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Search results

1000 results found for “DEAD Box Protein”

Name

Description

Product #

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  • View Data Sheet

    Name :

    C4 Human

    Description:

    Complement C4 Human

    Complement C4-A, Acidic complement C4, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2, C4A, CO4, CPAMD2.

    Product # :

    PRO-2688

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    Description

    Human Complement C4 produced in Human plasma having a molecular mass of 205 kDa.

    Source

    Human Plasma.

    Formulation

    C4 protein solution contains PBS, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Native human C4 is aglycosylated polypeptide containing 3 disulfide-linked chains. C4 is essential to the activation of both thelectin and the classical pathways of complement activation.Initiation of each pathway generates proteolytic enzyme complexes which are bound to the target surface. These enzymes cleave a peptide bond in C4 releasing the anaphylatoxin C4a and activating C4b. Like C3, the thioester of metastable C4b is highly reactive and is capable of reacting and covalently coupling C4b to amino or hydroxyl groups on the target surface. C4A and C4B are 2 variants of C4 that are common in manwhereas, in animals who have only 1 type usually have C4B.

    • Synonyms

      Complement C4-A, Acidic complement C4, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2, C4A, CO4, CPAMD2.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C4 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HTLV-I &II, STS and HBSAG.

    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.

    C4 Human
  • View Data Sheet

    Name :

    DCPS Human

    Description:

    Decapping Enzyme, Scavenger Human Recombinant

    Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.

    Product # :

    ENZ-159

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    Description

    DCPS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-337 a.a.) and having a molecular mass of 40.7kDa.DCPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCPS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Scavenger mRNA-decapping enzyme (DCPS) is a member of the HIT family. DCPS is required for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It was shown that DCPS hydrolyzes the residual m7GpppN cap structure after the complete 3'–5' degradation of the mRNA by the exosome. Furthermore, DCPS releases m7GMP and is incapable of cleaving cap structures attached to a long RNA chain.

    • Synonyms

      Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.

    • 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 MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ KVLRESARDK IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP PRQLNDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL LRNILHQGQE AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS.

    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.

    Dcps Human
  • View Data Sheet

    Name :

    RAP2B Human

    Description:

    RAP2B, Member RAS Oncogene Family Human Recombinant

    RAP2B, member of RAS oncogene family, Ras-related protein Rap-2b, Ras Family Small GTP Binding Protein RAP2B2, Small GTP Binding Protein.

    Product # :

    PRO-1364

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    Description

    RAP2B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-183 a.a) and having a molecular mass of 22.9kDa. RAP2B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RAP2B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ras-related protein Rap-2b (RAP2B) is a part of RAS-related genes family. RAP2B has a threonine residue at aa 61Unlike normal ras proteins which have a nontransforming glutamine residue at that position. The threonine residue makes the intrinsic GTPase activity for Rap2B lower, by this means allows RAP2B to exist in the activated state for a longer period of time than normal ras proteins. RAP2B is a platelet protein which is activated by thrombin and involved in platelet activation. RAP2B may be a candidate oncogene which takes part in carcinogenesis through activation of NF-kappaB pathway.

    • Synonyms

      RAP2B, member of RAS oncogene family, Ras-related protein Rap-2b, Ras Family Small GTP Binding Protein RAP2B2, Small GTP Binding 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 MGSMREYKVV VLGSGGVGKS ALTVQFVTGS FIEKYDPTIE DFYRKEIEVD SSPSVLEILD TAGTEQFASM RDLYIKNGQG FILVYSLVNQ QSFQDIKPMR DQIIRVKRYE RVPMILVGNK VDLEGEREVS YGEGKALAEE WSCPFMETSA KNKASVDELF AEIVRQMNYA AQPNGDEGCC SACVIL.

    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.

    Rap2B Human
  • View Data Sheet

    Name :

    ZFAND1 Human

    Description:

    Zinc Finger, AN1-Type Domain 1 Human Recombinant

    AN1-type zinc finger protein 1, ZFAND1, Zinc finger AN1-type domain 1.

    Product # :

    PRO-1564

    Price :

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    Description

    ZFAND1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 291 amino acids (1-268 a.a) and having a molecular mass of 33.2kDa.ZFAND1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ZFAND1 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

      AN1-type zinc finger protein 1 isoform a (ZFAND1) is a member of the Zinc-finger proteins. Proteins from this family contain DNA-binding domains and have an extensive variety of functions, most of which encompass some form of transcriptional activation or repression. ZFAND1 is a 268 amino acid protein, which contains two AN1-type zinc fingers that are repeatedly found in proteins which contain an ubiquitin-like domain and for that reason have a role in the ubiquitination pathway ZFAND1 is comprised of 6 conserved cysteines and 2 histidines and have a dimetal (zinc)-bound alpha/beta fold. As a result of alternative splicing events two isoforms of ZFAND1 are produced.

    • Synonyms

      AN1-type zinc finger protein 1, ZFAND1, Zinc finger AN1-type domain 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAELDIG QHCQVEHCRQ RDFLPFVCDD CSGIFCLEHR SRESHGCPEV TVINERLKTD QHTSYPCSFK DCAERELVAV ICPYCEKNFC LRHRHQSDHE CEKLEIPKPR MAATQKLVKD IIDSKTGETA SKRWKGAKNS ETAAKVALMK LKMHADGDKS LPQTERIYFQ VFLPKGSKEK SKPMFFCHRW SIGKAIDFAA SLARLKNDNN KFTAKKLRLC HITSGEALPL DHTLETWIAK EDCPLYNGGN IILEYLNDEE QFCKNVESYL E.

    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.

    Zfand1 Human
  • View Data Sheet

    Name :

    MBP (27-392) E.Coli

    Description:

    Maltose Binding Protein E.coli Recombinant

    Product # :

    PRO-616

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    Description

    Maltose Binding Protein E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (27-392) with additional 20aa linker and having a molecular mass of 42kDa.

    Source

    Escherichia Coli.

    Formulation

    The Maltose Binding Protein solution (1 mg/ml) contains 20mM Tris-HCl pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
      MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

    • 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

      MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIAVEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF KYENGKYDIK DVGVDNAGAK AGLTFLVDLI KNKHMNADTD YSIAEAAFNK GETAMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAVALKSYEE ELAKDPRIAA TMENAQKGEI MPNIPQMSAF WYAVRTAVIN AASGRQTVDE ALKDAQTNSS SNNNNNNNNN NLGIEGR.

    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.

    Maltose Binding Protein
  • View Data Sheet

    Name :

    S.Typhi OMP 52kDa

    Description:

    Salmonella Typhi Outer Membrane Protein 52kDa Recombinant

    Product # :

    STY-003

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    Description

    Recombinant S.Typhi OMP produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 52 kDa and fused to a His tag at C-terminus.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 1mg/ml in 20mM sodium carbonate pH-10.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized S.Typhi OMP between 2-8°C, do not freeze. Upon reconstitution S.Typhi OMP 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 S.Typhi OMP in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Styphi Omp 52Kda
  • View Data Sheet

    Name :

    C8G Human

    Description:

    Complement Component 8, Gamma Human Recombinant

    Complement component 8 gamma polypeptide, C8C, complement component C8 gamma chain, MGC142186.

    Product # :

    PRO-947

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    Description

    C8G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (21-202) and having a molecular mass of 22.6 kDa.The C8G is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The C8G solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      C8, a component of the complement system consists of three polypeptides C8A, C8B and C8G and takes part in the formation of Membrane Attack Complex (MAC). Patients with C8 deficiency are exposed to several bacteria infections. C8G, a member of the lipocalin family and calycin superfamily, is a secreted protein that can bind retinol. C8G is created in the liver, monocytes and fibroblast and has a role in clearing pathogens from an infected host.

    • Synonyms

      Complement component 8 gamma polypeptide, C8C, complement component C8 gamma chain, MGC142186.

    • 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 MQKPQRPRRP ASPISTIQPK ANFDAQQFAG TWLLVAVGSA CRFLQEQGHR AEATTLHVAP QGTAMAVSTF RKLDGICWQV RQLYGDTGVL GRFLLQARGA RGAVHVVVAE TDYQSFAVLY LERAGQLSVK LYARSLPVSD SVLSGFEQRV QEAHLTEDQI FYFPKYGFCE AADQFHVLDE VRR

    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.

    C8G Human
  • View Data Sheet

    Name :

    Anaplasma p44

    Description:

    Anaplasma phagocytophilum p44 Recombinant

    Product # :

    PRO-2566

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    Description

    Recombinant Anaplasma p44 produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 49kDa. Anaplasma p44 is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Anaplasma p44 is supplied at a 20mM HEPES buffer pH-8.0, 250mM NaCl and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Anaplasma p44 which belongs to the outer membrane antigen superfamily (OMP1/Msp2/p44), is a serodiagnostic antigen for HGA. Anaplasma p44 allows the bacterium to adhere to the host cell and prevents host immune surveillance.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG- and IgM-type human antibodies. 2. Immunodot test with positive/negative samples.

    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.

    Anaplasma Phagocytophilum P44
  • View Data Sheet

    Name :

    MAD2L1 Human

    Description:

    MAD2 Mitotic Arrest Deficient-Like 1 Human Recombinant

    Mitotic spindle assembly checkpoint protein MAD2A, HsMAD2, Mitotic arrest deficient 2-like protein 1, MAD2-like protein 1, MAD2L1, MAD2.

    Product # :

    PRO-934

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    Description

    MAD2L1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-205 a.a.) and having a molecular mass of 25.7kDa.MAD2L1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAD2L1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAD2L1-binding protein (MAD2L1) is a component of the mitotic spindle assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. MAD2L1 is vital for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate.

    • Synonyms

      Mitotic spindle assembly checkpoint protein MAD2A, HsMAD2, Mitotic arrest deficient 2-like protein 1, MAD2-like protein 1, MAD2L1, MAD2.

    • 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 MALQLSREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG LTLLVTTDLE LIKYLNNVVE QLKDWLYKCS VQKLVVVISN IESGEVLERW QFDIECDKTA KDDSAPREKS QKAIQDEIRS VIRQITATVT FLPLLEVSCS FDLLIYTDKD LVVPEKWEES GPQFITNSEE VRLRSFTTTI HKVNSMVAYK IPVND.

    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.

    Mad2L1 Human
  • View Data Sheet

    Name :

    STAP1 Human

    Description:

    Signal Transducing Adaptor Family Member 1 Human Recombinant

    Signal-transducing adaptor protein 1, STAP-1, BCR downstream-signaling protein 1, Docking protein BRDG1, Stem cell adaptor protein 1, STAP1, BRDG1.

    Product # :

    PRO-1110

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    Description

    STAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 319 amino acids (1-295 a.a) and having a molecular mass of 36.8kDa.STAP1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STAP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Signal-transducing adaptor protein 1 (STAP1) acts as a docking protein which operates downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The STAP1 protein is directly phosphorylated by Tec in vitro where it partakes in a positive feedback loop, increasing Tec activity.

    • Synonyms

      Signal-transducing adaptor protein 1, STAP-1, BCR downstream-signaling protein 1, Docking protein BRDG1, Stem cell adaptor protein 1, STAP1, BRDG1.

    • 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 MGSHMMAKKP PKPAPRRIFQ ERLKITALPL YFEGFLLIKR SGYREYEHYW TELRGTTLFF YTDKKSIIYV DKLDIVDLTC LTEQNSTEKN CAKFTLVLPK EEVQLKTENT ESGEEWRGFI LTVTELSVPQ NVSLLPGQVI KLHEVLEREK KRRIETEQST SVEKEKEPTE DYVDVLNPMP ACFYTVSRKE ATEMLQKNPS LGNMILRPGS DSRNYSITIR QEIDIPRIKH YKVMSVGQNY TIELEKPVTL PNLFSVIDYF VKETRGNLRP FICSTDENTG QEPSMEGRSE KLKKNPHIA.

    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.

    Stap1 Human
  • View Data Sheet

    Name :

    CRP (19-224 a.a) Human

    Description:

    c-Reactive Protein (19-224 a.a) Human Recombinant

    C-reactive protein, CRP, PTX1, MGC88244, MGC149895.

    Product # :

    PRO-914

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    Description

    CRP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (19-224 a.a.) and having a molecular mass of 23.2kDa.CRP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CRP protein solution (1mg/ml) containing 20mM Tris-HCl, pH8.0, 2M Urea and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.

    • Synonyms

      C-reactive protein, CRP, PTX1, MGC88244, MGC149895.

    • 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

      MQTDMSRKAF VFPKESDTSY VSLKAPLTKP LKAFTVCLHF YTELSSTRGY SIFSYATKRQ DNEILIFWSK DIGYSFTVGG SEILFEVPEV TVAPVHICTS WESASGIVEF WVDGKPRVRK SLKKGYTVGA EASIILGQEQ DSFGGNFEGS QSLVGDIGNV NMWDFVLSPD EINTIYLGGP FSPNVLNWRA LKYEVQGEVF TKPQLWP.

    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.

    CRP (19-224 a.a) Human
  • View Data Sheet

    Name :

    MGP Human

    Description:

    Matrix Gla Protein Human Recombinant

    Matrix Gla protein, Cell growth-inhibiting gene 36 protein, MGLAP, NTI.

    Product # :

    PRO-922

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    Description

    MGP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (20-96) and having a molecular mass of 11.8 kDa.The MGP is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MGP is vital for the regulation of calcification in the extracellular matrix, particularly in cartilage and arteries. The K-dependent vitamin MGP has five to six residues of Gla, a Ca2+ binding amino acid crucial for vitamin K-dependent gamma carboxylase for its formation. MGP is formed by COOH-terminal processing by carboxypeptidase B-like enzymatic activity and localized in the human bone.

    • Synonyms

      Matrix Gla protein, Cell growth-inhibiting gene 36 protein, MGLAP, NTI.

    • 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 MYESHESMES YELNPFINRR NANTFISPQQ RWRAKVQERI RERSKPVHEL NREACDDYRL CERYAMVYGY NAAYNRYF

    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.

    Mgp Human
  • View Data Sheet

    Name :

    YIF1B Human

    Description:

    Yip1 Interacting Factor Homolog B Human Recombinant

    Yip1 Interacting Factor Homolog B (S. Cerevisiae), YIP1-Interacting Factor Homolog B, Protein YIF1B, FinGER8, YIF1B.

    Product # :

    PRO-1970

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    Description

    YIF1B Human Recombinant produced in E. coli is a single polypeptide chain containing 179 amino acids (1-156) and having a molecular mass of 19.5 kDa.YIF1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YIF1B solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Yip1 Interacting Factor Homolog B (YIF1b) is a member of the YIF1 family.

    • Synonyms

      Yip1 Interacting Factor Homolog B (S. Cerevisiae), YIP1-Interacting Factor Homolog B, Protein YIF1B, FinGER8, YIF1B.

    • 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 MGSMHPAGLA AAAAGTPRLR KWPSKRRIPV SQPGMADPHQ LFDDTSSAQS RGYGAQRAPG GLSYPAASPT PHAAFLADPV SNMAMAYGSS LAAQGKELVD KNIDRFIPIT KLKYYFAVDT MYVGRKLGLL FFPYLHQDWE VQYQQDTPVA PRFDVNAPD.

    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.

    Yif1B Human
  • View Data Sheet

    Name :

    MINA Human

    Description:

    MYC Induced Nuclear Antigen Human Recombinant

    MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.

    Product # :

    PRO-2078

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    Description

    MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MINA protein solution (0.25mg/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

      MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.

    • Synonyms

      MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.

    • 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 MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.

    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.

    Mina Human
  • View Data Sheet

    Name :

    CEBP Alpha Human

    Description:

    CCAAT/enhancer binding protein CEBP Alpha Human Recombinant

    CCAAT/enhancer-binding protein alpha, C/EBP alpha, CEBPA, CEBP.

    Product # :

    PRO-433

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    Description

    CEBP-a Human Recombinant His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 126 (aa 270-358) and having a molecular mass of 14.5 kDa. The Human CEBP-a Human is fused to a 37 amino acids His-Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCAAT/enhancer binding protein(C/EBP) a is a family of transcription factors that all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and that form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBPs differ significantly in their physiological functions and in their downstream target genes. For example, mice lacking C/EBPa die shortly after birth due to severe hypoglycemia and the absence of glycogen storage in liver, whereas knockout of C/EBPb causes defects in female reproduction.

    • Synonyms

      CCAAT/enhancer-binding protein alpha, C/EBP alpha, CEBPA, CEBP.

    • 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 KDRWGSMGAG KAKKSVDKNS NEYRVRRERN NIAVRKSRDK AKQRNVETQQ KVLELTSDND RLRKRVEQLS RELDTLRGIF RQLPESSLVKAMGNCA.

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    Cebpa Human
  • View Data Sheet

    Name :

    HSBP 1 Human

    Description:

    Heat Shock Factor Binding Protein - 1 Human Recombinant

    NPC-A-13, HSBP1, Heat shock factor-binding protein 1, Nasopharyngeal carcinoma-associated antigen 13, HSF1BP, DKFZp686D1664, DKFZp686O24200.

    Product # :

    HSP-001

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    Description

    Recombinant Human HSBP1 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 8.5 kDa.

    Source

    Escherichia Coli.

    Formulation

    The HSBP1 protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH-7.5, 50mM NaCl, 1mM EDTA and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The heat-shock response is elicited by exposure of cells to thermal and chemical stress and through the activation of HSFs (heat shock factors) results in the elevated expression of heat-shock induced genes. Heat shock factor binding protein-1 (HSBP1), is a 76-amino-acid protein that binds to heat shock factor 1(HSF1), which is a transcription factor involved in the HS response. During HS response, HSF1 undergoes conformational transition from an inert non-DNA-binding monomer to active functional trimers. HSBP1 is nuclear-localized and interacts with the active trimeric state of HSF1 to negatively regulate HSF1 DNA-binding activity. Overexpression of HSBP1 in mammalian cells represses the transactivation activity of HSF1. When overexpressed in C.elegans HSBP1 has severe effects on survival of the animals after thermal and chemical stress consistent with a role of HSBP1 as a negative regulator of heat shock response.

    • Synonyms

      NPC-A-13, HSBP1, Heat shock factor-binding protein 1, Nasopharyngeal carcinoma-associated antigen 13, HSF1BP, DKFZp686D1664, DKFZp686O24200.

    • 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

      MAETDPKTVQ DLTSVVQTLL QQMQDKFQTM SDQIIGRIDD MSSRIDDLEK NIADLMTQAG VEELESENKI PATQKS.

    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.

    Hsbp 1 Human
  • View Data Sheet

    Name :

    HP-NAP

    Description:

    Neutrophil-activating protein A Helicobacter Pylori Recombinant

    DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.

    Product # :

    PRO-2035

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    Description

    HP-NAP Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Ala144) containing 154 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 18.2kDa.

    Source

    Escherichia Coli.

    Formulation

    HP-NAP was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.

    • Synonyms

      DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.

    • 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. HP-NAP is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASMKTFEILKHL QADAIVLFMK VHNFHWNVKG TDFFNVHKAT EEIYEEFADM FDDLAERIVQ LGHHPLVTLS EAIKLTRVKE ETKTSFHSKD IFKEILEDYK YLEKEFKELS NTAEKEGDKV TVTYADDQLA KLQKSIWMLQ AHLA.

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    Hp Nap
  • View Data Sheet

    Name :

    MICB Human

    Description:

    MHC Class-I chain related gene B Human Recombinant

    MHC class I polypeptide-related sequence B, MIC-B, MICB, PERB11.2.

    Product # :

    PRO-368

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    Description

    MICB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 326 amino acids and having a molecular mass of 37kDa. The sequence contains the extracellular domain of the mature human MICB (amino acid residues Ala23 – Tyr312). The MICB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing no additives.

    Purity

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

    Biological Activity

    Measured by its ability to bind MICB antibody in ELISA.

    More Info

    • Introduction

      MICB (MHC class I chain-related gene B) is a transmembrane glycoprotein that functions as a ligand for human NKG2D type II receptor. A closely related protein, MICA, shares 85% amino acid identity with MICB. These 2 proteins are distantly related to the MHC class I proteins. MICA and MICB (MICA/B) possess three extracellular immunoglobulin-like domains, but have no capacity to bind peptide or interact with ?2-microglobulin. The genes encoding MICA/B are found within the major histocompatibility complex on human chromosome 6. The MICB locus is polymorphic with more than 15 recognized human alleles. MICA/B are minimally expressed on normal cells, but are frequently expressed on epithelial tumors and can be induced by bacterial and viral infections. MICA/B are ligands for NKG2D, an activating receptor expressed on NK cells, NKT cells, ?? T cells, and CD8+ ?? T cells. Recognition of MICA/B by NKG2D results in the activation of cytolytic activity and/or cytokine production by these effector cells. MICA/B recognition is involved in tumor surveillance, viral infections, and autoimmune diseases. The release of soluble forms of MICA/B from tumors down-regulates NKG2D surface expression on effector cells resulting in the impairment of anti-tumor immune response.

    • Synonyms

      MHC class I polypeptide-related sequence B, MIC-B, MICB, PERB11.2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Mic B Human
  • View Data Sheet

    Name :

    MAEA Human

    Description:

    Macrophage Erythroblast Attacher Human Recombinant

    Macrophage Erythroblast Attacher, GID Complex Subunit 9 FYV10 Homolog, Lung Cancer-Related Protein 10, Proliferation-Inducing Gene 5, Human Lung Cancer Oncogene 10 Protein, Cell Proliferation-Inducing Gene 5 Protein, Erythroblast Macrophage Protein, FYV10 Homolog (S. Cerevisiae), GID Complex Subunit 9, EMLP, GID9, PIG5, HLC-10, EMP.

    Product # :

    PRO-1634

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    Description

    MAEA Human Recombinant (isoform 1) produced in E.coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (1-396) and having a molecular mass of 47.7kDa.MAEA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAEA solution contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAEA is a 396aa widely expressed adhesion protein which has 5 alternatively spliced isoforms. MAEA holds one CTLH domain and one LisH domain. MAEA forms a complex with F-actin, which takes part in regulating actin distribution in erythroblasts and macrophages and is known to assist in cell division and nuclear architecture. MAEA is confined with condensed chromatin at prophase, nuclear spindle poles at metaphase and in the contractile ring throughout cytokinesis phase and telophase.

    • Synonyms

      Macrophage Erythroblast Attacher, GID Complex Subunit 9 FYV10 Homolog, Lung Cancer-Related Protein 10, Proliferation-Inducing Gene 5, Human Lung Cancer Oncogene 10 Protein, Cell Proliferation-Inducing Gene 5 Protein, Erythroblast Macrophage Protein, FYV10 Homolog (S. Cerevisiae), GID Complex Subunit 9, EMLP, GID9, PIG5, HLC-10, EMP.

    • 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 MGSMAVQESA AQLSMTLKVQ EYPTLKVPYE TLNKRFRAAQ KNIDRETSHV TMVVAELEKT LSGCPAVDSV VSLLDGVVEK LSVLKRKAVE SIQAEDESAK LCKRRIEHLK EHSSDQPAAA SVWKRKRMDR MMVEHLLRCG YYNTAVKLAR QSGIEDLVNI EMFLTAKEVE ESLERRETAT CLAWCHDNKS RLRKMKSCLE FSLRIQEFIE LIRQNKRLDA VRHARKHFSQ AEGSQLDEVR QAMGMLAFPP DTHISPYKDL LDPARWRMLI QQFRYDNYRL HQLGNNSVFT LTLQAGLSAI KTPQCYKEDG SSKSPDCPVC SRSLNKLAQP LPMAHCANSR LVCKISGDVM NENNPPMMLP NGYVYGYNSL LSIRQDDKVV CPRTKEVFHF SQAEKVYIM

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    Maea Human
  • View Data Sheet

    Name :

    TXNL4A Human

    Description:

    Thioredoxin-Like 4A Human Recombinant

    Thioredoxin-like 4A, Spliceosomal U5 snRNP-specific 15 kDa protein, DIM1 protein homolog, HsT161, TXNL4, DIB1, U5-15kD.

    Product # :

    PRO-1100

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    Description

    TXNL4A Human Recombinant produced in E. coli is a single polypeptide chain containing 166 amino acids (1-142) and having a molecular mass of 19.3kDa.TXNL4A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TXNL4A solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TXNL4A is a member of the Dim protein family and has a vital part in pre-mRNA splicing. As a result of a failure to express early zygotic transcripts, deletion of the gene encoding TXNL4A in Schizosaccharomyces pombe results in embryonal lethality during gastrulation. Restricted to the nucleus, TXNL4A cooperates with hnRNP F, hnRNP H2, Cas-L and PQBP-1 to influence gene expression.

    • Synonyms

      Thioredoxin-like 4A, Spliceosomal U5 snRNP-specific 15 kDa protein, DIM1 protein homolog, HsT161, TXNL4, DIB1, U5-15kD.

    • 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 MGSHMSYMLP HLHNGWQVDQ AILSEEDRVV VIRFGHDWDP TCMKMDEVLY SIAEKVKNFA VIYLVDITEV PDFNKMYELY DPCTVMFFFR NKHIMIDLGT GNNNKINWAM EDKQEMVDII ETVYRGARKG RGLVVSPKDY STKYRY

    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.

    Txnl4A Human
  • View Data Sheet

    Name :

    PPP1R3B Human

    Description:

    Protein Phosphatase 1, Regulatory Subunit 3B Human Recombinant

    Protein phosphatase 1 regulatory subunit 3B, Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, Protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, Protein phosphatase 1 subunit GL, PTG, PPP1R4, PPP1R3B, Protein Phosphatase 1, Regulatory Subunit 3B, GL.

    Product # :

    PRO-1700

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    Description

    PPP1R3B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285) and having a molecular mass of 35.1 kDa.PPP1R3B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPP1R3B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Protein Phosphatase 1, Regulatory Subunit 3B (PPP1R3B) is the catalytic subunit of the serine/theonine phosphatase, protein phosphatase-1. PPP1R3B, which is expressed both in liver and in skeletal muscle tissue, regulates glycogen synthesis in these tissues. PPP1R3B is involved in type 2 diabetes and maturity-onset diabetes of the young.

    • Synonyms

      Protein phosphatase 1 regulatory subunit 3B, Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, Protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, Protein phosphatase 1 subunit GL, PTG, PPP1R4, PPP1R3B, Protein Phosphatase 1, Regulatory Subunit 3B, GL.

    • 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 MGSMMAVDIE YRYNCMAPSL RQERFAFKIS PKPSKPLRPC IQLSSKNEAS GMVAPAVQEK KVKKRVSFAD NQGLALTMVK VFSEFDDPLD MPFNITELLD NIVSLTTAES ESFVLDFSQP SADYLDFRNR LQADHVCLEN CVLKDKAIAG TVKVQNLAFE KTVKIRMTFD TWKSYTDFPC QYVKDTYAGS DRDTFSFDIS LPEKIQSYER MEFAVYYECN GQTYWDSNRG KNYRIIRAEL KSTQGMTKPH SGPDLGISFD QFGSPRCSYG LFPEWPSYLG YEKLGPYY.

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    Ppp1R3B Human
  • View Data Sheet

    Name :

    APP Human, HEK

    Description:

    Amyloid beta (A4) Precursor Protein Human Recombinant, HEK

    ABPP, APPI, Alzheimer disease amyloid A4 protein homolog, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Amyloid-beta A4 protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, A4, AD1, beta-amyloid peptide, beta-amyloid precursor protein, testicular tissue protein Li 2, AAA, ABETA, alpha-sApp, CTF gamma, PN2.

    Product # :

    PRO-2777

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    Description

    APP Human Recombinant is a single, glycosylated, polypeptide chain (18-701 a.a) containing a total of 690 amino acids, having a molecular mass of 78.2 kDa. APP is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

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

    Purity

    > 90% by SDS-PAGE.

    Biological Activity

    The inhibitory function of APP on activity of trypsin was measured by a fluorometric

    assay using Mca-RPKPVE-Nval-WRK(Dnp)-NH2 at pH 7.5 at 37C.  The IC50 ≤ 1 nM.

    More Info

    • Synonyms

      ABPP, APPI, Alzheimer disease amyloid A4 protein homolog, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Amyloid-beta A4 protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, A4, AD1, beta-amyloid peptide, beta-amyloid precursor protein, testicular tissue protein Li 2, AAA, ABETA, alpha-sApp, CTF gamma, PN2.

    • 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

      LEVPTDGNAG LLAEPQIAMF CGRLNMHMNV QNGKWDSDPS GTKTCIDTKE GILQYCQEVY PELQITNVVE ANQPVTIQNW CKRGRKQCKT HPHFVIPYRC LVGEFVSDAL LVPDKCKFLH QERMDVCETH LHWHTVAKET CSEKSTNLHD YGMLLPCGID KFRGVEFVCC PLAEESDNVD SADAEEDDSD VWWGGADTDY ADGSEDKVVE VAEEEEVAEV EEEEADDDED DEDGDEVEEE AEEPYEEATE RTTSIATTTT TTTESVEEVV REVCSEQAET GPCRAMISRW YFDVTEGKCA PFFYGGCGGN RNNFDTEEYC MAVCGSAMSQ SLLKTTQEPL ARDPVKLPTT AASTPDAVDK YLETPGDENE HAHFQKAKER LEAKHRERMS QVMREWEEAE RQAKNLPKAD KKAVIQHFQE KVESLEQEAA NERQQLVETH MARVEAMLND RRRLALENYI TALQAVPPRP RHVFNMLKKY VRAEQKDRQH TLKHFEHVRM VDPKKAAQIR SQVMTHLRVI YERMNQSLSL LYNVPAVAEE IQDEVDELLQ KEQNYSDDVL ANMISEPRIS YGNDALMPSL TETKTTVELL PVNGEFSLDD LQPWHSFGAD SVPANTENEV EPVDARPAAD RGLTTRPGSG LTNIKTEEIS EVKMDAEFRH DSGYEVHHQK LVFFAEDVGS NKGA HHHHHH.

    • Background

      Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the accumulation of amyloid plaques and neurofibrillary tangles in the brain, leading to cognitive decline and memory loss. The amyloid beta (Aβ) peptide, derived from the amyloid beta (A4) precursor protein, has been identified as a key player in the pathogenesis of AD. This research aims to explore the significance of the amyloid beta precursor protein, its processing, and the implications it holds for understanding and treating Alzheimer's disease.
      The amyloid beta precursor protein (APP) is a transmembrane protein widely expressed in various tissues, with higher concentrations found in the brain. APP undergoes sequential proteolytic processing by enzymes known as secretases, leading to the generation of Aβ peptides of different lengths. Of particular importance is the production of the Aβ42 peptide, which has a propensity to aggregate and form the characteristic amyloid plaques in AD.
      Understanding the processing and metabolism of APP is crucial for unraveling the mechanisms underlying AD pathology. Mutations in the APP gene and dysregulation of its processing have been associated with familial forms of AD, highlighting the pivotal role of APP in disease development. Investigating the function of APP and its proteolytic fragments can provide valuable insights into the molecular events leading to AD and potentially lead to the identification of therapeutic targets.
      This research will delve into the processing of the amyloid beta precursor protein, shedding light on the different cleavage pathways mediated by α-, β-, and γ-secretases. The paper will discuss the impact of these proteolytic events on the generation of Aβ peptides and how alterations in these pathways contribute to AD pathogenesis. Furthermore, it will explore the aggregation properties of Aβ peptides and their role in the formation of amyloid plaques, as well as their impact on neuronal function and viability.
      The study will also examine the potential of APP and Aβ as biomarkers for AD diagnosis and progression monitoring. Investigating the levels of APP and Aβ peptides in biological fluids and utilizing imaging techniques to detect amyloid plaques could enhance early diagnosis and facilitate the development of novel therapeutic interventions.
      By elucidating the molecular mechanisms involving APP and Aβ in AD, this research aims to contribute to the understanding of the disease pathogenesis and identify potential therapeutic targets. Additionally, it underscores the importance of ongoing research in this field to develop effective strategies for early diagnosis, disease modification, and improved patient outcomes.

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    App Protein
  • View Data Sheet

    Name :

    LBP Mouse

    Description:

    Lipopolysaccaride Mouse Recombinant

    Lipopolysaccharide-binding protein, LBP, Ly88.

    Product # :

    PRO-539

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    Description

    LBP is produced from mouse LBP transfected CHO-cells in serum free medium. For transfection we have cloned complete mouse LBP cDNA into expression vector pPOL-DHFR. Before transfection the complete mouse LBP cDNA was amplified by PCR and cloned into expression vector p-POL-DHFR. RmLBP was produced by his-tag by means of metal affinity purification with Talon and controlled by SDS page. Showing a 58kDa band on SDS-PAGE. Attention: His-tag at the c-terminal end of the LBP has no protease site and is not to split off.

    Source

    Chinese Hamster Ovarian Cells (CHO).

    Formulation

    Recombinant Mouse LBP was lyophilized from a protein solution (1 mg/ml) containing phosphate-buffered saline, pH 7.2.

    Biological Activity

    Up to 2µg/ml LBP mediates binding of FITC-LPS (0.5µg/ml) to CD14+CHO transfectants (2 x 106/ml).

    More Info

    • Introduction

      Lipopolysaccharides (LPS) are a type of glycolipids on the outer cell wall of Gram-negative bacteria. Lipopolysaccharide binding protein (aka LBP) is a plasma protein which facilitates the diffusion of bacterial LPS (endotoxin). LBP is involved in the acute-phase immunologic response to gram-negative bacterial infections. In cooperation with bactericidal permeability-increasing protein (BPI), LBP binds LPS and interacts with the CD14 receptor, most likely playing a role in regulating LPS-dependent monocyte responses. LBP belongs to a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). The LBP gene is found on chromosome 20, directly downstream of the BPI gene. LBP catalyzes the transfer of LPS monomers from LPS aggregates to HDL particles, to phospholipid bilayers, and to a binding site on soluble CD14 (sCD14). sCD14 is capable of speeding up the transfer by receiving an LPS monomer from an LPS aggregate, and then yielding it to an HDL particle, therefore acting as a soluble "shuttle" for an insoluble lipid.

    • Synonyms

      Lipopolysaccharide-binding protein, LBP, Ly88.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Lbp Mouse
  • View Data Sheet

    Name :

    Adiponectin Mouse, HEK

    Description:

    Adiponectin Mouse Recombinant, HEK

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

    Product # :

    CYT-435

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    Description

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

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

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

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

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

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

    Adiponectin Mouse Hek
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