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Search results

1000 results found for “nucleopurin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    POLR2I Human

    Description:

    Polymerase II Polypeptide I Human Recombinant

    hRPB14.5, RPB9, DNA-directed RNA polymerase II subunit RPB9, DNA-directed RNA polymerase II subunit I, RNA polymerase II 14.5 kDa subunit, RPB14.5.

    Product # :

    ENZ-669

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    Description

    POLR2I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (1-125 a.a.) and having a molecular mass of 17.0kDa.POLR2I is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    POLR2I protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Polymerase II Polypeptide I (POLR2I) is a member of the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family. POLR2I is a subunit of RNA polymerase II, which is a polymerase responsible for synthesizing messenger RNA in eukaryotes. DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. In addition POLR2I synthesizes mRNA precursors and numerous functional non-coding RNAs.

    • Synonyms

      hRPB14.5, RPB9, DNA-directed RNA polymerase II subunit RPB9, DNA-directed RNA polymerase II subunit I, RNA polymerase II 14.5 kDa subunit, RPB14.5.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEPDGTY EPGFVGIRFC QECNNMLYPK EDKENRILLY ACRNCDYQQE ADNSCIYVNK ITHEVDELTQ IIADVSQDPT LPRTEDHPCQ KCGHKEAVFF QSHSARAEDA MRLYYVCTAP HCGHRWTE.

    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.

    Polr2I Human
  • View Data Sheet

    Name :

    POLR2J2 Human

    Description:

    Polymerase II Polypeptide J2 Human Recombinant

    HRPB11B, RPB11b1, POLR2J2, DNA-directed RNA polymerase II subunit RPB11-b1.

    Product # :

    ENZ-689

    Price :

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    Description

    POLR2J2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115) and having a molecular mass of 15.5kDa. POLR2J2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The POLR2J2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT and 250mM Imidazole.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      POLR2J2 belongs to the RNA polymerase II subunit 11 gene family, that includes 3 genes in a cluster on chromosome 7q22.1 and a pseudogene on chromosome 7p13. DNA directed RNA polymerase II polypeptide J family encodes a subunit of RNA polymerase II, the polymerase which is responsible for synthesizing messenger RNA in eukaryotes. This locus produces multiple, otherwise spliced transcripts which express isoforms with distinct C-termini compared to DNA directed RNA polymerase II polypeptide J. Most or all variants are spliced to include additional non-coding exons at the 3' end that makes them candidates for nonsense-mediated decay (NMD). Therefore, it is unknown if this locus expresses a protein or proteins in vivo.

    • Synonyms

      HRPB11B, RPB11b1, POLR2J2, DNA-directed RNA polymerase II subunit RPB11-b1.

    • 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 MGSMNAPPAF ESFLLFEGEK ITINKDTKVP KACLFTINKE DHTLGNIIKS QLLKDPQVLF AGYKVPHPLE HKIIIRVQTT PDYSPQEAFT NAITDLISEL SLLEERFRTC LLPLRLLP.

    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.

    Polr2J2 Human
  • View Data Sheet

    Name :

    KRT18 Human, His

    Description:

    Cytokeratin 18 Human Recombinant , His Tag

    Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    Product # :

    PRO-484

    Price :

    Quantity :

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    Description

    KRT18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a calculated molecular mass of 52.42kDa.The KRT18 is fused to a His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KRT18 protein solution (0.8mg/ml) contains 20mM Tris pH 8, 5mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KRT18 encodes the type I intermediate filament chain keratin 18. Keratin 18, together with its filament partner keratin 8, are perhaps the most commonly found members of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 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. Please avoid freeze thaw cycles.

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

    Krt18 Human His
  • View Data Sheet

    Name :

    GDI1 Human

    Description:

    GDP Dissociation Inhibitor 1 Human Recombinant

    Rab GDP dissociation inhibitor alpha, Rab GDI alpha, GDP Dissociation Inhibitor 1, GDI1, Guanosine diphosphate dissociation inhibitor 1, GDI-1, Oligophrenin-2, XAP-4, GDIL, OPHN2, RABGDIA, XAP4, MRX41, MRX48, 1A, RABGD1A.

    Product # :

    PRO-2023

    Price :

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    Description

    GDI1 Human Recombinant produced in E. coli is a single polypeptide chain containing 470 amino acids (1-447) and having a molecular mass of 53 kDa.GDI1 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDI1 solution (0.25mg/1ml) 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.

    More Info

    • Introduction

      GDP Dissociation Inhibitor 1 (GDI1) is expressed mainly in neural and sensory tissues. GDI1 regulates the GDP/GTP exchange reaction of nearly all Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. GDI1 is also promoting the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Mutations in GDI1 have been associated with X-linked nonspecific mental retardation.

    • Synonyms

      Rab GDP dissociation inhibitor alpha, Rab GDI alpha, GDP Dissociation Inhibitor 1, GDI1, Guanosine diphosphate dissociation inhibitor 1, GDI-1, Oligophrenin-2, XAP-4, GDIL, OPHN2, RABGDIA, XAP4, MRX41, MRX48, 1A, RABGD1A.

    • 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 MGSMDEEYDV IVLGTGLTEC ILSGIMSVNG KKVLHMDRNP YYGGESSSIT PLEELYKRFQ LLEGPPESMG RGRDWNVDLI PKFLMANGQL VKMLLYTEVT RYLDFKVVEG SFVYKGGKIY KVPSTETEAL ASNLMGMFEK RRFRKFLVFV ANFDENDPKT FEGVDPQTTS MRDVYRKFDL GQDVIDFTGH ALALYRTDDY LDQPCLETVN RIKLYSESLA RYGKSPYLYP LYGLGELPQG FARLSAIYGG TYMLNKPVDD IIMENGKVVG VKSEGEVARC KQLICDPSYI PDRVRKAGQV IRIICILSHP IKNTNDANSC QIIIPQNQVN RKSDIYVCMI SYAHNVAAQG KYIAIASTTV ETTDPEKEVE PALELLEPID QKFVAISDLY EPIDDGCESQ VFCSCSYDAT THFETTCNDI KDIYKRMAGT AFDFENMKRK QNDVFGEAEQ.

    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.

    Gdi1 Human
  • View Data Sheet

    Name :

    PPIL2 Human

    Description:

    Cyclophilin-60 Human Recombinant

    CYC4, Cyp-60, CYP60, hCyP-60, Peptidyl-prolyl cis-trans isomerase-like 2, PPIase, Rotamase PPIL2, Cyclophilin-60, Cyclophilin-like protein Cyp-60, PPIL2, MGC787, FLJ39930, MGC33174.

    Product # :

    ENZ-497

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    Description

    PPIL2 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 547 amino acids (1-527 a.a.) and having a molecular mass of 61.6 kDa. The PPIL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPIL2 solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 290 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      PPIL2 is part of the cyclophilin family of peptidylprolyl isomerases which are highly conserved ubiquitous proteins that play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL2 interacts with the proteinase inhibitor eglin c and is localized in the nucleus. PPIL2 increases folding of proteins andcatalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

    • Synonyms

      CYC4, Cyp-60, CYP60, hCyP-60, Peptidyl-prolyl cis-trans isomerase-like 2, PPIase, Rotamase PPIL2, Cyclophilin-60, Cyclophilin-like protein Cyp-60, PPIL2, MGC787, FLJ39930, MGC33174.

    • Physical Appearance

      Sterile Filtered clear 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 MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK IIDPDEEKAK QDPSYYLKNT NAETRETLQE YKEFKGDEI LAATMKAPEK KKVDKLNAAH YSTGKVSASF TSTAMVPETT EAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV GKYINPAATE QQRKSPQPVP LSPCPRRSPV GVLGTSAPGS SRLPDDH.

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    Ppil2 Human
  • View Data Sheet

    Name :

    PPIL4 Human

    Description:

    Peptidylprolyl Isomerase (Cyclophilin)-Like 4 Human Recombinant

    Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.

    Product # :

    ENZ-026

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    Description

    PPIL4 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 512 amino acids (1-492 a.a.) and having a molecular mass of 59.3kDa. The PPIL4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 190 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      PPIL4 belongs to an evolutionarily conserved cyclophilin-type PPIase family of proteins. PPIL4, which is ubiquitously expressed with predominant expression in kidney localizes to the nucleus and contains one PPIase cyclophilin-type domain, a lysine-rich domain, a pair of bipartite nuclear targeting sequences and one RRM (RNA recognition motif) domain. The presence of the RRM domain along with nuclear targeting sequences implies that PPIL4 may be involved in transcriptional regulation.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.

    • 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 MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR.

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    Ppil4 Human
  • View Data Sheet

    Name :

    CDC37 Human, His

    Description:

    Cell Division Cycle 37 Human Recombinant, His Tag

    Cell Division Cycle 37 homolog, P50CDC37, CDC37, Hsp90 chaperone protein kinase-targeting subunit, CDC37 cell division cycle 37 homolog, hsp90 co-chaperone Cdc37, CDC37A.

    Product # :

    PRO-140

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    Description

    CDC37, His Protein is a 45.71 kDa protein containing 388 amino acids fused to a 10 aa N-Terminal His-tag.

    Source

    E. coli

    Formulation

    CDC37, His Human was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in
    20mM TRIS, 50mM NaCl, pH 7.5.

    More Info

    • Introduction

      CDC37, His protein is extremely parallel to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. CDC37 is a molecular chaperone with a detailed role in cell signal transduction. CDC37 forms a complex with Hsp90 and several protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, and eIF2 alpha kinases CDC37 has a vital part in directing Hsp90 to its target kinases.

    • Synonyms

      Cell Division Cycle 37 homolog, P50CDC37, CDC37, Hsp90 chaperone protein kinase-targeting subunit, CDC37 cell division cycle 37 homolog, hsp90 co-chaperone Cdc37, CDC37A.

    • Stability

      Store lyophilized CDC37 His human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted CDC37 can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDVSV

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    Cdc37 His Human
  • View Data Sheet

    Name :

    CENPA Human

    Description:

    Centromere Protein A Human Recombinant

    Histone H3-like centromeric protein A, Centromere protein A, CENP-A, Centromere autoantigen A, CENPA.

    Product # :

    PRO-389

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    Description

    CENPA Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 17,015 Dalton. CENPA is expressed with a -6x His tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    CENPA is supplied in 20mM HEPES buffer pH-8, 100mM sodium chloride, and 6M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Centromere proteins are a group of proteins which form and/or mediate the function of centromeres, the central structures of chromosomes to which spindle fibers/microtubuli attach and pull the chromosomes apart in cell division. Currently, 9 centromere proteins are known and designated CENPA to CENP-I. Most of the centromere proteins are targets of autoantibodies, the anti-centromere antibodies.
      CENPA is another important centromeric autoantigen in addition to CENPB: it has a molecular weight of approx. 20 kDa and is incorporated into centromeric chromatin due to its histone-like properties. CENPA antibodies are an important marker for correct diagnosis of Scleroderma / CREST syndrome in CENPB-autoantibody negative patients.

    • Synonyms

      Histone H3-like centromeric protein A, Centromere protein A, CENP-A, Centromere autoantigen A, CENPA.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels including CDC international reference sera).

    • coating concentration

      0.15-0.4 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.

    • Applications

      Western-Blot with monoclonal anti-hexa-His-tag antibody & Scleroderma patient sera.

    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.

    Cenpa Human
  • View Data Sheet

    Name :

    TXNRD1 Human 161-649 a.a.

    Description:

    Thioredoxin Reductase 1 161-649 a.a. Human Recombinant

    Thioredoxin reductase 1 cytoplasmic, TR, Gene associated with retinoic and interferon-induced mortality 12 protein, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.

    Product # :

    ENZ-042

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    Description

    TXNRD1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 510 amino acids (161-649 a.a.) and having a molecular mass of 55.9kDa. The TXNRD1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TXNRD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TXNRD1 belongs to the selenium-containing pyridine nucleotide-disulphide oxidoreductase family, which has a conserved catalytic site of Cys-Val-Asn-Val-Gly-Cys. TXNRD1 decreases thioredoxins as well as other substrates, and participates in selenium metabolism and protection against oxidative stress. Inhibition of TXNRD1 activity serves as a potential treatment for cancer, AIDS and other autoimmune diseases as well as bacterial infections and parasitic diseases.

    • Synonyms

      Thioredoxin reductase 1 cytoplasmic, TR, Gene associated with retinoic and interferon-induced mortality 12 protein, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.

    • 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 MYDYDLIIIG GGSGGLAAAK EAAQYGKKVM VLDFVTPTPL GTRWGLGGTC VNVGCIPKKL MHQAALLGQA LQDSRNYGWK VEETVKHDWD RMIEAVQNHI GSLNWGYRVA LREKKVVYEN AYGQFIGPHR IKATNNKGKE KIYSAERFLI ATGERPRYLG IPGDKEYCIS SDDLFSLPYC PGKTLVVGAS YVALECAGFL AGIGLDVTVM VRSILLRGFD QDMANKIGEH MEEHGIKFIR QFVPIKVEQI EAGTPGRLRV VAQSTNSEEI IEGEYNTVML AIGRDACTRK IGLETVGVKI NEKTGKIPVT DEEQTNVPYI YAIGDILEDK VELTPVAIQA GRLLAQRLYA GSTVKCDYEN VPTTVFTPLE YGACGLSEEK AVEKFGEENI EVYHSYFWPL EWTIPSRDNN KCYAKIICNT KDNERVVGFH VLGPNAGEVT QGFAAALKCG LTKKQLDSTI GIHPVCAEVF TTLSVTKRSG ASILQAGCCG.

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    Txnrd1 Human 161 649 Aa
  • View Data Sheet

    Name :

    CHGA Human, HEK

    Description:

    Chromogranin A Human Recombinant, HEK

    CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.

    Product # :

    PRO-2664

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    Description

    CHGA Human Recombinant is a single, glycosylated polypeptide chain containing 445 amino acids (19-457a.a) and having a molecular mass of 49.7kDa (calculated). CHGA is fused to a 6 a.a His tag at C-terminal.

    Source

    HEK293 cells.

    Formulation

    CHGA filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS, pH 7.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chromogranin A is a 439 amino acid protein which is encoded on chromosome 14 and is present in neuroendocrine cells throughout the body, including the neuroendocrine cells of the large and small intestine, adrenal medulla and pancreatic islets. It is an excellent marker for carcinoid tumors, phenochromocytomas, paragangliomas, and other neuroendocrine tumors.
      Coexpression of chromogranin A and neuron specific enolase (NSE) is common in neuroendocrine neoplasms.

    • Synonyms

      CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.

    • 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; 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.

    • Amino Acid Sequence

      LPVNSPMNKG DTEVMKCIVE VISDTLSKPS PMPVSQECFE TLRGDERILS ILRHQNLLKE LQDLALQGAK ERAHQQKKHS GFEDELSEVL ENQSSQAELK EAVEEPSSKD VMEKREDSKE AEKSGEATDG ARPQALPEPM QESKAEGNNQ APGEEEEEEE EATNTHPPAS LPSQKYPGPQ AEGDSEGLSQ GLVDREKGLS AEPGWQAKRE EEEEEEEEAE AGEEAVPEEE GPTVVLNPHP SLGYKEIRKG ESRSEALAVD GAGKPGAEEA QDPEGKGEQE HSQQKEEEEE MAVVPQGLFR GGKSGELEQE EERLSKEWED SKRWSKMDQL AKELTAEKRL EGQEEEEDNR DSSMKLSFRA RAYGFRGPGP QLRRGWRPSS REDSLEAGLP LQVRGYPEEK KEEEGSANRR PEDQELESLS AIEAELEKVA HQLQALRRGH HHHHH

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    Chga Human
  • View Data Sheet

    Name :

    GPC4 Human

    Description:

    Glypican-4 Human Recombinant

    Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.

    Product # :

    PRO-1912

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    Description

    GPC4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (401-529a.a) and having a molecular mass of 18kDa.GPC4 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GPC4 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.

    • Synonyms

      Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSSSLP SNVCNDERMA AGNGNEDDCW NGKGKSRYLF AVTGNGLANQ GNNPEVQVDT SKPDILILRQ IMALRVMTSK MKNAYNGNDV DFFDISDESS GEGSGSGCEY QQCPSEFDYN ATDHAGKSAN EKADS

    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.

    Gpc4 Human
  • View Data Sheet

    Name :

    CLPP Human

    Description:

    ClpP Caseinolytic Peptidase Human Recombinant

    Putative ATP-dependent Clp protease proteolytic subunit mitochondrial, Endopeptidase Clp, CLPP.

    Product # :

    ENZ-115

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    Description

    CLPP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (57-277 a.a.) and having a molecular mass of 24.2kDa.CLPP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLPP solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 2mM DTT, 20% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ATP-dependent Clp protease proteolytic subunit (CLPP) is a member of the peptidase family S14. CLPP cleaves peptides in a variety of proteins in a manner which requires ATP hydrolysis. CLPP being the catalytic core of the Clp proteolytic complex is commonly involved in many cellular processes via the regulation of intracellular protein quality. CLPP is responsible for a somewhat general and central housekeeping function rather than for the degradation of specific substrates.

    • Synonyms

      Putative ATP-dependent Clp protease proteolytic subunit mitochondrial, Endopeptidase Clp, CLPP.

    • 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

      MPLIPIVVEQ TGRGERAYDI YSRLLRERIV CVMGPIDDSV ASLVIAQLLF LQSESNKKPI HMYINSPGGV VTAGLAIYDT MQYILNPICT WCVGQAASMG SLLLAAGTPG MRHSLPNSRI MIHQPSGGAR GQATDIAIQA EEIMKLKKQL YNIYAKHTKQ SLQVIESAME RDRYMSPMEA QEFGILDKVL VHPPQDGEDE PTLVQKEPVE AAPAAEPVPA ST.

    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.

    Clpp Human
  • View Data Sheet

    Name :

    USP15 Human

    Description:

    Ubiquitin Specific Peptidase 15 Human Recombinant

    Ubiquitin Specific Peptidase 15, Ubiquitin Carboxyl-Terminal Hydrolase 15, Deubiquitinating Enzyme 15, Ubiquitin-Specific-Processing Protease 15, Ubiquitin Specific Protease 15, Ubiquitin Thiolesterase 15, KIAA0529, UNPH4, UNPH-2, EC 3.4.19.12, EC 3.1.2.15.

    Product # :

    PRO-1622

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    Description

    USP15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 258 amino acids (1-235) and having a molecular mass of 29.5kDa.USP15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The USP15 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      USP15 belongs to the ubiquitin specific protease (USP) family of deubiquitinating enzymes which has a vital role in ubiquitin-dependent processes through polyubiquitin chain disassembly and hydrolysis of ubiquitin-substrate bonds. USP15 connects with the COP9 signalosome, and takes part in transforming growth factor beta signalling through deubiquitination of receptor-activated SMAD transcription factors. Alternatively spliced transcript variants encoding multiple isoforms of this gene are known, and a pseudo gene of USP15 is sited on the long arm of chromosome 2.

    • Synonyms

      Ubiquitin Specific Peptidase 15, Ubiquitin Carboxyl-Terminal Hydrolase 15, Deubiquitinating Enzyme 15, Ubiquitin-Specific-Processing Protease 15, Ubiquitin Specific Protease 15, Ubiquitin Thiolesterase 15, KIAA0529, UNPH4, UNPH-2, EC 3.4.19.12, EC 3.1.2.15.

    • 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 MGSMAEGGAA DLDTQRSDIA TLLKTSLRKG DTWYLVDSRW FKQWKKYVGF DSWDKYQMGD QNVYPGPIDN SGLLKDGDAQ SLKEHLIDEL DYILLPTEGW NKLVSWYTLM EGQEPIARKV VEQGMFVKHC KVEVYLTELK LCENGNMNNV VTRRFSKADT IDTIEKEIRK IFSIPDEKET RLWNKYMSNT FEPLNKPDST IQDAGLYQGQ VLVIEQKNED GTWPRGPSTP KKPLEQSC

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    Usp15 Human
  • View Data Sheet

    Name :

    VASP Human

    Description:

    Vasodilator-Stimulated Phosphoprotein Human Recombinant

    Vasodilator-stimulated phosphoprotein, VASP.

    Product # :

    PRO-191

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    Description

    VASP 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 363 amino acids (1-343 a.a.) and having a molecular mass of 37.5kDa (Molecular weight on SDS-PAGE will appear higher). The VASP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VASP solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol, 200mM NaCl and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vasodilator-stimulated phosphoprotein (VASP) belongs to the Ena-VASP protein family. VASP is linked with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. In addition, VASP may be involved in the intracellular signaling pathways which regulate integrin-extracellular matrix interactions.

    • Synonyms

      Vasodilator-stimulated phosphoprotein, VASP.

    • 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 MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA QFAAGMASAL EALEGGGPPP PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE HIERRVSNAG GPPAPPAGGP PPPPGPPPPP GPPPPPGLPP SGVPAAAHGA GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK QEEASGGPTA PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSD.

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    Vasp Human
  • View Data Sheet

    Name :

    CNTF Human, His Active

    Description:

    Ciliary Neurotrophic Factor Human Recombinant, His Tag Active

    Ciliary neurotrophic factor, CNTF, HCNTF.

    Product # :

    CYT-909

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    Description

    CNTF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200 a.a) and having a molecular mass of 25kDa. CNTF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNTF protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.5), 1 mM DTT,30% Glycerol and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      Ciliary neurotrophic factor, CNTF, HCNTF.

    • 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 MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.

    • Background

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 25kDa.

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

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

      What is the Biological Activity of CNTF Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.

      What is the amino acid sequence of CNTF Protein?
      MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.

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

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

    Cntf Human His Active
  • View Data Sheet

    Name :

    WBP2 Human

    Description:

    WW Domain Binding Protein 2 Human Recombinant

    WW domain binding protein 2, WBP-2.

    Product # :

    PRO-1208

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    Description

    WBP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 30.5 kDa.WBP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The WBP2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      WW domain-binding protein 2 (WBP2) is a steroid hormone receptor coactivator, which contains 1 GRAM domain. The globular WW domain is comprised of 38-40 semiconserved amino acids shared by proteins of various functions including structural, regulatory, and signaling proteins. This domain is involved in mediating protein-protein interactions through the binding of polyproline ligands. WBP2 binds to the WW domain of Yes kinase-associated protein(YAP1) via its PY motifs.

    • Synonyms

      WW domain binding protein 2, WBP-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 MGSMALNKNH SEGGGVIVNN TESILMSYDH VELTFNDMKN VPEAFKGTKK GTVYLTPYRV IFLSKGKDAM QSFMMPFYLM KDCEIKQPVF GANYIKGTVK AEAGGGWEGS ASYKLTFTAG GAIEFGQRML QVASQASRGE VPSGAYGYSY MPSGAYVYPP PVANGMYPCP PGYPYPPPPP EFYPGPPMMD GAMGYVQPPP PPYPGPMEPP VSGPDVPSTP AAEAKAAEAA ASAYYNPGNP HNVYMPTSQP PPPPYYPPED KKTQ

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    Wbp2 Human
  • View Data Sheet

    Name :

    RBM17 Human

    Description:

    RNA Binding Motif Protein 17 Human Recombinant

    RNA Binding Motif Protein 17, SPF45, Splicing Factor 45kDa, RNA-Binding Motif Protein 17, Splicing Factor 45, 45 kDa-splicing factor, RBM17.

    Product # :

    PRO-1793

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    Description

    RBM17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (1-401 a.a) and having a molecular mass of 47.1kDa.RBM17 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RBM17 protein solution (0.5mg/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

      RNA binding motif protein 17 (RBM17) is a splice factor which binds to the single stranded 3'AG at the exon/intron border and promotes its utilization in the 2nd catalytic step. The RBM17 protein is involved in the regulation of alternative splicing and the utilization of cryptic splice sites. RBM17 protein also stimulates the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The ensuing frameshift leads to sickle cell anemia.

    • Synonyms

      RNA Binding Motif Protein 17, SPF45, Splicing Factor 45kDa, RNA-Binding Motif Protein 17, Splicing Factor 45, 45 kDa-splicing factor, RBM17.

    • 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 MSLYDDLGVE TSDSKTEGWS KNFKLLQSQL QVKKAALTQA KSQRTKQSTV LAPVIDLKRG GSSDDRQIVD TPPHVAAGLK DPVPSGFSAG EVLIPLADEY DPMFPNDYEK VVKRQREERQ RQRELERQKE IEEREKRRKD RHEASGFARR PDPDSDEDED YERERRKRSM GGAAIAPPTS LVEKDKELPR DFPYEEDSRP RSQSSKAAIP PPVYEEQDRP RSPTGPSNSF LANMGGTVAH KIMQKYGFRE GQGLGKHEQG LSTALSVEKT SKRGGKIIVG DATEKDASKK SDSNPLTEIL KCPTKVVLLR NMVGAGEVDE DLEVETKEEC EKYGKVGKCV IFEIPGAPDD EAVRIFLEFE RVESAIKAVV DLNGRYFGGR VVKACFYNLD KFRVLDLAEQ V.

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    Rbm17 Human
  • View Data Sheet

    Name :

    RCN2 Human

    Description:

    Reticulocalbin 2 Human Recombinant

    Reticulocalbin-2, Calcium-binding protein ERC-55, E6-binding protein, 6BP, RCN2, ERC55, E6BP, ERC-55, TCBP49.

    Product # :

    PRO-189

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    Description

    RCN2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (26-317 a.a.) and having a molecular mass of 36.8kDa (Molecular weight on SDS-PAGE will appear higher).RCN2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RCN2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Reticulocalbin-2 (RCN2) is a member of the CREC protein family. RCN2 is a calcium-binding protein found in the lumen of the ER. RCN2 contains 6 conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.

    • Synonyms

      Reticulocalbin-2, Calcium-binding protein ERC-55, E6-binding protein, 6BP, RCN2, ERC55, E6BP, ERC-55, TCBP49.

    • 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 MEELHYPLGE RRSDYDREAL LGVQEDVDEY VKLGHEEQQK RLQAIIKKID LDSDGFLTES ELSSWIQMSF KHYAMQEAKQ QFVEYDKNSD DTVTWDEYNI QMYDRVIDFD ENTALDDAEE ESFRKLHLKD KKRFEKANQD SGPGLSLEEF IAFEHPEEVD
      YMTEFVIQEA LEEHDKNGDG FVSLEEFLGD YRWDPTANED PEWILVEKDR FVNDYDKDND GRLDPQELLP WVVPNNQGIA QEEALHLIDE MDLNGDKKLS EEEILENPDL FLTSEATDYG RQLHDDYFYH DEL.

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    Rcn2 Human
  • View Data Sheet

    Name :

    Resistin Human, HEK

    Description:

    Resistin Human Recombinant, HEK

    RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.

    Product # :

    CYT-1183

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    Description

    Resistin Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (19-108 a.a) containing 96 amino acids and having a molecular mass of 10.3 kDa.Resistin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    Resistin protein (1mg/ml) contains 20% glycerol and 20mM Sodium citrate (pH3.0).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis.Resistin blocks insulinstimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of lowdensity lipoprotein (LDL), increasing the risk of heart disease.

    • Synonyms

      RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.

    • 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

      KTLCSMEEAI NERIQEVAGS LIFRAISSIG LECQSVTSRG DLATCPRGFA VTGCTCGSAC GSWDVRAETT CHCQCAGMDW TGARCCRVQP HHHHHH

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

    Resistin Protein
  • View Data Sheet

    Name :

    Resistin Mutant Human

    Description:

    Resistin Mutant Human Recombinant

    Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-585

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    Description

    9.9 kDa protein containing 93 amino acid residues, produced in E.coli. Mutant-Resistin has had a Cysteine residue mutated to prevent dimerization and possibly acts as an antagonist.

    Source

    Escherichia Coli.

    Formulation

    Recombinant Human Resistin was lyophilized from a concentrated (1mg/ml) solution containing 0.1% TFA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrophobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
      Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity and is stimulated by several antidiabetic drugs.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Stability

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

    • Solubility

      Add 0.2 ml of deionized water and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP.

    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.

    Resistin Mutant Human
  • View Data Sheet

    Name :

    ZWILCH Human

    Description:

    Zwilch Kinetochore Protein Human Recombinant

    hZwilch, KNTC1AP, Protein zwilch homolog, ZWILCH.

    Product # :

    PRO-1984

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    Description

    ZWILCH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 614 amino acids (1-591 a.a) and having a molecular mass of 69.6kDa. ZWILCH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Zwilch Kinetochore Protein which is also known as ZWILCH is a part of the ZWILCH family. ZWILCH is a vital part of the mitotic checkpoint. ZWILCH prevents the cells from exiting mitosis prematurely. ZWILCH is also necessary for the assembly of the dyneindynactin and MAD1-MAD2 complexes onto kinetochores.

    • Synonyms

      hZwilch, KNTC1AP, Protein zwilch homolog, ZWILCH.

    • 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 MGSMWERLNC AAEDFYSRLL QKFNEEKKGI RKDPFLYEAD VQVQLISKGQ PNPLKNILNE NDIVFIVEKV PLEKEETSHI EELQSEETAI SDFSTGENVG PLALPVGKAR QLIGLYTMAH NPNMTHLKIN LPVTALPPLW VRCDSSDPEG TCWLGAELIT TNNSITGIVL YVVSCKADKN YSVNLENLKN LHKKRHHLST VTSKGFAQYE LFKSSALDDT ITASQTAIAL DISWSPVDEI LQIPPLSSTA TLNIKVESGE PRGPLNHLYR ELKFLLVLAD GLRTGVTEWL EPLEAKSAVE LVQEFLNDLN KLDGFGDSTK KDTEVETLKH DTAAVDRSVK RLFKVRSDLD FAEQLWCKMS SSVISYQDLV KCFTLIIQSL QRGDIQPWLH SGSNSLLSKL IHQSYHGTMD TVSLSGTIPV QMLLEIGLDK LKKDYISFFI GQELASLNHL EYFIAPSVDI QEQVYRVQKL HHILEILVSC MPFIKSQHEL LFSLTQICIK YYKQNPLDEQ HIFQLPVRPT AVKNLYQSEK PQKWRVEIYS GQKKIKTVWQ LSDSSPIDHL NFHKPDFSEL TLNGSLEERI FFTNMVTCSQ VHFK.

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    AOD-9604
  • View Data Sheet

    Name :

    RPL22 Human

    Description:

    Ribosomal Protein L22 Human Recombinant

    Ribosomal Protein L22, Epstein-Barr-Encoded RNA-Associated Protein, Epstein-Barr Virus Small RNA-Associated Protein, 60S Ribosomal Protein L22, EBER-Associated Protein, EAP, HBP15/L22.

    Product # :

    PRO-1549

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    Description

    RPL22 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (1-128) and having a molecular mass of 17.0kDa.RPL22 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPL22 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      RPL22, a cytoplasmic ribosomal protein, is a member of the L22E family of ribosomal proteins and a component of the 60S subunit. RPL22 binds specifically to Epstein-Barr virus-encoded RNAs (EBERs) 1 and 2.

    • Synonyms

      Ribosomal Protein L22, Epstein-Barr-Encoded RNA-Associated Protein, Epstein-Barr Virus Small RNA-Associated Protein, 60S Ribosomal Protein L22, EBER-Associated Protein, EAP, HBP15/L22.

    • 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 MGSMAPVKKL VVKGGKKKKQ VLKFTLDCTH PVEDGIMDAA NFEQFLQERI KVNGKAGNLG GGVVTIERSK SKITVTSEVP FSKRYLKYLT KKYLKKNNLR DWLRVVANSK ESYELRYFQI NQDEEEEEDE D.

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    Rpl22 Human
  • View Data Sheet

    Name :

    BDNF Human, CHO

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant, CHO

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-1262

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    • sds-page

    Description

    Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    CHO Cells

    Formulation

    The protein was lyophilized with 5% trehalose and 1x PBS

    Purity

    Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

    Biological Activity

    BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

    sds-page

    bdnf human cho sds-page - Product image 1

    More Info

    • Introduction

      BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
      BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

      What is the source or expression system of BDNF Protein?
      CHO Cells

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

      What is the Biological Activity of BDNF Protein?
      BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

      What is the amino acid sequence of BDNF Protein?
      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • References

      Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
      Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
      Link:BDNF prospec publication

    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.

    Bdnf Human Cho
  • View Data Sheet

    Name :

    SCGB1A1 Mouse

    Description:

    Uteroglobin Mouse Recombinant

    Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

    Product # :

    CYT-746

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    Uteroglobin Mouse Recombinant produced in E.coli is a non-glycosylated disulfide-linked homodimeric protein containing 2x75 amino acids chains and having a molecular mass of 16.7kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Uteroglobin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, 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 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.

    More Info

    • Introduction

      Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.

    • Synonyms

      Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DICPGFLQVL EALLMESESG YVASLKPFNP GSDLQNAGTQ LKRLVDTLPQ ETRINIMKLT EKILTSPLCK QDLRF.

    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.

    Scgb1A1 Mouse
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