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Search results

281 results found for “nck adaptor protein”

Name

Description

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  • View Data Sheet

    Name :

    SNCA Delta-NAC Human

    Description:

    Alpha Synuclein Delta-NAC Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-161

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    • description
    • source
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    Description

    A-Synuclein Delta-NAC Human Recombinant which is a deletion mutant of the a-synuclein that lacks the NAC region (amino acid 61-95), produced in E.Coli is a single, non-glycosylated polypeptide chain of 111 amino acids having a molecular mass of 11.9kDa (molecular size on SDS-PAGE will appear higher), with 6 amino acids added as a linker. The Recombinant Human a-Synuclein Delta-NAC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA Delta-NAC protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK GTEIWMKKDQ LGKNEEGAPQ EGILEDMPVD PDNEAYEMPS EEGYQDYEPE A.

    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.

    Snca Delta Nac 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

    Price :

    Quantity :

    Shipping Method :

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    • description
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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.

    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.

    Hp Nap
  • View Data Sheet

    Name :

    Avidin Protein

    Description:

    Avidin

    Avidin, AVD, AVID.

    Product # :

    PRO-500

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • biological activity
    • More Info

    Description

    Avidin is a glycosylated polypeptide chain having a molecular mass of 68kDa and containing 4 subunits each with a binding site for biotin. The Avidin is purified by affinity chromatographic techniques.The purification procedure ensures minimal contamination by other proteins or DNA.The resulting high activity and purity of the product gives very low non-specific binding (NSB).

    Source

    Hen's egg white.

    Biological Activity

    15.0 units/mg protein, 1 unit binds 1µg biotin.

    More Info

    • Introduction

      Avidin is a tetrameric protein of 4 identical subunits (homotetramer) each of which can bind to biotin with a high degree of affinity and specificity. Avidin molecular weight in its tetrameric form is estimated to be between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of four to five mannose and three N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.

    • Synonyms

      Avidin, AVD, AVID.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Avidin 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 Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml 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.

    Avidin Avid
  • View Data Sheet

    Name :

    SNRPC Human

    Description:

    Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant

    U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    Product # :

    PRO-1004

    Price :

    Quantity :

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    • description
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    • formulation
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    Description

    SNRPC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-159 a.a.) and having a molecular mass of 19.8kDa (Molecular weight on SDS-PAGE will appear higher).SNRPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNRPC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.3M NaCl, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNRPC is a member of the U1 small nuclear ribonucleoprotein C family. The SNRPC protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle required for the formation of the spliceosome. SNRPC participates in the processing of nuclear precursor messenger RNA splicing. snRNP particles are tackled by autoantibodies frequently produced by patients with connective tissue diseases.

    • Synonyms

      U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    • 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 MGSMPKFYCD YCDTYLTHDS PSVRKTHCSG RKHKENVKDY YQKWMEEQAQ SLIDKTTAAF QQGKIPPTPF SAPPPAGAMI PPPPSLPGPP RPGMMPAPHM GGPPMMPMMG PPPPGMMPVG PAPGMRPPMG GHMPMMPGPP MMRPPARPMM VPTRPGMTRP DR.

    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.

    Snrpc Human
  • View Data Sheet

    Name :

    NSL1 Human

    Description:

    NSL1 Human Recombinant

    NSL1 MIS12 Kinetochore Complex Component, NSL1 MIND Kinetochore Complex Component Homolog (S. Cerevisiae), Kinetochore-Associated ProteinNSL1 Homolog, Chromosome 1 Open Reading Frame 48, C1orf48, MIS14.

    Product # :

    PRO-1557

    Price :

    Quantity :

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    • description
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    Description

    NSL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-281) and having a molecular mass of 34.6kDa.NSL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NSL1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      NSL1 holds two coiled-coil domains.NSL1 proteins, localized to kinetochores - chromosome associated structures which attach to microtubules and mediate chromosome movements throughout cell division. NSL1 is a fragment of a conserved protein complex that hold two chromodomain-containing proteins and a component of the outer plate of the kinetochore. NSL1 connect centromeric heterochromatin with the outer kinetochore structure. Several transcript variants are known to encod different isoforms for this gene.

    • Synonyms

      NSL1 MIS12 Kinetochore Complex Component, NSL1 MIND Kinetochore Complex Component Homolog (S. Cerevisiae), Kinetochore-Associated ProteinNSL1 Homolog, Chromosome 1 Open Reading Frame 48, C1orf48, MIS14.

    • 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 MGSMAGSPEL VVLDPPWDKE LAAGTESQAL VSATPREDFR VRCTSKRAVT EMLQLCGRFV QKLGDALPEE IREPALRDAQ WTFESAVQEN ISINGQAWQE ASDNCFMDSD IKVLEDQFDE IIVDIATKRK QYPRKILECV IKTIKAKQEI LKQYHPVVHP LDLKYDPDPA PHMENLKCRG ETVAKEISEA MKSLPALIEQ GEGFSQVLRM QPVIHLQRIH QEVFSSCHRK PDAKPENFIT QIETTPTETA SRKTSDMVLK RKQTKDCPQR KWYPLRPKKI NLDT

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    Nsl1 Human
  • View Data Sheet

    Name :

    LAT Human

    Description:

    Linker for Activation of T Cells Human Recombinant

    Linker for activation of T cells, LAT1, 36 kDa phospho-tyrosine adapter protein, p36-38, pp36, linker for activation of T cells transmembrane adaptor, linker for activation of T-cells family member 1.

    Product # :

    PRO-948

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    Description

    LAT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (28-233) and having a molecular mass of 24.4 kDa (Molecular weight on SDS-PAGE will appear higher).LAT is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The LAT solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      LAT is a vital membrane protein that is phosphorylated by ZAP-70/Syk protein tyrosine kinases succeeding activation of the T-cell antigen receptor (TCR) signal transduction pathway. LAT is expressed in T lymphocytes in interstitial spaces, platelets and megakaryocytes.

    • Synonyms

      Linker for activation of T cells, LAT1, 36 kDa phospho-tyrosine adapter protein, p36-38, pp36, linker for activation of T cells transmembrane adaptor, linker for activation of T-cells family member 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 MHCHRLPGSY DSTSSDSLYP RGIQFKRPHT VAPWPPAYPP VTSYPPLSQP DLLPIPRSPQ PLGGSHRTPS SRRDSDGANS VASYENEEPA CEDADEDEDD YHNPGYLVVL PDSTPATSTA APSAPALSTP GIRDSAFSME SIDDYVNVPE SGESAEASLD GSREYVNVSQ ELHPGAAKTE PAALSSQEAE EVEEEGAPDY ENLQELN

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    Lat Human
  • View Data Sheet

    Name :

    BMP 4 Human

    Description:

    Bone Morphogenetic Protein-4 Human Recombinant

    BMP4, ZYME, BMP2B, BMP2B1.

    Product # :

    CYT-361

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    Description

    Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.

    Purity

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

    More Info

    • Introduction

      The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

    • Synonyms

      BMP4, ZYME, BMP2B, BMP2B1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

    • Background

      What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant

      As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.

      Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.

      Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!

      How Does Bone Morphogenetic Protein-4 (BMP-4) Work?

      Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.

      The Role of BMP-4

      This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.

      However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:

      • Embryonic development
      • Wound healing
      • Bone remodeling
      • Immune response modulation
      • Tissue repair
      • Cardiac development and function

      What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?

      To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.

      As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.

      More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:

      • Cancer therapy
      • Development of engineered tissues and organs
      • Bone regeneration for the treatment of osteoporosis and nonunion fractures
      • Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
      • Promotion of tissue repair and regeneration

      Final Thoughts BMP-4

      Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.

      However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.

      What is the molecular weight/Mw of BMP4 Protein?
      BMP4 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP4 Protein?
      Escherichia Coli.

      What is the Purity of BMP4 Protein?
      BMP4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP4 Protein?
      The biological functionality of BMP4 Protein will be determined in the future.

      What is the amino acid sequence of BMP4 Protein?
      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

      What applications can BMP4 Protein be used in?
      BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP4 Protein?
      The endotoxin level is minimal, BMP4 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.

    Bmp4 Human
  • View Data Sheet

    Name :

    NOV Human

    Description:

    Nephroblastoma Overexpressed Human Recombinant

    Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    Product # :

    CYT-805

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    Description

    Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.

    Purity

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

    Biological Activity

    Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

    More Info

    • Introduction

      Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

    • Synonyms

      Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M.

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    Nov Human
  • View Data Sheet

    Name :

    Protein-L Cys

    Description:

    Protein L Cys Recombinant

    Product # :

    PRO-1931

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    Description

    Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-L was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    sds-page, HPLC

    Protein-L Cys SDS-PAGE - Product image 1
    Protein-L cys HPLC - Product image 2

    More Info

    • Introduction

      The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

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    Protein L Cys
  • View Data Sheet

    Name :

    NAIF1 Human

    Description:

    Nuclear Apoptosis Inducing Factor 1 Human Recombinant

    bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    Product # :

    PRO-1978

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    Description

    NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.

    • Synonyms

      bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    • 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 MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.

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    Naif1 Human
  • View Data Sheet

    Name :

    LAMTOR4 Human

    Description:

    LAMTOR4 Human Recombinant

    Late Endosomal/Lysosomal Adaptor, MAPK And MTOR Activator 4, C7orf59, Late Endosomal/Lysosomal Adaptor And MAPK And MTOR Activator 4, Chromosome 7 Open Reading Frame 59, Ragulator Complex Protein LAMTOR4, UPF0539 Protein C7orf59, LAMTOR4.

    Product # :

    PRO-2065

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    Description

    LAMTOR4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 122 amino acids (1-99 a.a) and having a molecular mass of 13.1kDa. LAMTOR4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LAMTOR4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      LAMTOR4 is implicated in amino acid sensing and activation of mTORC1, which is a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. LAMTOR4 is activated by amino acids via a mechanism which involves the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases both function as a scaffold recruiting mTORC1 to lysosomes where it is sequentially activated.

    • Synonyms

      Late Endosomal/Lysosomal Adaptor, MAPK And MTOR Activator 4, C7orf59, Late Endosomal/Lysosomal Adaptor And MAPK And MTOR Activator 4, Chromosome 7 Open Reading Frame 59, Ragulator Complex Protein LAMTOR4, UPF0539 Protein C7orf59, LAMTOR4.

    • 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 MGSMTSALTQ GLERIPDQLG YLVLSEGAVL ASSGDLENDE QAASAISELV STACGFRLHR GMNVPFKRLS VVFGEHTLLV TVSGQRVFVV KRQNRGREPI DV.

    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.

    Lamtor4 Human
  • View Data Sheet

    Name :

    NCR3LG1 Human

    Description:

    Natural Cytotoxicity Triggering Receptor 3 Ligand 1 Human Recombinant

    B7H6, B7-H6, B7 Homolog 6

    Product # :

    PRO-2762

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    Description

    NCR3LG1 Human Recombinant produced in HEK is a single, glycosylated polypeptide chain containing 477 amino acids (25-262 a.a) and having a molecular mass of 53.6 kDa. NCR3LG1 is fused to a 239 amino acid hIgG-His tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells

    Formulation

    NCR3LG1 protein solution (0.5mg/ml) containing 1X PBS (pH-7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Measured in a functional ELISA with Human NCR3. The ED50 range ≤500 ng/ml.

    More Info

    • Introduction

      The B7 proteins are crucial in the regulation of the adaptive immune system. Among them is NCR3LG1. NCR3LG1 is part of the B7 family and is expressed on tumor cells. NCR3LG1 Interaction with NKp30 protein results in cytotoxicity and natural killer cell activation.Humans and rats have a single NCR3LG1 gene; though, numerous B7H6 genes were detected in a single large cluster in the Xenopus genome. NCR3LG1, a ligand for the NK cell activating receptor NKp30, targest to produce CAR that targets multiple tumor types. NCR3LG1 is expressed on many primary human tumors, including leukemia, lymphoma and gastrointestinal stromal tumors, though it is not constitutively expressed on normal tissues.

    • Synonyms

      B7H6, B7-H6, B7 Homolog 6

    • 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

      DLKVEMMAGG TQITPLNDNV TIFCNIFYSQ PLNITSMGIT WFWKSLTFDK EVKVFEFFGD HQEAFRPGAI VSPWRLKSGD ASLRLPGIQL EEAGEYRCEV VVTPLKAQGT VQLEVVASPA SRLLLDQVGM KENEDKYMCE SSGFYPEAIN ITWEKQTQKF PHPIEISEDV ITGPTIKNMD GTFNVTSCLK LNSSQEDPGT VYQCVVRHAS LHTPLRSNFT LTAARHSLSE TEKTDNFS

      LE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH

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    Ncr3Lg1 Human
  • View Data Sheet

    Name :

    CXCL7 95 a.a Human

    Description:

    Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-277

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    Description

    NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      NAP 2 is supplied as a 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

      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

    • Background

      What is the molecular weight/Mw of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CXCL7 95 A.A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL7 95 A.A HUMAN Protein?
      The biological functionality of CXCL7 95 A.A HUMAN Protein will be determined in the future.

      What is the amino acid sequence of CXCL7 95 A.A HUMAN Protein?
      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

      What applications can CXCL7 95 A.A HUMAN Protein be used in?
      CXCL7 95 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL7 95 A.A HUMAN Protein?
      The endotoxin level is minimal, CXCL7 95 A.A HUMAN 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.

    Nap 2 95 Aa Human
  • View Data Sheet

    Name :

    Protein G

    Description:

    Protein G Recombinant

    Product # :

    PRO-402

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    • sds-page

    Description

    The Protein G is a single, non-glycosylated protein contains 200 amino acids having a molecular mass of 21.8kDa. The Protein-G migrates on SDS-PAGE around 32kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized white powder containing no additives.

    Purity

    >96% as determined by SDS-PAGE and RP-HPLC.

    sds-page

    Protein-G sds-page - Product image 1

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    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Reconstitution with deionized water or PBS.

    • Amino Acid Sequence

      LPKTDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDAT KTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFK QYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTL KGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE.

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    Protein G
  • View Data Sheet

    Name :

    Protein Cys-A/G

    Description:

    Protein Cys-A/G Recombinant

    Product # :

    PRO-1929

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE.

    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.

    Protein Cys A G
  • View Data Sheet

    Name :

    CRADD Human

    Description:

    Caspase and RIP Adapter with Death Domain Human Recombinant

    RAIDD, MGC9163, CRADD, Death domain-containing protein CRADD, Caspase and RIP adapter with death domain, RIP-associated protein with a death domain, CASP2 and RIPK1 domain containing adaptor with death domain.

    Product # :

    PRO-465

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    Description

    CRADD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.9 kDa. CRADD is fused to a 20 amino acids His-Tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The CRADD protein solution (1mg/ml) contains 20mM Tris-HCl pH-8 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRADD is a 22kDa, widely-expressed cytosolic adaptor/signaling protein that induces cell apoptosis/cell death in numerous tissues. CRADD is a death domain (CARD) that recruits, caspase 2/ICH1 to the cell death signal transduction complex that includes TNFR1A, RIPK1/RIP kinase, and numbers of other CARD domain-containing proteins.

    • Synonyms

      RAIDD, MGC9163, CRADD, Death domain-containing protein CRADD, Caspase and RIP adapter with death domain, RIP-associated protein with a death domain, CASP2 and RIPK1 domain containing adaptor with death domain.

    • 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 MEARDKQVLR SLRLELGAEV LVEGLVLQYL YQEGILTENH IQEINAQTTG LRKTMLMLDI LPSRGPKAFD TFLDSLQEFP WVREKLKKAR EEAMTDLPAG DRLTGIPSHI LNSSPSDRQI NQLAQRLGPE WEPMVLSLGL SQTDIYRCKA NHPHNVQSQV VEAFIRWRQR FGKQATFQSL HNGLRAVEVD PSLLLHMLE.

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    Cradd Human
  • View Data Sheet

    Name :

    STRADA Human

    Description:

    STE20-Related Kinase Adaptor Alpha Human Recombinant

    LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.

    Product # :

    PRO-1992

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    Description

    STRADA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314a.a) and having a molecular mass of 37kDa. STRADA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STRADA protein solution (1mg/ml) containing 20mM 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

      STE20-Related Kinase Adaptor Alpha (STRADA) is a part of the STE- 20 like kinase family which stimulates MAPK pathways by activating MAPKKK. STRADA is an upstream activator of LKB1 and also leads the sub-cellular localization of LKB1 by fixing it in the cytoplasm. The interaction between STRADA-LKB1 leads to phosphorylation of STRADA and enhanced autophosphorylation of LKB1.

    • Synonyms

      LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.

    • 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 MGSMSFLVSK PERIRTNDAS SESIASFSKQ EVMSSFLPEG GCYELLTVIG KGFEDLMTVN LARYKPTGEY VTVRRINLEA CSNEMVTFLQ GELHVSKLFN HPNIVPYRAT FIADNELWVV TSFMAYGSAK DLICTHFMDG MNELAIAYIL QGVLKALDYI HHMGYVHRSV KASHILISVD GKVYLSGLRS NLSMISHGQR QRVVHDFPKY SVKVLPWLSP EVLQQNLQGY DAKSDIYSVG ITACELANGH VPFKDMPATQ MLLEKLNGTV PCLLDTSTIP AEELTMSPSR SVANSGLSDS LTTSTPRPSN GPVPAPS.

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    Strada Human
  • View Data Sheet

    Name :

    SNCG Mouse

    Description:

    Gamma-Synuclein Mouse Recombinant

    Gamma-synuclein, Persyn.

    Product # :

    PRO-2490

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    Description

    SNCG Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 146 amino acids (1-123 a.a) and having a molecular mass of 15.5kDa.SNCG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNCG protein solution (1mg/ml) containing 20mM Tris-HCl(pH8.0) and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      g-synuclein(Originally known as a breast cancer specific gene product, BCSG1) is an acidic neuronal protein of 127 amino acids. Gamma-Synuclein is a member of the Synuclein protein family, which is believed to be involved in the pathogenesis of neurodegenerative diseases. High levels of Gamma-Synuclein have been found in advanced breast carcinomas suggesting a correlation between overexpression of SNCG and breast tumor development. Synuclein-Gamma is found mostly in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. SNCG is also identified in the brain, ovarian tumors, and in the olfactory epithelium. SNCG expression in breast tumors is a marker for tumor progression. A modification in the expression of gamma-synuclein has been detected in the retina of Alzheimer's patients.

    • Synonyms

      Gamma-synuclein, Persyn.

    • 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 MGSMDVFKKG FSIAKEGVVG AVEKTKQGVT EAAEKTKEGV MYVGTKTKEN VVQSVTSVAE KTKEQANAVS AVVSSVNTV ANKTVEEAEN IVVTTGVVRK EDLEPPAQDQ EAKEQEENEE AKSGED.

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    Sncg Mouse
  • View Data Sheet

    Name :

    MESDC2 Mouse

    Description:

    Mesoderm Development Candidate 2 Mouse Recombinant

    LDLR chaperone MESD, Mesoderm development candidate 2, Mesoderm development protein, Mesdc2, Mesd.

    Product # :

    PRO-2260

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    Description

    MESDC2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (30-224 a.a) and having a molecular mass of 24.4kDa. MESDC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MESDC2 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mesoderm development candidate 2 (MESDC2) is required for formation of the primitive streak and mesoderm during embryogenesis. MESDC2 binds to the Wnt co-receptors LRP5 and LRP6 in the endoplasmic reticulum and is required for their proper folding and cell surface expression.

    • Synonyms

      LDLR chaperone MESD, Mesoderm development candidate 2, Mesoderm development protein, Mesdc2, Mesd.

    • 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 MGSADTPGEA TPPPRKKKDI RDYNDADMAR LLEQWEKDDD IEEGDLPEHK RPSAPIDFSK LDPGKPESIL KMTKKGKTLM MFVTVSGNPT EKETEEITSL WQGSLFNANY DVQRFIVGSD RAIFMLRDGS YAWEIKDFLV SQDRCAEVTL EGQMYPGKGG GSKEKNKTKP EKAKKKEGDP KPRASKEDNR AGSRREDL.

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    Mesdc2 Mouse
  • View Data Sheet

    Name :

    DnaK SBD

    Description:

    DnaK Substrate Binding Domain 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-008

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    Description

    Recombinant DnaK Substrate Binding domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing (385-546 a.a.) 163 amino acids and having a molecular mass of 17.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 25mM Tris-HCl, pH7.5, 2mM B-ME and 1mM DTT.

    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. Dnak(residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK(amino acid 508-638) 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 SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HST.

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    Dnak Sbd
  • 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.

    More Info

    • 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 :

    EPCAM Human

    Description:

    Epithelial Cell Adhesion Molecule Human Recombinant

    Epithelial cell adhesion molecule, Ep-CAM, Adenocarcinoma-associated antigen, Cell surface glycoprotein Trop-1, Epithelial cell surface antigen, Epithelial glycoprotein, EGP, Epithelial glycoprotein 314, EGP314, hEGP314, KS 1/4 antigen, KSA, Major gastrointestinal tumor-associated protein GA733-2, Tumor-associated calcium signal transducer 1, CD326, EPCAM, GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1, ESA, MK-1, DIAR5, EGP-2, EGP40, KS1/4, HNPCC8.

    Product # :

    PRO-1322

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    Description

    EPCAM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (24-265 a.a.) and having a molecular mass of 30.1kDa.EPCAM is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EPCAM protein solution (1mg/ml) containing 20mM 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

      EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.

    • Synonyms

      Epithelial cell adhesion molecule, Ep-CAM, Adenocarcinoma-associated antigen, Cell surface glycoprotein Trop-1, Epithelial cell surface antigen, Epithelial glycoprotein, EGP, Epithelial glycoprotein 314, EGP314, hEGP314, KS 1/4 antigen, KSA, Major gastrointestinal tumor-associated protein GA733-2, Tumor-associated calcium signal transducer 1, CD326, EPCAM, GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1, ESA, MK-1, DIAR5, EGP-2, EGP40, KS1/4, HNPCC8.

    • 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 MGSHMQEECV CENYKLAVNC FVNNNRQCQC TSVGAQNTVI CSKLAAKCLV MKAEMNGSKL GRRAKPEGALQNNDGLYDPD CDESGLFKAK QCNGTSMCWC VNTAGVRRTD KDTEITCSER VRTYWIIIEL KHKAREKPYD SKSLRTALQK EITTRYQLDP KFITSILYEN NVITIDLVQN SSQKTQNDVD IADVAYYFEK DVKGESLFHS KKMDLTVNGE QLDLDPGQTL IYYVDEKAPE FSMQGLK.

    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.

    Epcam Human
  • View Data Sheet

    Name :

    AP1S2 Human

    Description:

    Adaptor-Related Protein Complex 1, Sigma 2 Human Recombinant

    Adaptor-related protein complex 1 sigma 2 subunit, SIGMA1B, Adaptor protein complex AP-1 sigma-1B subunit, Clathrin assembly protein complex 1 sigma-1B small chain, Golgi adaptor HA1/AP1 adaptin sigma-1B subunit, Sigma 1B subunit of AP-1 clathrin, MRX59, mental retardation X-linked 59, MGC:1902, AP-1 complex subunit sigma-2, golgi adaptor HA1/AP1 adaptin sigma 1B subunit.

    Product # :

    PRO-234

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    Description

    AP1S2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (1-157a.a) and having a molecular mass of 20.7kDa.AP1S2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AP1S2 protein solution (0.5mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AP1S2 belongs to the adaptin protein family and functions as the small subunit of AP-1 complex 1 which is found in the cytoplasmic face of coated vesicles placed at the Golgi complex. AP-1 complex 1 facilitates both the necessity of clathrin to the membrane and the identification of organizing signals within the cytosolic tails of transmembrane receptors.

    • Synonyms

      Adaptor-related protein complex 1 sigma 2 subunit, SIGMA1B, Adaptor protein complex AP-1 sigma-1B subunit, Clathrin assembly protein complex 1 sigma-1B small chain, Golgi adaptor HA1/AP1 adaptin sigma-1B subunit, Sigma 1B subunit of AP-1 clathrin, MRX59, mental retardation X-linked 59, MGC:1902, AP-1 complex subunit sigma-2, golgi adaptor HA1/AP1 adaptin sigma 1B subunit.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      AP1S2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQFMLLFSRQ GKLRLQKWYV PLSDKEKKKI TRELVQTVLA RKPKMCSFLE WRDLKIVYKR YASLYFCCAI EDQDNELITL EIIHRYVELL DKYFGSVCEL DIIFNFEKAY FILDEFLLGG EVQETSKKNV LKAIEQADLL QEEAETPRSV LEEIGLT

    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.

    Ap1S2 Human
  • View Data Sheet

    Name :

    CST3 Protein, His

    Description:

    Cystatin-C Human Recombinant, His Tag

    Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    Product # :

    PRO-656

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add 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 in the cell culture.

    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.

    Cystatin C Human Recombinant
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