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Search results

1000 results found for “NOV”

Name

Description

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  • View Data Sheet

    Name :

    NNMT Human

    Description:

    Nicotinamide N-Methyltransferase Human Recombinant

    Nicotineamide N-methyltransferase, NNMT.

    Product # :

    ENZ-418

    Price :

    Quantity :

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    Description

    NNMT Human Recombinant fused with a 20 amino acid His-Tag tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 284 amino acids (1-264 a.a.) and having a molecular mass of 31.7 kDa.The NNMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NNMT solution contains 20mM Tris pH 8.0 & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.

    • Synonyms

      Nicotineamide N-methyltransferase, NNMT.

    • 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 MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC LDGVKGDLLI DIGSGPTIYQLLSACESFKE IVVTDYSDQN LQELEKWLKK EPEAFDWSPV VTYVCDLEGN RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG AVPLPPADCV LSTLCLDAAC PDLPTYCRAL RNLGSLLKPG GFLVIMDALK SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ SYSSTMANNEGLFSLVARKL SRPL.

    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.

    Nnmt Human
  • View Data Sheet

    Name :

    POMC Human

    Description:

    Proopiomelanocortin Human Recombinant

    Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.

    Product # :

    PRO-236

    Price :

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    Description

    POMC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (27-267 a.a) and having a molecular mass of 28.9kDa (molecular weight on SDS-PAGE will appear higher).POMC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POMC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 50% glycerol, 0.1mM PMSF, 0.1M Imidazole and 0.2M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pro-opiomelanocortin preproprotein (POMC) is a polypeptide hormone precursor which experiences extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. POMC regulates the corticosteroid production in the adrenal cortex. Furthermore, POMC is cleaved into ten hormone chains named NPP, g-MSH, ACTH, a-MSH, CLIP, Lipotropin b, Lipotropin g, b-MSH,b endorphin and Met-enkephalin. POMC gene defects are the cause of POMC deficiency, which is characterized by red hair and adrenal insufficiency.

    • Synonyms

      Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.

    • 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 MWCLESSQCQ DLTTESNLLE CIRACKPDLS AETPMFPGNG DEQPLTENPR KYVMGHFRWD RFGRRNSSSS GSSGAGQKRE DVSAGEDCGP LPEGGPEPRS DGAKPGPREG KRSYSMEHFR WGKPVGKKRR PVKVYPNGAE DESAEAFPLE FKRELTGQRL
      REGDGPDGPA DDGAGAQADL EHSLLVAAEK KDEGPYRMEH FRWGSPPKDK RYGGFMTSEK SQTPLVTLFK NAIIKNAYKK GE.

    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.

    Pomc Human
  • View Data Sheet

    Name :

    PTPN11 Human, Active

    Description:

    Protein Tyrosine Phosphatase Non Receptor Type-11 Human Recombinant, Active

    PTPN11, Tyrosine-protein phosphatase non-receptor type 11, Protein-tyrosine phosphatase 1D, PTP-1D, Proteintyrosine phosphatase 2C, PTP-2C, SH-PTP2, SH-PTP3, BPTP3, CFC, JMML, METCDS, NS1, SHP-2, shp-2, PTP2C, SHPTP2.

    Product # :

    PKA-126

    Price :

    Quantity :

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    • More Info

    Description

    PTPN11 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 602 amino acids ( 1-593 a.a.) and having a molecular mass of 69.1 kDa.PTPN11 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    PTPN11 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 grather than 400 unit/mg  and is defined as the amount of enzyme that hydrolyze 1.0 nmole of pnitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      Protein Tyrosine Phosphatase Non Receptor Type-11 or PTPN11 has 2 Src homology 2 domains and part of the tyrosine phosphatase group of proteins. PTPN11 is responsible for the catalyzation of tyrosine residues dephosphorylation in proteins and takes part in the stimulation and activation of Erk/MAP kinase transduction via signals from tyrosine kinase. Noonan syndrome and acute myeloid leukemia can be caused from mutations in PTPN11.

    • Synonyms

      PTPN11, Tyrosine-protein phosphatase non-receptor type 11, Protein-tyrosine phosphatase 1D, PTP-1D, Proteintyrosine phosphatase 2C, PTP-2C, SH-PTP2, SH-PTP3, BPTP3, CFC, JMML, METCDS, NS1, SHP-2, shp-2, PTP2C, SHPTP2.

    • 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

      ADPMTSRRWF HPNITGVEAE NLLLTRGVDG SFLARPSKSN PGDFTLSVRR NGAVTHIKIQ NTGDYYDLYG GEKFATLAEL VQYYMEHHGQ LKEKNGDVIE LKYPLNCADP TSERWFHGHL SGKEAEKLLT EKGKHGSFLV RESQSHPGDF VLSVRTGDDK GESNDGKSKV THVMIRCQEL KYDVGGGERF DSLTDLVEHY KKNPMVETLG TVLQLKQPLN TTRINAAEIE SRVRELSKLA ETTDKVKQGF WEEFETLQQQ ECKLLYSRKE GQRQENKNKN RYKNILPFDH TRVVLHDGDP NEPVSDYINA NIIMPEFETK CNNSKPKKSY IATQGCLQNT VNDFWRMVFQ ENSRVIVMTT KEVERGKSKC VKYWPDEYAL KEYGVMRVRN VKESAAHDYT LRELKLSKVG QGNTERTVWQ YHFRTWPDHG VPSDPGGVLD FLEEVHHKQE SIMDAGPVVV HCSAGIGRTG TFIVIDILID
      IIREKGVDCD IDVPKTIQMV RSQRSGMVQT EAQYRFIYMA VQHYIETLQR RIEEEQKSKR KGHEYTNIKY SLADQTSGDQ SPLPPCTPTP PCAEMREDSA RVYENVGLMQ QQKSFRHHHH 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.

    Ptpn11 Enzyme
  • View Data Sheet

    Name :

    VOPP1 Human

    Description:

    Vesicular Overexpressed in Cancer, Prosurvival Protein 1 Human Recombinant

    Vesicular overexpressed in cancer prosurvival protein 1, EGFR-coamplified and overexpressed protein, ECop, Glioblastoma-amplified secreted protein, Putative NF-kappa-B-activating protein 055N, VOPP1, ECOP, GASP, FLJ20532, DKFZp564K0822.

    Product # :

    PRO-200

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    • More Info

    Description

    VOPP1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 112 amino acids (82-172 a.a.) and having a molecular mass of 12kDa. The VOPP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VOPP1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.2M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vesicular overexpressed in cancer prosurvival protein 1 (VOPP1) has been previously shown to be over-expressed in human glioblastoma multiform and squamous cell carcinoma. VOPP1 is a crucial regulator of NF-kappaB signaling, and this high-level, amplification-mediated VOPP1 expression, such as that occurring in tumors with amplified EGFR, might impact the resistance to apoptosis.

    • Synonyms

      Vesicular overexpressed in cancer prosurvival protein 1, EGFR-coamplified and overexpressed protein, ECop, Glioblastoma-amplified secreted protein, Putative NF-kappa-B-activating protein 055N, VOPP1, ECOP, GASP, FLJ20532, DKFZp564K0822.

    • 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 MRRRMYPPPL IEEPAFNVSY TRQPPNPGPG AQQPGPPYYT DPGGPGMNPV GNSMAMAFQV PPNSPQGSVA CPPPPAYCNT PPPPYEQVVK AK.

    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.

    Vopp1 Human
  • View Data Sheet

    Name :

    NUCB2 Human

    Description:

    Nucleobindin-2 Human Recombinant

    Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    Product # :

    PRO-492

    Price :

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    Description

    The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 9.7kDa containing 82 amino acid residues of the human NUCB2.

    Source

    Escherichia Coli.

    Formulation

    The NUCB2 protein was 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.

    More Info

    • Introduction

      Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.

    • Synonyms

      Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 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 NUCB2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.

    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.

    Nucb2 Human
  • View Data Sheet

    Name :

    CoV-2 N (127 a.a.)

    Description:

    Coronavirus 2019 Nucleocapsid (127 a.a.), Recombinant

    Product # :

    SARS-043

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    Description

    The E.Coli derived recombinant protein contains the Coronavirus 2019 C-terminal region 127 a.a. from the Nucleocapsid protein and fused to GST-6xHis tag at N-terminal and having a Mw. of 39.4 kDa.

    Source

    E.Coli.

    Formulation

    CoV-2 Nucleocapsid protein solution is supplied in 50mM Tris-HCl pH 8, 1M Urea, and 50% Glycerol.

    Purity

    CoV-2 Nucleocapsid protein is >95% pure as determined SDS-PAGE.

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      CoV-2 Spike Protein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Purification Method

      NTA Sepharose-Affinity Purification.

    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.

    product_image.jpg
  • View Data Sheet

    Name :

    ANXA11 Human

    Description:

    Annexin A11 Human Recombinant

    Annexin A11, 56 kDa autoantigen, Annexin XI, Annexin-11, Calcyclin-associated annexin 50, CAP-50, ANXA11, ANX11, CAP50.

    Product # :

    PRO-278

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    Description

    ANXA11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 525 amino acids (1-505) and having a molecular mass of 56.6 kDa. The ANXA11 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA11 solution (0.25mg/ml) contains 20mM MES buffer (Ph 5.0), 20% glycerol, 2mM DTT and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Annexin A11 (ANXA11) belongs to the annexin family, which is a group of calcium-dependent phospholipid-binding proteins. Annexins have distinctive N-terminal domains and conserved C-terminal domains, which contain the calcium-dependent phospholipid-binding sites. Annexin A11 binds specifically to calcyclin in a calcium-dependent manner. Moreover, ANXA11 is required for midbody formation and completion of the terminal phase of cytokinesis. The ANXA11 protein is a 56kDa antigen recognized by sera from patients with various autoimmune diseases.

    • Synonyms

      Annexin A11, 56 kDa autoantigen, Annexin XI, Annexin-11, Calcyclin-associated annexin 50, CAP-50, ANXA11, ANX11, CAP50.

    • 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 MSYPGYPPPP GGYPPAAPGG GPWGGAAYPP PPSMPPIGLD NVATYAGQFN QDYLSGMAAN MSGTFGGANM PNLYPGAPGA GYPPVPPGGF GQPPSAQQPV PPYGMYPPPG NPPSRMPSY PPYPGAPVPG QPMPPPGQQP PGAYPGQPPV TYPGQPPVPL PGQQQPVPSY PGYPGSGTVT PAVPPTQFGS RGTITDAPGF DPLRDAEVLR KAMKGFGTDE QAIIDCLGSR SNKQRQQILL SFKTAYGKDL IKDLKSELSG NFEKTILALM KTPVLFDIYE IKEAIKGVGT DEACLIEILA SRSNEHIREL NRAYKAEFKK TLEEAIRSDT GHFQRLLIS LSQGNRDEST NVDMSLAQRD AQELYAAGEN RLGTDESKFN AVLCSRSRAH LVAVFNEYQR MTGRDIEKSI CREMSGDLEE GMLAVVKCLK NTPAFFAERL NKAMRGAGTK DRTLIRIMVS RSETDLLDIR SEYKRMYGKS LYHDISGDTS GDYRKILLKI CGGND.

    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.

    Anxa11 Human
  • View Data Sheet

    Name :

    NRGN Human

    Description:

    Neurogranin Human Recombinant

    hng, RC3, Neurogranin, Ng, NRGN.

    Product # :

    CYT-293

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    Description

    NRGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a.) and having a molecular mass of 10.0kDa (molecular size on SDS-PAGE will appear higher). NRGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NRGN protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH7.0), 30% glycerol 0.1mM PMSF and 1mM EDTA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neurogranin (NRGN) is a calmodulin-binding protein which is expressed solely in the brain, mainly in dendritic spines. NRGN is also taking part in the protein kinase C signaling pathway by being a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. NRGN binds to calmodulin in the absence of calcium. NRGN protein’s phosphorylation by protein kinase C lowers its binding ability.

    • Synonyms

      hng, RC3, Neurogranin, Ng, NRGN.

    • 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 MGSMDCCTEN ACSKPDDDIL DIPLDDPGAN AAAAKIQASF RGHMARKKIK SGERGRKGPG PGGPGGAGVA RGGAGGGPSG D.

    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.

    Nrgn Human
  • View Data Sheet

    Name :

    NUBP2 Human

    Description:

    Nucleotide Binding Protein 2 Human Recombinant

    Nucleotide Binding Protein 2, Nucleotide Binding Protein 2 (MinD Homolog, E. Coli), NBP 2,CFD1, C447E6.1 (Nucleotide Binding Protein 1 (E.Coli MinD Like) ), Homolog Of Yeast Cytosolic Fe-S Cluster Deficient 1, Nucleotide Binding Protein 2 (E.Coli MinD Like), Cytosolic Fe-S Cluster Assembly Factor NUBP2, Nucleotide-Binding Protein 2, NUBP1, NUBP2.

    Product # :

    PRO-2133

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    Description

    NUBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (1-271 a.a) and having a molecular mass of 31.2kDa.NUBP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUBP2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 50% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleotide Binding Protein 2, also known as NUBP2 is an adenosine triphosphate (ATP) as well as metal-binding protein which is essential for the assembly of cyotosolic iron-sulfur proteins. NUBP2 performs in a heterotetramer with nucleotide-binding protein 1 (NUBP1). Moreover, alternative splicing results in multiple transcript variants have been found for NUBP2.

    • Synonyms

      Nucleotide Binding Protein 2, Nucleotide Binding Protein 2 (MinD Homolog, E. Coli), NBP 2,CFD1, C447E6.1 (Nucleotide Binding Protein 1 (E.Coli MinD Like) ), Homolog Of Yeast Cytosolic Fe-S Cluster Deficient 1, Nucleotide Binding Protein 2 (E.Coli MinD Like), Cytosolic Fe-S Cluster Assembly Factor NUBP2, Nucleotide-Binding Protein 2, NUBP1, NUBP2.

    • 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 MGSMEAAAEP GNLAGVRHII LVLSGKGGVG KSTISTELAL ALRHAGKKVG ILDVDLCGPS IPRMLGAQGR AVHQCDRGWA PVFLDREQSI SLMSVGFLLE KPDEAVVWRG PKKNALIKQF VSDVAWGELD YLVVDTPPGT SDEHMATIEA LRPYQPLGAL VVTTPQAVSV GDVRRELTFC RKTGLRVMGI VENMSGFTCP HCTECTSVFS RGGGEELAQL AGVPFLGSVP LDPALMRTLE EGHDFIQEFP GSPAFAALTS IAQKILDATP ACLP

    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.

    Nubp2 Human
  • View Data Sheet

    Name :

    THAP11 Human

    Description:

    THAP Domain Containing, Apoptosis Associated Protein 11 Human Recombinant

    THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.

    Product # :

    PRO-2009

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    Description

    THAP11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 36.8kDa.THAP11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The THAP11 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      THAP Domain Containing, Apoptosis Associated Protein 11 (THAP11) is a part of the thanatos-associated protein family. THAP11 plays a role as a transcriptional repressor and interacts with HCF1 through a coiled coil domain. THAP11 which is localized to the nucleus and cytoplasm takes part in embryogenesis and pluripotency of embryonic stem cells by recruiting epigenetic modifiers.

    • Synonyms

      THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.

    • 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 MGSMPGFTCC VPGCYNNSHR DKALHFYTFP KDAELRRLWL KNVSRAGVSG CFSTFQPTTG HRLCSVHFQG GRKTYTVRVP TIFPLRGVNE RKVARRPAGA AAARRRQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQSSPSA STAQTAQLQP NLVSASAAVL LTLQATVDSS QAPGSVQPAP ITPTGEDVKP IDLTVQVEFA AAEGAAAAAA ASELQAATAG LEAAECPMGP QLVVVGEEGF PDTGSDHSYS LSSGTTEEEL LRKLNEQRDI LALMEVKMKE MKGSIRHLRL TEAKLREELR EKDRLLAMAV IRKKHGM.

    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.

    Thap11 Human
  • View Data Sheet

    Name :

    IFN A Neut Antibody

    Description:

    Interferon-alpha Neutralizing, Mouse Anti-Human

    Product # :

    ANT-122

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    • More Info

    Formulation

    1mg/ml in PBS (after reconstitution).

    More Info

    • Introduction

      IFN-alpha is produced by macrophages, IFN-alpha has antiviral activities and stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.

    • Solubility

      Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      r.Human IFN Alpha.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      NYRhIFN-A (neut).

    • Applications

      Direct ELISA (Does not work in Western Blotting). This is a Neutralizing antibody.

    • Note

      The antibody can be used for Capture ELISA together with ProSpec’s Mouse Anti Human IFN-alpha Western Blot antibody.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Ion exchange.

    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.

    Interferon Alpha Neutralizing Antibody
  • View Data Sheet

    Name :

    DNAJB11 Human

    Description:

    DnaJ (Hsp40) Homolog, Subfamily B, Member 11 Human Recombinant

    DnaJ homolog subfamily B member 11, APOBEC1-binding protein 2, ABBP-2, DnaJ protein homolog 9, ER-associated DNAJ, ER-associated Hsp40 co-chaperone, ER-associated dnaJ protein 3, ERdj3, ERj3p, HEDJ, Human DnaJ protein 9, hDj-9, PWP1-interacting protein 4, DNAJB11, EDJ, ERJ3, HDJ9, DJ9, Dj-9, ABBP2, UNQ537, PRO1080.

    Product # :

    HSP-042

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    Description

    DNAJB11 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (23-358 a.a.) and having a molecular mass of 40.5kDa.DNAJB11 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DNAJB11 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DNAJB11 is a member of the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJB11 serves as a co-chaperone for HSPA5 and binds directly to both unfolded proteins which are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed.

    • Synonyms

      DnaJ homolog subfamily B member 11, APOBEC1-binding protein 2, ABBP-2, DnaJ protein homolog 9, ER-associated DNAJ, ER-associated Hsp40 co-chaperone, ER-associated dnaJ protein 3, ERdj3, ERj3p, HEDJ, Human DnaJ protein 9, hDj-9, PWP1-interacting protein 4, DNAJB11, EDJ, ERJ3, HDJ9, DJ9, Dj-9, ABBP2, UNQ537, PRO1080.

    • 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 MGRDFYKILG VPRSASIKDI KKAYRKLALQ LHPDRNPDDP QAQEKFQDLG AAYEVLSDSE KRKQYDTYGE EGLKDGHQSS HGDIFSHFFG DFGFMFGGTP RQQDRNIPRG SDIIVDLEVT LEEVYAGNFV EVVRNKPVAR QAPGKRKCNC RQEMRTTQLG PGRFQMTQEV VCDECPNVKL VNEERTLEVE IEPGVRDGME YPFIGEGEPH VDGEPGDLRF RIKVVKHPIF ERRGDDLYTN VTISLVESLV GFEMDITHLD GHKVHISRDK ITRPGAKLWK KGEGLPNFDN NNIKGSLIIT FDVDFPKEQL TEEAREGIKQ LLKQGSVQKV YNGLQGY.

    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.

    Dnajb11 Human
  • View Data Sheet

    Name :

    MAPK11 Human

    Description:

    Mitogen-Activated Protein Kinase 11 Human Recombinant

    Mitogen-activated protein kinase 11, PRKM11, SAPK2, p38-2, p38Beta, Mitogen-activated protein kinase p38 beta, Stress-activated protein kinase 2b, SAPK2B, MAP kinase 11, MAP kinase p38 beta, MAPK 11, P38BETA2, mitogen-activated protein kinase p38-2, EC 2.7.11, EC 2.7.11.24.

    Product # :

    PKA-013

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    Description

    MAPK11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-364 a.a.) and having a molecular mass of 43.8kDa.MAPK11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAPK11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 2mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE analysis.

    More Info

    • Introduction

      MAPK11 belongs to the MAP kinase family and is most associated with p38 MAP kinases (MAPKs). MAPKs are activated mainly as a reaction to cellular stress and inflammatory cytokines, and inhibitors that target the MAPK14 and MAPK11 have demonstrated ability to cure inflammatory disease. MAPK11 cooperates with HDAC3 and Promyelocytic leukemia protein and takes part in a signal transduction pathway which is activated by alterations in the osmolarity of the extracellular environment, by environmental stress, or by cytokines.

    • Synonyms

      Mitogen-activated protein kinase 11, PRKM11, SAPK2, p38-2, p38Beta, Mitogen-activated protein kinase p38 beta, Stress-activated protein kinase 2b, SAPK2B, MAP kinase 11, MAP kinase p38 beta, MAPK 11, P38BETA2, mitogen-activated protein kinase p38-2, EC 2.7.11, EC 2.7.11.24.

    • 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 MGSMSGPRAG FYRQELNKTV WEVPQRLQGL RPVGSGAYGS VCSAYDARLR QKVAVKKLSR PFQSLIHARR TYRELRLLKH LKHENVIGLL DVFTPATSIE DFSEVYLVTT LMGADLNNIV KCQALSDEHV QFLVYQLLRG LKYIHSAGII HRDLKPSNVA VNEDCELRIL DFGLARQADE EMTGYVATRW YRAPEIMLNW MHYNQTVDIW SVGCIMAELL QGKALFPGSD YIDQLKRIME VVGTPSPEVL AKISSEHART YIQSLPPMPQ KDLSSIFRGA NPLAIDLLGR MLVLDSDQRV SAAEALAHAY FSQYHDPEDE PEAEPYDESV EAKERTLEEW KELTYQEVLS FKPPEPPKPP GSLEIEQ.

    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.

    Mapk11 Human
  • View Data Sheet

    Name :

    NUTF2 Human

    Description:

    Nuclear Transport Factor 2 Human Recombinant

    Nuclear transport factor 2, NTF-2, Placental protein 15, PP15, NUTF2, NTF2.

    Product # :

    PRO-844

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    Description

    NUTF2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids (1-127 a.a.) and having a molecular mass of 16.6 kDa. The NUTF2 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUTF2 Human solution containing 20mM Tris HCL pH-8, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NUTF2 assists in protein transport into the nucleus and interacts with the nucleoporin p62 and with Ran. NUTF2 plays a role at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. NUTF2 is part of a multicomponent system of cytosolic factors that come together at the pore complex during nuclear import.

    • Synonyms

      Nuclear transport factor 2, NTF-2, Placental protein 15, PP15, NUTF2, NTF2.

    • 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 MGDKPIWEQI GSSFIQHYYQ LFDNDRTQLG AIYIDASCLT WEGQQFQGKA AIVEKLSSLP FQKIQHSITA QDHQPTPDSC IISMVVGQLK ADEDPIMGFH QMFLLKNIND AWVCTNDMFR LALHNFG.

    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.

    Nutf2 Human
  • View Data Sheet

    Name :

    ENO2 Protein

    Description:

    Enolase-2 Human

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

    Product # :

    ENZ-371

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    • More Info

    Description

    Human Neurone Specific Enolase produced in Human CNS having a molecular mass of 45kDa.

    Source

    Human CNS.

    Formulation

    The protein solution is in 10mM NaH2PO4 buffer pH 7.4 containing 150mM NaCl and 5mM MgSO4.

    Purity

    Greater than 96.0%.

    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

      Human NSE although stable at 4°C for 1 week, should be stored at -18°C.

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

    Eno2 Human
  • View Data Sheet

    Name :

    WNV Pre-M

    Description:

    West Nile Virus Pre-M Recombinant

    Product # :

    WNV-002

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    Description

    The E.Coli derived 20kda recombinant protein contains the West-Nile N-Terminal Pre-M Virus immunodominant regions. The protein is fused with 6xHis tag at c-terminal.

    Source

    Escherichia Coli.

    Formulation

    20mM phosphate buffer pH 7.5.

    Purity

    Protein is >95% pure as determined by SDS-PAGE.

    More Info

    • Introduction

      West Nile virus (WNV) is a virus of the family Flaviviridae part of the Japanese encephalitis (JE) antigenic complex of viruses. Image reconstructions and cryoelectron microscopyreveal a 45-50 nm virion covered with a relatively smooth proteinsurface. This structure is similar to virus; both belong to the genus flavivirus within the family Flaviviridae. WNV is a positive-sense, single strand of RNA, it is between 11,000 and 12,000 nucleotides long which encode seven non-structural proteins and three structural proteins. The RNA strand is held within a nucleocapsid formed from 12 kDaprotein blocks; the capsid is contained within a host-derived membrane altered by two viral glycoproteins.

    • Stability

      WNV Pre-M although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRA MDVGYLCEDTITYECPVLAAGNDPEDIDCWCTKSSVYVR
      YGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWLDSTK
      ATRYLVKTESWILRNPGYALE.

    • Applications

      Antigen in ELISA and Western blots, excellent antigen for detection of West-Nile virus with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of West Nile virus infected individuals.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    Wnv Pre M
  • View Data Sheet

    Name :

    NAP 2 Human

    Description:

    Neutrophil Activating Protein-2 Human Recombinant (CXCL7)

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-274

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    Description

    Neutrophil Activating Protein-2 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7609 Dalton. The NAP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXCL7 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

    Greater than 97% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL7should 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 Neutrophil Activating Protein-2in 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 Ala-Glu-Leu-Arg-Cys.

    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.

    Nap2 Human
  • View Data Sheet

    Name :

    NPM1 Human

    Description:

    Nucleophosmin Human Recombinant

    Nucleophosmin, NPM, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin, NPM1, NPM, B23.

    Product # :

    PRO-1120

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    Description

    NPM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-294 a.a) and having a molecular mass of 34.7kDa.NPM1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NPM1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleophosmin (NPM1) is a phosphoprotein which shuffles between the nucleus and the cytoplasm. NPM1 is assumed to be involved in a number of processes including regulation of the ARF/p53 pathway. Several genes fusion partners have been described, particularly the anaplastic lymphoma kinase gene on chromosome 2. NPM1 gene mutations are linked with acute myeloid leukemia.

    • Synonyms

      Nucleophosmin, NPM, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin, NPM1, NPM, B23.

    • 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 MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA
      DEDDDDDDEE DDDEDDDDDD FDDEEAEEKA PVKKSIRDTP AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL.

    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.

    Npm1 Human
  • View Data Sheet

    Name :

    NXT1 Human

    Description:

    NTF2-like Export Factor 1 Human Recombinant

    NTF2-like export factor 1, MTR2, Protein P15, NTF2-related export protein 1, NUTF-like export factor 1, NTX2-like export factor1.

    Product # :

    PRO-218

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    Description

    NXT1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140a.a.) and having a molecular mass of 18.0kDa. The NXT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NXT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NXT1 operates as a nuclear export factor in both RAN and CRM1 dependent pathways. NXT1 is known to stimulate the export of U1 snRNA in RAN (Ras-related nuclear protein) and CRM1 (chromosome region maintenance) dependent pathways and the export of tRNA and mRNA in a CRM1-independent pathway. This protein heterodimerizes with Tap protein and regulates the ability of Tap protein to intermediate nuclear mRNA export.

    • Synonyms

      NTF2-like export factor 1, MTR2, Protein P15, NTF2-related export protein 1, NUTF-like export factor 1, NTX2-like export factor1.

    • 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 MASVDFKTYV DQACRAAEEF VNVYYTTMDK RRRLLSRLYM GTATLVWNGN AVSGQESLSE FFEMLPSSEF QISVVDCQPV HDEATPSQTT VLVVICGSVK FEGNKQRDFN QNFILTAQAS PSNTVWKIAS DCFRFQDWAS.

    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.

    Nxt1 Human
  • View Data Sheet

    Name :

    proBDNF Human

    Description:

    Precursor Brain-Derived Neurotrophic Factor Human Recombinant

    proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

    Product # :

    CYT-014

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    Description

    proBDNF Human Recombinant produced in E.Coli is a single, non-glycosylated, non-covalently linked homodimer with each polypeptide chain containing 229 amino acids and having a molecular mass of 52kDa. The proBDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    proBDNF was lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH 8.0 and 500mM NaCl.

    Purity

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

    More Info

    • Introduction

      proBDNF (the precursor form of Brain-derived neurotrophic factor) interacts preferentially with p75NTR (the pan-neurotrophin receptor p75) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, while the mature BDNF selectively binds with great affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. Since proneurotrophins and mature neurotrophins bring forth opposite biological effects, proBDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. proBDNF has an important role in negative regulation of neurotrophic actions in the brain.

    • Synonyms

      proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized proBDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution proBDNF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized proBDNF in sterile 18M-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 Met-Ala-Pro-Met-Lys.

    • Background

      Precursor Brain-Derived Neurotrophic Factor Human Recombinant: Unveiling the Potential of a Key Neurotrophic Factor

      Abstract:

      Precursor Brain-Derived Neurotrophic Factor (proBDNF) human recombinant is a pivotal neurotrophic factor that plays a critical role in neuronal development, survival, and synaptic plasticity. This research paper provides a comprehensive overview of proBDNF, including its characteristics, processing mechanisms, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of proBDNF human recombinant are proposed, highlighting its future implications in the field of neuroregenerative medicine.

      Introduction:

      Understanding the intricate processes underlying neuronal development and function is crucial for advancing neuroregenerative strategies. Neurotrophic factors, such as proBDNF, have garnered significant attention due to their pivotal roles in supporting neuronal growth and survival. This paper delves into the unique features of proBDNF and presents novel approaches for its production and optimization.

      Characteristics and Processing Mechanisms:

      proBDNF is a precursor protein consisting of 247 amino acids and is processed into mature brain-derived neurotrophic factor (mBDNF) through proteolytic cleavage. The ratio between proBDNF and mBDNF is tightly regulated and determines the balance between neuronal survival and apoptosis. Additionally, proBDNF exerts distinct biological functions through its receptor interactions, modulating synaptic plasticity and neuronal activity.

      Production of proBDNF Human Recombinant:

      Efficient production methodologies are essential to harness the therapeutic potential of proBDNF human recombinant. Various expression systems, including bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents unique advantages and challenges, necessitating careful selection to achieve high yields and protein quality. Optimization strategies, such as codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality proBDNF recombinant.

      Potential Therapeutic Applications:

      proBDNF human recombinant holds immense promise for neuroregenerative medicine. Its role in promoting neuronal survival, axonal growth, and synaptic plasticity positions it as a valuable therapeutic agent for neurodegenerative disorders, spinal cord injuries, and stroke. Additionally, the balance between proBDNF and mBDNF presents a potential therapeutic target for fine-tuning neuronal processes and restoring proper brain function.

      Conclusion:

      proBDNF human recombinant represents a crucial neurotrophic factor with diverse therapeutic applications in neuroregenerative medicine. Optimizing production methodologies and further understanding its processing mechanisms will enhance its clinical utility. With its potential implications in neurodegenerative disorders and neuronal repair, proBDNF human recombinant holds immense promise as a transformative tool for promoting neural health and regeneration.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 52kDa.

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

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

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

      What is the amino acid sequence of BDNF Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.

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

      What is the endotoxin level for BDNF Protein?
      The endotoxin level is minimal, BDNF 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.

    Probdnf Human
  • View Data Sheet

    Name :

    SARS-CoV

    Description:

    SARS-CoV Nucleocapsid (422a.a) Recombinant

    Product # :

    SARS-250

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    Description

    The Recombinant SARS-CoV Nucleocapsid Protein is manufactured with N-terminal fusion His Tag. The Recombinant SARS-CoV Nucleocapsid His-Tagged Fusion Protein is 47.8kDa containing 437 amino acid residues of the SARS-CoV Nucleocapsid protein and 16 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia coli.

    Formulation

    Sterile filtered (0,4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.

    • 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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/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.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMSDNG PQSNQRSAPR ITFGGPTDST DNNQNGGRNG ARPKQRRPQG LPNNTASWFT ALTQHGKEEL RFPRGQGVPI NTNSGPDDQI GYYRRATRRV RGGDGKMKEL SPRWYFYYLG TGPEASLPYG ANKEGIVWVA TEGALNTPKD HIGTRNPNNN AATVLQLPQG TTLPKGFYAE GSRGGSQASS RSSSRSRGNS RNSTPGSSRG NSPARMASGG GETALALLLL DRLNQLESKV SGKGQQQQGQ TVTKKSAAEA SKKPRQKRTA TKQYNVTQAF GRRGPEQTQG NFGDQDLIRQ GTDYKHWPQI AQFAPSASAF FGMSRIGMEV TPSGTWLTYH GAIKLDDKDP QFKDNVILLN KHIDAYKTFP PTEPKKDKKK KTDEAQPLPQ RQKKQPTVTL LPAADMDDFS RQLQNSMSGA SADSTQA.

    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.

    product_image.jpg
  • View Data Sheet

    Name :

    RAB11A Human

    Description:

    RAB11A, Member RAS Oncogene Family Human Recombinant

    RAB11, YL8, Ras-related protein Rab-11A, RAB11A.

    Product # :

    PRO-826

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    Description

    RAB11A Human Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 249 amino acids (1-213a.a.) and having a molecular mass of 28.1 kDa. RAB11A protein is fused to a 36 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    RAB11A Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 1mM EDTA & 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAB11A is part of the small GTPase superfamily, Rab family. RAB11A is related with both constitutive and regulated secretory pathways, and takes part in protein transport. RAB11A is a well-known marker for protein trafficking, sorting, and recycling in the endosomal pathway. RAB11A is a main regulator of membrane delivery during cytokinesis.

    • Synonyms

      RAB11, YL8, Ras-related protein Rab-11A, RAB11A.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGTR DDEYDYLFKV VLIGDSGVGK SNLLSRFTRN EFNLESKSTI GVEFATRSIQ VDGKTIKAQI WDTAGQERYR AITSAYYRGA VGALLVYDIA KHLTYENVER WLKELRDHAD SNIVIMLVGN KSDLRHLRAV PTDEARAFAE KNGLSFIETS ALDSTNVEAA FQTILTEIYR IVSQKQMSDR RENDMSPSNN VVPIHVPPTT ENKPKVQCC.

    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.

    Rab11A Human
  • View Data Sheet

    Name :

    NME4 Human

    Description:

    Non-Metastatic Cells 4 Human Recombinant

    Non-metastatic cells 4, nm23-H4, NM23H4, Nucleoside diphosphate kinase D, NDK, NDPKD, NDP kinase mitochondrial, EC 2.7.4.6, NDPK-D.

    Product # :

    PRO-219

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    Description

    NME4 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 176 amino acids (33-187a.a.) and having a molecular mass of 19.6kDa. The NME4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NME4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 40% glycerol and 0.2M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NME4 is a member of the NDK family. NME4 are ubiquitous enzymes which catalyze transfer of gamma-phosphates, using a phosphohistidine intermediate, between nucleoside and dioxynucleoside tri- and diphosphates. The enzymes are products of the nm23 gene family that include NME4. NME4 has a key part in the synthesis of nucleoside triphosphates other than ATP.

    • Synonyms

      Non-metastatic cells 4, nm23-H4, NM23H4, Nucleoside diphosphate kinase D, NDK, NDPKD, NDP kinase mitochondrial, EC 2.7.4.6, NDPK-D.

    • 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 MPSWTRERTL VAVKPDGVQR RLVGDVIQRF ERRGFTLVGM KMLQAPESVL AEHYQDLRRK PFYPALIRYM SSGPVVAMVW EGYNVVRASR AMIGHTDSAE AAPGTIRGDF SVHISRNVIH ASDSVEGAQR EIQLWFQSSE LVSWADGGQH SSIHPA.

    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.

    Nme4 Human
  • View Data Sheet

    Name :

    NPL Human

    Description:

    N-acetylneuraminate Pyruvate Lyase Human Recombinant

    N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.

    Product # :

    ENZ-125

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    Description

    NPL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-320 a.a.) and having a molecular mass of 37.3kDa.NPL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-acetylneuraminate lyase (NPL) is an enzyme which catalyzes the chemical reaction (N-acetylneuraminate ->N-acetyl-D-mannosamine + pyruvate). NPL is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NPL participates in amino sugars metabolism.

    • Synonyms

      N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.

    • 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 MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL KSLDFLSFTD LKDGNLEAGS.

    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.

    Npl Human
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