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Search results

1000 results found for “Uroplakin”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    sRANKL Human

    Description:

    RANK Ligand Soluble Human Recombinant

    Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    Product # :

    CYT-334

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • HPLC, SDS-PAGE

    Description

    sRANKL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19.7kDa.

    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 analysis by SDS-PAGE.

    Biological Activity

    The activity of RAW-Blue was measured to be 46.96 ng/ml, corresponding to a specific activity of 2.1x104 units/mg.

    HPLC, SDS-PAGE

    sRANKL Human HPLC - Product image 1
    sRANKL Human SDS PAGE - Product image 2

    More Info

    • Introduction

      RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

    • Synonyms

      Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANKL 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 sRANKL in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EKAMVDGSW LDLAKRSKLE AQPFAHLTIN ATDIPSGSHK VSLSSWYHDR GWAKISNMTF SNGKLIVNQD GFYYLYANIC FRHHETSGDL ATEYLQLMVY VTKTSIKIPS SHTLMKGGST KYWSGNSEFH FYSINVGGFF KLRSGEEISI EVSNPSLLDP DQDATYFGAF KVRDID.

    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.

    Rankl Human
  • View Data Sheet

    Name :

    RPS4X Human

    Description:

    Ribosomal Protein 4X Human Recombinant

    Ribosomal protein S4, X-linked, CCG2; DXS306, RPS4, S4, SCAR, SCR10, 40S ribosomal protein S4, X isoform, Single copy abundant mRNA protein, RPS4X.

    Product # :

    PRO-1799

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
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    • More Info

    Description

    RPS4X Human Recombinant produced in E. coli is a single polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 32kDa. RPS4X is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPS4X solution (0.5mg/ml) contains 20mM Tris-HCl(pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribosomal Protein 4X (RPS4X) is ribosomal protein S4, a component of the 40S subunit which is a part from the S4E family of ribosomal proteins. Ribosomal protein S4 is the only ribosomal protein known to be encoded by more than one gene, that is RPS4X and ribosomal protein S4, Y-linked (RPS4Y). Both isoforms encoded by these genes are not the same, but are functionally alike.

    • Synonyms

      Ribosomal protein S4, X-linked, CCG2; DXS306, RPS4, S4, SCAR, SCR10, 40S ribosomal protein S4, X isoform, Single copy abundant mRNA protein, RPS4X.

    • 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 MGSMARGPKK HLKRVAAPKH WMLDKLTGVF APRPSTGPHK LRECLPLIIF LRNRLKYALT GDEVKKICMQ RFIKIDGKVR TDITYPAGFM DVISIDKTGE NFRLIYDTKG RFAVHRITPE EAKYKLCKVR KIFVGTKGIP HLVTHDARTI RYPDPLIKVN DTIQIDLETG KITDFIKFDT GNLCMVTGGA NLGRIGVITN RERHPGSFDV VHVKDANGNS FATRLSNIFV IGKGNKPWIS LPRGKGIRLT IAEERDKRLA AKQSSG.

    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.

    RPS4X Human
  • View Data Sheet

    Name :

    MRPL1 Human

    Description:

    Mitochondrial Ribosomal Protein L1 Human Recombinant

    BM022, L1MT, MRP-L1, 39S ribosomal protein L1, mitochondria, MRPL1.

    Product # :

    PRO-1431

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    MRPL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (51-325) and having a molecular mass of 33.8kDa. MRPL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MRPL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitochondrial Ribosomal Protein L1 (MRPL1) exists as a component of the 39S ribosomal subunit and operates in conjunction with other MRPs to mediate protein synthesis. Mitochondrial ribosomes consist of a large 39S subunit and a small 28S subunit, both of which are consist of multiple mitochondrial ribosomal proteins (MRPs) that are encoded by nuclear genes and are vital for protein synthesis within mitochondria. MRPL1 exists as 2 isoforms produced by alternative splicing. Isoform 1 of MRPL1 is ubiquitously expressed while isoform 2 is particularly expressed in heart.

    • Synonyms

      BM022, L1MT, MRP-L1, 39S ribosomal protein L1, mitochondria, MRPL1.

    • 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 MGSKKTKKGA KEKTPDEKKD EIEKIKAYPY MEGEPEDDVY LKRLYPRQIY EVEKAVHLLK KFQILDFTSP KQSVYLDLTL DMALGKKKNV EPFTSVLSLP YPFASEINKV AVFTENASEV KIAEENGAAF AGGTSLIQKI WDDEIVADFY VAVPEIMPEL NRLRKKLNKK YPKLSRNSIG RDIPKMLELF KNGHEIKVDE ERENFLQTKI ATLDMSSDQI AANLQAVINE VCRHRPLNLG PFVVRAFLRS STSEGLLLKI DPLLPKEVKN EESEKEDA.

    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.

    Mrpl1 Human
  • View Data Sheet

    Name :

    SERPING1 Human HEK

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant HEK

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

    Product # :

    PRO-1639

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

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

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPING1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPING1 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized SERPING1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTT
      EPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKK
      VETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAI
      RDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTT
      FDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQ
      ALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQ
      HQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFMLWDQQHKFPVFMGRVYDPRAVDHHHHHH

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

    Serping1 Human Hek
  • View Data Sheet

    Name :

    EFNB3 Human

    Description:

    Ephrin- B3 Human Recombinant

    Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.

    Product # :

    PRO-1169

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    Description

    EFNB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-226 a.a) and having a molecular mass of 24.6kDa.EFNB3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    EFNB3 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

      Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.

    • Synonyms

      Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.

    • 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 MGSHMLSLEP VYWNSANKRF QAEGGYVLYP QIGDRLDLLC PRARPPGPHS SPNYEFYKLY LVGGAQGRRC EAPPAPNLLL TCDRPDLDLR FTIKFQEYSP NLWGHEFRSH HDYYIIATSD GTREGLESLQ GGVCLTRGMK VLLRVGQSPR GGAVPRKPVS EMPMERDRGA AHSLEPGKEN LPGDPTSNAT SRGAEGPLPP PSMP.

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    Efnb3 Human
  • View Data Sheet

    Name :

    GALE Human

    Description:

    UDP-Galactose-4-Epimerase Human Recombinant

    UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.

    Product # :

    ENZ-537

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    Description

    GALE Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40.4 kDa. The GALE is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GALE Human solution containing 20mM Tris pH-8, 5mM DTT, 0.1M NaCl, 1mM EDTA & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.

    • Synonyms

      UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.

    • 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 MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR RVQELTGRSV EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK PLDYYRVNLT GTIQLLEIMK AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT GGCTNPYGKS KFFIEEMIRD LCQADKTWNA VLLRYFNPTG AHASGCIGED PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD YIHVVDLAKG HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA.

    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.

    Gale Human
  • View Data Sheet

    Name :

    POLR2H Human

    Description:

    Polymerase (RNA) II (DNA directed) Polypeptide H Human Recombinant

    DNA-directed RNA polymerases I, II, and III subunit RPABC3, RNA polymerases I, II, and III subunit ABC3, DNA-directed RNA polymerase II subunit H, DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide, RPB17, RPB8 homolog, hRPB8, POLR2H, polymerase (RNA) II (DNA directed) polypeptide H, RPB8, RPABC3.

    Product # :

    PRO-1443

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    Description

    POLR2H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-150 a.a) and having a molecular mass of 19.5kDa.POLR2H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POLR2H protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      POLR2H is an essential and highly conserved subunit of RNA polymerase II which is shared by the other 2 eukaryotic DNA-directed RNA polymerases, I and III. The three eukaryotic RNA polymerases are complex multisubunit enzymes which play a vital role in the transcription of nuclear genes. POLR2H encodes an essential and highly conserved subunit of RNA polymerase II which is shared by the other two eukaryotic DNA-directed RNA polymerases, I and III.

    • Synonyms

      DNA-directed RNA polymerases I, II, and III subunit RPABC3, RNA polymerases I, II, and III subunit ABC3, DNA-directed RNA polymerase II subunit H, DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide, RPB17, RPB8 homolog, hRPB8, POLR2H, polymerase (RNA) II (DNA directed) polypeptide H, RPB8, RPABC3.

    • 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 MGSMAGILFE DIFDVKDIDP EGKKFDRVSR LHCESESFKM DLILDVNIQI YPVDLGDKFR LVIASTLYED GTLDDGEYNP TDDRPSRADQ FEYVMYGKVY RIEGDETSTE AATRLSAYVS YGGLLMRLQG DANNLHGFEV DSRVYLLMKK LAF.

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    Polr2H Human
  • View Data Sheet

    Name :

    KRT20 Human, His

    Description:

    Cytokeratin 20 Human Recombinant, His Tag

    Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.

    Product # :

    PRO-1358

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    Description

    KRT20 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424 a.a) and having a molecular mass of 50.9kDa. KRT20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT20 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Recombinant Human Cytokeratin 20 His Tag (KRT20) belongs to the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins is comprised of acidic proteins that are organized in pairs of heterotypic keratin chains. KRT20 is a main cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa.

    • Synonyms

      Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.

    • 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 MGSMDFSRRS FHRSLSSSLQ APVVSTVGMQ RLGTTPSVYG GAGGRGIRIS NSRHTVNYGS DLTGGGDLFV GNEKMAMQNL NDRLASYLEK VRTLEQSNSK LEVQIKQWYE TNAPRAGRDY SAYYRQIEEL RSQIKDAQLQ NARCVLQIDN AKLAAEDFRL KYETERGIRL TVEADLQGLN KVFDDLTLHK TDLEIQIEEL NKDLALLKKE HQEEVDGLHK HLGNTVNVEV DAAPGLNLGV IMNEMRQKYE VMAQKNLQEA KEQFERQTAV LQQQVTVNTE ELKGTEVQLT ELRRTSQSLE IELQSHLSMK ESLEHTLEET KARYSSQLAN LQSLLSSLEA QLMQIRSNME RQNNEYHILL DIKTRLEQEI ATYRRLLEGE DVKTTEYQLS TLEERDIKKT RKIKTVVQEV VDGKVVSSEV KEVEENI.

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    Krt20 Human His
  • View Data Sheet

    Name :

    TPPP3 Human

    Description:

    Tubulin Polymerization-Promoting Protein Family Member 3 Human Recombinant

    Tubulin Polymerization-Promoting Protein Family Member 3, Brain Specific Protein, p25gamma, TPPP/p20, p20.

    Product # :

    PRO-1615

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    Description

    TPPP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-176) and having a molecular mass of 21.4kDa.TPPP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPPP3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      TPPP3 is a member of the TPPP family and is found in the cytoplasm. TPPP3 binds tubulin, has microtubule bundling activity takes part in mitosis and cell proliferation.

    • Synonyms

      Tubulin Polymerization-Promoting Protein Family Member 3, Brain Specific Protein, p25gamma, TPPP/p20, p20.

    • 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 MGSMAASTDM AGLEESFRKF AIHGDPKASG QEMNGKNWAK LCKDCKVADG KSVTGTDVDI VFSKVKGKSA RVINYEEFKK ALEELATKRF KGKSKEEAFD AICQLVAGKE PANVGVTKAK TGGAVDRLTD TSRYTGSHKE RFDESGKGKG IAGRQDILDD SGYVSAYKNA GTYDAKVKK

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    Tppp3 Human
  • View Data Sheet

    Name :

    TUBG1 Human

    Description:

    Tubulin Gamma 1 Human Recombinant

    Tubulin gamma 1, TUBG, TUBGCP1, tubulin gamma polypeptide, Gamma-tubulin complex component 1, GCP-1, gamma-1-tubulin, Tubulin gamma-1 chain.

    Product # :

    PRO-982

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    Description

    TUBG1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 471 amino acids (1-451 a.a.) and having a molecular mass of 53.3kDa.TUBG1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TUBG1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1M Urea, and 5% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TUBG1 belongs to the tubulin superfamily. TUBG1 localizes to the centrosome and binds to microtubules to create the gamma-tubulin ring complex. TUBG1 facilitates the microtubule nucleation and is essential for microtubule formation and progression of the cell cycle.

    • Synonyms

      Tubulin gamma 1, TUBG, TUBGCP1, tubulin gamma polypeptide, Gamma-tubulin complex component 1, GCP-1, gamma-1-tubulin, Tubulin gamma-1 chain.

    • 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 MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK REAFLEQFRK EDMFKDNFDE MDTSREIVQQ LIDEYHAATR PDYISWGTQE Q.

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    Tubg1 Human
  • View Data Sheet

    Name :

    UBE2L6 Human

    Description:

    Ubiquitin Conjugating Enzyme E2L 6 Human Recombinant

    RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.

    Product # :

    ENZ-347

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    Description

    UBE2L6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-152 a.a.) & having a molecular mass of 21.7 kDa. The UBE2L6 is fused to a 36 amino acid His Tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 20mM Tris pH-8, 0.1mM PMSF, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2L6 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2L6 enzyme is very similar in its primary structure to the enzyme encoded by UBE2L3 gene. UBE2L6 catalyzes the covalent attachment of ubiquitin to other proteins. UBE2L6 functions in the e6/e6-ap-induced ubiquitination of p53/tp53.

    • Synonyms

      RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASM RVVKELEDLQ KKPPPYLRNL SSDDANVLVW HALLLPDQPP YHLKAFNLRI SFPPEYPFKP PMIKFTTKIY HPNVDENGQI CLPIISSENW KPCTKTCQVL EALNVLVNRP NIREPLRMDL ADLLTQNPEL FRKNAEEFTL RFGVDRPS.

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    Ube2L6 Human
  • View Data Sheet

    Name :

    NUCB2 Human

    Description:

    Nucleobindin-2 Human Recombinant

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

    Product # :

    PRO-492

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    Description

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

    Source

    Escherichia Coli.

    Formulation

    The NUCB2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NUCB2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.

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

    Nucb2 Human
  • View Data Sheet

    Name :

    RLN2 Human, Sf9

    Description:

    Relaxin-2 Human Recombinant, Sf9

    Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.

    Product # :

    PRO-2406

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    Description

    RLN2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (25-185a.a.) and having a molecular mass of 19.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).RLN2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RLN2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prorelaxin H2 (RLN2) is a member of the insulin gene superfamily. This family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing oxytocin and vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.

    • Synonyms

      Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.

    • 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

      ADPDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFCHHHHHH.

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    Rln2 Human Sf9
  • View Data Sheet

    Name :

    IL 6 Human

    Description:

    Interleukin-6 Human Recombinant

    B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2,Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    Product # :

    CYT-213

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    • biological activity
    • More Info

    Description

    Interleukin-6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 21000 Dalton. The IL6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2um filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine 7TD1 cells is less than 0.1 ng/ml, corresponding to the specific activity of 1.0 x 10,000,000 Units per mg.

    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

      B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2,Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 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 Interleukin-6 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Val-Pro-Pro.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.47 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-6 as a Reference Standard.

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

    Il 6 Human
  • View Data Sheet

    Name :

    LIF Human

    Description:

    Leukemia Inhibitory Factor Human Recombinant

    CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    Product # :

    CYT-644

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    Description

    Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.

    • Background

      Leukemia Inhibitory Factor (LIF) Background

      Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.

      LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.

      Function and Applications of LIF

      LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.

      Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.

      Structure and Interactions

      LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.

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    Lif Human
  • View Data Sheet

    Name :

    IL15 Human, HEK

    Description:

    Interleukin-15 Human Recombinant, HEK

    IL-15, IL15, Interleukin-15, MGC9721.

    Product # :

    CYT-967

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    Description

    Interleukin-15 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight of 12.8kDa.The IL15 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The IL-15 protein was lyophilized from 1842µl filtered (0.2µm) solution in PBS, pH 7.4 and 10% Trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity was determined by the dose dependent stimulation of the proliferation of CTLL-2 cells, the ED50 is typically less than 0.5ng/ml, corresponding to a specific activity of >2 x 106 Unit/mg.

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.

    • Synonyms

      IL-15, IL15, Interleukin-15, MGC9721.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL15 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 IL15 with 2500µl PBS to a stock solution of 400µg/ml.

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    Il15 Human Hek
  • View Data Sheet

    Name :

    LYPLAL1 Human

    Description:

    Lysophospholipase Like I Human Recombinant

    Lysophospholipase-like protein 1, LYPLAL1.

    Product # :

    ENZ-644

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    Description

    LYPLAL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 261 amino acids (1-237) and having a molecular mass of 28.9kDa.LYPLAL1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LYPLAL1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lysophospholipase-like protein 1 (LYPLAL1) is a member of the AB hydrolase 2 family. LYPLAL1 doesn’t exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates as a result of its shallow active site.

    • Synonyms

      Lysophospholipase-like protein 1, LYPLAL1.

    • 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 MGSHMAAASG SVLQRCIVSP AGRHSASLIF LHGSGDSGQG LRMWIKQVLN QDLTFQHIKI IYPTAPPRSY TPMKGGISNV WFDRFKITND CPEHLESIDV MCQVLTDLID EEVKSGIKKN RILIGGFSMG GCMAMHLAYR NHQDVAGVFA LSSFLNKASA VYQALQKSNG VLPELFQCHG TADELVLHSW AEETNSMLKS LGVTTKFHSF PNVYHELSKT ELDILKLWIL TKLPGEMEKQ K.

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    Lypla1 Human
  • View Data Sheet

    Name :

    NREP Human

    Description:

    Neuronal Regeneration Related Protein Human Recombinant

    Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.

    Product # :

    PRO-1780

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    Description

    NREP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (1-68) and having a molecular mass of 10.3kDa.NREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NREP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuronal Regeneration Related Protein (NREP) has roles in neural function. NREP promotes axonal regeneration. In addition, NREP has functions in cellular differentiation. NREP protein induces differentiation of fibroblast into myofibroblast and increases retinoic-acid regulation of lipid-droplet biogenesis. NREP down-regulates the expression of TGFB1 and TGFB2 but not of TGFB3. NREP has a role in the regulation of alveolar generation.

    • Synonyms

      Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMVYYPEL FVWVSQEPFP NKDMEGRLPK GRLPVPKEVN RKKNDETNAA SLTPLGSSEL RSPRISYLHF F.

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    Nrep Human
  • View Data Sheet

    Name :

    GDI2 Human

    Description:

    GDP Dissociation Inhibitor 2 Human Recombinant

    GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.

    Product # :

    PRO-1948

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    Description

    GDI2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 468 amino acids (1-445) and having a molecular mass of 53.1 kDa.GDI2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDI2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Rab GDP dissociation inhibitor beta isoform 1 (GDI2) is a member of the GDP dissociation inhibitors (GDIs) family. GDI proteins can bind and release GDP-bound Rab proteins from membranes. GDI1 interacts with virtually all of the Rab proteins, whereas GDI2 interacts with Rabll but not Rab3A. GDI2 distributes ubiquitously, presenting a membrane bound location in perinuclear regions of cells.

    • Synonyms

      GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.

    • 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 MGSMNEEYDV IVLGTGLTEC ILSGIMSVNG KKVLHMDRNP YYGGESASIT PLEDLYKRFK IPGSPPESMG RGRDWNVDLI PKFLMANGQL VKMLLYTEVT RYLDFKVTEG SFVYKGGKIY KVPSTEAEAL ASSLMGLFEK RRFRKFLVYV ANFDEKDPRT FEGIDPKKTT MRDVYKKFDL GQDVIDFTGH ALALYRTDDY LDQPCYETIN RIKLYSESLA RYGKSPYLYP LYGLGELPQG FARLSAIYGG TYMLNKPIEE IIVQNGKVIG VKSEGEIARC KQLICDPSYV KDRVEKVGQV IRVICILSHP IKNTNDANSC QIIIPQNQVN RKSDIYVCMI SFAHNVAAQG KYIAIVSTTV ETKEPEKEIR PALELLEPIE QKFVSISDLL VPKDLGTESQ IFISRTYDAT THFETTCDDI KNIYKRMTGS EFDFEEMKRK KNDIYGED.

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    Gdi2 Human
  • View Data Sheet

    Name :

    TSSK2 Human

    Description:

    Testis Specific Serine Kinase 2 Human Recombinant

    800x600 Testis-specific serine/threonine-protein kinase 2, DGS-G, SPOGA2, STK22B, TSK2, TSK-2, TSSK-2, TSSK2, DiGeorge syndrome protein G, Serine/threonine-protein kinase 22B, DGSG, Testis Specific Serine Kinase 2.

    Product # :

    PKA-057

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    Description

    TSSK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 43kDa.TSSK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TSSK2 protein solution (0.25mg/ml) containing 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

      TSSK2 is a testis-specific serine/threonine-protein kinase required during spermatid development which phosphorylates TSKS at 'Ser-288' and SPAG16. TSSK2 takes part in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, TSSK2 is necessary for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.

    • Synonyms

      Testis-specific serine/threonine-protein kinase 2, DGS-G, SPOGA2, STK22B, TSK2, TSK-2, TSSK-2, TSSK2, DiGeorge syndrome protein G, Serine/threonine-protein kinase 22B, DGSG, Testis Specific Serine Kinase 2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMDDATVL RKKGYIVGIN LGKGSYAKVK SAYSERLKFN VAVKIIDRKK TPTDFVERFL PREMDILATV NHGSIIKTYE IFETSDGRIY IIMELGVQGD LLEFIKCQGA LHEDVARKMF RQLSSAVKYC HDLDIVHRDL KCENLLLDKD FNIKLSDFGF SKRCLRDSNG RIILSKTFCG SAAYAAPEVL QSIPYQPKVY DIWSLGVILY IMVCGSMPYD DSDIRKMLRI QKEHRVDFPR SKNLTCECKD LIYRMLQPDV SQRLHIDEIL SHSWLQPPKP KATSSASFKR EGEGKYRAEC KLDTKTGLRP DHRPDHKLGA KTQHRLLVVP ENENRMEDRL AETSRAKDHH ISGAEVGKAS T.

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    Tssk2 Human
  • View Data Sheet

    Name :

    IL31 Canine

    Description:

    Interleukin-31 Canine Recombinant

    IL-31, Interleukin 31, IL31.

    Product # :

    CYT-1137

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    Description

    IL31 Canine produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 136 amino acids (24-159 aa) and having a molecular mass of 15.3kDa.IL31 is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The IL31 solution (0.25mg/ml) contains 20% Glycerol and Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
      Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis.

    • Synonyms

      IL-31, Interleukin 31, IL31.

    • 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

      SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN
      SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS
      LNSGPQ

    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 31 Canine
  • View Data Sheet

    Name :

    PLGF2 Human, HEK

    Description:

    Placental Growth Factor-2, HEK Human Recombinant

    PIGF, PGF, PlGF-2, PLGF-2.

    Product # :

    CYT-1228

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    Description

    PLGF2 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-170) containing 158 amino acids and having a molecular mass of 18.1kDa. PLGF2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    PLGF2 protein (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human VEGFR1/Flt-1.

    More Info

    • Synonyms

      PIGF, PGF, PlGF-2, PLGF-2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RRHHHHHH.

    • Background

      PLGF2, a homodimeric glycoprotein, exhibits a unique structural configuration essential for its interactions with VEGF receptors and other signaling molecules. The human recombinant form provides a controlled platform for studying the three-dimensional structure of PLGF2, elucidating its binding affinities and conformational dynamics. Understanding its structure is fundamental for deciphering how PLGF2 mediates angiogenic signaling and vascular remodeling.

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    Pigf2 Human
  • View Data Sheet

    Name :

    Thymosin beta 4

    Description:

    Thymosin β4

    Thymosin beta-4. TB500, TB-500

    Product # :

    HOR-275

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    Description

    Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.

    • Synonyms

      Thymosin beta-4. TB500, TB-500

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.

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    Thymosin Beta 4
  • View Data Sheet

    Name :

    EPO Mouse

    Description:

    Erythropoietin Mouse Recombinant

    Erythropoietin, erythropoietin isoform 1 precursor, Epo.

    Product # :

    CYT-1171

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    • sds-page

    Description

    EPO Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 176 amino acids (27-192 aa) and having a molecular mass of 19.8kDa.EPO is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EPO Mouse protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

    sds-page

    EPO-sds-page - Product image 1

    More Info

    • Introduction

      Erythropoietin or EPO is a hormone (glycoprotein), part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.

    • Synonyms

      Erythropoietin, erythropoietin isoform 1 precursor, Epo.

    • 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

      ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.

    • Background

      What is the molecular weight/Mw of EPO Protein?
      EPO Protein has a total Mw of 19.8kDa.

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

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

      What is the Biological Activity of EPO Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

      What is the amino acid sequence of EPO Protein?
      ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.

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

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

    Epo Mouse
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