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Search results

1000 results found for “septin”

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  • View Data Sheet

    Name :

    STIP1 Human, His

    Description:

    Stress-Induced-Phosphoprotein 1 Human Recombinant, His Tag

    HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.

    Product # :

    PRO-753

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    Description

    Recombinant Human STIP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543 a.a) and having a molecular mass of 64.8kDa. STIP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The STIP1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM DTT, 1mM EDTA, 0.2mM PMSF and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

    • Synonyms

      HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPDWGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLRNKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDKAKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH TPDVLKKCQQAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC QLEPTFIKGYTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.

    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.

    Stip1 Human
  • View Data Sheet

    Name :

    ErbB3 Human, sf9

    Description:

    Tyrosine Kinase ErbB-3 Human Recombinant, sf9

    Tyrosine Kinase ErbB-3, sf9, ErbB3 sf9, Receptor tyrosine-protein kinase erbB-3, ERBB3, Proto-oncogene-like protein c-ErbB-3, Tyrosine kinase-type cell surface receptor HER3, HER3, Receptor tyrosine-protein kinase erbB-3 isoform, c-erbB-3, ErbB-3, erbB3-S, LCCS2, MDA-BF-1, p180-ErbB3, p45-sErbB3, p85-sErbB3.

    Product # :

    PKA-081

    Price :

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    Description

    ErbB3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 863 amino acids (20-643 a.a.) and having a molecular mass of 95.6kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).ErbB3 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ErbB3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.

    • Synonyms

      Tyrosine Kinase ErbB-3, sf9, ErbB3 sf9, Receptor tyrosine-protein kinase erbB-3, ERBB3, Proto-oncogene-like protein c-ErbB-3, Tyrosine kinase-type cell surface receptor HER3, HER3, Receptor tyrosine-protein kinase erbB-3 isoform, c-erbB-3, ErbB-3, erbB3-S, LCCS2, MDA-BF-1, p180-ErbB3, p45-sErbB3, p85-sErbB3.

    • 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

      SEVGNSQAVC PGTLNGLSVT GDAENQYQTL YKLYERCEVV MGNLEIVLTG HNADLSFLQW IREVTGYVLV AMNEFSTLPL PNLRVVRGTQ VYDGKFAIFV MLNYNTNSSH ALRQLRLTQL TEILSGGVYI EKNDKLCHMD TIDWRDIVRD RDAEIVVKDN GRSCPPCHEV CKGRCWGPGS EDCQTLTKTI CAPQCNGHCF GPNPNQCCHD ECAGGCSGPQ DTDCFACRHF NDSGACVPRC PQPLVYNKLT FQLEPNPHTK YQYGGVCVAS CPHNFVVDQT SCVRACPPDK MEVDKNGLKM CEPCGGLCPK ACEGTGSGSR FQTVDSSNID GFVNCTKILG NLDFLITGLN GDPWHKIPAL DPEKLNVFRT VREITGYLNI QSWPPHMHNF SVFSNLTTIG GRSLYNRGFS LLIMKNLNVT SLGFRSLKEI SAGRIYISAN RQLCYHHSLN WTKVLRGPTE ERLDIKHNRP RRDCVAEGKV CDPLCSSGGC WGPGPGQCLS CRNYSRGGVC VTHCNFLNGE PREFAHEAEC FSCHPECQPM EGTATCNGSG SDTCAQCAHF RDGPHCVSSC PHGVLGAKGP IYKYPDVQNE CRPCHENCTQ GCKGPELQDC LGQTLVLIGK THLTRSPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

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

    Erbb3 Human Sf9
  • View Data Sheet

    Name :

    LGMN Mouse

    Description:

    Legumain Mouse Recombinant

    Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.

    Product # :

    ENZ-933

    Price :

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    • sds-page

    Description

    LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (18-435a.a.) and having a molecular mass of 48.6kDa. LGMN is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    LGMN Mouse sds-page - Product image 1

    More Info

    • Introduction

      Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.

    • Synonyms

      Legumain, Asparaginyl endopeptidase, Protease, cysteine 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

      VPVGVDDPED GGKHWVVIVA GSNGWYNYRH QADACHAYQI IHRNGIPDEQ IIVMMYDDIA NSEENPTPGV VINRPNGTDV YKGVLKDYTG EDVTPENFLA VLRGDAEAVK GKGSGKVLKS GPRDHVFIYF TDHGATGILV FPNDDLHVKD LNKTIRYMYE HKMYQKMVFY IEACESGSMM NHLPDDINVY ATTAANPKES SYACYYDEER GTYLGDWYSV NWMEDSDVED LTKETLHKQY HLVKSHTNTS HVMQYGNKSI STMKVMQFQG MKHRASSPIS LPPVTHLDLT PSPDVPLTIL KRKLLRTNDV KESQNLIGQI QQFLDARHVI EKSVHKIVSL LAGFGETAER HLSERTMLTA HDCYQEAVTH FRTHCFNWHS VTYEHALRYL YVLANLCEAP YPIDRIEMAM DKVCLSHYLE 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.

    Lgmn Mouse
  • View Data Sheet

    Name :

    METAP1 Human

    Description:

    Methionyl Aminopeptidase 1 Human Recombinant

    Methionine aminopeptidase 1, MAP 1, MetAP 1, Peptidase M 1, METAP1, KIAA0094, MAP1A, MetAP1A.

    Product # :

    ENZ-604

    Price :

    Quantity :

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    • description
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    Description

    METAP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386) and having a molecular mass of 45.7kDa.METAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The METAP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 3mM DTT, 40% glycerol, 200mM NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Methionine aminopeptidase 1 (METAP1) is a member of the peptidase M24A family. METAP1 removes the amino-terminal methionine from nascent proteins. METAP1 releases N-terminal amino acids, preferentially methionine, from peptides and arylamides. METAP1 is essential for normal progression through the cell cycle. The active site of METAP1 contains 2 adjacent divalent metal ions linked by a water molecule or hydroxide ion.

    • Synonyms

      Methionine aminopeptidase 1, MAP 1, MetAP 1, Peptidase M 1, METAP1, KIAA0094, MAP1A, MetAP1A.

    • 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 MGSMAAVETR VCETDGCSSE AKLQCPTCIK LGIQGSYFCS QECFKGSWAT HKLLHKKAKD EKAKREVSSW TVEGDINTDP WAGYRYTGKL RPHYPLMPTR PVPSYIQRPD YADHPLGMSE SEQALKGTSQ IKLLSSEDIE GMRLVCRLAR EVLDVAAGMI
      KPGVTTEEID HAVHLACIAR NCYPSPLNYY NFPKSCCTSV NEVICHGIPD RRPLQEGDIV NVDITLYRNG YHGDLNETFF VGEVDDGARK LVQTTYECLM QAIDAVKPGV RYRELGNIIQ KHAQANGFSV VRSYCGHGIH KLFHTAPNVP HYAKNKAVGV MKSGHVFTIE PMICEGGWQD
      ETWPDGWTAV TRDGKRSAQF EHTLLVTDTG CEILTRRLDS ARPHFMSQF.

    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.

    Metap1 Human
  • View Data Sheet

    Name :

    CRYZ Human

    Description:

    Crystallin Zeta Human Recombinant

    Quinone oxidoreductase, NADPH:quinone reductase, Zeta-crystallin, CRYZ, Quinone oxidoreductase isoform a, Crystallin, zeta (quinone reductase), Crystallin Zeta.

    Product # :

    PRO-2016

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    Description

    CRYZ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329 a.a.) and having a molecular mass of 37.6kDa.CRYZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Crystallin Zeta, also known as CRYZ, Binds NADP and participates in a one-electron transfer process. CRYZ takes part in the detoxification of xenobiotics and Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. CRYZ improves the mRNA coding for BCL2.

    • Synonyms

      Quinone oxidoreductase, NADPH:quinone reductase, Zeta-crystallin, CRYZ, Quinone oxidoreductase isoform a, Crystallin, zeta (quinone reductase), Crystallin Zeta.

    • 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 MGSMATGQKL MRAVRVFEFG GPEVLKLRSD IAVPIPKDHQ VLIKVHACGV NPVETYIRSG TYSRKPLLPY TPGSDVAGVI EAVGDNASAF KKGDRVFTSS TISGGYAEYA LAADHTVYKL PEKLDFKQGA AIGIPYFTAY RALIHSACVK AGESVLVHGA SGGVGLAACQ IARAYGLKIL GTAGTEEGQK IVLQNGAHEV FNHREVNYID KIKKYVGEKG IDIIIEMLAN VNLSKDLSLL SHGGRVIVVG SRGTIEINPR DTMAKESSII GVTLFSSTKE EFQQYAAALQ AGMEIGWLKP VIGSQYPLEK VAEAHENIIH GSGATGKMIL LL.

    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.

    Cryz Human
  • View Data Sheet

    Name :

    CSTF1 Human

    Description:

    Cleavage Stimulation Factor 1 Human Recombinant

    Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

    Product # :

    PRO-1170

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    Description

    CSTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-431 a.a) and having a molecular mass of 49.4kDa.CSTF1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSTF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.

    • Synonyms

      Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

    • 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

      MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DVEHHHHHH.

    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.

    Cstf1 Human
  • View Data Sheet

    Name :

    SERPINB5 Human

    Description:

    Serpin Peptidase Inhibitor, Clade B Member 5 Human Recombinant

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

    Product # :

    PRO-202

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    Description

    SERPINB5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 375 amino acids and having a molecular mass of 42.2 KDa.The SERPINB5 Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.0.

    Purity

    Greater than 97.0% as determined by
    (a) Analysis by HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • 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 White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPINB5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPINB5 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 SERPINB5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MDALQLANSA FAVDLFKQLC EKEPLGNVLF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF ENVKDIPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL STEFISSTKR PYAKELETVD FKDKLEETKG QINNSIKDLT DGHFENILAD NSVNDQTKIL VVNAAYFVGK WMKKFPESET KECPFRLNKT DTKPVQMMNM EATFCMGNID SINCKIIELP FQNKHLSMFI LLPKDVEDES TGLEKIEKQL NSESLSQWTN PSTMANAKVK LSIPKFKVEK MIDPKACLEN LGLKHIFSED TSDFSGMSET KGVALSNVIH KVCLEITEDG GDSIEVPGAR ILQHKDELNA DHPFIYIIRH NKTRNIIFFG KFCSP.

    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.

    Maspin Human
  • View Data Sheet

    Name :

    STIP1 Human

    Description:

    Stress-Induced-Phosphoprotein 1 Human Recombinant

    Stress Induced Phosphoprotein 1, Transformation-Sensitive Protein IEF SSP 3521, Renal Carcinoma Antigen NY-REN-11, Stress-Induced-Phosphoprotein 1, Hsp70/Hsp90-Organizing Protein, Hsc70/Hsp90-Organizing Protein, STI1, HOP, Epididymis Secretory Sperm Binding Protein Li 94n, NY-REN-11 Antigen, IEF-SSP-3521, HEL-S-94n, STI1L, P60.

    Product # :

    PRO-2334

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    Description

    STIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 543 amino acids (1-543 a.a) and having a molecular mass of 62.6kDa. STIP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STIP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

    • Synonyms

      Stress Induced Phosphoprotein 1, Transformation-Sensitive Protein IEF SSP 3521, Renal Carcinoma Antigen NY-REN-11, Stress-Induced-Phosphoprotein 1, Hsp70/Hsp90-Organizing Protein, Hsc70/Hsp90-Organizing Protein, STI1, HOP, Epididymis Secretory Sperm Binding Protein Li 94n, NY-REN-11 Antigen, IEF-SSP-3521, HEL-S-94n, STI1L, P60.

    • 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

      MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLR NKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDK AKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.

    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.

    Human Stip1
  • View Data Sheet

    Name :

    EXOSC7 Human

    Description:

    Exosome Component 7 Human Recombinant

    Exosome Component 7, RRP42, Ribosomal RNA-Processing Protein 42, P8, Exosome Complex Exonuclease RRP42, Exosome Complex Component RRP42, KIAA0116, HRrp42p, EAP1.

    Product # :

    PRO-2144

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    Description

    EXOSC7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-291 a.a.) and having a molecular mass of 34.2kDa.EXOSC7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EXOSC7 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EXOSC7, a component of the RNA exosome complex, is a member of the RNase PH family. EXOSC7 takes part is several pathways such as transfer to a nascent protein and Unfolded Protein Response and Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO). A significant paralog of this gene is EXOSC9.

    • Synonyms

      Exosome Component 7, RRP42, Ribosomal RNA-Processing Protein 42, P8, Exosome Complex Exonuclease RRP42, Exosome Complex Component RRP42, KIAA0116, HRrp42p, EAP1.

    • 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 MGSMASVTLS EAEKVYIVHG VQEDLRVDGR GCEDYRCVEV ETDVVSNTSG SARVKLGHTD ILVGVKAEMG TPKLEKPNEG YLEFFVDCSA SATPEFEGRG GDDLGTEIAN TLYRIFNNKS SVDLKTLCIS PREHCWVLYV DVLLLECGGN LFDAISIAVK AALFNTRIPR VRVLEDEEGS KDIELSDDPY DCIRLSVENV PCIVTLCKIG YRHVVDATLQ EEACSLASLL VSVTSKGVVT CMRKVGKGSL DPESIFEMME TGKRVGKVLH ASLQSVVHKE ESLGPKRQKV GFLG

    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.

    Exosc7 Human
  • View Data Sheet

    Name :

    PLGF1 Human, Sf9

    Description:

    Placental Growth Factor-1 Human Recombinant, Sf9

    PIGF, PGF, PLGF-1.

    Product # :

    CYT-419

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    Description

    Placenta Growth Factor-1 Human Recombinant produced in insect cells is a homodimer, glycosylated polypeptide chain containing 2 x 131 amino acids and having a total molecular mass of approximately 34 kDa. The PLGF-1 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 50mM acetic acid.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to bind to immobilized rh-sFlt-1 in a functional ELISA. PlGF-1 human Recombinant can bind to immobilized rh-sFlt-1 (100ng/well) with a linear range at 0.5-10ng/ml, corresponding to a Specific Activity of 1x105-2x106units/mg.

    More Info

    • Introduction

      PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.

    • Synonyms

      PIGF, PGF, PLGF-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Placenta Growth Factor 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF1 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 Placenta Growth Factor 1 in sterile 0.1M acetic acid 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-Leu-Pro-Ala-Val.

    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.

    Pigf Human
  • View Data Sheet

    Name :

    PLGF3 Human, sf9

    Description:

    Placental Growth Factor-3 Human Recombinant, sf9

    Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.

    Product # :

    CYT-961

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    Description

    PLGF3 Human Recombinant produced in Spodoptera frugiperda is a glycosylated homodimer containing 2 chains of 203 amino acids (Leu19-Arg221) and having a molecular mass of 58kDa.The PLGF-3 is purified by proprietary chromatographic techniques.

    Source

    Spodoptera frugiperda.

    Formulation

    PLGF-3 protein was lyophilized from a 0.2µm filtered solution in HCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its binding ability to rHuVEGF R1 in a functional ELISA, is less than 3ng/ml.

    More Info

    • Introduction

      PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.

    • Synonyms

      Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PLGF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF-3 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 PLGF3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Plgf3 Human
  • View Data Sheet

    Name :

    Latexin Human

    Description:

    Latexin Human Recombinant

    LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    Product # :

    ENZ-407

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    Description

    Recombinant Human Latexin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids and having a molecular mass of 25.7kDa. Latexin is purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Latexin protein solution contains 20mM Tris-HCl, pH-7.5, 50mM NaCl and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.

    • Synonyms

      LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    • 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

      MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYRLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFTFEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDYTILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE.

    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.

    Latexin Human
  • View Data Sheet

    Name :

    GMNN Human

    Description:

    Geminin Human Recombinant

    GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    Product # :

    PRO-579

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    Description

    Geminin Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris pH 8, 100mM NaCl and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.

    • Synonyms

      GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    • 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 KDRWGSMNPS MKQKQEEIKE NIKNSSVPRR TLKMIQPSAS GSLVGRENEL SAGLSKRKHR NDHLTSTTSS PGVIVPESSE NKNLGGVTQE SFDLMIKENP SSQYWKEVAE KRRKALYEAL KENEKLHKEI EQKDNEIARL KKENKELAEV AEHVQYMAEL IERLNGEPLD NFESLDNQEF DSEEETVEDS LVEDSEIGTC AEGTVSSSTD
      AKPCI.

    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.

    Geminin Human
  • View Data Sheet

    Name :

    GrpE E.Coli

    Description:

    HSP-70 Cofactor (HSP24) E.Coli Recombinant

    HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    Product # :

    HSP-014

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    Description

    GrpE Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids and having a molecular mass of 21.8 kDa. The GrpE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSP24 protein solution contains 20mM Tris-HCl pH-8 and 0.1M NaCl.

    Purity

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

    More Info

    • Introduction

      GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

    • Synonyms

      HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    • 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

      MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKIANLEAQ LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA.

    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.

    Grpe Ecoli
  • View Data Sheet

    Name :

    PTX3 Human

    Description:

    Pentraxin-3 Human Recombinant

    TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

    Product # :

    PRO-694

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    Description

    Recombinant Human PTX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (18-381 a.a) and having a molecular mass of 44.4 kDa. PTX3 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTX3 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.

    • Synonyms

      TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

    • 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 KDRWGSMENS DDYDLMYVNL DNEIDNGLHP TEDPTPCDCG QEHSEWDKLF IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA RPCAPGAPAE ARLTSALDEL LQATRDAGRR LARMEGAEAQ RPEEAGRALA AVLEELRQTR ADLHAVQGWA ARSWLPAGCE TAILFPMRSK KIFGSVHPVR PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL SYQSIVFVVG GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE TGGAESCHIR GNIVGWGVTE IQPHGGAQYV S.

    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.

    Ptx3 Human
  • View Data Sheet

    Name :

    CPLX1 Human

    Description:

    Complexin-1 Human Recombinant

    CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.

    Product # :

    PRO-645

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    Description

    CPLX1 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 154 amino acids (1-134 a.a) and having a molecular mass of 17.1kDa (molecular weight on SDS-PAGE will appear higher).The CPLX1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CPLX1protein solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 90% by SDS-PAGE.

    More Info

    • Introduction

      CPLX1 is part of the SNARE family complex binding proteins that are catalysts or inhibitors of vesicle exocytosis. CPLX1 shows reduced Ca2+-triggered fast neurotransmitter release at hippocampal glutamatergic synapses, indicating that CPLX1 is a positive regulator of transmitter release. In contrast, CPLX1 inhibits SNARE-mediated liposome and cell fusions in vitro, that result in hypothesis thus acts as a fusion clamp of synaptic exocytosis. CPLX1 regulates a late step in synaptic vesicle exocytosis.

    • Synonyms

      CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.

    • 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 MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE AVRQGIRDKYGIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV IKYLPGPLQD MLKK.

    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.

    Cplx1 Human
  • View Data Sheet

    Name :

    DEFB116 Human

    Description:

    Beta Defensin 116 Human Recombinant

    Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.

    Product # :

    CYT-713

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    • sds-page

    Description

    DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    sds-page

    DEFB116-sds-page - Product image 1

    More Info

    • Introduction

      Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.

    • Synonyms

      Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.

    • 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 MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.

    • Background

      Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications

      Abstract:


      Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.

      Introduction:


      Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.

      Production and Characterization:


      Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.

      Antimicrobial Properties:


      BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.

      Therapeutic Implications:


      The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.

      Conclusion:


      Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.

      What is the molecular weight/Mw of DEFB116 Protein?
      DEFB116 Protein has a total Mw of 11.5kDa.

      What is the source or expression system of DEFB116 Protein?
      Escherichia Coli.

      What is the Purity of DEFB116 Protein?
      DEFB116 Protein is >80% pure as determined by SDS-PAGE.

      What is the Biological Activity of DEFB116 Protein?
      The biological functionality of DEFB116 Protein will be determined in the future.

      What is the amino acid sequence of DEFB116 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.

      What applications can DEFB116 Protein be used in?
      DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for DEFB116 Protein?
      The endotoxin level is minimal, DEFB116 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.

    Defb116 Human
  • View Data Sheet

    Name :

    Fibronectin Human

    Description:

    Fibronectin Human

    Product # :

    PRO-448

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    Description

    Human Fibronectin produced purified from Human Plasma having a Molecular Weight of 440kDa.

    Source

    Human Plasma.

    Formulation

    The Fibronectin was lyophilized from a non sterile 2mg/ml buffer of 10mM sodium phosphate, pH 7.5 and 0.15M NaCl.

    Purity

    ≥ 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin plays a role in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. Fibronectin consists in two main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the extracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin also takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      We suggest reconstituting the 1mg Fibronectin with a chaotropic agent such as urea at room temperature at a concentration of 0.2mg/ml using sterile water. Let stand 1-2 hours. The recommended concentration is 4M-5M urea.

      When using the protein as an attachment factor, wash the urea off after attaching the fibronectin to the growth surface (plate or dish).

    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.

    Fibronectin Human
  • View Data Sheet

    Name :

    Midkine Human

    Description:

    Midkine Human Recombinant

    NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    Product # :

    CYT-192

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    Description

    Midkine Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids and having a molecular mass of 13.4kDa. The Midkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml corresponding to a specific activity of 100,000-10,000,000IU/mg.

    More Info

    • Introduction

      Midkine (MK) is the product of a retinoic acid responsive gene. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
      Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
      The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
      Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
      Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
      Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

    • Synonyms

      NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAKKKDKVKK GGPGSECAEW AWGPCTPSSK DCGVGFREGT CGAQTQRIRC RVPCNWKKEF GADCKYKFEN WGACDGGTGT KVRQGTLKKA RYNAQCQETI RVTKPCTPKT KAKAKAKKGK GKD.

    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.

    Midkine Human
  • View Data Sheet

    Name :

    HSP90B1 Human, HEK

    Description:

    Heat Shock Protein 90kDa Beta (GRP94) Member 1 Human Recombinant, HEK

    ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.

    Product # :

    HSP-061

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    Description

    HSP90B1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asp22-Glu798) containing a total of 789 amino acids, having a calculated molecular mass of 90.9kDa. HSP90B1 is fused to a 2 aa N-terminal linker, a 4 aa C-terminal linker and a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    HSP90B1 was filtered (0.4 µm) and lyophilized in phosphate buffered saline (PBS) pH 8.0, 1% (w/v) Sucrose and 4% (w/v) Mannitol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSP90B1 is an abundant molecular chaperone resident endoplasmic reticulum (ER) lumenal stress protein which is part of the Hsp90 family. HSP90B1 is involved in maintaining protein homeostasis in the secretory pathway as well as functioning in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. HSP90B1 has key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90B1 protein associates with numerous cochaperones and involved in folding of newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is highly expressed in human gastric carcinoma BGC-823 cells during the whole cell cycle.

    • Synonyms

      ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. HSP90B1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      ASDDEVDVDG TVEEDLGKSR EGSRTDDEVV QREEEAIQLD GLNASQIREL REKSEKFAFQ AEVNRMMKLI INSLYKNKEI FLRELISNAS DALDKIRLIS LTDENALSGN EELTVKIKCD KEKNLLHVTD TGVGMTREEL VKNLGTIAKS GTSEFLNKMT EAQEDGQSTS ELIGQFGVGF YSAFLVADKV IVTSKHNNDT QHIWESDSNE FSVIADPRGN TLGRGTTITL VLKEEASDYL ELDTIKNLVK KYSQFINFPI YVWSSKTETV EEPMEEEEAA KEEKEESDDE AAVEEEEEEK KPKTKKVEKT VWDWELMNDI KPIWQRPSKE VEEDEYKAFY KSFSKESDDP MAYIHFTAEG EVTFKSILFV PTSAPRGLFD EYGSKKSDYI KLYVRRVFIT DDFHDMMPKY LNFVKGVVDS DDLPLNVSRE TLQQHKLLKV IRKKLVRKTL DMIKKIADDK YNDTFWKEFG TNIKLGVIED HSNRTRLAKL LRFQSSHHPT DITSLDQYVE RMKEKQDKIY FMAGSSRKEA ESSPFVERLL KKGYEVIYLT EPVDEYCIQA LPEFDGKRFQ NVAKEGVKFD ESEKTKESRE AVEKEFEPLL NWMKDKALKD KIEKAVVSQR LTESPCALVA SQYGWSGNME RIMKAQAYQT GKDISTNYYA SQKKTFEINP RHPLIRDMLR RIKEDEDDKT VLDLAVVLFE TATLRSGYLL PDTKAYGDRI ERMLRLSLNI DPDAKVEEEP EEEPEETAED TTEDTEQDED EEMDVGTDEE ETAKESTAE G PKLHHHHHH.

    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.

    Hsp90B1 Human Hek
  • View Data Sheet

    Name :

    IL 6 Mouse, Sf9

    Description:

    Interleukin-6 Mouse Recombinant, Sf9

    Interleukin-6, IL-6, B-cell hybridoma growth factor, Interleukin HP-1.

    Product # :

    CYT-904

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    Description

    Interleukin-6 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 193 amino acids (25-211a.a.) and having a molecular mass of 22.5kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL 6 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effect is less or equal to 0.1 ng/ml.

    More Info

    • Introduction

      Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.

    • Synonyms

      Interleukin-6, IL-6, B-cell hybridoma growth factor, Interleukin HP-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

      FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQTHHH HHH.

    • Background

      Research Paper on Interleukin-6 Mouse Recombinant, Sf9

      Abstract:

      Exploring Interleukin-6 Mouse Recombinant, Sf9, a fascinating research topic! This paper provides an extensive description of Interleukin-6 (IL-6) Mouse Recombinant expressed in Sf9 insect cells. We delve into the molecular properties of IL-6, its significance in immune responses and inflammation, and its synonyms, including DIF, TNFA, and TNFSF2. Join us as we uncover the potential applications of IL-6 research using this novel recombinant mouse protein.

      Introduction:

      Introducing Interleukin-6 Mouse Recombinant, Sf9. This paper sheds light on the production and characteristics of IL-6 expressed in Sf9 insect cells. As researchers, we are intrigued by the versatility and applications of this recombinant protein in immunological studies.

      An Extensive Description of Interleukin-6 Mouse Recombinant:

      We present a comprehensive overview of Interleukin-6 Mouse Recombinant, focusing on its structure and functions. This recombinant protein enables us to explore IL-6's role in various cellular processes, making it a valuable tool for investigating immune regulation.

      Significance in Immune Responses:

      Marvel at IL-6's critical role in orchestrating immune responses! As a key cytokine, IL-6 plays a central role in immune cell activation and the regulation of inflammatory processes. Its pleiotropic effects contribute to maintaining homeostasis in the immune system.

      Interactions and Synonyms:

      Learn about the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2. Understanding these synonyms enhances our understanding of the interconnectedness of cytokine signaling. The complex interactions between IL-6 and other molecules further enrich our knowledge of immune responses.

      Potential Applications in Immunological Research:

      Explore the wide range of applications of Interleukin-6 Mouse Recombinant in immunological studies. From cell-based assays to therapeutic developments, this recombinant protein offers novel avenues for advancing immunology research. It serves as a valuable tool in deciphering the intricate immune system functions.

      Novel Production Method using Sf9 Insect Cells:

      Discover the innovative use of Sf9 insect cells for producing Interleukin-6. This expression system provides a scalable and efficient approach for obtaining large quantities of functional IL-6. The use of Sf9 cells opens up possibilities for large-scale protein production and downstream applications.

      Conclusion:

      Concluding our exploration of Interleukin-6 Mouse Recombinant, Sf9, we recognize its significance in immunological research. The extensive description of this recombinant protein broadens our understanding of IL-6 biology and its potential applications in various fields. As researchers, we are excited about the potential discoveries that lie ahead with the help of this valuable tool.

    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.

    Il 6 Mouse Sf9
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    Name :

    TES Human

    Description:

    Testis Derived Transcript Human Recombinant

    TESS, TESS-2, Testin.

    Product # :

    PRO-549

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    Description

    TES Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 441amino acids (1-421 a.a.) and having a molecular mass of 50.1 kDa. The TES protein is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TES 0.5mg/ml protein solution contains 20mM Tris pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TES also called Testin is a tumor suppressor protein which is involved in cell adhesion, cell spreading and in the restructuring of the actin cytoskeleton. TES protein localizes to cell-cell contacts and actin stress fibres, and interacts with a diversity of cytoskeletal proteins such as Zyxin, Mena, VASP, Talin and Actin. The ability of TES to associate with alpha-actinin, paxillin and Zyxin is dependent on the conformational form of the protein.

    • Synonyms

      TESS, TESS-2, Testin.

    • 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 MDLENKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDVLLSNEED RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA KKNVSINTVT YEWAPPVQNQ ALARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPR EVKEMEQFVK KYKSEALGVG DVKLPCEMDA QGPKQMNIPG GDRSTPAAVG AMEDKSAEHK RTQYSCYCCK LSMKEGDPAI YAERAGYDKL WHPACFVCST CHELLVDMIY FWKNEKLYCG RHYCDSEKPR CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDSILAGEIY VMVNDKPVCK PCYVKNHAVV CQGCHNAIDP EVQRVTYNNF SWHASTECFL CSCCSKCLIG QKFMPVEGMV FCSVECKKRM S.

    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.

    Tes Human
  • View Data Sheet

    Name :

    TPST2 Human, sf9

    Description:

    Tyrosylprotein Sulfotransferase 2, sf9 Human Recombinant

    Tyrosylprotein Sulfotransferase 2, EC 2.8.2.20, TPST-2, Transport And Golgi Organization 13 Homolog B (Drosophila), Transport And Golgi Organization 13 Homolog B, Protein-Tyrosine Sulfotransferase 2, Tyrosylprotein Phosphotransferase 2, Tyrosylprotein Sulfotransferase-2, TANGO13B.

    Product # :

    ENZ-949

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    Description

    TPST2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 361 amino acids (26-377 a.a.) and having a molecular mass of 40.4kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TPST2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TPST2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosylprotein Sulfotransferase 2 (TPST2) is a member of the protein sulfotransferase family. TPST2 is a widely expressed protein, which catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The TPST2 protein is a type II integral membrane protein located in the Golgi body.

    • Synonyms

      Tyrosylprotein Sulfotransferase 2, EC 2.8.2.20, TPST-2, Transport And Golgi Organization 13 Homolog B (Drosophila), Transport And Golgi Organization 13 Homolog B, Protein-Tyrosine Sulfotransferase 2, Tyrosylprotein Phosphotransferase 2, Tyrosylprotein Sulfotransferase-2, TANGO13B.

    • 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

      ADPQQVLECR AVLAGLRSPR GAMRPEQEEL VMVGTNHVEY RYGKAMPLIF VGGVPRSGTT LMRAMLDAHP EVRCGEETRI IPRVLAMRQA WSKSGREKLR LDEAGVTDEV LDAAMQAFIL EVIAKHGEPA RVLCNKDPFT LKSSVYLSRL FPNSKFLLMV RDGRASVHSM ITRKVTIAGF DLSSYRDCLT KWNKAIEVMY AQCMEVGKEK CLPVYYEQLV LHPRRSLKLI LDFLGIAWSD AVLHHEDLIG KPGGVSLSKI ERSTDQVIKP VNLEALSKWT GHIPGDVVRD MAQIAPMLAQ LGYDPYANPP NYGNPDPFVI NNTQRVLKGD YKTPANLKGY FQVNQNSTSS HLGSSHHHHH H.

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

    Tpst2 Human Sf9
  • View Data Sheet

    Name :

    Adiponectin Mouse, HEK

    Description:

    Adiponectin Mouse Recombinant, HEK

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-435

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    Description

    The Acrp30 Mouse Recombinant is fused with FLAG tag having a total Mw of 26kDa.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M PBS buffer,0.075M NaCl, pH7.4.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml.  An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.

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    • Introduction

      Adiponectin is an important negative regulator in hematopoiesis and immune systems. It may be involved in ending inflammatory responses through its inhibitory functions. Inhibits endothelial nf-kappa-b signaling through a camp-dependent pathway. Inhibits tnf-alpha- induced expression of endothelial adhesion molecules. Involved in the control of fat metabolism and insulin sensitivity.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Stability

      Store lyophilized APM-1 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to reconstitute the lyophilized Acrp30 Mouse in sterile 18M-cm H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293.

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of ADIPONECTIN Protein?
      Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml. An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.

      What is the amino acid sequence of ADIPONECTIN Protein?
      EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.

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

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

    Adiponectin Mouse Hek
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