PEHVAAALYQ PRASEMQHLR RMPRVRSLFQ EQEEPEPGME EAGEMEQKQL QKRFGGFTGA RKSARKLANQ KRFSEFMRQY LVLSMQSSQR RRTLHQNGNV.

    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.

    Pnoc Human
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