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Search results

1000 results found for “GTP-Binding Protein”

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Description

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  • 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 :

    CIAPIN1 Human

    Description:

    Cytokine Induced Apoptosis Inhibitor 1 Human Recombinant

    DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.

    Product # :

    PRO-024

    Price :

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    Description

    CIAPIN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312 a.a.) and having a molecular mass of 36kDa.CIAPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CIAPIN1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Anamorsin, ( CIAPIN) is a member of anamorsin family. CIAPIN mainly expressed in the cytoplasm of liver, pancreas and heart tissue cells and does not show any homology to known apoptosis regulatory molecules of the Bcl-2 or CASP families, or to signal transduction molecules. CIAPIN1 Expression is reliant on growth factor stimulation. It is a ubiquitously expressed protein, and when it is overexpressed, it grants apoptotic resistance.

    • Synonyms

      DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.

    • 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 MGSMADFGIS AGQFVAVVWD KSSPVEALKG LVDKLQALTG NEGRVSVENI KQLLQSAHKE SSFDIILSGL VPGSTTLHSA EILAEIARIL RPGGCLFLKE PVETAVDNNS KVKTASKLCS ALTLSGLVEV KELQREPLTP EEVQSVREHL GHESDNLLFV QITGKKPNFE VGSSRQLKLS ITKKSSPSVK PAVDPAAAKL WTLSANDMED DSMDLIDSDE LLDPEDLKKP DPASLRAASC GEGKKRKACK NCTCGLAEEL EKEKSREQMS SQPKSACGNC YLGDAFRCAS CPYLGMPAFK PGEKVLLSDS NLHDA.

    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.

    Ciapin1 Human
  • View Data Sheet

    Name :

    RPS16 Human

    Description:

    Ribosomal Protein S16 Human Recombinant

    Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.

    Product # :

    PRO-1555

    Price :

    Quantity :

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    Description

    RPS16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146) and having a molecular mass of 18.8kDa.RPS16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPS16 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribosomes are the organelles which catalyze protein synthesis and comprised of a small 40S subunit and a large 60S subunit. Combined, the small 40S and large 60S subunits are composed of 4 RNA types and about 80 structurally distinct proteins. RPS16, a ribosomal protein, is a component of the 40S subunit and a member of the S9P family of ribosomal proteins. RPS16 is situated in the cytoplasm. Just like other genes encoding ribosomal proteins, there are numerous processed pseudogenes of RPS16 spread through the genome.

    • Synonyms

      Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.

    • 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 MGSMPSKGPL QSVQVFGRKK TATAVAHCKR GNGLIKVNGR PLEMIEPRTL QYKLLEPVLL LGKERFAGVD IRVRVKGGGH VAQIYAIRQS ISKALVAYYQ KYVDEASKKE IKDILIQYDR TLLVADPRRC ESKKFGGPGA RARYQKSYR

    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.

    Rps16 Human
  • View Data Sheet

    Name :

    EIF3K (50-94) Human

    Description:

    Eukaryotic Translation Initiation Factor 3K (50-94 a.a.) Human Recombinant

    PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.

    Product # :

    PRO-2833

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    The EIF3KHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The EIF3KHis-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 45 amino acid residues of the EIF3KHuman, 50-94 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized EIF3Kat -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Background

      Eukaryotic Translation Initiation Factor 3K (EIF3K) is a part of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a few other subunits of the 40S ribosomal subunit and eIF3. EIF3K is found both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4. EIF3K is conserved among high eukaryotes, including mammals, plants and insects and is expressed in human tissues.

    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.

    Eif3K Protein
  • View Data Sheet

    Name :

    C10ORF54 Human

    Description:

    Chromosome 10 Open Reading Frame 54 Human Recombinant

    C10orf54, Chromosome 10 Open Reading Frame 54, V-Domain Ig Suppressor Of T Cell Activation, Stress-Induced Secreted Protein-1, Sisp-1, SISP1, Stress Induced Secreted Protein 1, Death Domain1alpha, DD1alpha, PP2135, B7-H5, VISTA, B7H5, GI24.

    Product # :

    PRO-2259

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    Description

    C10ORF54 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (33-194 a.a) and having a molecular mass of 19.1kDa. (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). C10ORF54 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    C10ORF54 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chromosome 10 Open Reading Frame 54, also known as C10ORF54 is part of the immunoglobulin superfamily. Like a transmembrane molecule, C10ORF54 is expressed in the bone on embryonic stem cells (ESCs), and on tumor cell surface as well. Accordingly, C10ORF54 supports the differentiation of ESC and ehhances BMP4 induced signaling in ESC, however C10ORF54 is also down regulated following to BMP4 exposure.

    • Synonyms

      C10orf54, Chromosome 10 Open Reading Frame 54, V-Domain Ig Suppressor Of T Cell Activation, Stress-Induced Secreted Protein-1, Sisp-1, SISP1, Stress Induced Secreted Protein 1, Death Domain1alpha, DD1alpha, PP2135, B7-H5, VISTA, B7H5, GI24.

    • 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

      FKVATPYSLY VCPEGQNVTL TCRLLGPVDK GHDVTFYKTW YRSSRGEVQT CSERRPIRNL TFQDLHLHHG GHQAANTSHD LAQRHGLESA SDHHGNFSIT MRNLTLLDSG LYCCLVVEIR HHHSEHRVHG AMELQVQTGK DAPSNCVVYP SSSQDSENIT AAVEHHHHHH.

    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.

    C10Orf54 Human
  • View Data Sheet

    Name :

    HB-EGF Human

    Description:

    HB-EGF Human Recombinant

    HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    Product # :

    CYT-119

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    Description

    HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

    More Info

    • Introduction

      HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

    • Synonyms

      HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC

      KYVKELRAPS CICHPGYHGE RCHGLSL.

    • Background

      What is the molecular weight/Mw of HB-EGF Protein?
      HB-EGF Protein has a total Mw of 9.9kDa.

      What is the source or expression system of HB-EGF Protein?
      Escherichia Coli.

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

      What is the Biological Activity of HB-EGF Protein?
      The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

      What is the amino acid sequence of HB-EGF Protein?
      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
      KYVKELRAPS CICHPGYHGE RCHGLSL.

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

      What is the endotoxin level for HB-EGF Protein?
      The endotoxin level is minimal, HB-EGF 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.

    Hb Egf Human
  • View Data Sheet

    Name :

    SERPINA3

    Description:

    Alpha-1 AntiChymotrypsin Human Recombinant

    Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    Product # :

    PRO-750

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    Description

    SERPINA3 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 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.The SERPINA3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINA3 solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1-ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
      Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT.

    • Synonyms

      Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    • 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 MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ A.

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    Serpina3 Human Recombinant
  • View Data Sheet

    Name :

    PRRT2 Human

    Description:

    Proline-Rich Transmembrane Protein 2 Human Recombinant

    Proline-Rich Transmembrane Protein 2, Infantile Convulsions And Paroxysmal Choreoathetosis, Dispanin Subfamily B Member 3, DSPB3, BFIC2, BFIS2, DYT10, EKD1, PKC, FICCA, IFITMD1, ICCA.

    Product # :

    PRO-1852

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    Description

    PRRT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 291 amino acids (1-268) and having a molecular mass of 29.7 kDa. PRRT2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The PRRT2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transmembrane protein PRRT2 holds a proline-rich domain in its N-terminal half. PRRT2 is known to be primarily expressed in brain and spinal cord in embryonic and postnatal stages. Alterations in this gene are the cause for paroxysmal kinesigenic dyskinesia. PRRT2 mutations were found in nearly 30% of sporadic PKC patients.

    • Synonyms

      Proline-Rich Transmembrane Protein 2, Infantile Convulsions And Paroxysmal Choreoathetosis, Dispanin Subfamily B Member 3, DSPB3, BFIC2, BFIS2, DYT10, EKD1, PKC, FICCA, IFITMD1, ICCA.

    • 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 MGSMAASSSE ISEMKGVEES PKVPGEGPGH SEAETGPPQV LAGVPDQPEA PQPGPNTTAA PVDSGPKAGL APETTETPAG ASETAQATDL SLSPGGESKA NCSPEDPCQE TVSKPEVSKE ATADQGSRLE SAAPPEPAPE PAPQPDPRPD SQPTPKPALQ PELPTQEDPT PEILSESVGE KQENGAVVPL QAGDGEEGPA PEPHSPPSKK SPPANGAPPR VLQQLVEEDR MRRAHSGHPG SPRGSLSRHP SSQLAGPGVE GGEGTQKPRD Y.

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    Prrt2 Human
  • View Data Sheet

    Name :

    Protein-L

    Description:

    Protein L Recombinant

    SPL.

    Product # :

    PRO-1790

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    Description

    Protein-L Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 365 amino acids and having a molecular mass of 40.5 kDa but it migrates with an apparent molecular mass of 45 kDa in SDS-PAGE.The Protein-L is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Protein-L was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      The recombinant Protein L is genetically engineered protein and holds 5 IgG-binding regions of protein L and it has the exclusive capability to bind through kappa light chain interactions without interfering with the antibody’s antigen-binding site. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies and it binds to human, mouse, rat and pig IgG.

    • Synonyms

      SPL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPEEKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG

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    Protein L
  • View Data Sheet

    Name :

    TGFBI Human, 182 a.a.

    Description:

    Transforming Growth Factor Beta-Induced (182 a.a.) Human Recombinant

    Transforming growth factor-beta-induced protein ig-h3, Beta ig-h3, Kerato-epithelin, RGD-containing collagen-associated protein, RGD-CAP, TGFBI, BIGH3, CSD, CDB1, CDG2, CSD1, CSD2, CSD3, EBMD, LCD1, CDGG1.

    Product # :

    PRO-672

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    Description

    TGFBI Recombinant Human produced in e.Coli is a single, non-glycosylated, polypeptide containing 182 amino acids (502-683) and having a molecular mass of 19.9 kDa (Molecular weight on SDS-PAGE will appear higher). The TGFBI recombinant Human protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TGFBI 182 a.a. recombinant Human is formulated in 20mM Tris-HCl pH-8, 1mM EDTA, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TGFBI is an extracellular matrix protein induced by transforming growth factor (TGF)-beta 1. TGFBI protein is involved in cell growth, cell differentiation, wound healing and cell adhesion. In addition, some missense mutations of TGFBI were identified in families affected with human autosomal dominant corneal dystrophies. TGFBI gene encodes for a 683 amino-acid protein containing an RGD motif and four internal repeated domains which have highly conserved sequences founded in several species (Fasciclin domain).

    • Synonyms

      Transforming growth factor-beta-induced protein ig-h3, Beta ig-h3, Kerato-epithelin, RGD-containing collagen-associated protein, RGD-CAP, TGFBI, BIGH3, CSD, CDB1, CDG2, CSD1, CSD2, CSD3, EBMD, LCD1, CDGG1.

    • Physical Appearance

      Sterile filtered liquid formulation.

    • 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

      MGTVMDVLKG DNRFSMLVAA IQSAGLTETL NREGVYTVFA PTNEAFRALP PRERSRLLGD AKELANILKY HIGDEILVSG GIGALVRLKS LQGDKLEVSL KNNVVSVNKE PVAEPDIMAT NGVVHVITNV LQPPANRPQE RGDELADSAL EIFKQASAFS RASQRSVRLA PVYQKLLERM KH.

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    Tgfbi Human 182 Aa
  • View Data Sheet

    Name :

    RCHY1 Human

    Description:

    Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant

    ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    Product # :

    PRO-1536

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    Description

    RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RCHY1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.

    • Synonyms

      ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    • 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 MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.

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    Rchy1 Human
  • View Data Sheet

    Name :

    MRTO4 Human

    Description:

    mRNA Turnover 4 Human Recombinant

    MRNA Turnover 4 Homolog (S. Cerevisiae), MRT4 MRNA Turnover 4 Homolog (S. Cerevisiae), 60S Acidic Ribosomal Protein PO, Chromosome 1 Open Reading Frame 33, C1orf33, MRT4, DJ657E11.4.

    Product # :

    PRO-1233

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    Description

    MRTO4 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (1-239) and having a molecular mass of 29.9 kDa.MRTO4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MRTO4 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      mRNA turnover protein 4 homolog (MRTO4) is a member of the ribosomal protein L10P family. MRTO4 is a protein sharing a low level of sequence similarity with ribosomal protein P0. Though the precise function of the MRTO4 is presently unknown, it seems to be involved in mRNA turnover and ribosome assembly. MRTO4 is a nucleolar component of the ribosome assembly apparatus which shares remarkable similarity and contends for binding to the 25S rRNA GAR domain with the ribosomal protein P0. The MRTO4 gene is located on human chromosome 1, which extends over 260 million base pairs, is comprised of over 3,000 genes and contains approximately 8% of the human genome.

    • Synonyms

      MRNA Turnover 4 Homolog (S. Cerevisiae), MRT4 MRNA Turnover 4 Homolog (S. Cerevisiae), 60S Acidic Ribosomal Protein PO, Chromosome 1 Open Reading Frame 33, C1orf33, MRT4, DJ657E11.4.

    • 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 MGSMPKSKRD KKVSLTKTAK KGLELKQNLI EELRKCVDTY KYLFIFSVAN MRNSKLKDIR NAWKHSRMFF GKNKVMMVAL GRSPSDEYKD NLHQVSKRLR GEVGLLFTNR TKEEVNEWFT KYTEMDYARA GNKAAFTVSL DPGPLEQFPH SMEPQLRQLG LPTALKRGVV TLLSDYEVCK EGDVLTPEQA RVLKLFGYEM AEFKVTIKYM WDSQSGRFQQ MGDDLPESAS ESTEESDSED DD

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    Mrto4 Human
  • View Data Sheet

    Name :

    ARL4A Human

    Description:

    ADP-Ribosylation Factor-Like 4A Human Recombinant

    ADP-ribosylation factor-like protein 4A, ARL4A.

    Product # :

    PRO-895

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    Description

    ARL4A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200) and having a molecular mass of 24.7 kDa.The ARL4A is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ARL4A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARL4A is related Specifically to ARL6 and ARL7 and belongs to the ARF-like protein (ARL) subfamily of small GTPases. However, unlike ARFs, ARL4 does not activate the cholera toxin ADP-ribosyltranferase. ARL4A takes part in neurogenesis during embryonic development and somitogenesis in the early stages of adult spermatogenesis.

    • Synonyms

      ADP-ribosylation factor-like protein 4A, ARL4A.

    • 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 MGNGLSDQTS ILSNLPSFQS FHIVILGLDC AGKTTVLYRL QFNEFVNTVP TKGFNTEKIK VTLGNSKTVT FHFWDVGGQE KLRPLWKSYT RCTDGIVFVV DSVDVERMEE AKTELHKITR ISENQGVPVL IVANKQDLRN SLSLSEIEKL LAMGELSSST PWHLQPTCAI IGDGLKEGLE KLHDMIIKRR KMLRQQKKKR

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    Arl4A Human
  • View Data Sheet

    Name :

    ARL9 Human

    Description:

    ADP-Ribosylation Factor-Like 9 Human Recombinant

    ADP-ribosylation factor-like protein 9, ARL9.

    Product # :

    PRO-1009

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    Description

    ARL9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (1-123 a.a.) and having a molecular mass of 15.9kDa. ARL9 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARL9 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-ribosylation factor-like protein 9 (ARL9) is a member of to 2 novel subfamilies coding for small GTPases that were found to be highly conserved among eukaryotes.

    • Synonyms

      ADP-ribosylation factor-like protein 9, ARL9.

    • 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 MEFLEIGGSK PFRSYWEMYL SKGLLLIFVV DSADHSRLPE AKKYLHQLIA ANPVLPLVVF ANKQDLEAAY HITDIHEALA LSEVGNDRKM FLFGTYLTKN GSEIPSTMQD AKDLIAQLAA DVQ.

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    Arl9 Human
  • View Data Sheet

    Name :

    FCGR2A Human, HEK

    Description:

    CD32a Human Recombinant, HEK

    CD32, CD32A, CDw32, FcGR, IGFR2, MGC23887, MGC30032, Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a, Fc-gamma-RIIa, FcRII-a, FCG2, FCGR2A1.

    Product # :

    PRO-2775

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    Description

    FCGR2A Human Recombinant is a single, glycosylated, polypeptide chain (30-218 a.a) containing a total of 195 amino acids, having a molecular mass of 21.6kDa. FCGR2A is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    FCGR2A protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤5 ug/ml. and is measured by its binding ability in a functional ELISA with Human IgG1 Fc (CAT# pro-2763). 

    More Info

    • Synonyms

      CD32, CD32A, CDw32, FcGR, IGFR2, MGC23887, MGC30032, Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a, Fc-gamma-RIIa, FcRII-a, FCG2, FCGR2A1.

    • 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

      SADSQAAAPP KAVLKLEPPW INVLQEDSVT LTCQGARSPE SDSIQWFHNG NLIPTHTQPS YRFKANNNDS GEYTCQTGQT SLSDPVHLTV LSEWLVLQTP HLEFQEGETI MLRCHSWKDK PLVKVTFFQN GKSQKFSHLD PTFSIPQANH SHSGDYHCTG NIGYTLFSSK PVTITVQVPS MGSSSPMGIH HHHHH.

    • Background

      The immune system is a complex network of cells and molecules that play a crucial role in protecting the body against pathogens and maintaining homeostasis. Fc gamma receptors (FcγRs) are a family of cell surface receptors that mediate the effector functions of antibodies, particularly immunoglobulin G (IgG). Among these receptors, FCGR2A, also known as CD32a, is a prominent member expressed on the surface of various immune cells. This research aims to investigate the structure, function, and implications of FCGR2A protein in immune responses, with a focus on its relevance to human health and therapeutic applications.

      Structure and Expression of FCGR2A:

      FCGR2A is a transmembrane glycoprotein composed of two extracellular immunoglobulin-like domains, a transmembrane domain, and a cytoplasmic tail. It is primarily expressed on immune cells such as macrophages, monocytes, and dendritic cells. The unique structure of FCGR2A allows it to bind to the Fc portion of IgG antibodies, initiating immune effector functions.

      Role of FCGR2A in Immune Responses:

      FCGR2A plays a crucial role in modulating immune responses through its involvement in antibody-dependent cellular cytotoxicity (ADCC) and phagocytosis. Upon binding to IgG antibodies, FCGR2A triggers intracellular signaling cascades that activate immune effector cells, leading to the elimination of antibody-bound pathogens or targeted cells. Furthermore, FCGR2A is involved in immune complex clearance, regulation of cytokine production, and modulation of cellular activation, thus contributing to the overall immune response.

      Implications of FCGR2A in Human Health:

      The dysregulation of FCGR2A has been implicated in various immune-related diseases. Genetic variations in FCGR2A have been associated with increased susceptibility to autoimmune disorders, such as systemic lupus erythematosus and rheumatoid arthritis. Altered FCGR2A expression or function has also been observed in infectious diseases, including HIV and malaria, affecting disease progression and immune control. Understanding the role of FCGR2A in these conditions is crucial for developing targeted therapeutic strategies.

      Therapeutic Potential of FCGR2A:

      The unique properties of FCGR2A make it an attractive target for therapeutic interventions. Modulating FCGR2A activity and function can potentially enhance immune responses against pathogens or tumor cells. For example, monoclonal antibodies that target FCGR2A have shown promising results in cancer immunotherapy by promoting ADCC and phagocytosis of tumor cells. Furthermore, strategies aimed at selectively activating or inhibiting FCGR2A signaling could lead to the development of novel immunotherapeutic approaches.

      Challenges and Future Perspectives:

      While the study of FCGR2A holds great promise, several challenges need to be addressed. Further research is required to unravel the intricate interplay between FCGR2A and other immune receptors and signaling molecules. Additionally, the development of therapeutic agents that selectively target FCGR2A without compromising normal immune functions remains a challenge.

      Conclusion:

      The investigation of FCGR2A protein provides insights into its pivotal role in immune responses and its implications for human health and therapeutics. Understanding the structure, function, and dysregulation of FCGR2A in immune-related diseases opens avenues for the development of targeted therapies. Continued research on FCGR2A and its interactions within the immune system will contribute to advancements in immunotherapy and personalized medicine.

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    Fcgr2A Human Hek
  • View Data Sheet

    Name :

    S100A14 Human

    Description:

    S100 Calcium Binding Protein A14 Human Recombinant

    Protein S100-A14, S100 calcium-binding protein A14, S114, S100A14, S100A15, BCMP84.

    Product # :

    PRO-154

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    Description

    S100A14 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 124 amino acids (1-104 a.a.) and having a molecular mass of 13.8kDa. The S100A14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A14 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A14 belongs to a subfamily of proteins related by EF-hand Ca2+ binding protein superfamily. The extracellular functions of the S100 family include the ability to boost neurite outgrowth, involvement in inflammation, and motility of tumor cells. S100A14 contains 2 EF-hand Ca2+-binding domains, a myristoylation motif, a glycosylation site, and a number of potential protein kinase phosphorylation sites. S100A14 is expressed at high levels in the colon and at moderate levels in the thymus, kidney, liver, small intestine, and lung.

    • Synonyms

      Protein S100-A14, S100 calcium-binding protein A14, S114, S100A14, S100A15, BCMP84.

    • 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 MGQCRSANAE DAQEFSDVER AIETLIKNFH QYSVEGGKET LTPSELRDLV TQQLPHLMPS NCGLEEKIAN LGSCNDSKLE FRSFWELIGE AAKSVKLERP VRGH.

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    S100A14 Human
  • View Data Sheet

    Name :

    SGK1 Human

    Description:

    Serum/Glucocorticoid Regulated Kinase 1 Human Recombinant

    Serine/threonine-protein kinase Sgk1, Serum/glucocorticoid-regulated kinase 1, SGK1, SGK.

    Product # :

    PKA-272

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    Description

    SGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (60-431 a.a.) and having a molecular mass of 44.5kDa.SGK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SGK1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serum-and glucocorticoid-regulated kinase (SGK1) is a serine/threonine protein kinase and a member of the “AGC” subfamily, which includes protein kinases A, G, and C. The SGK1 protein has an imperative role in activating specific potassium, sodium and chloride channels, suggesting a participation in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. SGK1 is activated in vitro by PDK-1 (3-phosphoinositide-dependent protein kinase-1) and in vivo in reaction to signals which activate phosphatidylinositol (PI) 3-kinase.

    • Synonyms

      Serine/threonine-protein kinase Sgk1, Serum/glucocorticoid-regulated kinase 1, SGK1, SGK.

    • 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 MISQPQEPEL MNANPSPPPS PSQQINLGPS SNPHAKPSDF HFLKVIGKGS FGKVLLARHK AEEVFYAVKV LQKKAILKKK EEKHIMSERN VLLKNVKHPF LVGLHFSFQT ADKLYFVLDY INGGELFYHL QRERCFLEPR ARFYAAEIAS ALGYLHSLNI VYRDLKPENI LLDSQGHIVL TDFGLCKENI EHNSTTSTFC GTPEYLAPEV LHKQPYDRTV DWWCLGAVLY EMLYGLPPFY SRNTAEMYDN ILNKPLQLKP NITNSARHLL EGLLQKDRTK RLGAKDDFME IKSHVFFSLI NWDDLINKKI TPPFNPNVSG PNDLRHFDPE FTEEPVPNSI GKSPDSVLVT ASVKEAAEAF LGFSYAPPTD SFL.

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    Sgk1 Human
  • View Data Sheet

    Name :

    DGCR6L Human

    Description:

    DiGeorge Syndrome Critical Region Gene 6-Like Human Recombinant

    Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.

    Product # :

    PRO-1454

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    Description

    DGCR6L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27.3kDa.DGCR6L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DGCR6L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 1mM DTT and 250mM Imidazole.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      DiGeorge syndrome critical region 6-like protein (DGCR6L) shares homology with the Drosophila gonadal protein, it is expressed in gonadal tissues and germ cells, and with the human laminin gamma-1 chain which functions in cell attachment and migration. DGCR6L is located in a region of chromosome 22 involved in the DiGeorge syndrome, one aspect of a wider collection of anomalies referred to as the CATCH 22 syndrome. Moreover, it is one of two functional genes encoding nearly identical proteins which have analogous expression patterns.

    • Synonyms

      Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.

    • 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 MGSMERYAAA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVVQA AQQRELEAVE HRIREEQRAM DQKIILELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCRAGNAA LGLGGPWQSP AAQCDQKGSP VPP.

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    Dgcr6L Human
  • View Data Sheet

    Name :

    NAP1L4 Human

    Description:

    Nucleosome Assembly Protein 1-Like 4 Human Recombinant

    Nucleosome assembly protein 1-like 4, Nucleosome assembly protein 2, NAP-2, NAP1L4, NAP2, hNAP2, NAP1L4b, NAP2L.

    Product # :

    PRO-1693

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    Description

    NAP1L4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-375) and having a molecular mass of 45.2 kDa.NAP1L4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NAP1L4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Nucleosome Assembly Protein 1-Like 4 (NAP1L4) is a part of the nucleosome assembly protein (NAP) family which interacts with both core and linker histones. NAP1L4 plays a role as a histone chaperone due to his ability to shuttle between the cytoplasm and nucleus. NAP1L4 modulates transcriptional activation by target nuclear receptors. NAP1L4 is one of several located near the imprinted gene domain of 11p15.5 which is an important tumor-suppressor gene region.

    • Synonyms

      Nucleosome assembly protein 1-like 4, Nucleosome assembly protein 2, NAP-2, NAP1L4, NAP2, hNAP2, NAP1L4b, NAP2L.

    • 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 MGSMADHSFS DGVPSDSVEA AKNASNTEKL TDQVMQNPRV LAALQERLDN VPHTPSSYIE TLPKAVKRRI NALKQLQVRC AHIEAKFYEE VHDLERKYAA LYQPLFDKRR EFITGDVEPT DAESEWHSEN EEEEKLAGDM KSKVVVTEKA AATAEEPDPK GIPEFWFTIF RNVDMLSELV QEYDEPILKH LQDIKVKFSD PGQPMSFVLE FHFEPNDYFT NSVLTKTYKM KSEPDKADPF SFEGPEIVDC DGCTIDWKKG KNVTVKTIKK KQKHKGRGTV RTITKQVPNE SFFNFFNPLK ASGDGESLDE DSEFTLASDF EIGHFFRERI VPRAVLYFTG EAIEDDDNFE EGEEGEEEEL EGDEEGEDED DAEINPKV.

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    Nap1L4 Human
  • View Data Sheet

    Name :

    DnaK E.coli

    Description:

    DnaK (HSP70) E.Coli Recombinant

    HSP-70, HSP70, DnaK, , Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

    Product # :

    HSP-006

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    Description

    Recombinant Dnak produced in E.Coli is a single, non-glycosylated polypeptide chain containing 638 amino acids and having a molecular mass of 69 kDa.

    Source

    Escherichia Coli.

    Formulation

    The DnaK protein contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial HSP70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.

    • Synonyms

      HSP-70, HSP70, DnaK, , Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

    • 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

      MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVTNPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVLKKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIINEPTAAALAYGLDKGTGNRTI AVYDLGGGTFDISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYLVEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKVTRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKEPRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPTKHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMPQIEVTFDIDADGILHVSAKD KNSGKEQKITIKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGDHLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLMEIAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK.

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    Dnak Ecoli
  • View Data Sheet

    Name :

    CCL9 Mouse

    Description:

    Macrophage Inflammatory Protein-1 Gamma Mouse Recombinant (CCL9)

    CCL9/10, MRP2, CCF18.

    Product # :

    CHM-257

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    Description

    MIP-1 gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 101 amino acids and having a molecular mass of 11.6 kDa. The MIP-1 gamma is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MIP-1 gamma was lyophilized from 1xPBS solution pH-7.4.

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

      Mouse MIP-1 gamma is 75% identical in its amino acid compostion as compared to the rat specie. MIP-1 gamma is a CC chemokine localized in murine blood and a widespread range of murine tissues, without having an identified human homolog. MIP-1 gamma signals through the CCR1 receptor. MIP-1 gamma chemoattracts neutrophils and also inhibits colony formation of bone marrow myeloid immature progenitors. MIP-1 gamma has six cysteines including the four highly conserved cysteine residues present in CC chemokines.

    • Synonyms

      CCL9/10, MRP2, CCF18.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-1 gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL9/10 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 MIP-1 gamma in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QITHATETKE VQSSLKAQQG LEIEMFHMGF QDSSDCCLSY NSRIQCSRFI GYFPTSGGCT RPGIIFISKR GFQVCANPSD RRVQRCIERL EQNSQPRTYK Q.

    • Background

      What is the molecular weight/Mw of CCL9 MOUSE Protein?
      CCL9 MOUSE Protein has a total Mw of 11.6kDa.

      What is the source or expression system of CCL9 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL9 MOUSE Protein?
      CCL9 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL9 MOUSE Protein?
      Defined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml, corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL9 MOUSE Protein?
      QITHATETKE VQSSLKAQQG LEIEMFHMGF QDSSDCCLSY NSRIQCSRFI GYFPTSGGCT RPGIIFISKR GFQVCANPSD RRVQRCIERL EQNSQPRTYK Q.

      What applications can CCL9 MOUSE Protein be used in?
      CCL9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL9 MOUSE Protein?
      The endotoxin level is minimal, CCL9 MOUSE Protein was purified using conventional chromatography techniques.


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    Mip 1 Gamma Mouse
  • View Data Sheet

    Name :

    GTF3C6 Human

    Description:

    General Transcription Factor IIIC Polypeptide 6 Human Recombinant

    bA397G5.3, C6orf51, TFIIIC35, General transcription factor 3C polypeptide 6, Transcription factor IIIC 35 kDa subunit, TFIIIC 35 kDa subunit, TFIIIC35, Transcription factor IIIC subunit 6, CDA020, NPD020.

    Product # :

    PRO-2127

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    Description

    GTF3C6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-213 a.a) and having a molecular mass of 26.4kDa.GTF3C6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GTF3C6 protein solution (0.5mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      In the absence of additional proteins - the general transcription factors (GTFs) RNA polymerases are unable to initiate RNA synthesis. GTFs accumulate in a complex on the DNA promoter and recruit the RNA polymerase. GTF3C family proteins are vital for RNA polymerase III to produce several small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin.

    • Synonyms

      bA397G5.3, C6orf51, TFIIIC35, General transcription factor 3C polypeptide 6, Transcription factor IIIC 35 kDa subunit, TFIIIC 35 kDa subunit, TFIIIC35, Transcription factor IIIC subunit 6, CDA020, NPD020.

    • 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 MGSMAAAADE RSPEDGEDEE EEEQLVLVEL SGIIDSDFLS KCENKCKVLG IDTERPILQV DSCVFAGEYE DTLGTCVIFE ENVEHADTEG NNKTVLKYKC HTMKKLSMTR TLLTEKKEGE ENIGGVEWLQ IKDNDFSYRP NMICNFLHEN EDEEVVASAP DKSLELEEEE IQMNDSSNLS CEQEKPMHLE IEDSGPLIDI PSETEGSVFM ETQMLP.

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    Gtf3C6 Human
  • View Data Sheet

    Name :

    ARL2 Human

    Description:

    ADP-Ribosylation Factor-Like 2 Human Recombinant

    ADP-ribosylation factor-like protein 2, ARL2, ARFL2.

    Product # :

    PRO-074

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    Description

    ARL2 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 204 amino acids (1-184 a.a.) and having a molecular mass of 23kDa. The ARL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARL2 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF, 1mM DTT and 40% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARL2 is a member of the ADP-ribosylation factor (ARF) family. ARL2 functions as a component of a secretory pathway which is involved in the Ca2-dependent release of acetylcholine. ARL2 has a role in the folding of tubule proteins, thus playing a significant role in microtubule dynamics and cell cycle progression. Unlike other members of the ARF family, ARL2 doesn’t act as an activator of the catalytic subunit of cholera toxin.

    • Synonyms

      ADP-ribosylation factor-like protein 2, ARL2, ARFL2.

    • 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 MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL LIFANKQDLP GALSSNAIRE ALELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI FTAD.

    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.

    Arl2 Human
  • View Data Sheet

    Name :

    COMMD1 Human

    Description:

    Copper Metabolism Domain Containing 1 Human Recombinant

    MURR1, C2orf5, COMMD1, Copper Metabolism Domain Containing 1, MGC27155.

    Product # :

    PRO-862

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    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    COMMD1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-190 a.a.) and having a molecular mass of 23.3 kDa. The COMMD1 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COMMD1 Human solution containing 20mM Tris pH-8, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COMMD1 is accountable for inhibition of TNF-induced NFκB p50 and n facilitats of biliary copper excretion within hepatocytes. High expression of COMMD1 is localized in liver tissue, with lower expressions in lung, heart, kidney and brain tissue. COMMD1 interacts directly with COMMD6 and ATP7B, and indirectly with IκB-β and COMMD7.

    • Synonyms

      MURR1, C2orf5, COMMD1, Copper Metabolism Domain Containing 1, MGC27155.

    • 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 MAAGELEGGK PLSGLLNALA QDTFHGYPGI TEELLRSQLY PEVPPEEFRP FLAKMRGILK SIASADMDFN QLEAFLTAQT KKQGGITSDQ AAVISKFWKS HKTKIRESLM NQSRWNSGLR GLSWRVDGKS QSRHSAQIHT PVAIIELELG KYGQESEFLC LEFDEVKVNQ ILKTLSEVEE SISTLISQPN.

    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.

    Commd1 Human
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