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Search results

1000 results found for “SNRP”

Name

Description

Product #

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  • View Data Sheet

    Name :

    FCGRT Mouse

    Description:

    Fc Fragment Of IgG Receptor And Transporter Mouse Recombinant

    IgG receptor FcRn large subunit p51, FcRn, IgG Fc fragment receptor transporter alpha chain, Neonatal Fc receptor, Fcgrt, Fcrn.

    Product # :

    PRO-2376

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    Description

    FCGRT Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 285 amino acids (22-297 a.a) and having a molecular mass of 32.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).FCGRT is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fc Fragment Of IgG Receptor And Transporter also known as FCGRT is a transmembrane glycoprotein with structural homology to MHC class 1 proteins. FCGRT is widely expressed in endothelial and epithelial cells and takes a vital part in IgG homeostasis. Moreover, FCGRT is expressed in neutrophils in addition myeloid antigen presenting cells. FCGRT can enhance IgG-meditated phagocytosis as well as antigen presentation by heses cells, however it promotes the degradation of opsonizing IgG rather than returning it to the circulation.

    • Synonyms

      IgG receptor FcRn large subunit p51, FcRn, IgG Fc fragment receptor transporter alpha chain, Neonatal Fc receptor, Fcgrt, Fcrn.

    • 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

      ADPSETRPPL MYHLTAVSNP STGLPSFWAT GWLGPQQYLT YNSLRQEADP CGAWMWENQV SWYWEKETTD LKSKEQLFLE ALKTLEKILN GTYTLQGLLG CELASDNSSV PTAVFALNGE EFMKFNPRIG NWTGEWPETE IVANLWMKQP DAARKESEFL LNSCPERLLG HLERGRRNLE WKEPPSMRLK ARPGNSGSSV LTCAAFSFYP PELKFRFLRN GLASGSGNCS TGPNGDGSFH AWSLLEVKRG DEHHYQCQVE HEGLAQPLTV DLDSSARSSH 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.

    Fcgrt Mouse
  • View Data Sheet

    Name :

    POU5F1 Human, PolyR

    Description:

    POU Class 5 Homeobox 1 Human Recombinant, Polyarginine-Tag

    POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.

    Product # :

    PRO-091

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    Description

    POU5F1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 360 amino acids and having a molecular mass of 38.6kDa.The POU5F1 is fused to a C-terminal poly-arginine tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POU5F1 0.2µm filtered solution in PBS, pH7.4 and 5% glycerol.

    Purity

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

    More Info

    • Introduction

      POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.

    • Synonyms

      POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.

    • 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.Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Gly-His-Leu.

    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.

    Pou5F1 Human Polyr
  • View Data Sheet

    Name :

    TRIM21 Human

    Description:

    Tripartite Motif Containing 21 (RO52) Human Recombinant

    52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.

    Product # :

    PRO-328

    Price :

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    • description
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    Description

    TRIM21 Human Recombinant produced in SF9 is a polypeptide chain having a calculated molecular mass of 52 kDa. TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TRIM21 solution is supplied in 20mM HEPES pH-7.5, 0.01mM EDTA and 0.02% SDS.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.

    • Synonyms

      52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.

    • 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. Avoid multiple freeze-thaw cycles.

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

    Trim21 Human
  • View Data Sheet

    Name :

    RPL12 Human

    Description:

    Ribosomal Protein L12 Human Recombinant

    Ribosomal Protein L12, L12, 60S ribosomal protein L12.

    Product # :

    ENZ-693

    Price :

    Quantity :

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    • description
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    Description

    RPL12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 20.2kDa. RPL12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RPL12 protein solution (0.5mg/ml) containing 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

      Ribosomes, the organelles which catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are comprised of four RNA species and approximately 80 structurally distinct proteins. Ribosomal Protein L12 (RPL12) protein is a member of the L11P family of ribosomal proteins. RPL12 is a component of the 60S subunit, which is located in the cytoplasm. RPL12 binds directly to the 26S rRNA.

    • Synonyms

      Ribosomal Protein L12, L12, 60S ribosomal protein L12.

    • 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 MGSMPPKFDP NEIKVVYLRC TGGEVGATSA LAPKIGPLGL SPKKVGDDIA KATGDWKGLR ITVKLTIQNR QAQIEVVPSA SALIIKALKE PPRDRKKQKN IKHSGNITFD EIVNIARQMR HRSLARELSG TIKEILGTAQ SVGCNVDGRH PHDIIDDINS GAVECPAS.

    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.

    Rpl12 Human
  • View Data Sheet

    Name :

    SARS MERS, Sf9 Active

    Description:

    SARS MERS Spike Recombinant, Sf9 Active

    Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein

    Product # :

    SARS-061

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    • description
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    • biological activity
    • More Info

    Description

    SARS MERS Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1285 amino acids (18-1296 aa) and having a molecular mass of 141.6kDa. SARS MERS is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The SARS MERS solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human DPPIV/CD26 (CAT# enz-1187).

    More Info

    • Synonyms

      Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      YVDVGPDSVK SACIEVDIQQ TFFDKTWPRP IDVSKADGII YPQGRTYSNI TITYQGLFPY QGDHGDMYVY SAGHATGTTP QKLFVANYSQ DVKQFANGFV VRIGAAANST GTVIISPSTS ATIRKIYPAF MLGSSVGNFS DGKMGRFFNH TLVLLPDGCG TLLRAFYCIL EPRSGNHCPA GNSYTSFATY HTPATDCSDG NYNRNASLNS FKEYFNLRNC TFMYTYNITE DEILEWFGIT QTAQGVHLFS SRYVDLYGGN MFQFATLPVY DTIKYYSIIP HSIRSIQSDR KAWAAFYVYK LQPLTFLLDF SVDGYIRRAI DCGFNDLSQL HCSYESFDVE SGVYSVSSFE AKPSGSVVEQ AEGVECDFSP LLSGTPPQVY NFKRLVFTNC NYNLTKLLSL FSVNDFTCSQ ISPAAIASNC YSSLILDYFS YPLSMKSDLS VSSAGPISQF NYKQSFSNPT CLILATVPHN LTTITKPLKY SYINKCSRLL SDDRTEVPQL VNANQYSPCV SIVPSTVWED GDYYRKQLSP LEGGGWLVAS GSTVAMTEQL QMGFGITVQY GTDTNSVCPK LEFANDTKIA SQLGNCVEYS LYGVSGRGVF QNCTAVGVRQ QRFVYDAYQN LVGYYSDDGN YYCLRACVSV PVSVIYDKET KTHATLFGSV ACEHISSTMS QYSRSTRSML KRRDSTYGPL QTPVGCVLGL VNSSLFVEDC KLPLGQSLCA LPDTPSTLTP RSVRSVPGEM RLASIAFNHP IQVDQLNSSY FKLSIPTNFS FGVTQEYIQT TIQKVTVDCK QYVCNGFQKC EQLLREYGQF CSKINQALHG ANLRQDDSVR NLFASVKSSQ SSPIIPGFGG DFNLTLLEPV SISTGSRSAR SAIEDLLFDK VTIADPGYMQ GYDDCMQQGP ASARDLICAQ YVAGYKVLPP LMDVNMEAAY TSSLLGSIAG VGWTAGLSSF AAIPFAQSIF YRLNGVGITQ QVLSENQKLI ANKFNQALGA MQTGFTTTNE AFQKVQDAVN NNAQALSKLA SELSNTFGAI SASIGDIIQR LDVLEQDAQI DRLINGRLTT LNAFVAQQLV RSESAALSAQ LAKDKVNECV KAQSKRSGFC GQGTHIVSFV VNAPNGLYFM HVGYYPSNHI EVVSAYGLCD AANPTNCIAP VNGYFIKTNN TRIVDEWSYT GSSFYAPEPI TSLNTKYVAP QVTYQNISTN LPPPLLGNST GIDFQDELDE FFKNVSTSIP NFGSLTQINT TLLDLTYEML SLQQVVKALN ESYIDLKELG NYTYYNKWPH HHHHH.

    • Background

      Severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) have caused significant outbreaks with severe respiratory illness in recent years. The spike proteins of these viruses play a crucial role in viral entry and host cell recognition. This research aims to explore the structure, function, and implications of SARS and MERS spike proteins in viral pathogenesis and the development of therapeutic interventions. Understanding the mechanisms of viral entry can provide valuable insights into the design of effective antiviral strategies.

      Structure and Function of SARS and MERS Spike Proteins:

      The spike proteins of SARS-CoV and MERS-CoV are trimeric glycoproteins located on the viral surface. They consist of S1 and S2 subunits, with the S1 subunit responsible for receptor binding and the S2 subunit involved in membrane fusion. The spike proteins contain key domains, including the receptor-binding domain (RBD) and the fusion peptide, which mediate the interactions with host cell receptors and membrane fusion during viral entry.

      Interaction with Host Cell Receptors:

      The SARS-CoV spike protein primarily interacts with the angiotensin-converting enzyme 2 (ACE2) receptor, which is expressed in various tissues, including the respiratory tract. The binding of the SARS-CoV spike protein to ACE2 is crucial for viral entry into host cells. Similarly, the MERS-CoV spike protein interacts with the dipeptidyl peptidase 4 (DPP4) receptor, which is predominantly expressed in the lungs and other tissues. These receptor interactions determine the host range and tissue tropism of the viruses.

      Implications for Viral Pathogenesis:

      The interaction between the spike proteins of SARS-CoV and MERS-CoV and their respective receptors initiates a cascade of events leading to viral entry and replication. The binding of the spike protein to the receptor triggers conformational changes that expose the fusion peptide, facilitating membrane fusion and viral entry into host cells. The specificity and affinity of the spike-receptor interaction play a critical role in determining viral tropism, disease severity, and transmission dynamics.

      Therapeutic Strategies Targeting Spike Proteins:

      The spike proteins of SARS-CoV and MERS-CoV present attractive targets for the development of antiviral interventions. Various approaches have been explored, including the development of neutralizing antibodies that specifically target the spike proteins and inhibit viral entry. Additionally, small molecule inhibitors and peptide-based therapeutics are being investigated to disrupt the spike-receptor interaction and block viral entry. Vaccine development efforts have also focused on generating immune responses against the spike proteins to prevent infection.

      Challenges and Future Directions:

      Although significant progress has been made in understanding the structure and function of SARS and MERS spike proteins, several challenges remain. The emergence of novel coronavirus variants necessitates continuous surveillance and adaptation of therapeutic strategies. Additionally, potential cross-reactivity and immunogenicity concerns need to be addressed to ensure the safety and efficacy of spike protein-based therapeutics.

      Conclusion:

      The study of SARS and MERS spike proteins provides valuable insights into the mechanisms of viral entry and pathogenesis. Understanding the interactions between spike proteins and host cell receptors is crucial for the development of effective antiviral strategies. Further research on spike protein structure, receptor binding, and fusion mechanisms is essential to combat current and future coronavirus outbreaks. By unraveling the complexities of viral entry, we can pave the way for the development of novel therapeutics to mitigate the impact of SARS-CoV, MERS-CoV, and related coronaviruses.

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  • View Data Sheet

    Name :

    SARS Nucleocapsid Polyclonal

    Description:

    SARS-Nucleocapsid protein, Polyclonal Antibody

    Product # :

    ANT-180

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    Formulation

    1mg/ml in PBS and 0.02% sodium azide.

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    • 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.
      It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.

    • Stability

      Store at 4°C, stable for 2 weeks. For long-term storage, store at -20°C.

    • Immunogen

      The antibody was developed by immunizing rabbits with synthetic peptides corresponding to amino a.a. 399-411 of putative SARS nucleocapsid (Genbank accession no. YP_009724397.2).

    • Applications

      Western Blot 1:100-1:2000, Immunohistochemistry, Immunocytochemistry/Immunofluorescence 1:10-1:500

    • Isotype

      Rabbit IgG.

    • Type

      Polyclonal Rabbit Antibody.

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    Sars Nucleocapsid Polyclonal Antibody
  • View Data Sheet

    Name :

    S100A4 Human

    Description:

    S100 Calcium-Binding Protein A4 Human Recombinant

    Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.

    Product # :

    PRO-698

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    Description

    S100A4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.8 kDa.The S100A4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A4 protein at in 20mM Tris-HCl, pH-8 & 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      S100A4 is part of the S100 super-family of proteins containing 2 EF-hand calcium binding domains. S100A4 is ubiquitously overexpressed and is localized in the cytoplasm and/or nucleus. S100A4 is involved in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.

    • Synonyms

      Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.

    • 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 MACPLEKALD VMVSTFHKYS GKEGDKFKLN KSELKELLTR ELPSFLGKRT DEAAFQKLMS NLDSNRDNEVDFQEYCVFLS CIAMMCNEFF EGFPDKQPRK K.

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    S100A4 Human His
  • View Data Sheet

    Name :

    SAR1A Human

    Description:

    GTP-Binding Protein SAR1A Human Recombinant

    GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.

    Product # :

    PRO-709

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    Description

    SAR1A Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 218 amino acids (1- 198 a.a.) and having a molecular mass of 24.5kDa.The SAR1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAR1A solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      SAR1A is a member of the small GTPase superfamily. SAR1A is a vital component of COPII vesicle coats involved in export of cargo from the ER (Endoplasmic Reticulum). The GTPase activity of SAR1A serves as a molecular switch to control protein-protein and protein-lipid interactions which dictate vesicle budding from the ER. SAR1A, while GDP-bound interacts with the membrane-bound exchange factor Sec12 and trades its bound GDP for GTP. SAR1A is also involved in the transport from the ER to the Golgi apparatus. SAR1A is required to maintain SEC16A localization at distinct locations on the ER membrane possibly by preventing its dissociation. SAR1A-GTP-dependent compilation of SEC16A on the ER membrane creates a structured scaffold defining endoplasmic reticulum exit sites.

    • Synonyms

      GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.

    • 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 MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHSRLVE SKVELNALMT DETISNVPIL ILGNKIDRTD AISEEKLREI FGLYGQTTGK GNVTLKELNA RPMEVFMCSV LKRQGYGEGF RWLSQYID.

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    Sar1A Human
  • View Data Sheet

    Name :

    Agrin Rat

    Description:

    Agrin Rat Recombinant

    Agrin, Agrn, C90, C22, Agrin N-terminal 110 kDa subunit, Agrin C-terminal 110 kDa subunit, Agrin C-terminal 90 kDa fragment, Agrin C-terminal 22 kDa fragment, AGR

    Product # :

    PRO-2627

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    Description

    Agrin Rat produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 766 amino acids (997-1753 a.a.) and having a molecular mass of 82.5kDa.Agrin is fused to a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Agrin solution (0.5mg/ml) contains 10% Glycerol in Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Agrin or AGRN is a large protein (proteoglycan) that has a crucial part in the development of neuromuscular junction amid embryogenesis. The protein has an involvement in the collection and aggregation of acetylcholine receptors through synaptogenesis. The agrin gene can be found and expressed in rat embryonic nervous system andmuscle tissue. This Agrin protein is aggregated in the synapses, there it can take part in regeneration & development. The protein binds to receptors on the surface of skeletal muscle.

    • Synonyms

      Agrin, Agrn, C90, C22, Agrin N-terminal 110 kDa subunit, Agrin C-terminal 110 kDa subunit, Agrin C-terminal 90 kDa fragment, Agrin C-terminal 22 kDa fragment, AGR

    • 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

      ADPSCYNSPL GCCSDGKTPS LDSEGSNCPA TKAFQGVLEL EGVEGQELFY TPEMADPKSE LFGETARSIE STLDDLFRNS DVKKDFWSVR LRELGPGKLV RAIVDVHFDP TTAFQASDVG QALLRQIQVS RPWALAVRRP LQEHVRFLDF DWFPTFFTGA ATGTTAAMAT ARATTVSRLP ASSVTPRVYP SHTSRPVGRT TAPPTTRRPP TTATNMDRPR TPGHQQPSKS CDSQPCLHGG
      TCQDQDSGKG FTCSCTAGRG GSVCEKVQPP SMPAFKGHSF LAFPTLRAYH TLRLALEFRA LETEGLLLYN GNARGKDFLA LALLDGRVQF RFDTGSGPAV LTSLVPVEPG RWHRLELSRH WRQGTLSVDG ETPVVGESPS GTDGLNLDTN LYVGGIPEEQ VAMVLDRTSV GVGLKGCIRM LDINNQQLEL SDWQRAAVQS SGVGECGDHP CLPNPCHGGA LCQALEAGMF LCQCPPGRFG PTCADEKSPC QPNPCHGAAP CRVLSSGGAK CECPLGRSGT FCQTVLETAG SRPFLADFNG FSYLELKGLH TFERDLGEKM ALEMVFLARG PSGLLLYNGQ KTDGKGDFVS LALHNRHLEF CYDLGKGAAV IRSKEPIALG TWVRVFLERN GRKGALQVGD GPRVLGESPK SRKVPHTMLN LKEPLYIGGA PDFSKLARGA AVSSGFSGVI QLVSLRGHQL LTQEHVLRAV DVSPFADHPC TQALGNPCLN GGSCVPREAT YECLCPGGFS GLHCEKGLVE HHHHHH

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

    Agrin Protein Rat
  • View Data Sheet

    Name :

    AHSP Human

    Description:

    Alpha Hemoglobin Stabilizing Protein Human Recombinant

    Alpha-hemoglobin-stabilizing protein, Erythroid-associated factor, Erythroid differentiation-related factor, AHSP, EDRF, ERAF.

    Product # :

    PRO-720

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    Description

    AHSP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 102 amino acids (1-102 a.a.) and having a molecular mass of 11.8kDa.The AHSP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AHSP protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Alpha-hemoglobin stabilizing protein (AHSP) is an erythroid-specific protein that acts as a chaperone to prevent the aggregation of A-hemoglobin during normal erythroid cell development. AHSP specifically protects free A-hemoglobin from precipitation in live cells and in solution. AHSP is expected to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia. Furthermore, AHSP promotes alpha globin chain stability in human erythropoiesis. In addition, the AHSP stabilizes the alpha-Hb chain, thus avoiding its precipitation and its ability to generate ROS, which is implicated in cell death. AHSP is expressed in blood and bone marrow. AHSP subunit is a monomer, it forms a heterodimer with free alpha-hemoglobin. On the other hand, AHSP does not bind beta-hemoglobin nor alpha2beta2 hemoglobin A. AHSP is downregulated in TSEs (transmissible spongiform encephalopathies).

    • Synonyms

      Alpha-hemoglobin-stabilizing protein, Erythroid-associated factor, Erythroid differentiation-related factor, AHSP, EDRF, ERAF.

    • 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

      MALLKANKDL ISAGLKEFSV LLNQQVFNDP LVSEEDMVTV VEDWMNFYIN YYRQQVTGEP QERDKALQEL RQELNTLANP FLAKYRDFLK SHELPSHPPP SS.

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    Ahsp Human
  • View Data Sheet

    Name :

    SecB

    Description:

    Protein Export Protein SecB Recombinant

    Protein-export protein secB, secB, b3609, JW3584.

    Product # :

    PRO-697

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    Description

    Recombinant E.Coli SecB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids and having a molecular mass of 17.2 kDa. SecB was over-expressed in E. coli and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The SecB protein solution (1mg/ml) contains 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      SecB, a significant chaperone that takes part in protein export, binds various ligands rapidly with high affinity and low specificity. SecB plays an important role during protein export through the general secretory pathway by modulating the partitioning of precursors between folding or aggregation and delivery to the membrane-bound translocation apparatus. SecB has the potential to take part in functions outside of export acting as a universal nonspecific chaperone to provide buffering capacity of the nonnative state of proteins in the cytosolic pool.

    • Synonyms

      Protein-export protein secB, secB, b3609, JW3584.

    • 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

      MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA.

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    Secb
  • View Data Sheet

    Name :

    SEPT6 Human

    Description:

    Septin-6 Human Recombinant

    Septin 6, Septin 2, SEP2, KIAA0128, SEPT2.

    Product # :

    PRO-949

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    Description

    SEPT6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (1-434) and having a molecular mass of 52.1 kDa.SEPT6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SEPT6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      SEPT6 is a member of the septin family of GTPases and is functionally involved in cytokinesis and conservation of cellular morphology. SEPT6 interact with SEPT2. The genes encoding the mixed-lineage leukemia and SEPT2 breakpoint proteins are associated with one type of pediatric acute myeloid leukemia which is caused by reciprocal translocation between chromosomes 11 and X.

    • Synonyms

      Septin 6, Septin 2, SEP2, KIAA0128, SEPT2.

    • 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 MGSMAATDIA RQVGEGCRTV PLAGHVGFDS LPDQLVNKSV SQGFCFNILC VGETGLGKST LMDTLFNTKF EGEPATHTQP GVQLQSNTYD LQESNVRLKL TIVSTVGFGD QINKEDSYKP IVEFIDAQFE AYLQEELKIR RVLHTYHDSR IHVCLYFIAP TGHSLKSLDL VTMKKLDSKV NIIPIIAKAD AISKSELTKF KIKITSELVS NGVQIYQFPT DDESVAEING TMNAHLPFAV IGSTEELKIG NKMMRARQYP WGTVQVENEA HCDFVKLREM LIRVNMEDLR EQTHTRHYEL YRRCKLEEMG FKDTDPDSKP FSLQETYEAK RNEFLGELQK KEEEMRQMFV QRVKEKEAEL KEAEKELHEK FDRLKKLHQD EKKKLEDKKK SLDDEVNAFK QRKTAAELPQ SQGSQAGGSQ TLKRDKEKKN NPWLCTE

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    Sept6 Human
  • View Data Sheet

    Name :

    SERPINB5 Human, His

    Description:

    Serpin Peptidase Inhibitor, Clade B Member 5 Human Recombinant, His tag

    PI5, maspin, SERPINB5, serpin peptidase inhibitor clade B (ovalbumin) member 5, Serpin B5, Protease inhibitor 5.

    Product # :

    PRO-704

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    Description

    SERPINB5 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 395 amino acids (1-375 a.a.) and having a molecular mass of 44.2 kDa.The SERPINB5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINB5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      SERPINB5 (Maspin) is a tumor suppressor protein of the serine proteinase inhibitor family. Maspin plays a vital role in embryonic development through critical functions in cell adhesion. In addition, Maspin is present in normal breast and prostatic epithelial cells although down regulated in the particular carcinomas. SERPINB5 impedes the growth, invasion, and metastatic properties of mammary tumors as well as the invasive ability of pancreatic ductal adenocarcinoma cells. SERPINB5 being a breast tumor suppressor gene is a significant marker of the disease progression in breast neoplasms. Furthermore, high expression of maspin is linked to squamous cell carcinoma in non-small-cell lung cancer. Moreover, maspin expression has been directly linked with the biological aggressiveness of ovarian carcinoma. Maspin exhibits no serine protease inhibitory activity since it does not undergo the stressed to relaxed conformational transition typical of active serpins.

    • Synonyms

      PI5, maspin, SERPINB5, serpin peptidase inhibitor clade B (ovalbumin) member 5, Serpin B5, Protease inhibitor 5.

    • 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 MDALQLANSA FAVDLFKQLC EKEPLGNVLF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF ENVKDVPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL STEFISSTKR PYAKELETVD FKDKLEETKG QINNSIKDLT DGHFENILAD NSVNDQTKILVVNAAYFVGK WMKKFPESET KECPFRVNKT DTKPVQMMNM EATFCMGNID SINCKIMELP FQNKHLSMFI LLPKDVEDES TGLEKIEKQLNSESLSQWTN PSTMANAKVK LSIPKFKVEK MIDPKACLEN LGLKHIFSED TSDFSGMSET KGVALSNVIH KVCLEITEDG GDSIEVPGAR ILQHKDELNA DHPFIYIIRH NKTRNIIFFG KFCSP.

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    Serpinb5 Human
  • View Data Sheet

    Name :

    SERPING1 Human HEK

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant HEK

    C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    Product # :

    PRO-1639

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    Description

    SERPING1 Human Recombinant produced by transfected human cells is a single polypeptide chain containing 486 amino acids (23-500). SERPING1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    SERPING1 was lyophilized from a 0.2 µM filtered solution of 20mM Tris-HCl and 150mM NaCl, pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

    • Synonyms

      C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPING1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPING1 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 SERPING1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTT
      EPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKK
      VETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAI
      RDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTT
      FDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQ
      ALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQ
      HQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFMLWDQQHKFPVFMGRVYDPRAVDHHHHHH

    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.

    Serping1 Human Hek
  • View Data Sheet

    Name :

    NCF4 Human

    Description:

    Neutrophil Cytosolic Factor 4 Human Recombinant

    Neutrophil cytosol factor 4, NCF-4, Neutrophil NADPH oxidase factor 4, SH3 and PX domain-containing protein 4, p40-phox, p40phox, NCF4, SH3PXD4, NCF, SH3PXD4.

    Product # :

    PRO-1258

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    Description

    NCF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-339 a.a) and having a molecular mass of 41.1kDa.NCF4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NCF4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Neutrophil Cytosolic Factor 4 (NCF4) is a cytosolic regulatory factor of the superoxide-producing phagocyte NADPH-oxidase, which is a multicomponent enzyme system imperative for host defense. The NCF4 protein is preferentially expressed in cells of myeloid lineage. NCF4 interacts mainly with neutrophil cytosolic factor 2 (NCF2/p67-phox) to create a complex with neutrophil cytosolic factor (NCF1/p47-phox), which further interacts with the small G protein RAC1 and translocates to the membrane upon cell stimulation. This complex subsequently activates flavocytochrome b, the membrane-integratedcatalytic core of the enzyme system. The PX domain of the NCF4 protein can bind phospholipid products of the PI(3) kinase, suggesting its part in PI(3) kinase-mediated signaling events. The phosphorylation of the NCF4 protein negatively regulates the enzyme activity.

    • Synonyms

      Neutrophil cytosol factor 4, NCF-4, Neutrophil NADPH oxidase factor 4, SH3 and PX domain-containing protein 4, p40-phox, p40phox, NCF4, SH3PXD4, NCF, SH3PXD4.

    • 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 MAVAQQLRAE SDFEQLPDDV AISANIADIE EKRGFTSHFV FVIEVKTKGG SKYLIYRRYR QFHALQSKLE ERFGPDSKSS ALACTLPTLP AKVYVGVKQE IAEMRIPALN AYMKSLLSLP VWVLMDEDVR IFFYQSPYDS EQVPQALRRL RPRTRKVKSV SPQGNSVDRM AAPRAEALFD FTGNSKLELN FKAGDVIFLL SRINKDWLEG TVRGATGIFP LSFVKILKDF PEEDDPTNWL RCYYYEDTIS TIKDIAVEED LSSTPLLKDL LELTRREFQR EDIALNYRDA EGDLVRLLSD EDVALMVRQA RGLPSQKRLF PWKLHITQKD NYRVYNTMP.

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    Ncf4 Human
  • View Data Sheet

    Name :

    SHH Mouse

    Description:

    Sonic Hedgehog Mouse Recombinant

    SHH, HHG-1, HHG1, Sonic hedgehog protein.

    Product # :

    CYT-597

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    Description

    Sonic Hedgehog Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8 kDa. The Mouse Sonic Hedgehog is 99% homologous to the human gene.Cysteine at position 25 has been substituted with Ile.The Sonic HedgeHog is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 10mM Na2PO4 pH-7.5.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by the dose-dependent induction of alkaline phosphatase production by C3H/10T1/2 (CCL-226) fibroblasts and is typically 0.48-0.72 µg/ml.

    More Info

    • Introduction

      Recombinant Mouse Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Mouse Sonic Hedgehog is 99% homologous to the human gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

    • Synonyms

      SHH, HHG-1, HHG1, Sonic hedgehog protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGG.

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    Sonic Hedgehog Mouse
  • View Data Sheet

    Name :

    ARPC3 Human

    Description:

    Actin Related Protein 2/3 Complex, Subunit 3 Human Recombinant

    ARC21, p21-Arc, Actin-related protein 2/3 complex subunit 3, Arp2/3 complex 21 kDa subunit, ARPC3.

    Product # :

    PRO-1413

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    Description

    ARPC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-178 a.a) and having a molecular mass of 22.9kDa. ARPC3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ARPC3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Actin-related protein 2/3 complex subunit 3 (ARPC3) which Belongs to the ARPC3 family is one of 7 subunits of the human Arp2/3 protein complex. The Arp2/3 complex is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. ARPC3 which is localized to the cytoplasm and cytoskeleton, interacts with p20-ARC and takes part in the structural integrity of the protein complex.

    • Synonyms

      ARC21, p21-Arc, Actin-related protein 2/3 complex subunit 3, Arp2/3 complex 21 kDa subunit, ARPC3.

    • 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 MGSMPAYHSS LMDPDTKLIG NMALLPIRSQ FKGPAPRETK DTDIVDEAIY YFKANVFFKN YEIKNEADRT LIYITLYISE CLKKLQKCNS KSQGEKEMYT LGITNFPIPG EPGFPLNAIY AKPANKQEDE VMRAYLQQLR QETGLRLCEK VFDPQNDKPS KWWTCFVKRQ FMNKSLSGPG Q.

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    Arpc3 Human
  • View Data Sheet

    Name :

    NFKBIB Human

    Description:

    NF-kappa-B Inhibitor Beta Human Recombinant

    NF-kappa-B inhibitor beta, NF-kappa-BIB, I-kappa-B-beta, IkB-B, IkB-beta, IkappaBbeta, Thyroid receptor-interacting protein 9, TR-interacting protein 9, TRIP-9, NFKBIB, IKBB, TRIP9.

    Product # :

    PRO-1046

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    Description

    NFKBIB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-356 a.a) and having a molecular mass of 40.3kDa (Molecular weight on SDS-PAGE will appear higher).NFKBIB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      NF-kappa-B inhibitor beta (NFKBIB) is a member of the NF-kappa-B inhibitor family, which inhibit NF-kappa-B by complexing with, and trapping it in the cytoplasm. Phosphorylation of serine residues on these proteins by kinases marks them for destruction via the ubiquitination pathway, thus allowing activation of the NF-kappa-B, which translocates to the nucleus to act as a transcription factor.

    • Synonyms

      NF-kappa-B inhibitor beta, NF-kappa-BIB, I-kappa-B-beta, IkB-B, IkB-beta, IkappaBbeta, Thyroid receptor-interacting protein 9, TR-interacting protein 9, TRIP-9, NFKBIB, IKBB, TRIP9.

    • 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 MGSHMAGVAC LGKAADADEW CDSGLGSLGP DAAAPGGPGL GAELGPGLSW APLVFGYVTE DGDTALHLAV IHQHEPFLDF LLGFSAGTEY MDLQNDLGQT ALHLAAILGE TSTVEKLYAA GAGLCVAERR GHTALHLACR VGAHACARAL LQPRPRRPRE
      APDTYLAQGP DRTPDTNHTP VALYPDSDLE KEEEESEEDW KLQLEAENYE GHTPLHVAVI HKDVEMVRLL RDAGADLDKP EPTCGRSPLH LAVEAQAADV LELLLRAGAN PAARMYGGRT PLGSAMLRPN PILARLLRAH GAPEPEGEDE KSGPCSSSSD SDSGDEGDEY DDIVVHSSRS QTRLPPTPAS KPLPDDPRPV.

    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.

    Nfkbib Human
  • View Data Sheet

    Name :

    NFU1 Human

    Description:

    NFU1 Human Recombinant

    CGI-33, HIRIP, HIRIP5, MMDS1, Nfu, NifU, NIFUC, NFU1 iron-sulfur cluster scaffold homolog, mitochondrial, HIRA-interacting protein 5.

    Product # :

    PRO-2129

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    Description

    NFU1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 268 amino acids (10-254 a.a) and having a molecular mass of 29.9kDa.NFU1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NFU1 protein solution (0.5mg/ml) containing Phosphate buffer saline (pH 7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      NFU1 is a protein which is localized to mitochondria and plays a vital role in iron-sulfur cluster biogenesis. The NFU1 protein constructs and transfers 4Fe-4S clusters to target apoproteins including succinate dehydrogenase and lipoic acid synthase. NFU1 gene mutations cause multiple mitochondrial dysfunctions syndrome-1, and pseudogenes of the NFU1 gene are located on the short arms of chromosomes 1 and 3.

    • Synonyms

      CGI-33, HIRIP, HIRIP5, MMDS1, Nfu, NifU, NIFUC, NFU1 iron-sulfur cluster scaffold homolog, mitochondrial, HIRA-interacting protein 5.

    • 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 MGSGAAAVAA GLRRRFCHML KNPYTIKKQP LHQFVQRPLF PLPAAFYHPV RYMFIQTQDT PNPNSLKFIP GKPVLETRTM DFPTPAAAFR SPLARQLFRI EGVKSVFFGP DFITVTKENE ELDWNLLKPD IYATIMDFFA SGLPLVTEET PSGEAGSEED DEVVAMIKEL LDTRIRPTVQ EDGGDVIYKG FEDGIVQLKL QGSCTSCPSS IITLKNGIQN MLQFYIPEVE GVEQVMDDES DEKEANSP.

    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.

    Nfu1 Human
  • View Data Sheet

    Name :

    NOV Mouse

    Description:

    Nephroblastoma Overexpressed Mouse Recombinant

    Protein NOV homolog, NovH, CCN family member 3, Nephroblastoma-overexpressed gene protein homolog, Nov, Ccn3, C130088N23Rik.

    Product # :

    CYT-171

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    Description

    NOV Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 333 amino acids and having a molecular mass of 36.4kDa.The NOV is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NOV protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.5 and 150mM NaCl.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 μg/ml, corresponding to a specific activity of > 1000 IU/mg.

    More Info

    • Introduction

      Nephroblastoma Overexpressed (NOV) is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein is comprised of 4 structural domains, which present distinct, and sometimes opposing, biological activities. An elevated expression of NOV is linked with certain tumors, including Wilm’s tumor and most nephroblastomas. On the other hand, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is associated with decreased NOV expression.

    • Synonyms

      Protein NOV homolog, NovH, CCN family member 3, Nephroblastoma-overexpressed gene protein homolog, Nov, Ccn3, C130088N23Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QVSASLRCPS RCPPKCPSIS PTCAPGVRSV LDGCSCCPVC ARQRGESCSE MRPCDQSSGL YCDRSADPNN QTGICMVPEG DNCVFDGVIY RNGEKFEPNC QYFCTCRDGQ IGCLPRCQLD VLLPGPDCPA PRKVAVPGEC CEKWTCGSDE QGTQGTLGGL ALPAYRPEAT VGVEVSDSSI NCIEQTTEWS ACSKSCGMGV STRVTNRNRQ CEMVKQTRLC IVRPCEQEPE EVTDKKGKKC LRTKKSLKAI HLQFENCTSL YTYKPRFCGV CSDGRCCTPH NTKTIQVEFQ CLPGEIIKKP VMVIGTCTCY SNCPQNNEAF LQDLELKTSR GEI.

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    Nov Mouse
  • View Data Sheet

    Name :

    SOD1 Human

    Description:

    Superoxide Dismutase 1 Human Recombinant

    Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.

    Product # :

    PRO-648

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    Description

    Recombinant Human Cu/Zn Superoxide Dismutase produced in E.Coli is a single monomeric non-glycosylated polypeptide chain containing 154 amino acids and having a total molecular mass of 15.9 kDa.The SOD1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOD1 filtered solution (1mg/ml) contains 20mM Tris-HCl pH-7.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 500 units/mg, in which one unit will inhibit the rate of reduction of cytochrome c by 50% in a coupled system, using xanthine and Xanthine oxidase at pH 7.8 at 25°C.

    More Info

    • Introduction

      Human Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. SOD1 binds copper and zinc ions and is 1 of 3 isozymes accountable for destroying free superoxide radicals in the body. The encoded protein neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis.

    • Synonyms

      Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.

    • 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

      MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVIGIAQ.

    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.

    Sod1 Human
  • View Data Sheet

    Name :

    SOD2 Human

    Description:

    Superoxide Dismutase-2 Human Recombinant

    MNSOD, MVCD6, IPOB, Mn superoxide dismutase, EC=1.15.1.1.

    Product # :

    PRO-819

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    Description

    SOD2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 219 amino acids (25-222 a.a.) and having a molecular mass of 24.4kDa. SOD2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SOD2 Human solution containing 20mM Tris-HCl pH-8 & 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,200 units/mg, in which one unit will inhibit the rate of reduction of cytochrome c by 50% in a coupled system, using xanthine and Xanthine oxidase at pH 7.8 at 25C in a 1.5 ml reaction volume.

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    • Introduction

      SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems.

    • Synonyms

      MNSOD, MVCD6, IPOB, Mn superoxide dismutase, EC=1.15.1.1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKHSLPDLPY DYGALEPHIN AQIMQLHHSK HHAAYVNNLN VTEEKYQEAL AKGDVTAQIA LQPALKFNGG GHINHSIFWT NLSPNGGGEP KGELLEAIKR DFGSFDKFKE KLTAASVGVQ GSGWGWLGFN KERGHLQIAA CPNQDPLQGT TGLIPLLGID VWEHAYYLQY KNVRPDYLKA IWNVINWENV TERYMACKK.

    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.

    Sod2 Human
  • View Data Sheet

    Name :

    NUDCD2 Human

    Description:

    NudC Domain Containing 2 Human Recombinant

    NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 2.

    Product # :

    PRO-1881

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    Description

    NUDCD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (1-157 a.a) and having a molecular mass of 20kDa.NUDCD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUDCD2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      NudC Domain Containing 2 also known as NUDCD2 contains 1 CS domain and interacts with LIS1. NUDCD2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone.

    • Synonyms

      NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSAPFEE RSGVVPCGTP WGQWYQTLEE VFIEVQVPPG TRAQDIQCGL QSRHVALSVG GREILKGKLF DSTIADEGTW TLEDRKMVRI VLTKTKRDAA NCWTSLLESE YAADPWVQDQ MQRKLTLERF QKENPGFDFS GAEISGNYTK GGPDFSNLEK

    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.

    Nudcd2 Human
  • View Data Sheet

    Name :

    NUDT16 Human

    Description:

    Nudix Type Motif 16 Human Recombinant

    Nudix (nucleoside diphosphate linked moiety X)-Type Motif 16, FLJ31265, FLJ34034, FLJ36248, U8 snoRNA-binding protein H29K, U8 snoRNA-decapping enzyme.

    Product # :

    ENZ-053

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NUDT16 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids (1-195a.a.) and having a molecular mass of 23.4kDa.NUDT16 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT16 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      NUDT16 is nuclear nucleoside diphosphatase proteins restricted in foci in the nucleolus and nucleoplasm. NUDT16 is a RNA-decapping enzyme. It binds specifically to U8 snoRNA and can remove m7G and m227G caps from RNAs, rendering them substrates for 5’-3’ exonucleases for degradation in vivo.

    • Synonyms

      Nudix (nucleoside diphosphate linked moiety X)-Type Motif 16, FLJ31265, FLJ34034, FLJ36248, U8 snoRNA-binding protein H29K, U8 snoRNA-decapping enzyme.

    • 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.Please avoid freeze thaw cycles

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGARRLELG EALALGSGWR HACHALLYAP DPGMLFGRIP LRYAILMQMR FDGRLGFPGG FVDTQDRSLE DGLNRELREE LGEAAAAFRV ERTDYRSSHV GSGPRVVAHF YAKRLTLEEL LAVEAGATRA KDHGLEVLGL VRVPLYTLRD GVGGLPTFLE NSFIGSAREQ LLEALQDLGL LQSGSISGLK IPAHH

    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.

    Nudt16 Human
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