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  • MEC (CCL28)

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Search results

1000 results found for “CDNF”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    BMF Human

    Description:

    Bcl2 Modifying Factor, Isoform 3 Human Recombinant

    Bcl-2-modifying factor, FLJ00065, BMF.

    Product # :

    PRO-700

    Price :

    Quantity :

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    • source
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    • More Info

    Description

    Bcl2 modifying factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids (1-129 a.a.) and having a molecular mass of 15.6 kDa.The Bcl2 modifying factor is fused to 15 amino acid His Tag at Nterminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Bcl2 modifying factor solution contains 20mM Tris pH-7.5, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Bcl2 modifying factor, is a member of the Bcl2 protein family of apoptosis mediators. Bcl2 modifying factor is widely expressed in many tissues.
      Bcl2 modifying factor contains a single Bcl2 homology domain 3 (BH3), and binds Bcl2 proteins and functions as an apoptotic activator. Also, Bcl2 modifying factor is important for histone deacetylase (HDAC) inhibitors which alters the balance between acetylation and deacetylation, significantly increasing histone acetylation, while strongly inducing apoptosis in a variety of cancer cell types. Bcl2 modifying factor supports Bim in regulating cell death processes in response to many stimuli. A synergistic role for bim and Bcl2 modifying factor in an apoptotic pathway leading to the clearance of Neisseria gonorrhoeae -infected cells.

    • Synonyms

      Bcl-2-modifying factor, FLJ00065, BMF.

    • 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

      MASMTGGQQM GRGSHMEPSQ CVEELEDDVF QPEDGEPVTQ PGSLLSADLF AQSLLDCPLS RLQLFPLTHC CGPGLRPTSQ EDKATQTLSPASPSQGVMLP CGVTEEPQRL FYAPAEPKSC VVADPPLPAQ PCFEWRREQE RGRP.

    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.

    Bcl2 Modifying Factor Human
  • View Data Sheet

    Name :

    TACI Human, Sf9

    Description:

    Tumor Necrosis Factor Receptor 13B Human Recombinant, Sf9

    Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.

    Product # :

    CYT-982

    Price :

    Quantity :

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    Description

    TACI produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 407 amino acids (1-165a.a.) and having a molecular mass of 45.8kDa (Molecular size on SDS-PAGE will appear at approximately 25-50kDa). TACI is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    TACI a protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.

    • 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

      ADLMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYSLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

    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.

    Taci Human Sf9
  • View Data Sheet

    Name :

    CENPP Human

    Description:

    Centromere Protein-P Human Recombinant

    Centromere protein P, CENP-P, CENPP.

    Product # :

    PRO-1784

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CENPP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-288 a.a) and having a molecular mass of 35.3kDa.CENPP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Centromere protein P (CENPP) is component of the CENPA-CAD (nucleosome distal) complex, which is a complex recruited to centromeres and involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. CENPP protein is involved in incorporation of newly synthesized CENPA into centromeres by way of its interaction with the CENPA-NAC complex.

    • Synonyms

      Centromere protein P, CENP-P, CENPP.

    • 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 MDAELAEVRA LQAEIAALRR ACEDPPAPWE EKSRVQKSFQ AIHQFNLEGW KSSKDLKNQL GHLESELSFL STLTGINIRN HSKQTEDLTS TEMTEKSIRK VLQRHRLSGN CHMVTFQLEF QILEIQNKER LSSAVTDLNI IMEPTECSEL SEFVSRAEER KDLFMFFRSL HFFVEWFEYR KRTFKHLKEK YPDAVYLSEG PSSCSMGIRS ASRPGFELVI VWRIQIDEDG KVFPKLDLLT KVPQRALELD KNRAIETAPL SFRTLVGLLG IEAALESLIK SLCAEENN.

    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.

    Cenpp Human
  • View Data Sheet

    Name :

    Exodus-2 Mouse, Sf9

    Description:

    Exodus-2 (CCL21) Mouse Recombinant, Sf9

    Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    Product # :

    CHM-043

    Price :

    Quantity :

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    • More Info

    Description

    Exodus-2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (24-133aa) and having a molecular mass of 13.1kDa.Exodus-2 is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Exodus-2 solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Exodus-2 protein or CCL21 is a cytokine, part of the CC chemokines subgroup. Because of its 6 conserved residues of the cysteine amino acid (instead of the 4 residues we usually see in chemokines), the protein is also named 6Ckine and SLC (secondary lymphoid-tissue chemokine). The gene that codes for this protein is located on chromosome 9 in humans. The Exodus-2 is binding to the CCR7 receptor, which is a chemokine receptor located to the cell’s surface.

    • Synonyms

      Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    • 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

      ADPSDGGGQD CCLKYSQKKI PYSIVRGYRK QEPSLGCPIP AILFSPRKHS KPELCANPEE GWVQNLMRRL DQPPAPGKQS PGCRKNRGTS KSGKKGKGSK GCKRTEQTQP SRGHHHHHH

    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.

    Exodus 2 Mouse
  • View Data Sheet

    Name :

    CXCL17 Rat

    Description:

    VEGF Co-regulated Chemokine 1 Rat Recombinant

    Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.

    Product # :

    CHM-281

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.

    Purity

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

    Biological Activity

    Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.

    More Info

    • Introduction

      Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.

    • Synonyms

      Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.

    • Background

      What is the molecular weight/Mw of CXCL17 RAT Protein?
      CXCL17 RAT Protein has a total Mw of 11.5kDa.

      What is the source or expression system of CXCL17 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL17 RAT Protein?
      CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL17 RAT Protein?
      Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.

      What is the amino acid sequence of CXCL17 RAT Protein?
      SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.

      What applications can CXCL17 RAT Protein be used in?
      CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL17 RAT Protein?
      The endotoxin level is minimal, CXCL17 RAT 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.

    Cxcl17 Rat
  • View Data Sheet

    Name :

    KGF Human

    Description:

    Keratinocyte Growth Factor Human Recombinant

    HBGF-7, FGF7, FGF-7, KGF.

    Product # :

    CYT-219

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    Description

    Keratinocyte Growth Factor-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 18995 Dalton.The FGF-7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 8.0, 1M NaCl.

    Purity

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

    Biological Activity

    The biological activity was determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing KGF receptors yielding an ED50 <10ng/ml, corresponding to a Specific Activity of 1.0×105 IU/mg.

    More Info

    • Introduction

      KGF is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.

    • Synonyms

      HBGF-7, FGF7, FGF-7, KGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Keratinocyte Growth Factor1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 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 Keratinocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MCNDMTPEQM ATNVNCSSPE RHTRSYDYME GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNNYNIMEI RTVAVGIVAI KGVESEFYLA MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHNG GEMFVALNQK GIPVRGKKTK KEQKTAHFLP MAIT.

    • Background

      FGF stands for fibroblast growth factor that have proteins encoded inside them. The FGF family possess broad mitogenetic activities and are involved in a lot of processes in the body. Some of the biological processes that they are included in are embryonic development, cell growth, tumor growth and tissue repair. FGF-7 is often also commonly referred to as keratinocyte growth factor or KGF and studies have focused on the link between the protein and certain tumor growth.

      Structure
      Studies have found that the crystal structure of FGF7 is comparatively similar to that of FGF10. For instance, FGF7 does interact with D2, linker as well as D3 of the receptor. Similar to other FGFs much of interaction to do with D2 is confined to conserved residues as well as the residue Arg 251 in the linker domain and the hydrophobic surface of D2. That said there are notable differences and some models predict that FGF7 actually interacts with three loops in D3.

      Mechanism
      A member of the FGF family, this factor acts completely exclusively through a subset of FGF receptor isoforms. These are mainly expressed by epithelial cells. Indeed, studies suggest that the factor specifically acts on epithelial cells. This in turn causes increased proliferation differentiation and migrations of the aforementioned cells.

      Interactions
      FGF7 and FGF10 can interact with one of the FGF receptors that is expressed by the epithelial cells. As such, it could be the case that this interaction could cause a protective factor for these epithelial tissues. The protein has also been shown to interact with Perlecan. Also referred to as basement membrane specific heparan sulfate proteoglycan core protein, this is encoded by the HSPG2 gene. A large multi domain this cross-links and binds to various extracellular matrix components as well as self surface molecules. Since FGF7 binds specifically with the perlecan protein, research suggests that i should be considered a novel biological ligand for FGF-7. This could mean that interaction has an influence on both tissue remodeling and cancer growth.

      Function
      Studies have shown that FGF-7 expression is completely unregulated during minor or even chronic injury. This has lead researchers to believe that the protein is used to heal or repair epithelial cells. Furthermore, FGF-1 also triggers the formation of apical ectodermal ridge throughout the development of limbs in the body.
      Recently, it has seemed to be the case that FGF-7 has been linked to skin injury repair, and has also been found to play some sort of role in breast cancer. As well as this, it is a vital regulator of HPC’s. It is vital because it can induce de novo activation of these HPCs.

      Further research has shown that FGF6 is a niche signal that is required for the stimulation of adult liver progenitor cells and this can support liver regeneration. This research has lead to the suggestion that FGF7 could be a possibility therapeutic target for those suffering from liver diseases.
      Studies like this are just one of the reasons why researchers continue to explore fgf-7, it’s functions and interactions.

    • Protein content

      Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.9 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of KGF as a Reference Standard.

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    Kgf Human
  • View Data Sheet

    Name :

    SHH Human

    Description:

    Sonic HedgeHog Human Recombinant

    SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    Product # :

    CYT-676

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    Description

    Sonic HedgeHog Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 20.2kDa. The Cys at position 2 has been substituted with 2 Ile’s.

    Source

    Escherichia Coli.

    Formulation

    SHH is lyophilized from 10mM Na3PO4, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 is measured by the dose-dependent induction of alkaline phosphatase production by CCL-226 fibroblasts and is 1.47μg/ml corresponding to a specific activity of 680U/mg.

    More Info

    • Introduction

      Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

    • Synonyms

      SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRALDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGGCFP

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    Sonic Hedgehog Human
  • View Data Sheet

    Name :

    NDUFV3 Human

    Description:

    NADH Dehydrogenase Flavoprotein 3 Human Recombinant

    NADH Dehydrogenase (Ubiquinone) Flavoprotein 3 10kDa, Renal Carcinoma Antigen NY-REN-4, NADH-Ubiquinone Oxidoreductase 9 KDa Subunit, EC 1.6.5.311, CI-10k, Complex I 10kDa

    Product # :

    ENZ-749

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    Description

    NDUFV3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (35-108) and having a molecular mass of 10.8kDa.NDUFV3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFV3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NDUFV3 is one of no less than 41 subunits which form the NADH-ubiquinone oxidoreductase complex that is involved in the mitochondrial respiratory chain and assists in catalyzing the rotenone-sensitive oxidation of NADH and the reduction of ubiquinone. NDUFV3 is 1 of 3 proteins found in the flavoprotein fraction of the complex but it exact function is unknown. Two transcript variants encoding altered isoforms are known for this gene.

    • Synonyms

      NADH Dehydrogenase (Ubiquinone) Flavoprotein 3 10kDa, Renal Carcinoma Antigen NY-REN-4, NADH-Ubiquinone Oxidoreductase 9 KDa Subunit, EC 1.6.5.311, CI-10k, Complex I 10kDa

    • 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 MGSSAESGKS EKGQPQNSKK QSPPKKPAPV PAEPFDNTTY KNLQHHDYST YTFLDLNLEL SKFRMPQPSS GRESPRH

    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.

    Ndufv3 Human
  • View Data Sheet

    Name :

    CCL22 Mouse

    Description:

    Macrophage-Derived Chemokine Mouse Recombinant (CCL22)

    C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.

    Product # :

    CHM-370

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    Description

    CCL22 Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.8kDa. The Mouse CCL22 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCL22 filtered (0.2µm) and lyophilized from a concentrated solution containing 20mM phosphate buffer & 150mM NaCl pH-7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4. CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph

    • Synonyms

      C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL22 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 CCL22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPYGANVEDS ICCQDYIRHP LPSRLVKEFF WTSKSCRKPG VVLITVKNRD ICADPRQVWV KKLLHKLS.

    • Background

      What is the molecular weight/Mw of CCL22 MOUSE Protein?
      CCL22 MOUSE Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CCL22 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL22 MOUSE Protein?
      CCL22 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL22 MOUSE Protein?
      Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL22 MOUSE Protein?
      GPYGANVEDS ICCQDYIRHP LPSRLVKEFF WTSKSCRKPG VVLITVKNRD ICADPRQVWV KKLLHKLS.

      What applications can CCL22 MOUSE Protein be used in?
      CCL22 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL22 MOUSE Protein?
      The endotoxin level is minimal, CCL22 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.

    Mdc Mouse
  • View Data Sheet

    Name :

    GMNN Human

    Description:

    Geminin Human Recombinant

    GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    Product # :

    PRO-579

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    Description

    Geminin Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris pH 8, 100mM NaCl and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.

    • Synonyms

      GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNPS MKQKQEEIKE NIKNSSVPRR TLKMIQPSAS GSLVGRENEL SAGLSKRKHR NDHLTSTTSS PGVIVPESSE NKNLGGVTQE SFDLMIKENP SSQYWKEVAE KRRKALYEAL KENEKLHKEI EQKDNEIARL KKENKELAEV AEHVQYMAEL IERLNGEPLD NFESLDNQEF DSEEETVEDS LVEDSEIGTC AEGTVSSSTD
      AKPCI.

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    Geminin Human
  • View Data Sheet

    Name :

    DKK3 Human, Sf9

    Description:

    Dickkopf-Related Protein 3 Human Recombinant, Sf9

    Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

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    PRO-2391

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    Description

    DKK3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 338 amino acids (22-350a.a.) and having a molecular mass of 37.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).DKK3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    DKK3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.

    • Synonyms

      Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    • 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

      ADPAPAPTAT SAPVKPGPAL SYPQEEATLN EMFREVEELM EDTQHKLRSA VEEMEAEEAA AKASSEVNLA NLPPSYHNET NTDTKVGNNT IHVHREIHKI TNNQTGQMVF SETVITSVGD EEGRRSHECI IDEDCGPSMY CQFASFQYTC QPCRGQRMLC TRDSECCGDQ LCVWGHCTKM ATRGSNGTIC DNQRDCQPGL CCAFQRGLLF PVCTPLPVEG ELCHDPASRL LDLITWELEP DGALDRCPCA SGLLCQPHSH SLVYVCKPTF VGSRDQDGEI LLPREVPDEY EVGSFMEEVR QELEDLERSL TEEMALREPA AAAAALLGGE EIHHHHHH.

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    Dkk3 Human Sf9
  • View Data Sheet

    Name :

    ACSF2 Human

    Description:

    Acyl-CoA Synthetase Family Member 2 Human Recombinant

    Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.

    Product # :

    ENZ-919

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    Description

    ACSF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (42-615 a.a) and having a molecular mass of 66.1kDa. ACSF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ACSF2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline pH 7.4 and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      Acyl-CoA synthetase family member 2, also known as ACSF2 is a member of the ATP-dependent AMP-binding enzyme family. Acyl-CoA synthetases are a family of enzymes which catalyze the thioesterification of fatty acids with coenzymeA to form activated intermediates, which play a basic part in lipid metabolism as well as homeostasis of lipid-related processes. ACSF2 is required for the complex of lipid synthesis, energy production via beta-oxidation, protein acylation and fatty-acid dependent transcriptional regulation. Moreover, ACSF2 is required for fatty acid import into cells by the process of vectorial acylation.

    • Synonyms

      Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.

    • 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 MGSLSSREVD RMVSTPIGGL SYVQGCTKKH LNSKTVGQCL ETTAQRVPER EALVVLHEDV RLTFAQLKEE VDKAASGLLS IGLCKGDRLG MWGPNSYAWV LMQLATAQAG IILVSVNPAY QAMELEYVLK KVGCKALVFP KQFKTQQYYN VLKQICPEVE NAQPGALKSQ RLPDLTTVIS VDAPLPGTLL LDEVVAAGST RQHLDQLQYN QQFLSCHDPI NIQFTSGTTG SPKGATLSHY NIVNNSNILG ERLKLHEKTP EQLRMILPNP LYHCLGSVAG TMMCLMYGAT LILASPIFNG KKALEAISRE RGTFLYGTPT MFVDILNQPD FSSYDISTMC GGVIAGSPAP PELIRAIINK INMKDLVVAY GTTENSPVTF AHFPEDTVEQ KAESVGRIMP HTEARIMNME AGTLAKLNTP GELCIRGYCV MLGYWGEPQK TEEAVDQDKW YWTGDVATMN EQGFCKIVGR SKDMIIRGGE NIYPAELEDF FHTHPKVQEV QVVGVKDDRM GEEICACIRL KDGEETTVEE IKAFCKGKIS HFKIPKYIVF VTNYPLTISG KIQKFKLREQ MERHLNL.

    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.

    Acsf2 Human
  • View Data Sheet

    Name :

    aFGF Bovine

    Description:

    Fibroblast Growth Factor Acidic Bovine

    HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

    Product # :

    CYT-613

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    Description

    Fibroblast Growth Factor-acidic Bovine (FGF-1) purified from Bovine Brain contains a 17 kDa and a 20 kDa polypeptide chain. The 17 kDa peptide is derived from the 20K peptide by restricted proteolysis. (See Jaye et al²). The FGF acidic is purified by proprietary chromatographic techniques.

    Source

    Bovine Brain.

    Formulation

    Each 5µg aFGF were lyophilized from 0.5ml solution containing 1mM sodium phosphate, pH 7 after filtration over a low binding membrane.

    Purity

    Greater than 90%.

    Biological Activity

    Stimulates growth of bovine capillary endothelial cells by 3-5 fold over 5% calf serum at 10-25ng/ml FGF.

    More Info

    • Introduction

      Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized aFGF in sterile 50mM Na2HPO4 pH-7, and 0.5% albumin. The Recommended concentration in cell culture: 1-20ng/ml.

    • Background

      What is the molecular weight/Mw of AFGF Protein?
      AFGF Protein has a total Mw of 17kDa.

      What is the source or expression system of AFGF Protein?
      Bovine Brain.

      What is the Purity of AFGF Protein?
      AFGF Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of AFGF Protein?
      Stimulates growth of bovine capillary endothelial cells by 3-5 fold over 5% calf serum at 10-25ng/ml FGF.

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

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

    Afgf Bovine
  • View Data Sheet

    Name :

    KLF12 Human

    Description:

    Kruppel-Like Factor 12 Human Recombinant

    AP-2rep, AP2REP, HSPC122, Krueppel-like factor 12, Transcriptional repressor AP-2rep.

    Product # :

    PRO-2090

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    Description

    KLF12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-402 a.a) and having a molecular mass of 46.6kDa.KLF12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLF12 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH8.0) ,10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Krueppel-like factor 12 (KLF12) belongs to the Kruppel-like zinc finger protein family and can repress expression of the AP-2 alpha gene by binding to a particular site in the AP-2 alpha gene promoter. AP-2 alpha (Activator protein-2 alpha) is a developmentally-regulated transcription factor and vital regulator of gene expression during vertebrate development and carcinogenesis. KLF12 gene repression entails binding with a corepressor, CtBP1.

    • Synonyms

      AP-2rep, AP2REP, HSPC122, Krueppel-like factor 12, Transcriptional repressor AP-2rep.

    • 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 MGSMNIHMKR KTIKNINTFE NRMLMLDGMP AVRVKTELLE SEQGSPNVHN YPDMEAVPLL LNNVKGEPPE DSLSVDHFQT QTEPVDLSIN KARTSPTAVS SSPVSMTASA SSPSSTSTSS SSSSRLASSP TVITSVSSAS SSSTVLTPGP LVASASGVGG QQFLHIIHPV PPSSPMNLQS NKLSHVHRIP VVVQSVPVVY TAVRSPGNVN NTIVVPLLED GRGHGKAQMD PRGLSPRQSK SDSDDDDLPN VTLDSVNETG STALSIARAV QEVHPSPVSR VRGNRMNNQK FPCSISPFSI ESTRRQRRSE SPDSRKRRIH RCDFEGCNKV YTKSSHLKAH RRTHTGEKPY KCTWEGCTWK FARSDELTRH YRKHTGVKPF KCADCDRSFS RSDHLALHRR RHMLV.

    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.

    Klf12 Human
  • View Data Sheet

    Name :

    NFATC1 Antibody

    Description:

    Nuclear factor of activated T-cells cytoplasmic 1, Mouse Anti Human

    Nuclear factor of activated T-cells cytoplasmic 1, NFAT transcription complex cytosolic component, NF-ATc1, NFATc1, NF-ATc, NFATc, NFAT2, MGC138448.

    Product # :

    ANT-436

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    Formulation

    1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide and 10% Glycerol.

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    • Introduction

      NFATC1 is a component of the nuclear factor of activated T cells DNA-binding transcription complex. This complex consists of at least 2 components: a preexisting cytosolic component that translocates to the nucleus upon T cell receptor (TCR) stimulation, and an inducible nuclear component. Proteins belonging to this family of transcription factors play an essential role in inducible gene transcription during immune response. NFATC1 is an inducible nuclear component. NFATC1 functions as a major molecular target for the immunosuppressive drugs such as cyclosporin A. Different isoforms of NFATC1 may regulate inducible expression of different cytokine genes.

    • Synonyms

      Nuclear factor of activated T-cells cytoplasmic 1, NFAT transcription complex cytosolic component, NF-ATc1, NFATc1, NF-ATc, NFATc, NFAT2, MGC138448.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human NFATC1 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NFATC1 amino acids 428-716 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and κ light chain.

    • Clone

      PAT1C3AT.

    • Applications

      NFATC1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      NFATC1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Nfatc1 Antibody
  • View Data Sheet

    Name :

    C17ORF103 Human

    Description:

    Chromosome 17 Open Reading Frame 103 Human Recombinant

    Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.

    Product # :

    PRO-1619

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    Description

    C17ORF103 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113) and having a molecular mass of 15.4kDa.C17ORF103 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C17ORF103 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      C17orf103 is a member of the GTLF3B family and is encoded by a gene which is located in human chromosome 17p11.2. BRCA1 and p53 are 2 main tumor suppressor genes which are linked to chromosome 17. Tumor suppressor p53 is necessary for maintenance of cellular genetic integrity by moderating cell fate through DNA repair versus cell death. C17orf103 is also related to neurofibromatosis, a disorder characterized by neural and epidermal lesions, and dysregulated Schwann cell growth.

    • Synonyms

      Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.

    • 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 MGSMAHSAAA VPLGALEQGC PIRVEHDRRR RQFTVRLNGC HDRAVLLYEY VGKRIVDLQH TEVPDAYRGR GIAKHLAKAA LDFVVEEDLK AHLTCWYIQK YVKENPLPQY LERLQP

    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.

    C17Orf103 Human
  • View Data Sheet

    Name :

    CD14 Human, CHO

    Description:

    CD14 Human Recombinant, CHO

    Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein, CD14.

    Product # :

    PRO-536

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    Description

    The CD14 is produced from human CD14 transfected CHO-cells. Before transfection the complete human CD14-cDNA was amplified by PCR and cloned into expression vector p-POL-DHFR. The myeloid differentiation antigen CD14 acts as the major receptor for bacterial LPS. The dominant form of the recombinant wild type CD14 is the 50-kDa protein containing 335 amino acids and lacks the GPI-Anchor.

    Source

    CHO-cells.

    Formulation

    CD14 was lyophilized from a concentrated protein solution (1.0 mg/ml) containing phosphate-buffered saline, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Up to 20 µg/ml CD14 inhibit binding of FITC-LPS (0.5µg/ml) to 600,000 CD14+CHO transfectants (FACS).

    More Info

    • Introduction

      CD14 (also known lipopolysaccharide (LPS) receptor) is expressed strongly on monocytes and macrophage and weakly on the surface of neutrophils. CD14 is anchored to cells by linkage to glycosylphosphatidylinositol (GPI) and functions as a high affinity receptor for complexes of LPS and LPS binding protein (LBP). Soluble CD14, also binding to LPS, acts at physiological concentration as an LPS agonist and has, at higher concentrations, an LPS antagonizing effect in cell activation. CD14 has been shown to bind apoptotic cells.

    • Synonyms

      Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein, CD14.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CD14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD14 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 CD14 in sterile 18MΩ-cm H2O not less than 100µg/ml. Further dilutions should be made with phosphate buffered saline (PBS).

    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.

    Cd14 Human Cho
  • View Data Sheet

    Name :

    CCL28 Human, His

    Description:

    Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28), His Tag

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-366

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    Description

    CCL28 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 126 amino acids (23-127 a.a.) and having a molecular mass of 14.3 kDa. The CCL28 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL28 protein contains 10mM Sodium Citrate pH3.5 and 10% Glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • 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 MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.

    • Background

      What is the molecular weight/Mw of CCL28 HUMAN, HIS Protein?
      CCL28 HUMAN, HIS Protein has a total Mw of 14.3kDa.

      What is the source or expression system of CCL28 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL28 HUMAN, HIS Protein?
      CCL28 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 HUMAN, HIS Protein?
      The biological functionality of CCL28 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL28 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.

      What applications can CCL28 HUMAN, HIS Protein be used in?
      CCL28 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL28 HUMAN, HIS 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.

    Ccl28 Human His
  • View Data Sheet

    Name :

    CX3CL1 Human

    Description:

    Fractalkine Human Recombinant (CX3CL1)

    Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    Product # :

    CHM-235

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    Description

    Fractalkine Human Recombinant- produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8638 Dalton. The Fractalkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CX3CL1 was lyophilized from a 0.2μm filtered concentrated (1.0 mg/ml) solution in 20mM Phosphate buffer, pH 7.4, 50mM NaCl.

    Purity

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

    Biological Activity

    The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

      Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CX3CL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CX3CL1 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 CX3CL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.

    • Background

      What is the molecular weight/Mw of CX3CL1 HUMAN Protein?
      CX3CL1 HUMAN Protein has a total Mw of 8.63kDa.

      What is the source or expression system of CX3CL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CX3CL1 HUMAN Protein?
      CX3CL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 HUMAN Protein?
      The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.

      What is the amino acid sequence of CX3CL1 HUMAN Protein?
      QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.

      What applications can CX3CL1 HUMAN Protein be used in?
      CX3CL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 HUMAN Protein?
      The endotoxin level is minimal, CX3CL1 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.

    Fractalkine Human
  • View Data Sheet

    Name :

    CAMK2N2 Human

    Description:

    Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 2 Human Recombinant

    Calcium/calmodulin-dependent protein kinase II inhibitor 2, CAMK2N2, CaM-KII inhibitory protein, CaM-KIIN, CAMKIIN, Calcium/calmodulin-dependent protein kinase II.

    Product # :

    PKA-311

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    Description

    CAMK2N2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (1-79a.a) and having a molecular mass of 11kDa.CAMK2N2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CAMK2N2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 2 (CAMK2N2) is a protein coding gene which regulates cell growth when overexpressed in colon adenocarcinoma LoVo cells. CAMK2N2 plays a role as a cellular inhibitor of CaM-kinase II (CAMK2).

    • Synonyms

      Calcium/calmodulin-dependent protein kinase II inhibitor 2, CAMK2N2, CaM-KII inhibitory protein, CaM-KIIN, CAMKIIN, Calcium/calmodulin-dependent protein kinase II.

    • 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 MGSMSEILPY SEDKMGRFGA DPEGSDLSFS CRLQDTNSFF AGNQAKRPPK LGQIGRAKRV VIEDDRIDDV LKGMGEKPPS GV.

    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.

    Camk2N2 Human
  • View Data Sheet

    Name :

    DCTN6 Human

    Description:

    Dynactin 6 Human Recombinant

    Dynactin 6, WS3, Dynactin Subunit P27, Protein WS-3, P27, Novel RGD-Containing Protein, Dynactin Subunit 6, WS-3, Dynactin subunit 6.

    Product # :

    PRO-2094

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    Description

    DCTN6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a) and having a molecular mass of 23.1kDa. DCTN6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCTN6 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dynactin 6, also known as DCTN6 is a member of the dynactin subunits 5/6 family. DCTN6 includes an RGD (Arg-Gly-Asp) motif in the N-terminal region, which confers adhesive properties to macromolecular proteins such as fibronectin. DCTN6 has a high degree of sequence resemblance with the mouse homolog, which has been found to participate in mitochondrial biogenesis. Moreover, the precise biological function of DCTN6 is unknown.

    • Synonyms

      Dynactin 6, WS3, Dynactin Subunit P27, Protein WS-3, P27, Novel RGD-Containing Protein, Dynactin Subunit 6, WS-3, Dynactin subunit 6.

    • 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 MGSMAEKTQK SVKIAPGAVV CVESEIRGDV TIGPRTVIHP KARIIAEAGP IVIGEGNLIE EQALIINAYP DNITPDTEDP EPKPMIIGTN NVFEVGCYSQ AMKMGDNNVI ESKAYVGRNV ILTSGCIIGA CCNLNTFEVI PENTVIYGAD CLRRVQTERP QPQTLQLDFL MKILPNYHHL KKTMKGSSTP VKN.

    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.

    Dctn6 Human
  • View Data Sheet

    Name :

    IFNAR1 Human

    Description:

    Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant

    IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.

    Product # :

    CYT-1138

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    • SDS-PAGE

    Description

    IFNAR1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 415 amino acids (28-436a.a.) and having a molecular mass of 47.9kDa. IFNAR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    IFNAR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    IFNAR1 Human - Product image 1

    More Info

    • Introduction

      Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.

    • Synonyms

      IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 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

      KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

    • Background

      What is the molecular weight/Mw of IFNAR1 HUMAN Protein?
      IFNAR1 HUMAN Protein has a total Mw of 47.9kDa.

      What is the source or expression system of IFNAR1 HUMAN Protein?
      Sf9, Insect cells.

      What is the Purity of IFNAR1 HUMAN Protein?
      IFNAR1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNAR1 HUMAN Protein?
      The biological functionality of IFNAR1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IFNAR1 HUMAN Protein?
      KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

      What applications can IFNAR1 HUMAN Protein be used in?
      IFNAR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNAR1 HUMAN Protein?
      The endotoxin level is minimal, IFNAR1 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.

    Ifnar1 Human
  • View Data Sheet

    Name :

    NEFL Human

    Description:

    Neurofilament Light Human Recombinant

    Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    Product # :

    PRO-2584

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    Description

    NEFL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (2-543 a.a) containing 551 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 62.5kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    NEFL filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 15mM Tris and 85mM Glycine, pH 8.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NEFL or Neurofilament light polypeptide is a protein that is encoded through the NEFL gene. NEFL is correlated to a disease called Charcot–Marie–Tooth. The protein’s light subunit is determined by immunoassays in the plasma and cerebrospinal fluid, if present, it can indicate on axonal damage in neurological diseases. By doing so, NEFL can act as a marker for Huntington's disease, Amyotrophic Lateral Sclerosis and multiple sclerosis.

    • Synonyms

      Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKHHHHHHAS SFSYEPYYST SYKRRYVETP RVHISSVRSG YSTARSAYSS YSAPVSSSLS VRRSYSSSSG SLMPSLENLD LSQVAAISND LKSIRTQEKA QLQDLNDRFA SFIERVHELE QQNKVLEAEL LVLRQKHSEP SRFRALYEQE IRDLRLAAED ATNEKQALQG EREGLEETLR NLQARYEEEV LSREDAEGRL MEARKGADEA ALARAELEKR IDSLMDEISF LKKVHEEEIA ELQAQIQYAQ ISVEMDVTKP DLSAALKDIR AQYEKLAAKN MQNAEEWFKS RFTVLTESAA KNTDAVRAAK DEVSESRRLL KAKTLEIEAC RGMNEALEKQ LQELEDKQNA DISAMQDTIN KLENELRTTK SEMARYLKEY QDLLNVKMAL DIEIAAYRKL LEGEETRLSF TSVGSITSGY SQSSQVFGRS AYGGLQTSSY LMSTRSFPSY YTSHVQEEQI EVEETIEAAK AEEAKDEPPS EGEAEEEEKD KEEAEEEEAA EEEEAAKEES EEAKEEEEGG EGEEGEETKE AEEEEKKVEG AGEEQAAKKK D.

    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.

    Hepsin Human
  • View Data Sheet

    Name :

    MIF Human His N

    Description:

    Macrophage Migration Inhibitory Factor Human, Recombinant His Tag N-Terminus

    Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    Product # :

    CYT-431

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    Description

    MIF human Recombinant, fused to 40 a.a. His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques. Macrophage Inducing Factor Human Recombinant ( 1-115 a.a. ) is a single, non-glycosylated, polypeptide chain having a total amino acids of 155 and molecular mass of 17kDa.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml solution containing 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

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.

    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.

    Mif Human His N
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