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Search results

1000 results found for “noggin”

Name

Description

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  • View Data Sheet

    Name :

    NUDT21 Human

    Description:

    Nudix Type Motif 21 Human Recombinant

    Cleavage and polyadenylation specificity factor subunit 5, Cleavage and polyadenylation specificity factor 25 kDa subunit, CFIm25, CPSF 25 kDa subunit, Nucleoside diphosphate-linked moiety X motif 21, Nudix motif 21, Pre-mRNA cleavage factor Im 25 kDa subunit, NUDT21, CFIM25, CPSF25, CPSF5, DKFZp686H1588.

    Product # :

    ENZ-080

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    Description

    NUDT21 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 247 amino acids (1-227 a.a.) and having a molecular mass of 28.3kDa. The NUDT21 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT21 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NUDT21 belongs to the Nudix hydrolase family of pyrophosphatases. NUDT21 localizes to the paraspeckles and forms a heterodimer with CPSF6 or CPSF7 to comprise the CFIm (mammalian cleavage factor I) complex. NUDT21 being the smaller subunit of the complex, is present in all heterodimer combinations. NUDT21 has a vital role in pre-mRNA 3' cleavage and polyadenylation processing.

    • Synonyms

      Cleavage and polyadenylation specificity factor subunit 5, Cleavage and polyadenylation specificity factor 25 kDa subunit, CFIm25, CPSF 25 kDa subunit, Nucleoside diphosphate-linked moiety X motif 21, Nudix motif 21, Pre-mRNA cleavage factor Im 25 kDa subunit, NUDT21, CFIM25, CPSF25, CPSF5, DKFZp686H1588.

    • 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 MSVVPPNRSQ TGWPRGVTQF GNKYIQQTKP LTLERTINLY PLTNYTFGTK EPLYEKDSSV AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG TTFFKLPGGE LNPGEDEVEG LKRLMTEILG RQDGVLQDWV IDDCIGNWWR PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ EKALFAVPKN YKLVAAPLFE LYDNAPGYGP IISSLPQLLS RFNFIYN.

    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.

    Nudt21 Human
  • View Data Sheet

    Name :

    OAZ1 Human

    Description:

    Ornithine Decarboxylase Antizyme 1 Human Recombinant

    Ornithine decarboxylase antizyme 1, OAZ, ODC-Az, AZI, antizyme 1, MGC138338.

    Product # :

    PRO-1200

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    Description

    OAZ1 Human Recombinant produced in E. coli is a single polypeptide chain containing 251 amino acids (1-228) and having a molecular mass of 27.8 kDa.OAZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The OAZ1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      OAZ1 is a member of the ODC antizyme family. OAZ1 is auto-regulated expressed by polyamine-enhanced translational frame shifting. OAZ1 negatively controls polyamine synthesis by increasing the negative feedback loop regulating ornithine decarboxylase (ODC) activity. The OAZ1 protein inhibits ornithine decarboxylase and speeds up its detraction.

    • Synonyms

      Ornithine decarboxylase antizyme 1, OAZ, ODC-Az, AZI, antizyme 1, MGC138338.

    • 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 MGSMVKSSLQ RILNSHCFAR EKEGDKPSAT IHASRTMPLL SLHSRGGSSS ESSRVSLHCC SNPGPGPRWC SDAPHPPLKI PGGRGNSQRD HNLSANLFYS DDRLNVTEEL TSNDKTRILN VQSRLTDAKR INWRTVLSGG SLYIEIPGGA LPEGSKDSFA VLLEFAEEQL RADHVFICFH KNREDRAALL RTFSFLGFEI VRPGHPLVPK RPDACFMAYT FERESSGEEE E

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

    Oaz1 Human
  • View Data Sheet

    Name :

    BDNF Human, His

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant, His Tag

    Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.

    Product # :

    CYT-881

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    • sds-page

    Description

    BDNF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (129-247 a.a) and having a molecular mass of 15.8kDa. BDNF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BDNF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    BDNF-sds-page - Product image 1

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.

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

    • Background

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 15.8kDa.

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

      What is the Purity of BDNF Protein?
      BDNF Protein is >85% pure as determined by SDS-PAGE.

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

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

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

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

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

    Bdnf Human His
  • View Data Sheet

    Name :

    OTUB1 Human

    Description:

    Ubiquitin Aldehyde Binding 1 Human Recombinant

    Ubiquitin thioesterase OTUB1, Otubain-1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Ubiquitin-specific-processing protease OTUB1, Deubiquitinating enzyme OTUB1, OTUB1, OTB1, OTU1, HSPC263, MGC4584, FLJ20113, FLJ40710, MGC111158.

    Product # :

    PRO-711

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    • description
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    • formulation
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    • More Info

    Description

    OTUB1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1- 271 a.a.) and having a molecular mass of 33.4kDa.The OTUB1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OTUB1 solution contains 20mM Tris buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Otubain 1 (OTUB1) belongs to the ovarian tumor (OUT) superfamily of predicted cysteine proteases and inhibits cytokine gene transcription in the immune system through its interaction with a ubiquitin protease and E3 ubiquitin ligase. OTUB1 is a highly specific ubiquitin iso-peptidase, it cleaves ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates. OTUB1 is believed to work in specific ubiquitin-dependent pathways, possibly by providing an editing function of polyubiquitin chain growth. OTUB1 is a hydrolase that removes conjugated ubiquitin from proteins in vitro and may therefore have a significant regulatory role in the level of protein turnover by preventing degradation. Additionally, OTUB1 is a regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered impassive to antigen re-challenge and no longer respond to their cognate antigen. OTUB1 acts via its interaction with RNF128/GRAIL, which is an essential inductor of CD4 T-cell anergy.

    • Synonyms

      Ubiquitin thioesterase OTUB1, Otubain-1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Ubiquitin-specific-processing protease OTUB1, Deubiquitinating enzyme OTUB1, OTUB1, OTB1, OTU1, HSPC263, MGC4584, FLJ20113, FLJ40710, MGC111158.

    • 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 MAAEEPQQQK QEPLGSDSEG VNCLAYDEAI MAQQDRIQQE IAVQNPLVSE RLELSVLYKE YAEDDNIYQQ KIKDLHKKYS YIRKTRPDGN CFYRAFGFSH LEALLDDSKE LQRFKAVSAK SKEDLVSQGF TEFTIEDFHN TFMDLIEQVE KQTSVADLLA SFNDQSTSDY LVVYLRLLTS GYLQRESKFF EHFIEGGRTV KEFCQQEVEP MCKESDHIHI IALAQALSVS IQVEYMDRGE GGTTNPHIFP EGSEPKVYLL YRPGHYDILY K.

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

    Otub1 Human
  • View Data Sheet

    Name :

    IL 3 Human

    Description:

    Interleukin-3 Human Recombinant

    MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    Product # :

    CYT-210

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    Description

    Interleukin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 0.3 mg/ml of NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000 IU/mg.

    More Info

    • Introduction

      IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.

    • Synonyms

      MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 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 Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Met-Thr-Gln.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.84 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 standard solution of IL-3 as a Reference Standard.

    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.

    Il 3 Human
  • View Data Sheet

    Name :

    C10ORF54 Human

    Description:

    Chromosome 10 Open Reading Frame 54 Human Recombinant

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

    Product # :

    PRO-2259

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    C10Orf54 Human
  • View Data Sheet

    Name :

    FGB Human

    Description:

    Fibrinogen Beta Chain Human Recombinant

    Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.

    Product # :

    PRO-2210

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    Description

    FGB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 351 amino acids (164-491a.a) and having a molecular mass of 40kDa. FGB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fibrinogen Beta Chain 9 (FGB) is the beta component of fibrinogen, a blood-borne glycoprotein composed of 3 pairs of nonidentical polypeptide chains. When vascular injury accrues, fibrinogen is cleaved by thrombin to form fibrin which is found in abundance in blood clots.

    • Synonyms

      Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.

    • 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 MGSDNENVVN EYSSELEKHQ LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM SMKIRPFFPQ Q.

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    Fgb Human
  • View Data Sheet

    Name :

    IL21R Human

    Description:

    Interleukin-21 Receptor Human Recombinant

    Interleukin 21 Receptor, Novel Interleukin Receptor, IL-21 Receptor, NILR, Interleukin-21 Receptor, CD360 Antigen, IL-21R, CD360.

    Product # :

    CYT-911

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    Description

    IL21R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (20-232 a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 221 amino acids and having a molecular mass of 25.6kDa.IL21R shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL21R protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-21 receptor, also known as IL21R is a member of the type I cytokine receptors family. IL21R forms a heterodimeric receptor complex with the common gamma-chain, a receptor subunit which is also shared by the receptors for interleukin 2, 4, 7, 9, and 15. Furthermore, IL21 receptor transduces the growth promoting signal of IL21, and is significant for the proliferation as well as differentiation of T cells, B cells, and natural killer (NK) cells. The ligand binding of IL21 receptor leads to the activation of numerous downstream signaling molecules, including JAK1, JAK3, STAT1, as well as STAT3.

    • Synonyms

      Interleukin 21 Receptor, Novel Interleukin Receptor, IL-21 Receptor, NILR, Interleukin-21 Receptor, CD360 Antigen, IL-21R, CD360.

    • 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

      CPDLVCYTDY LQTVICILEM WNLHPSTLTL TWQDQYEELK DEATSCSLHR SAHNATHATY TCHMDVFHFM ADDIFSVNIT DQSGNYSQEC GSFLLAESIK PAPPFNVTVT FSGQYNISWR SDYEDPAFYM LKGKLQYELQ YRNRGDPWAV SPRRKLISVD SRSVSLLPLE FRKDSSYELQ VRAGPMPGSS YQGTWSEWSD PVIFQTQSEE LKEVEHHHHH H

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    Il21R Human
  • View Data Sheet

    Name :

    Calumenin Human

    Description:

    Calumenin Human Recombinant

    CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.

    Product # :

    PRO-2465

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    Description

    Calumenin Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (20-315) and having a molecular mass of 35kDa. Calumenin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Calumenin solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The IC50 value is < 2.0nM. The inhibitory function of Cystatin 5 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.

    More Info

    • Introduction

      Calumenin is a calcium-binding protein located in the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin belongs to a family of multiple EF-hand proteins (CERC) that include reticulocalbin, ERC-55, and Cab45 and the product of this gene. Calumenin binds 7 calcium ions having low affinity and takes part in such ER functions as protein folding and sorting.

    • Synonyms

      CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.

    • 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

      MKPTEKKDRV HHEPQLSDKV HNDAQSFDYD HDAFLGAEEA KTFDQLTPEE SKERLGKIVS KIDGDKDGFV TVDELKDWIK FAQKRWIYED VERQWKGHDL NEDGLVSWEE YKNATYGYVL DDPDPDDGFN YKQMMVRDER RFKMADKDGD LIATKEEFTA FLHPEEYDYM KDIVVQETME DIDKNADGFI DLEEYIGDMY SHDGNTDEPE WVKTEREQFV EFRDKNRDGK MDKEETKDWI LPSDYDHAEA EARHLVYESD QNKDGKLTKE EIVDKYDLFV GSQATDFGEA LVRHDEF.

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    Calumenin Human 2
  • View Data Sheet

    Name :

    FGF17 Human

    Description:

    Fibroblast Growth Factor 17 Human Recombinant

    Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    Product # :

    CYT-817

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    Description

    FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 22.6kDa.

    Source

    Escherichia Coli.

    Formulation

    FGF17 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

    More Info

    • Introduction

      Fibroblast Growth Factor 17 (FGF17) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.

    • Synonyms

      Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF17 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 FGF17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

    • Background

      What is the molecular weight/Mw of FGF17 Protein?
      FGF17 Protein has a total Mw of 22.6kDa.

      What is the source or expression system of FGF17 Protein?
      Escherichia Coli.

      What is the Purity of FGF17 Protein?
      FGF17 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF17 Protein?
      Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

      What is the amino acid sequence of FGF17 Protein?
      MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

      What applications can FGF17 Protein be used in?
      FGF17 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF17 Protein?
      The endotoxin level is minimal, FGF17 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.

    Fgf 17 Human
  • View Data Sheet

    Name :

    CCDC25 Human

    Description:

    Coiled-Coil Domain Containing 25 Human Recombinant

    Coiled-coil domain-containing protein 25, CCDC25.

    Product # :

    PRO-1655

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    Description

    CCDC25 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-208 a.a) and having a molecular mass of 26.9kDa.CCDC25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CCDC25 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Coiled-Coil Domain Containing 25 (CCDC25) is a 208 amino acid protein belonging to the CCDC25 family.

    • Synonyms

      Coiled-coil domain-containing protein 25, CCDC25.

    • 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 MGSMVFYFTS SSVNSSAYTI YMGKDKYENE DLIKHGWPED IWFHVDKLSS AHVYLRLHKG ENIEDIPKEV LMDCAHLVKA NSIQGCKMNN VNVVYTPWSN LKKTADMDVG QIGFHRQKDV KIVTVEKKVN EILNRLEKTK VERFPDLAAE KECRDREERN EKKAQIQEMK KREKEEMKKK REMDELRSYS SLMKVENMSS NQDGNDSDEF M.

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    Ccdc25 Human
  • View Data Sheet

    Name :

    CX3CL1 Mouse

    Description:

    Fractalkine Mouse Recombinant (CX3CL1)

    Fractalkine, C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1, Cx3cl1, Cx3c, Fkn, Scyd1, CX3C, ABCD-3, AB030188, AI848747, D8Bwg0439e.

    Product # :

    CHM-017

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    Description

    Fractalkine Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa. The CX3CL1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 µg/ml, corresponding to a specific activity of > 2000IU/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, C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1, Cx3cl1, Cx3c, Fkn, Scyd1, CX3C, ABCD-3, AB030188, AI848747, D8Bwg0439e.

    • 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

      QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG.

    • Background

      What is the molecular weight/Mw of CX3CL1 MOUSE Protein?
      CX3CL1 MOUSE Protein has a total Mw of 8.7kDa.

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

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

      What is the Biological Activity of CX3CL1 MOUSE Protein?
      The ED50as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 µg/ml, corresponding to a specific activity of > 2000IU/mg.

      What is the amino acid sequence of CX3CL1 MOUSE Protein?
      QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG.

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

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

    Fractalkine Mouse
  • View Data Sheet

    Name :

    GKN2 Human

    Description:

    Gastrokine 2 Human Recombinant

    Gastrokine-2, Blottin, Down-regulated in gastric cancer, Trefoil factor interactions(z) 1, GKN2, BLOT, GDDR, TFIZ1, PRO813, BRICD1B, VLTI465.

    Product # :

    PRO-1588

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    Description

    Gastrokine 2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 21-184) containing 174 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 19.6kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    GKN2 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gastrokine-2 (GKN2) is expressed in the gastric mucosa. GKN2 forms a heterodimer with TFF1- disulfide linked. GKN2 interacts with TFF2.

    • Synonyms

      Gastrokine-2, Blottin, Down-regulated in gastric cancer, Trefoil factor interactions(z) 1, GKN2, BLOT, GDDR, TFIZ1, PRO813, BRICD1B, VLTI465.

    • 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 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely at 37°C. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. GKN2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASYEVFNIISPS NNGGNVQETV TIDNEKNTAI INIHAGSCSS TTIFDYKHGY IASRVLSRRA CFILKMDHQN IPPLNNLQWY IYEKQALDNM FSSKYTWVKY NPLESLIKDV DWFLLGSPIE KLCKHIPLYK GEVVENTHNV GAGGCAKAGL LGILGISICA DIHV.

    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.

    Gkn2 Human
  • View Data Sheet

    Name :

    LTBR Human

    Description:

    Lymphotoxin Beta Receptor Human Recombinant

    Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

    Product # :

    CYT-853

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    Description

    LTBR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-227 a.a) and having a molecular mass of 24.6kDa.LTBR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LTBR protein solution (0.5mg/ml) containing PBS buffer (pH7.4) 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lymphotoxin Beta Receptor, also known as LTBR takes part in signaling during the development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. In addition, the activity of this receptor has been associated to carcinogenesis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for LTBR.

    • Synonyms

      Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

    • 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 MGSMSQPQAV PPYASENQTC RDQEKEYYEP QHRICCSRCP PGTYVSAKCS RIRDTVCATC AENSYNEHWN YLTICQLCRP CDPVMGLEEI APCTSKRKTQ CRCQPGMFCA AWALECTHCE LLSDCPPGTE AELKDEVGKG NNHCVPCKAG HFQNTSSPSA RCQPHTRCEN QGLVEAAPGT AQSDTTCKNP LEPLPPEMSG TMLM

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    Ltbr Human
  • View Data Sheet

    Name :

    LYG2 Human

    Description:

    Lysozyme G-Like 2 Human Recombinant

    Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.

    Product # :

    PRO-1245

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    Description

    LYG2 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (20-212) and having a molecular mass of 23.9 kDa. LYG2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The LYG2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      lysozyme G-like 2 and LYGH (LYG2), is a member of the glycosyl hydrolase 23 family. Lysozyme takes part in human innate immunity by causing bacterial cell lysis. LYG2 contains a SLT domain, a protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc).

    • Synonyms

      Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.

    • 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 MGSSYPFSHS MKPHLHPRLY HGCYGDIMTM KTSGATCDAN SVMNCGIRGS EMFAEMDLRA IKPYQTLIKE VGQRHCVDPA VIAAIISRES HGGSVLQDGW DHRGLKFGLM QLDKQTYHPV GAWDSKEHLS QATGILTERI KAIQKKFPTW SVAQHLKGGL SAFKSGIEAI ATPSDIDNDF VNDIIARAKF YKRQSF.

    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.

    Lyg2 Human
  • View Data Sheet

    Name :

    MANF Mouse

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Mouse Recombinant

    Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    Product # :

    CYT-827

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    Description

    MANF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18.2kDa.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using rat C6 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

    More Info

    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIEEELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDNQ IDLSTVDLKK LRVKELKKIL DDWGEMCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.

    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.

    Manf Mouse
  • View Data Sheet

    Name :

    RAC3 Human

    Description:

    Ras-Related C3 Botulinum Toxin Substrate 3 Human Recombinant

    Ras-related C3 substrate 3, p21-Rac3, RAC3.

    Product # :

    PRO-073

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    Description

    RAC3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 189 amino acids (1-189 a.a.) and having a total molecular mass of 21kDa.RAC3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RAC3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 200mM NaCl, 0.1mM PMSF and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAC3 belongs to the Rac subfamily of the Rho small G proteins. RAC3 is a small (approximately 21kDa) monomeric GTP-binding protein, which is an important component of intracellular signaling pathway, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases.

    • Synonyms

      Ras-related C3 substrate 3, p21-Rac3, RAC3.

    • 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

      MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPHTPI LLVGTKLDLR DDKDTIERLR DKKLAPITYP QGLAMAREIG SVKYLECSAL TQRGLKTVFD EAIRAVLCPP PVKKPGKKC.

    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.

    Rac3 Human
  • View Data Sheet

    Name :

    Visfatin Mouse

    Description:

    Visfatin Mouse Recombinant

    PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    Product # :

    CYT-447

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    Description

    Visfatin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-491) containing a 20 aa His tag and having 511 amino acids. The total molecular mass is 57kDa. The Visfatin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 1x PBS pH-7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-?, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
      Visfatin exerts insulin-mimetic effects that are dose-dependent and quantitatively similar to those of insulin in stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its insulin-mimetic effects, visfatin was as effective as insulin in reducing hyperglycemia in insulin-deficient diabetic mice. Visfatin was also found to be bound to and activate insulin receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin and insulin did not compete for binding to the insulin receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes.

    • Synonyms

      PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    • Physical Appearance

      Sterile Filtered colorless 1mg/ml solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECREKKTENSKVR KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERGWNYILEKYDG HLPIEVKAVP EGSVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPITVATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVTENSKG YKLLPPYLRV IQGDGVDINT LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG VNVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL EEYGHDLLHTVFKNGKVTKS YSFDEVRKNA QLNIEQDVAP H.

    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.

    Visfatin Mouse
  • View Data Sheet

    Name :

    ZCCHC17 Human

    Description:

    Zinc Finger, CCHC Domain Containing 17 Human Recombinant

    Zinc finger CCHC domain containing 17, PS1D, pNO40, HSPC251, Pnn-interacting nucleolar protein, Putative S1 RNA-binding domain protein, RP11-266K22.1, Nucleolar protein of 40 kDa, PS1D protein.

    Product # :

    PRO-183

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    Description

    ZCCHC17 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-241a.a.) and having a molecular mass of 30.0 kDa (Molecular weight on SDS-PAGE will appear higher). ZCCHC17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ZCCHC17 protein solution (0.25mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 2mM DTT, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ZCCHC17 protein interacts with PNN and associates with the 60S ribosomal subunit. Universally expressed, ZCCHC17 is localizing to the nucleolus, and takes part in ribosome maturation and biogenesis.

    • Synonyms

      Zinc finger CCHC domain containing 17, PS1D, pNO40, HSPC251, Pnn-interacting nucleolar protein, Putative S1 RNA-binding domain protein, RP11-266K22.1, Nucleolar protein of 40 kDa, PS1D protein.

    • 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 MGSMNSGRPE TMENLPALYT IFQGEVAMVT DYGAFIKIPG CRKQGLVHRT HMSSCRVDKP SEIVDVGDKV WVKLIGREMK NDRIKVSLSM KVVNQGTGKD LDPNNVIIEQ EERRRRSFQD YTGQKITLEA VLNTTCKKCG CKGHFAKDCF MQPGGTKYSL IPDEEEEKEE AKSAEFEKPD PTRNPSRKRK KEKKKKKHRD RKSSDSDSSD SESDTGKRAR HTSKDSKAAK KKKKKKKHKK KHKE.

    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.

    Zcchc17 Human
  • View Data Sheet

    Name :

    Leptin Human, Mutant

    Description:

    Leptin Mutant D23L Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1243

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    Description

    Human Leptin Mutant D23L is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. Leptin Mutant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    Leptin Mutant was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Human Leptin Mutant D23L is fully biologically active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human Leptin Mutant D23L although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Mutant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids of recombinant human leptin was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Background

      Leptin’s main part is to regulate long-term energy balance. Leptin is a hormone which mainly produced by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

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    Mutant Leptin
  • View Data Sheet

    Name :

    Eotaxin Human, His

    Description:

    Eotaxin Human Recombinant (CCL11), His Tag

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    Product # :

    CHM-344

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    Description

    Eotaxin His Tag Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids fragment (24-87) corresponding to the mature Eotaxin protein and having a molecular mass of 8345.9 Dalton with an amino-terminal hexahistidine tag.The Eotaxin-His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Eotaxin-His is supplied liquid In Phosphate Buffered Saline pH7.4 containing 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP

    • Background

      What is the molecular weight/Mw of EOTAXIN HUMAN, HIS Protein?
      EOTAXIN HUMAN, HIS Protein has a total Mw of 8.34kDa.

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

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

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

      What is the amino acid sequence of EOTAXIN HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP

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

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

    Eotaxin Human His
  • View Data Sheet

    Name :

    BMP 2 Human, Monomer

    Description:

    Bone Morphogenetic Protein-2 Human Recombinant, Monomer

    BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.

    Product # :

    CYT-627

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    Description

    Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 115 amino acids (283-396) and having a molecular mass of 13009 Dalton. The BMP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-2 solution contains 10mM NaAc pH=3.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.

    • Synonyms

      BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.

    • Background

      What is the molecular weight/Mw of BMP2 Protein?
      BMP2 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP2 Protein?
      Escherichia Coli.

      What is the Purity of BMP2 Protein?
      BMP2 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP2 Protein?
      The biological functionality of BMP2 Protein will be determined in the future.

      What is the amino acid sequence of BMP2 Protein?
      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.

      What applications can BMP2 Protein be used in?
      BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP2 Protein?
      The endotoxin level is minimal, BMP2 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.

    Bmp 2 Human Monomer
  • View Data Sheet

    Name :

    IL-4 Porcine

    Description:

    Interleukin-4 Porcine Recombinant

    BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

    Product # :

    CYT-1098

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    Shipped at Room temp

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

    Description

    Interleukin-4 Porcine Recombinant produced in E. coli is a non-glycosylated monomer chain containing 110 amino acids and having a molecular mass of 12.7kDa. IL-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10 mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as determined by TF-1 cell proliferation is 0.504ng/ml corresponding to a specific activity which is 2.0 x 10^6 units/mg.

    More Info

    • Introduction

      IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which contributes to various overlapping roles of this cytokine and IL13. STAT6, a signal transducer and activator of transcription plays a main role in mediating the immune regulatory signal of this cytokine. IL4, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are regulated co-ordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome.

    • Synonyms

      BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MHKCDITLQE IIKTLNILTA RKNSCMELPV TDVFAAPENT TEKETFCRAS TVLRHIYRHH TCMKSLLSGL DRNLSSMANM TCSVHEAKKS TLKDFLERLK TIMKEKYSKC.

    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.

    Il4 Porcine
  • View Data Sheet

    Name :

    CFP Human, Native

    Description:

    Complement Factor Properdin Human

    Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, Properdin.

    Product # :

    PRO-2702

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    Shipped with Ice Packs

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    • description
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    Description

    CFP Human produced in Human plasma having a molecular weight of 53kDa.

    Source

    Human Plasma.

    Formulation

    CFP solution contains PBS, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor Properdin (CFP) which is a plasma glycoprotein, is a positive regulator of the alternative complement pathway of the innate immune system. CFP binds and stabilizes the C3- and C5-convertase enzyme complexes in a feedback loop that eventually ends with formation of the membrane attack complex and lysis of the target cell. Mutations in CFP lead to 2 forms of properdin deficiency that cause high susceptibility to meningococcal infections.

    • Synonyms

      Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, Properdin.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

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

    • Human Virus Test

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

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

    Complement Factor Properdin
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