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Search results

1000 results found for “DEAD Box Protein”

Name

Description

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  • View Data Sheet

    Name :

    Dnak SBD C-terminus E.Coli

    Description:

    Dnak Substrate Binding Domain C-terminal E.Coli Recombinant

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

    Product # :

    HSP-009

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    Description

    Recombinant Dnak Substrate Binding Domain C-terminal produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids and having a molecular mass of 27.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The DnaK protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.The protein coding region of the substrate binding domain of DnaK (amino acids 385-638) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQGERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HSTRKQVEEA GDKLPADDKTAIESALTALE TALKGEDKAA IEAKMQELAQ VSQKLMEIAQ QQHAQQQTAG ADASANNAKD DDVVDAEFEE VKDKK.

    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.

    Dnak Sbd C Terminal
  • View Data Sheet

    Name :

    Chitinase Protein

    Description:

    Chitinase Clostridium Paraputrificum Recombinant

    Product # :

    ENZ-031

    Price :

    Quantity :

    Shipping Method :

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    Description

    Chitinase Clostridium Paraputrificum Recombinant fused with a His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 582 amino acids and having a molecular mass of 64.2kDa. The Chitinase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Chitinase lyophilized from a 0.2µm filtered concentrated solution in PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chitinase is a digestive enzyme which breaks down glycosidic bonds in chitin. Due to chitin being a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are usually found in organisms that either need to remake their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria genuses such as Aeromonas, Bacillus, Vibrio, among others, which may be pathogenic or detritivorous. Chitinase expression is mediated by the NPR1 gene and the salicylic acid pathway, both of which are involved in resisting fungal and insect attack. Human chitinases appear in gastric juices. They are likely to be digestive chitinases, for catabolic activity. Chitinase activity is identified systemically in humans, in the blood, and possibly cartilage. Chitinase has been related to allergies, asthma in particular has been linked to enhanced chitinase expression levels, also dust mites and mold spores which are both chitin covered.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MRGSGSHHHH HHMYYGDWSI WGGQGNFYPK DIPADKLTHL NFAFMDFNSS GELIYCDKDA AIGHPLGNLG VTYGDVNGGI LNAFQVLKSE NPNLKIGVSL GGWSKSGDFS TIAATPSIRA KFVENVMKFI KYTNMDFVDI DWEYPGDYRE PDKTDNINDE GTPNASAGDK ENYILLLQDL KEALNKQGKE LGKVYELSVA LPAGVSKIEK GIDVDKLFNI VDFANIMTYD MAGAWSTTSG HQTALYTNPN APEEYKGLSV DESVKYYISQ GAEREKIVVG AAYYTRGWEQ VSDKGTDPNN PGLFGEAAVV NKDADLSPTP GALNEAPMKN GEGGRAGGVW GYNALDKLKS KYTGLKEYWD DSAKAPYLYN SETGAFFTYD NIRSIQEKAK YVKENNLGGI IGWMASQDAT TNSTKRDELT TATKESLFGK EDLPKYEIKY TENDITCTVT PVKQSWGSGG VLKMSITNNE KLDESGEVLS TVETSAKTVK NMKVYIKTDG IAITGSQYPA GPVTKEGDYY VIDFGKISDG KLMKAGITFT FDLNLDKAIE DTNNIISIEV SQRMYQTSPE FNRQTIWENT NS.

    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.

    Chitinase
  • View Data Sheet

    Name :

    C1Q Mouse

    Description:

    Complement Component C1q Mouse

    Component C1q, Complement C1q, Complement Component C1q, C1q.

    Product # :

    PRO-2703

    Price :

    Quantity :

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    Description

    Mouse Complement C1Q produced in Mouse plasma having a molecular weight of 439.5kDa.

    Source

    Mouse Plasma.

    Formulation

    C1Q solution contains 10mM HEPES and 300mM NaCl, pH 7.2.

    Purity

    Greater than 92.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C1q is the first component of the classical pathway of complement activation. C1q along with the enzymatically active components C1r and C1s forms the C1 complex. When C1 binds to immunoglobulins in the form of immune complexes, it leads to activation of C1r and C1s proteases and a further activates the classical pathway of complement. C1q is a glycoprotein that belongs to the collectin family, having a molecular weight of about 410-462 kDa. C1q is a hexamer composed of globular heads attached to collagen-like triple-helix tails. The globular heads of C1q exclusively bind to the CH2 domain of IgG molecules or the CH3 domain of IgM. Each heavy chain of the immunoglobulin molecule contains a single binding site for C1q. Given that C1q must bind to no less than two heavy chains in order to alter its conformation and activate C1r and C1s, its activation follows only after binding to immunoglobulins in the form of immune complexes bound to multivalent antigens. C1q’s main physiological role is in the clearance of immune complexes and apoptotic bodies from the organism. Interruption of this process may lead to development of autoimmunity. Individuals with genetic deficiencies of C1q or other components of the classical pathway are at risk to develop SLE. C1q specifically binds to apoptotic bodies of human keratinocytes, vascular endothelial cells and lymphocytes. Complement components C1q and bound C3 mediate the clearance of apoptotic bodies. Hence, C1q may advance the clearance of autoantigens, avoiding stimulation of the immune system. Nonetheless, an extended exposition of the immune system to the neoepitope exposed on C1q molecules bound to immune complexes or apoptotic bodies could ultimately lead to an autoimmune response against C1q itself and to an altered complement function. C1q deficiency may also lead to disruption of the negative selection of autoreactive B cells. C1q along with other specific recognition proteins bind to the highly conserved lupus antigens (dsDNA and nuclear proteins) and activate the complement system. Autoantibodies against C1q (anti-C1q) are found in a number of autoimmune and infectious diseases like glomerulonephritis (GN) and lupus erythematosus (SLE), these antibodies are significant in clinical practice due to their negative predictive value.

    • Synonyms

      Component C1q, Complement C1q, Complement Component C1q, C1q.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C1Q Mouse 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.

    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.

    C1Q Mouse
  • View Data Sheet

    Name :

    NANOG-TAT Human

    Description:

    NANOG-TAT Human Recombinant

    NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.

    Product # :

    PRO-090

    Price :

    Quantity :

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    Description

    NANOG Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 304 amino acids and c-terminal 13 amino acid TAT peptide having a molecular mass of 36.1kDa.The NANOG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NANOG protein solution contains PBS and 50mM Arginine.

    Purity

    Greater than 95.0% as determined by SDS-PAGE analysis.

    More Info

    • Introduction

      NANOG is a multidomain homeobox transcription factor which functions to maintain the undifferentiated state of pluripotent stem cells. NANOG expression counteracts the differentiation-promoting signals induced by the extrinsic factors LIF, Stat3 and BMP. Once NANOG expression is downregulated, cell differentiation can proceed. Proteins which regulate NANOG expression include transcription factors Oct4, SOX2, FoxD3, and Tcf3 and tumor suppressor p53.

    • Synonyms

      NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.

    • 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. 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

      VDPACPQSL PCFEASDCKE SSPMPVICGP EENYPSLQMS SAEMPHTETV SPLPSSMDLL IQDSPDSSTS PKGKQPTSAE NSVAKKEDKV PVKKQKTRTV FSSTQLCVLN DRFQRQKYLS LQQMQELSNI LNLSYKQVKT WFQNQRMKSK RWQKNNWPKN SNGVTQKASA PTYPSLYSSY HQGCLVNPTG NLPMWSNQTW NNSTWSNQTQ NIQSWSNHSW NTQTWCTQSW NNQAWNSPFY NCGEESLQSC MQFQPNSPAS DLEAALEAAG EGLNVIQQTT RYFSTPQTMD LFLNYSMNMQ PEDVGGYGRK KRRQRRR

    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.

    Nanog Tat Human
  • View Data Sheet

    Name :

    STIP1 Mouse

    Description:

    Stress-Induced-Phosphoprotein 1 Mouse Recombinant

    Hop, p60, Sti1, STI1, mSTI1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein.

    Product # :

    PRO-2396

    Price :

    Quantity :

    Shipping Method :

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    Description

    STIP1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543) and having a molecular mass of 64.7kDa. STIP1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STIP1 solution (1mg/ml) contains 20mM Tris-HCl(pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      Hop, p60, Sti1, STI1, mSTI1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein.

    • 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 MEQVNELKEK GNKALSAGNI DDALQCYSEA IKLDPQNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNLQLKE GLQNMEARLA ERKFMNPFNL PNLYQKLEND PRTRSLLSDP TYRELIEQLQ NKPSDLGTKL QDPRVMTTLS VLLGVDLGSM DEEEEAATPP PPPPPKKEPK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDKALKHYDR AKELDPTNMT YITNQAAVHF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PRDAKLYSNR AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.

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    Stip1 Mouse
  • View Data Sheet

    Name :

    DKK2 Human

    Description:

    Dickkopf-Related Protein 2 Human Recombinant

    Dickkopf 2 homolog (Xenopus laevis), dickkopf related protein-2, hDkk-2.

    Product # :

    PRO-1205

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    Description

    DKK2 Human Recombinant produced in E. coli is a single polypeptide chain containing 250 amino acids (34-259) and having a molecular mass of 27.6 kDa.DKK2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DKK2 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dickkopf-related protein 2 (DKK2) is a member of the dickkopf family, which has a vital role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In adults, Dkks are involved in bone formation and bone disease, cancer and Alzheimer disease. DKK2 contains 2 cysteine rich regions and is implicated in embryonic development through its interactions with the Wnt signaling pathway. DKK2 may function as either an agonist or antagonist of Wnt/beta-catenin signaling, depending on the cellular environment and the presence of the co-factor kremen 2. DKK2 protein activity is also controlled by binding to the Wnt co-receptor LRP6 (LDL-receptor related protein 6).

    • Synonyms

      Dickkopf 2 homolog (Xenopus laevis), dickkopf related protein-2, hDkk-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 MGSMKLNSIK SSLGGETPGQ AANRSAGMYQ GLAFGGSKKG KNLGQAYPCS SDKECEVGRY CHSPHQGSSA CMVCRRKKKR CHRDGMCCPS TRCNNGICIP VTESILTPHI PALDGTRHRD RNHGHYSNHD LGWQNLGRPH TKMSHIKGHE GDPCLRSSDC IEGFCCARHF WTKICKPVLH QGEVCTKQRK KGSHGLEIFQ RCDCAKGLSC KVWKDATYSS KARLHVCQKI.

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    Dkk2 Human
  • View Data Sheet

    Name :

    RUNX3 Human

    Description:

    Runt-Related Transcription Factor 3 Human Recombinant

    AML2, CBFA3, PEBP2aC, PEBP2A3, FLJ34510, MGC16070, RUNX3, Oncogene AML-2, Runt-related transcription factor 3, Core-binding factor subunit alpha-3, Acute myeloid leukemia 2 protein, Polyomavirus enhancer-binding protein 2 alpha C subunit, SL3-3 enhancer factor 1 alpha C subunit, SL3/AKV core-binding factor alpha C subunit.

    Product # :

    PRO-836

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    Description

    RUNX3 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (53-186 a.a.) and having a molecular mass of 17.1 kDa. The RUNX3 is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RUNX3 Human 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

      RUNX3 is part of the RUNX family that mediates the expression of genes which participate in cellular differentiation and cell cycle progression. RUNX3 heterodimer and the beta subunit form a complex that binds to the core DNA sequence 5''-PYGPYGGT-3'' found in several enhancers and promoters, and can either activate or suppress transcription. RUNX3 interacts with additional transcription factors. RUNX3 is a good candidate for gastric cancer tumor suppressor diagnosis.

    • Synonyms

      AML2, CBFA3, PEBP2aC, PEBP2A3, FLJ34510, MGC16070, RUNX3, Oncogene AML-2, Runt-related transcription factor 3, Core-binding factor subunit alpha-3, Acute myeloid leukemia 2 protein, Polyomavirus enhancer-binding protein 2 alpha C subunit, SL3-3 enhancer factor 1 alpha C subunit, SL3/AKV core-binding factor alpha C subunit.

    • 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 MRSMVDVLAD HAGELVRTDS PNFLCSVLPS HWRCNKTLPV AFKVVALGDV PDGTVVTVMA GNDENYSAEL RNASAVMKNQ VARFNDLRFV GRSGRGKSFT LTITVFTNPT QVATYHRAIK VTVDGPREPR RHRQK.

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    Runx3 Human
  • View Data Sheet

    Name :

    PITPNB Human

    Description:

    Phosphatidylinositol Transfer Protein Beta Human Recombinant

    Phosphatidylinositol transfer protein beta isoform, PI-TP-beta, PtdIns transfer protein beta, PtdInsTP beta, PITPNB, VIB1B, PtdInsTP.

    Product # :

    PRO-003

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    Description

    PITPNB 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 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa. The PITPNB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphatidylinositol transfer protein beta isoform (PITPNB) is found in the cytoplasm, where it catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes. PITPNB mobilizes PI from the endoplasmic reticulum and regulates its release from stored vesicles in the Golgi network. PITPNB is extensively expressed in various tissues.

    • Synonyms

      Phosphatidylinositol transfer protein beta isoform, PI-TP-beta, PtdIns transfer protein beta, PtdInsTP beta, PITPNB, VIB1B, PtdInsTP.

    • 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 MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEK DGEKGQYTHK IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN EYMKDDFFIK IETWHKPDLG TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFQSVKTKR GPLGPNWKKE LANSPDCPQM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNFHRQLFC WIDKWIDLTM EDIRRMEDET QKELETMRKR GSVRGTSAAD V.

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    Pitpnb Human
  • View Data Sheet

    Name :

    ARMS2 Human

    Description:

    Age-Related Maculopathy Susceptibility 2 Human Recombinant

    Age-related maculopathy susceptibility protein 2, ARMD8

    Product # :

    PRO-2628

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    Description

    ARMS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-107a.a.) and having a molecular mass of 13.8kDa.ARMS2 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ARMS2 protein solution (0.25mg/ml) containing 20 mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Age-Related Maculopathy Susceptibility 2 or ARMS2 is a protein that is is being researches for its ability to take part in diseases in old age. Mutations in Age-Related Maculopathy Susceptibility 2 is related to age-caused molecular degeneration.

    • Synonyms

      Age-related maculopathy susceptibility protein 2, ARMD8

    • 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 MGSMLRLYPG PMVTEAEGKG GPEMASLSSS VVPVSFISTL RESVLDPGVG GEGASDKQRS KLSLSHSMIP AAKIHTELCL PAFFSPAGTQ RRFQQPQHHL TLSIIHTAAR

    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.

    Arms2 Human
  • View Data Sheet

    Name :

    GDNF Mouse

    Description:

    Glial-Derived Neurotrophic Factor Mouse Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-243

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    Description

    Glial derived Neurotrophic Factor Mouse Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2 x 135 amino acids and having a total molecular mass of 30.2kDa. GDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.

    • Background

      What is the molecular weight/Mw of GDNF MOUSE Protein?
      GDNF MOUSE Protein has a total Mw of 30.2kDa.

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

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

      What is the Biological Activity of GDNF MOUSE Protein?
      The ED50 as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

      What is the amino acid sequence of GDNF MOUSE Protein?
      MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.
      What applications can GDNF MOUSE Protein be used in?
      GDNF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Gdnf Mouse
  • View Data Sheet

    Name :

    ARC Human

    Description:

    Activity-Regulated Cytoskeleton-Associated Protein Human Recombinant

    Arg3.1, KIAA0278, Activity-regulated cytoskeleton-associated protein, Activity-regulated gene 3.1 protein homolog, ARC.

    Product # :

    PRO-1403

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    Description

    ARC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 416 amino acids (1-396 a.a.) and having a molecular mass of 47.4kDa. ARC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ARC protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Activity-regulated cytoskeleton-associated protein (ARC) takes part in the regulation of cell morphology and cytoskeletal organization and is required for consolidation of synaptic plasticity as well as formation of long-term memory. ARC regulates endocytosis of AMPA receptors in response to synaptic activity and is also required for homeostatic synaptic scaling of AMPA receptors. ARC is required in the stress fiber dynamics and cell migration.

    • Synonyms

      Arg3.1, KIAA0278, Activity-regulated cytoskeleton-associated protein, Activity-regulated gene 3.1 protein homolog, ARC.

    • 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 MELDHRTSGG LHAYPGPRGG QVAKPNVILQ IGKCRAEMLE HVRRTHRHLL AEVSKQVERE LKGLHRSVGK LESNLDGYVP TSDSQRWKKS IKACLCRCQE TIANLERWVK REMHVWREVF YRLERWADRL ESTGGKYPVG SESARHTVSV GVGGPESYCH EADGYDYTVS PYAITPPPAA GELPGQEPAE AQQYQPWVPG EDGQPSPGVD TQIFEDPREF LSHLEEYLRQ VGGSEEYWLS QIQNHMNGPA KKWWEFKQGS VKNWVEFKKE FLQYSEGTLS REAIQRELDL PQKQGEPLDQ FLWRKRDLYQ TLYVDADEEE IIQYVVGTLQ PKLKRFLRHP LPKTLEQLIQ RGMEVQDDLE QAAEPAGPHL PVEDEAETLT PAPNSESVAS DRTQPE.

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    Arc Human
  • View Data Sheet

    Name :

    KLK3 Protein

    Description:

    Kallikrein-3 Recombinant Human

    Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.

    Product # :

    ENZ-1102

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    Description

    Kallikrein-3 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 237 amino acids and having a molecular mass of 26.1kDa.KLK3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 3% trehalose.

    Purity

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

    More Info

    • Introduction

      Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.

    • Synonyms

      Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KLK3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kallikrein-3 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 Kallikrein-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IVGGWECEKH SQPWQVLVAS RGRAVCGGVL VHPQWVLTAA HCIRNKSVIL LGRHSLFHPE DTGQVFQVSH SFPHPLYDMS LLKNRFLRPG DDSSHDLMLL RLSEPAELTDA VKVMDLPTQE PALGTTCYAS GWGSIEPEEF LTPKKLQCVD LHVISNDVCA QVHPQKVTKF MLCAGRWTGG KSTCSGDSGG PLVCNGVLQG ITSWGSEPCA LPERPSLYTK VVHYRKWIKD TIVANP.

    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.

    Klk3 Protein
  • View Data Sheet

    Name :

    PET117 Human

    Description:

    PET117 Human Recombinant

    Protein PET117 homolog, mitochondrial, PET117, UNQ607/PRO1194.

    Product # :

    PRO-1686

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    Description

    PET117 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 82 amino acids (23-81) and having a molecular mass of 9.5kDa.PET117 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PET117 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PET117 is nuclear gene essential for the assembly of active cytochrome c oxidase in S. cerevisiae. Nevertheless the gene products are not subunits of the final assembled cytochrome c oxidase complex. PET117 is found in chromosome V proximate the HIS1 gene.

    • Synonyms

      Protein PET117 homolog, mitochondrial, PET117, UNQ607/PRO1194.

    • 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 MGSVHVKQQW DQQRLRDGVI RDIERQIRKK ENIRLLGEQI ILTEQLEAER EKMLLAKGSQ KS.

    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.

    Pet117 Human
  • View Data Sheet

    Name :

    Adiponectin Human, His

    Description:

    Adiponectin Human Recombinant, His tag

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

    Product # :

    CYT-433

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    Description

    The Acrp30 Human is created as a recombinant protein with N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is 26.4 kDa protein containing 230 amino acid residues of the Acrp30 Human and 12 additional amino acid residues - HisTag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Acrp30 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.02M Tris buffer pH7.5, 0.15M NaCl.

    Purity

    Acrp30 Human purity is greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Amino Acid Sequence

      MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.

    • Background

      What is the molecular weight / Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26.4kDa.
      What is the source or expression system of ADIPONECTIN Protein?
      Escherichia Coli.

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.

      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 Human His
  • View Data Sheet

    Name :

    Ku P70/P80 Human

    Description:

    Ku P70/P80 Human Recombinant

    ATP-dependent DNA helicase 2 subunit 1, ATP-dependent DNA helicase II 70 kDa subunit, Lupus Ku autoantigen protein p70, Ku70, 70 kDa subunit of Ku antigen, Thyroid-lupus autoantigen, TLAA, CTC box-binding factor 75 kDa subunit, CTCBF, CTC75, DNA-repair protein XRCC6, G22P1, XRCC6, ML8.

    Product # :

    PRO-397

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    Description

    KuP70/P80 Human Recombinant produced in SF9 insect cells is a glycosylated, polypeptide chain having a molecular mass of 70,638 Dalton for the p70 subunit and 83,528 Dalton for the p80 subunit. Ku (P70/P80) is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    KuP70/P80is supplied in 16mM HEPES buffer pH-8, 160mM NaCl, and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ku antigen consists of two polypeptides (70 kDa and 80 kDa; the p80 subunit is occasionally called p86). The Ku heterodimer provides DNA-binding and regulatory functions to DNA-dependent protein kinase which is a central enzyme for DNA recombination processes in eucaryotic cells. The Ku protein plays important roles in multiple nuclear processes including DNA repair, V(D)J recombination, telomere maintenance, and the regulation of specific gene transcription.
      Antibodies to Ku were originally reported in scleroderma-polymyositis overlap syndrome (up to 20% of patients) but have also been detectable in about 20 % of patients with primary pulmonary hypertension (as a complication of overlap), in 5-10 % of SLE and MCTD patients, and in up to 20 % of patients with primary Sj?gren's syndrome.
      In IIF using HEp-2 cells, Ku-positive sera yield a dense, fine granular pattern with nucleolar staining that is typical but not specific for anti-Ku. Detection of Ku antibodies by Western blot may bear false-negative results since the main reactive epitope on the p70/p80 heterodimer is conformation-dependent.

    • Synonyms

      ATP-dependent DNA helicase 2 subunit 1, ATP-dependent DNA helicase II 70 kDa subunit, Lupus Ku autoantigen protein p70, Ku70, 70 kDa subunit of Ku antigen, Thyroid-lupus autoantigen, TLAA, CTC box-binding factor 75 kDa subunit, CTCBF, CTC75, DNA-repair protein XRCC6, G22P1, XRCC6, ML8.

    • 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. 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

      0.2-0.6 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.

    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.

    Ku P70 P80 Human
  • View Data Sheet

    Name :

    SPARC Mouse

    Description:

    Secreted Protein Acidic & Rich in Cysteine Mouse Recombinant

    Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine

    Product # :

    PRO-2658

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    Description

    SPARC Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (18-302a.a) and having a molecular mass of 33.3kDa.SPARC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The SPARC solution (0.25mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Secreted Protein Acidic & Rich in Cysteine (SPARC) protein is coded by the SPARC gene in humans. SPARC is a glycoprotein located in bones that binds to calcium. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, mainly in areas of tissue morphogenesis and remodelling. Asides from calcium, SPARC can also bind to collagen.

    • Synonyms

      Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine

    • 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

      APQQTEVAEE IVEEETVVEE TGVPVGANPV QVEMGEFEDG AEETVEEVVA DNPCQNHHCK HGKVCELDES NTPMCVCQDP TSCPAPIGEF EKVCSNDNKT FDSSCHFFAT KCTLEGTKKG HKLHLDYIGP CKYIAPCLDS ELTEFPLRMR DWLKNVLVTL YERDEGNNLL TEKQKLRVKK IHENEKRLEA GDHPVELLAR DFEKNYNMYI FPVHWQFGQL DQHPIDGYLS HTELAPLRAP LIPMEHCTTR FFETCDLDND KYIALEEWAG CFGIKEQDIN KDLVIHHHHH H

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    Sparc Mouse
  • View Data Sheet

    Name :

    FABP1 Mouse

    Description:

    Fatty Acid Binding Protein-1 Mouse Recombinant

    Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.

    Product # :

    PRO-1121

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    • description
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    Description

    Fatty Acid Binding Protein-1 Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The FABP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    More Info

    • Introduction

      FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel beta strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acid. This protein binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm; it may be involved in intracellular lipid transport and metabolism.

    • Synonyms

      Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FABP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FABP1 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 FABP1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MNFSGKYQLQ SQENFEPFMK AIGLPEDLIQ KGKDIKGVSE IVHEGKKIKL TITYGPKVVR NEFTLGEECE LETMTGEKVK AVVKLEGDNK MVTTFKGIKS VTELNGDTIT NTMTLGDIVY KRVSKRI.

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    Fabp1 Mouse
  • View Data Sheet

    Name :

    SPARC Human, His

    Description:

    Secreted Protein acidic & Rich in Cysteine Human Recombinant, His Tag

    Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.

    Product # :

    PRO-582

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    Description

    Osteonectin Human Recombinant fused with 6X His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 295 amino acids and having a molecular mass of 34 kDa.SPARC is expressed with a 6 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPARC (1 mg/ml) was lyophilized after extensive dialyses against 20mM PBS pH-7.4.

    Purity

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

    More Info

    • Introduction

      SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.

    • Synonyms

      Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Osteonectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BM-40 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 SPARC in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSYYHHHHHHPQQEALPDETEVVEETVAEVTEVSVGANPVQVEVGEFD
      DGAEETEEEVVAENPCQNHHCKHGKVCELDENNTPMCVCQDPTSCP
      APIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCK
      YIPPCLDSELTEFPLRMRDWLKNVLVTLYERDEDNNLLTKQKLRVKKI
      HENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGY
      LSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALDEWAGCFGIKQK
      DIDKDLVI.

    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.

    Osteonectin Human
  • View Data Sheet

    Name :

    VEGI Human, His

    Description:

    Vascular Endothelial Growth InhibitorHuman Recombinant, His Tag

    Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.

    Product # :

    CYT-589

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    Description

    VEGI 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 201 amino acids(72-251a.a.) and having a molecular mass of 22.7kDa. The VEGI is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VEGI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50% glycerol, 1mM DTT and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.

    • 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 MLKGQEFAPS HQQVYAPLRA DGDKPRAHLT VVRQTPTQHF KNQFPALHWE HELGLAFTKN RMNYTNKFLL IPESGDYFIY SQVTFRGMTS ECSEIRQAGR PNKPDSITVV ITKVTDSYPE PTQLLMGTKS VCEVGSNWFQ PIYLGAMFSL QEGDKLMVNV SDISLVDYTK EDKTFFGAFL L

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    Vegi Human His
  • View Data Sheet

    Name :

    TIFA Human

    Description:

    TRAF-Interacting Protein with Forkhead-Associated Domain Human Recombinant

    TRAF-interacting protein with FHA domain-containing protein A, Putative MAPK-activating protein PM14, Putative NF-kappa-B-activating protein 20, TRAF2-binding protein, TIFA, T2BP, T6BP, TIFAA.

    Product # :

    PRO-1041

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    Description

    TIFA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-184 a.a.) and having a molecular mass of 24kDa.TIFA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      TRAF-interacting protein with FHA domain-containing protein A (TIFA) is an adapter protein that mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, triggering the downstream activation of NF-kappa-B and AP-1 pathways. The TIFA protein stimulates the oligomerization and polyubiquitination of TRAF6, leading to the activation of TAK1 and IKK through a proteasome-independent mechanism.

    • Synonyms

      TRAF-interacting protein with FHA domain-containing protein A, Putative MAPK-activating protein PM14, Putative NF-kappa-B-activating protein 20, TRAF2-binding protein, TIFA, T2BP, T6BP, TIFAA.

    • 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 MGSHMTSFED ADTEETVTCL QMTVYHPGQL QCGIFQSISF NREKLPSSEV VKFGRNSNIC HYTFQDKQVS RVQFSLQLFK KFNSSVLSFE IKNMSKKTNL IVDSRELGYL NKMDLPYRCM VRFGEYQFLM EKEDGESLEF FETQFILSPR SLLQENNWPP HRPIPEYGTY SLCSSQSSSP TEMDENES.

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    Tifa Human
  • View Data Sheet

    Name :

    ASB13 Human

    Description:

    Ankyrin Repeat And SOCS Box Containing 13 Human Recombinant

    Ankyrin repeat and SOCS box protein 13, ASB-13, ASB13, ankyrin repeat and SOCS box containing 13.

    Product # :

    PRO-2060

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    Description

    ASB13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (1-278 a.a.) and having a molecular mass of 32.4kDa.ASB13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ASB13 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASB13 belongs to the ankyrin repeat and SOCS box-containing (ASB) family of proteins which contains ankyrin repeat sequence and a SOCS box domain. ASB13 is a protein coding gene that plays a role as a substrate-recognition part of a SCF-like ECS E3 ubiquitin-protein ligase complex which arbitrates the ubiquitination and subsequent proteasomal degradation of target proteins.

    • Synonyms

      Ankyrin repeat and SOCS box protein 13, ASB-13, ASB13, ankyrin repeat and SOCS box containing 13.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMEPRAAD GCFLGDVGFW VERTPVHEAA QRGESLQLQQ LIESGACVNQ VTVDSITPLH AASLQGQARC VQLLLAAGAQ VDARNIDGST PLCDACASGS IECVKLLLSY GAKVNPPLYT ASPLHEACMS GSSECVRLLI DVGANLEAHD CHFGTPLHVA CAREHLDCVK VLLNAGANVN AAKLHETALH HAAKVKNVDL IEMLIEFGGN IYARDNRGKK PSDYTWSSSA PAKCFEYYEK TPLTLSQLCR VNLRKATGVR GLEKIAKLNI PPRLIDYLSY N.

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    Asb13 Human
  • View Data Sheet

    Name :

    C10ORF54 Human

    Description:

    Chromosome 10 Open Reading Frame 54 Human Recombinant

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

    Product # :

    PRO-2259

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    C10Orf54 Human
  • View Data Sheet

    Name :

    Mouse OX40L

    Description:

    OX40 Ligand Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l

    Product # :

    CYT-1191

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    Description

    OX40L Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 157 amino acids (51-198 aa) and having a molecular mass of 17.7kDa.OX40L is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its binding ability in a functional ELISA with Human TNFRSF4 (CAT# cyt-1039).

    More Info

    • Introduction

      OX40 Ligandis a part of the tumor necrosis factor (TNF)receptor family. OX40L receptor is OX40 which is expressed predominantly on activated CD4+ T cells.OX40 Ligandis expressed on various antigen-presenting cells such asmacrophages, DC2sand activated Blymphocytes. Expression of OX40 is momentary following engagement of T cell receptors. The ligation of OX40-OX40L stimulates proliferation anddifferentiation of activated B cells,increases immunoglobulin secretion and is also a sourceof survival signal for T cells and enables the development of memory T cells.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l

    • 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

      ADPSSSPAKD PPIQRLRGAV TRCEDGQLFI SSYKNEYQTM EVQNNSVVIK CDGLYIIYLK GSFFQEVKID LHFREDHNPI SIPMLNDGRR IVFTVVASLA FKDKVYLTVN APDTLCEHLQ INDGELIVVQ LTPGYCAPEG SYHSTVNQVP LHHHHHH

    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.

    Ox40L Mouse
  • View Data Sheet

    Name :

    SOD2 Mouse

    Description:

    Superoxide Dismutase-2 Mouse Recombinant

    Superoxide dismutase [Mn], Superoxide Dismutase-2, mitochondrial, Sod-2.

    Product # :

    PRO-2192

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    SOD2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (25-222 a.a) and having a molecular mass of 24.6kDa.SOD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOD2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems.

    • Synonyms

      Superoxide dismutase [Mn], Superoxide Dismutase-2, mitochondrial, Sod-2.

    • 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 MGSKHSLPDL PYDYGALEPH INAQIMQLHH SKHHAAYVNN LNATEEKYHE ALAKGDVTTQ VALQPALKFN GGGHINHTIF WTNLSPKGGG EPKGELLEAI KRDFGSFEKF KEKLTAVSVG VQGSGWGWLG FNKEQGRLQI AACSNQDPLQ GTTGLIPLLG IDVWEHAYYL QYKNVRPDYL KAIWNVINWE NVTERYTACK K.

    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.

    Sod2 Mouse
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