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Search results

1000 results found for “serpin”

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  • View Data Sheet

    Name :

    EMAP II Human

    Description:

    Endothelial-Monocyte Activating Polypeptide II Human Recombinant

    AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

    Product # :

    CYT-607

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    Description

    EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.

    Purity

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

    Biological Activity

    Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

    More Info

    • Introduction

      EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.

    • Synonyms

      AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

    • Background

      What is the molecular weight/Mw of EMAP II HUMAN Protein?
      EMAP II HUMAN Protein has a total Mw of 18.3kDa.

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

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

      What is the Biological Activity of EMAP II HUMAN Protein?
      Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

      What is the amino acid sequence of EMAP II HUMAN Protein?
      SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

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

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

    Emap Ii
  • View Data Sheet

    Name :

    CXCL5 Rat

    Description:

    Epithelial Neutrophil-Activating Protein 78 Rat Recombinant (CXCL5)

    C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

    Product # :

    CHM-267

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    Description

    Epithelial Neutrophil-Activating Protein 78 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids and having a molecular mass of 10.0kDa.The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, 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 peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.

    • Synonyms

      C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ENA-78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.

    • Background

      What is the molecular weight/Mw of CXCL5 RAT Protein?
      CXCL5 RAT Protein has a total Mw of 10.0kDa.

      What is the source or expression system of CXCL5 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 RAT Protein?
      CXCL5 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 RAT Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

      What is the amino acid sequence of CXCL5 RAT Protein?
      APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.

      What applications can CXCL5 RAT Protein be used in?
      CXCL5 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 RAT Protein?
      The endotoxin level is minimal, CXCL5 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.

    Ena 78 Rat
  • View Data Sheet

    Name :

    PA2G4 Human

    Description:

    Proliferation-associated protein 2G4 Human Recombinant

    Proliferation-associated protein 2G4, Cell cycle protein p38-2G4 homolog, hG4-1, ErbB3-binding protein 1, PA2G4, EBP1, p38-2G4.

    Product # :

    PRO-782

    Price :

    Quantity :

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    Description

    PA2G4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 402 amino acids (1-394 a.a.) and having a molecular mass of 44.8kDa. PA2G4 is fused to 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PA2G4 protein solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PA2G4 belongs to the peptidase M24C family and functions as an RNA-binding protein involved in cellular proliferation and differentiation processes. PA2G4 is a component of pre-ribosomal ribonucleoprotein complexes, participating in ribosome assembly and regulating the later steps of rRNA processing. Also, PA2G4 interacts with ErbB-3 and may function as a modulator of the ErbB-3 mediated signal transduction pathway by regulating the effects of Neuregulin-1. Furthermore, PA2G4 is a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. PA2G4 is implicated in growth inhibition and the induction of differentiation of human cancer cells. In addition, PA2G4 mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site). PA2G4 associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA.

    • Synonyms

      Proliferation-associated protein 2G4, Cell cycle protein p38-2G4 homolog, hG4-1, ErbB3-binding protein 1, PA2G4, EBP1, p38-2G4.

    • 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

      MSGEDEQQEQ TIAEDLVVTK YKMGGDIANR VLRSLVEASS SGVSVLSLCE KGDAMIMEET GKIFKKEKEM KKGIAFPTSI SVNNCVCHFS PLKSDQDYIL KEGDLVKIDL GVHVDGFIAN VAHTFVVDVA QGTQVTGRKA DVIKAAHLCA EAALRLVKPG NQNTQVTEAW NKVAHSFNCT PIEGMLSHQL KQHVIDGEKT IIQNPTDQQK KDHEKAEFEV HEVYAVDVLV SSGEGKAKDA GQRTTIYKRD PSKQYGLKMK TSRAFFSEVE RRFDAMPFTL RAFEDEKKAR MGVVECAKHE LLQPFNVLYE KEGEFVAQFK FTVLLMPNGP MRITSGPFEP DLYKSEMEVQ DAELKALLQS SASRKTQKKK KKKASKTAEN ATSGETLEEN EAGDLEHHHH HH.

    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.

    Pa2G4 Human
  • View Data Sheet

    Name :

    C4BPB Human

    Description:

    Complement Component 4 Binding Protein, Beta Human Recombinant

    C4b-binding protein beta chain, C4BPB, C4BP.

    Product # :

    PRO-1174

    Price :

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    Description

    C4BPB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (18-252 a.a) and having a molecular mass of 29kDa.C4BPB is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    C4BPB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol and 0.15M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Component 4 Binding Protein, Beta (C4BPB) belongs to a superfamily of proteins composed primarily of tandemly arrayed short consensus repeats of approximately 60 amino acids. C4BPB has a regulatory role in the coagulation system also, mediated via the beta-chain binding of protein S, a vitamin K-dependent protein which functions as a cofactor of activated protein C. A single, unique beta-chain of the C4BPB assembles with 7 identical alpha-chains into the principal isoform of C4BPB, which is a multimeric protein that controls activation of the complement cascade via the classical pathway. C4BPB binds as a cofactor to C3b/C4b inactivator (C3bINA), which subsequently hydrolyzes the complement fragment C4b. In addition, C4BPB accelerates the degradation of the C4bC2a complex (C3 convertase) by detaching the complement fragment C2a. Furthermore, C4BPB interacts with anticoagulant protein S and with serum amyloid P component.

    • Synonyms

      C4b-binding protein beta chain, C4BPB, C4BP.

    • 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 MGSHMSDAEH CPELPPVDNS IFVAKEVEGQ ILGTYVCIKG YHLVGKKTLF CNASKEWDNT TTECRLGHCP DPVLVNGEFS SSGPVNVSDK ITFMCNDHYI LKGSNRSQCL EDHTWAPPFP ICKSRDCDPP GNPVHGYFEG NNFTLGSTIS YYCEDRYYLV GVQEQQCVDG EWSSALPVCK LIQEAPKPEC EKALLAFQES KNLCEAMENF MQQLKESGMT MEELKYSLEL KKAELKAKLL.

    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.

    C4Bpb Human
  • View Data Sheet

    Name :

    FN3KRP Human

    Description:

    Fructosamine 3 Kinase Related Protein Human Recombinant

    Ketosamine-3-kinase, Fructosamine-3-kinase-related protein, FN3K-RP, FN3K-related protein, FN3KRP, FN3KL.

    Product # :

    PKA-051

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    Description

    FN3KRP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 332 amino acids (1-309 a.a) and having a molecular mass of 36.8kDa.FN3KRP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FN3KRP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ketosamine-3-kinase (FN3KRP) catalyzes the phosphorylation of psicosamines and ribulosamines compared to the adjacent gene which encodes a highly analogous enzyme, fructosamine-3-kinase that has different substrate specificity. The activity of both enzymes may cause deglycation of proteins to reinstate their function. A high concentration of glucose can result in non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). The proteins altered in this way, are less active or functional.

    • Synonyms

      Ketosamine-3-kinase, Fructosamine-3-kinase-related protein, FN3K-RP, FN3K-related protein, FN3KRP, FN3KL.

    • 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 MGSMEELLRR ELGCSSVRAT GHSGGGCISQ GRSYDTDQGR VFVKVNPKAE ARRMFEGEMA SLTAILKTNT VKVPKPIKVL DAPGGGSVLV MEHMDMRHLS SHAAKLGAQL ADLHLDNKKL GEMRLKEAGT VGRGGGQEER PFVARFGFDV VTCCGYLPQV
      NDWQEDWVVF YARQRIQPQM DMVEKESGDR EALQLWSALQ LKIPDLFRDL EIIPALLHGD LWGGNVAEDS SGPVIFDPAS FYGHSEYELA IAGMFGGFSS SFYSAYHGKI PKAPGFEKRL QLYQLFHYLN HWNHFGSGYR GSSLNIMRNL VK.

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    Fn3Krp Human
  • View Data Sheet

    Name :

    GAGA-POZ

    Description:

    GAGA-POZ Drosophila Melanogaster Recombinant

    Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.

    Product # :

    PRO-435

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    Description

    GAGA-POZ Drosophila Melanogaster Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids & having a molecular mass of 14 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein containing 10mM HEPES (pH-7.4) and 25mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      The GAGA factor is a sequence-specific DNA-binding protein, which participates in the regulation of the expression of a variety of different classes of genes in Drosophila such as many developmentally regulated genes, stress induced genes, and cell cycle regulated genes, as well as housekeeping genes. GAGA contains a C-terminal glutamine-rich domain and a highly conserved N-terminal POZ domain which reported to be involved in self-oligomerization in a number of other POZ domain containing proteins. In case of GAGA protein, the N-terminal POZ domain mediates the formation of oligomers both in vitro and in vivo.

    • Synonyms

      Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.

    • 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

      MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLLDLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQTVTKDDYTTH.

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    Gaga Factor
  • View Data Sheet

    Name :

    CEBP Gamma Human

    Description:

    CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human

    CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.

    Product # :

    PRO-434

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    Description

    CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.

    • Synonyms

      CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.

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    Cebpg Human
  • View Data Sheet

    Name :

    CNOT7 Mouse

    Description:

    CCR4-NOT Transcription Complex, Subunit 7 Mouse Recombinant

    CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.

    Product # :

    PRO-908

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    Description

    CNOT7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-248 a.a) and having a molecular mass of 31.1kDa.CNOT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNOT7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

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    • Introduction

      CCR4-Not transcription complex, subunit 7 (CNOT7) is a ubiquitous transcription factor. CNOT7 is a component of the CCR4 complex which functions as a general transcription regulation complex. Furthermore, CNOT7 binds to an anti-proliferative protein, BTG1 (B-cell translocation protein 1), which negatively regulates cell proliferation.

    • Synonyms

      CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.

    • 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 MGSMPAATVD HSQRICEVWA CNLDEEMKKI RQVIRKYNYV AMDTEFPGVV ARPIGEFRSN ADYQYQLLRC NVDLLKIIQL GLTFMNEQGE YPPGTSTWQF NFKFNLTEDM YAQDSIELLT TSGIQFKKHE EEGIETQYFA ELLMTSGVVL CEGVKWLSFH SGYDFGYLIK ILTNSNLPEE ELDFFEILRL FFPVIYDVKY LMKSCKNLKM FFEDHIDDAK YCGHLYGLGS GSSYVQNGTG NAYEEEASKQ S.

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    Cnot7 Mouse
  • View Data Sheet

    Name :

    CCL7 Rat

    Description:

    Monocyte Chemotactic Protein-3 Rat Recombinant (CCL7)

    C-C motif chemokine 7, Monocyte chemoattractant protein 3, Monocyte chemotactic protein 3, MCP-3, Small-inducible cytokine A7, Ccl7, Mcp3, Scya7.

    Product # :

    CHM-280

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    Description

    MCP-3 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8.5kDa.The MCP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MCP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM 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 peripheral blood monocytes using a concentration range of 50.0-300.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3 (MCP3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature protein, it is classified among the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, in a large cluster containing many other CC chemokines and is most closely related to CCL2(previously called MCP1).

    • Synonyms

      C-C motif chemokine 7, Monocyte chemoattractant protein 3, Monocyte chemotactic protein 3, MCP-3, Small-inducible cytokine A7, Ccl7, Mcp3, Scya7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP3 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 MCP-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPDGTNSSTC CYVKKQKIPK RNLKSYRKIT SSRCPWEAVI FKTKKGMEVC AEAHQKWVEE AIAYLDMKTS TPKP.

    • Background

      What is the molecular weight/Mw of CCL7 RAT Protein?
      CCL7 RAT Protein has a total Mw of 8.5kDa.

      What is the source or expression system of CCL7 RAT Protein?
      Escherichia Coli.

      What is the Purity of CCL7 RAT Protein?
      CCL7 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL7 RAT Protein?
      Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 50.0-300.0 ng/ml.

      What is the amino acid sequence of CCL7 RAT Protein?
      QPDGTNSSTC CYVKKQKIPK RNLKSYRKIT SSRCPWEAVI FKTKKGMEVC AEAHQKWVEE AIAYLDMKTS TPKP.

      What applications can CCL7 RAT Protein be used in?
      CCL7 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL7 RAT Protein?
      The endotoxin level is minimal, CCL7 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.

    Mcp 3 Rat
  • View Data Sheet

    Name :

    CRADD Human

    Description:

    Caspase and RIP Adapter with Death Domain Human Recombinant

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

    Product # :

    PRO-465

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Cradd Human
  • View Data Sheet

    Name :

    MEP1A Human

    Description:

    Meprin A Subunit Alpha Human Recombinant

    Meprin A Subunit Alpha, PABA Peptide Hydrolase, N-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit Alpha, Meprin A, Alpha (PABA Peptide Hydrolase), Endopeptidase-2, EC 3.4.24.18, PPH Alpha, BA268F1.1 (Meprin A Alpha (PABA Peptide Hydrolase)), EC 3.4.24, PPHA, MEP1A.

    Product # :

    PRO-2349

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    Description

    MEP1A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 589 amino acids (22-601 a.a.) and having a molecular mass of 67.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). MEP1A is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MEP1A protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Meprin A subunit alpha (MEP1A) is a single-pass type I membrane protein which is a member of the peptidase M12A family. MEP1A is abundantly expressed in the kidney and intestinal epithelial cells, is secreted into the urinary tract and intestinal lumen, and found in leukocytes and cancer cells under certain conditions. MEP1A is capable of proteolytically degrading extracellular matrix proteins, proteolytically processing bioactive proteins, and has a role in inflammatory processes.

    • Synonyms

      Meprin A Subunit Alpha, PABA Peptide Hydrolase, N-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit Alpha, Meprin A, Alpha (PABA Peptide Hydrolase), Endopeptidase-2, EC 3.4.24.18, PPH Alpha, BA268F1.1 (Meprin A Alpha (PABA Peptide Hydrolase)), EC 3.4.24, PPHA, MEP1A.

    • 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

      ADPVPIKYLP EENVHDADFG EQKDISEINL AAGLDLFQGD ILLQKSRNGL RDPNTRWTFP IPYILADNLG LNAKGAILYA FEMFRLKSCV DFKPYEGESS YIIFQQFDGC WSEVGDQHVG QNISIGQGCA YKAIIEHEIL HALGFYHEQS RTDRDDYVNI WWDQILSGYQ HNFDTYDDSL ITDLNTPYDY ESLMHYQPFS FNKNASVPTI TAKIPEFNSI IGQRLDFSAI DLERLNRMYN CTTTHTLLDH CTFEKANICG MIQGTRDDTD WAHQDSAQAG EVDHTLLGQC TGAGYFMQFS TSSGSAEEAA LLESRILYPK RKQQCLQFFY KMTGSPSDRL VVWVRRDDST GNVRKLVKVQ TFQGDDDHNW KIAHVVLKEE QKFRYLFQGT KGDPQNSTGG IYLDDITLTE TPCPTGVWTV RNFSQVLENT SKGDKLQSPR FYNSEGYGFG VTLYPNSRES SGYLRLAFHV CSGENDAILE WPVENRQVII TILDQEPDVR NRMSSSMVFT TSKSHTSPAI NDTVIWDRPS RVGTYHTDCN CFRSIDLGWS GFISHQMLKR RSFLKNDDLI IFVDFEDITH LSQHHHHHH.

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    MEP1A Human
  • View Data Sheet

    Name :

    CTSC Mouse

    Description:

    Cathepsin-C Mouse Recombinant

    DPPI, Cathepsin C, CTSC

    Product # :

    PRO-2769

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    Description

    CTSC Mouse Recombinant produced in HEK293 cells is a single, polypeptide chain containing 444 amino acids (25-462 a.a.) and having a molecular mass of 50.5kDa. CTSC is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    > 50,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyzes 1pmole of GlyArg-AMC / minute at pH 6.0 at 37C.

    More Info

    • Introduction

      CTSC has an important role in the activation of granule serine proteases in inflammatory cells.CTSC catalyses excision of dipeptides from the N-terminus of protein and peptide substrates. Once activated by CTSC, proteases are capable of degrading extracellular matrix components, which can result in tissue damage and chronic inflammation. CTSCcomprises of 4 subunits, each composed of the N-terminal proregion fragment, heavy chain and light chains. Defects in the CTSC protein have been demonstratedto result in Papillon-Lefevre disease which is an autosomal recessive disorder.

    • Synonyms

      DPPI, Cathepsin C, CTSC

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      DTPANCTYPD LLGTWVFQVG PRSSRSDINC SVMEATEEKV VVHLKKLDTA YDELGNSGHF TLIYNQGFEI VLNDYKWFAF FKYEVRGHTA ISYCHETMTG WVHDVLGRNW ACFVGKKVES HIEKVNMNAA HLGGLQERYS ERLYTHNHNF VKAINTVQKS WTATAYKEYE KMSLRDLIRR SGHSQRIPRP KPAPMTDEIQ QQILNLPESW DWRNVQGVNY VSPVRNQESC GSCYSFASMG MLEARIRILT NNSQTPILSP QEVVSCSPYA QGCDGGFPYL IAGKYAQDFG VVEESCFPYT AKDSPCKPRE NCLRYYSSDY YYVGGFYGGC NEALMKLELV KHGPMAVAFE VHDDFLHYHS GIYHHTGLSD PFNPFELTNH AVLLVGYGRD PVTGIEYWII KNSWGSNWGE SGYFRIRRGT DECAIESIAV AAIPIPKL-HHHHHH

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    Ctsc Mouse
  • View Data Sheet

    Name :

    SDHAF1 Human

    Description:

    Succinate Dehydrogenase Complex Assembly Factor 1 Human Recombinant

    Succinate Dehydrogenase Complex Assembly Factor 1, LYR Motif-Containing Protein 8, LYR Motif Containing 8, SDH Assembly Factor 1, LYRM8, Succinate Dehydrogenase Assembly Factor 1, Mitochondrial, Succinate dehydrogenase assembly factor 1, mitochondrial.

    Product # :

    PRO-2123

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    Description

    SDHAF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 15.2kDa. SDHAF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SDHAF1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Succinate dehydrogenase assembly factor 1 (SDHAF1) is a member of the complex I LYR family. SDHAF1 plays an important role in succinate dehydrogenase complex (SDH) assembly, a complex which is involved in complex II of the mitochondrial electron transport chain. SDHAF1 functions through taking part in mitochondrial biosynthesis of iron-sulfur centers for complex II.

    • Synonyms

      Succinate Dehydrogenase Complex Assembly Factor 1, LYR Motif-Containing Protein 8, LYR Motif Containing 8, SDH Assembly Factor 1, LYRM8, Succinate Dehydrogenase Assembly Factor 1, Mitochondrial, Succinate dehydrogenase assembly factor 1, 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 MGSMSRHSRL QRQVLSLYRD LLRAGRGKPG AEARVRAEFR QHAGLPRSDV LRIEYLYRRG RRQLQLLRSG HATAMGAFVR PRAPTGEPGG VGSQPDDGDS PRNPHDSTGA PETRPDGR.

    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.

    Sdhaf1 Human
  • View Data Sheet

    Name :

    TFPI2 Human

    Description:

    Tissue Factor Pathway Inhibitor 2 Human Recombinant

    Tissue Factor Pathway Inhibitor 2, Placental Protein 5, TFPI-2, PP5, Retinal Pigment Epithelium Cell Factor 1, REF1, TFPI2.

    Product # :

    PRO-860

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    Description

    TFPI2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 199 amino acids (23-213 a.a.) and having a molecular mass of 22.9kDa (Migrates at 18-40kDa on SDS-PAGE under reducing conditions).TFPI2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TFPI2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TFPI2 takes part in the regulation of plasmin-mediated matrix remodeling. Inhibits trypsin, plasmin, factor VIIa/tissue factor and weakly factor Xa. TFPI2 doesn’t have any influence on thrombin.

    • Synonyms

      Tissue Factor Pathway Inhibitor 2, Placental Protein 5, TFPI-2, PP5, Retinal Pigment Epithelium Cell Factor 1, REF1, TFPI2.

    • 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

      DAAQEPTGNN AEICLLPLDY GPCRALLLRY YYDRYTQSCR QFLYGGCEGN ANNFYTWEAC DDACWRIEKV PKVCRLQVSV DDQCEGSTEK YFFNLSSMTC EKFFSGGCHR NRIENRFPDE ATCMGFCAPK KIPSFCYSPK DEGLCSANVT RYYFNPRYRT CDAFTYTGCG GNDNNFVSRE DCKRACAKAL KLEHHHHHH.

    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.

    Tfpi2 Human
  • View Data Sheet

    Name :

    Fibronectin Recombinant

    Description:

    Fibronectin Human Recombinant

    Product # :

    PRO-2621

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    Description

    Fibronectin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 574 amino acids and having a molecular mass of 62.6kDa. The Fibronectin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, with 5 % Trehalose and 0.02 % Tween-20.

    Purity

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

    Biological Activity

    Was measured by its ability to support cell attachment and spreading when used as a substratum for cell culture. The recommended concentration in this application for this effect is typically 1-5 μg/cm2. Fibronectin can also be added to the media to support cell spreading at a concentration of 0.5-50 μg/ml. Optimal concentrations will need to be determined for individual user applications.

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    • Introduction

      Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Fibronectin Recombinant
  • View Data Sheet

    Name :

    POR (43-677) Human

    Description:

    P450 Oxidoreductase Human Recombinant

    P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.

    Product # :

    ENZ-1186

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    Description

    POR Human Recombinant produced in Sf9 Insect cells is a single, glycosylated, polypeptide chain (43-677 a.a) containing a total of 642 amino acids, having a molecular mass of 73.0 kDa. POR is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,500 pmol/min/mg. Defined by the amount of enzyme that  reduction of 1 pmole cytochrome-C by NADPH/min. at pH-8 25C.

    More Info

    • Synonyms

      P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.

    • 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

      MLFRKKKEEV PEFTKIQTLT SSVRESSFVE KMKKTGRNII VFYGSQTGTA EEFANRLSKD AHRYGMRGMS ADPEEYDLAD LSSLPEIDNA LVVFCMATYG EGDPTDNAQD FYDWLQETDV DLSGVKFAVF GLGNKTYEHF NAMGKYVDKR LEQLGAQRIF ELGLGDDDGN LEEDFITWRE QFWPAVCEHF GVEATGEESS IRQYELVVHT DIDAAKVYMG EMGRLKSYEN QKPPFDAKNP FLAAVTTNRK LNQGTERHLM HLELDISDSK IRYESGDHVA VYPANDSALV NQLGKILGAD LDVVMSLNNL DEESNKKHPF PCPTSYRTAL TYYLDITNPP RTNVLYELAQ YASEPSEQEL LRKMASSSGE GKELYLSWVV EARRHILAIL QDCPSLRPPI DHLCELLPRL QARYYSIASS SKVHPNSVHI CAVVVEYETK AGRINKGVAT NWLRAKEPAG ENGGRALVPM FVRKSQFRLP FKATTPVIMV GPGTGVAPFI GFIQERAWLR QQGKEVGETL LYYGCRRSDE DYLYREELAQ FHRDGALTQL NVAFSREQSH KVYVQHLLKQ DREHLWKLIE GGAHIYVCGD ARNMARDVQN TFYDIVAELG AMEHAQAVDY IKKLMTKGRY SLDVWSHHHH HH.

    • Background

      P450 Oxidoreductase (POR) is a vital enzyme that plays a crucial role in the electron transfer system, specifically in the cytochrome P450 (CYP) enzyme family. POR acts as an electron donor for various CYP enzymes involved in drug metabolism, steroid biosynthesis, and detoxification processes. This research aims to explore the function, regulation, and significance of POR protein in human cells, shedding light on its role in maintaining cellular homeostasis and drug metabolism.

      Function of POR Protein:

      POR protein serves as an essential component in the redox reactions of the CYP enzymes. It transfers electrons from NADPH to the CYP enzymes, allowing them to catalyze a wide range of reactions involved in the metabolism of endogenous compounds, drugs, and toxins. Through its electron transfer function, POR enables the activation or inactivation of substrates, contributing to the regulation of cellular processes such as hormone synthesis, drug clearance, and xenobiotic detoxification.

      Regulation of POR Protein:

      The expression and activity of POR protein are tightly regulated to ensure proper functioning of the CYP enzymes. Several factors influence POR expression, including genetic variations, environmental stimuli, and hormonal signals. Transcriptional regulation of POR involves binding of specific transcription factors to its promoter region. Additionally, post-translational modifications, such as phosphorylation and protein-protein interactions, modulate POR activity, influencing its electron transfer efficiency and interaction with CYP enzymes.

      Role of POR Protein in Drug Metabolism:

      One of the prominent functions of POR protein is its involvement in drug metabolism. POR collaborates with CYP enzymes in the biotransformation of a wide array of drugs, converting them into more soluble and easily excretable forms. The interplay between POR and CYP enzymes determines the pharmacokinetics and therapeutic efficacy of numerous drugs. Understanding the role of POR in drug metabolism is crucial for predicting drug-drug interactions, optimizing drug dosing, and minimizing the risk of adverse reactions.

      Significance of POR Protein in Disease States:

      Emerging evidence suggests that POR protein dysregulation can contribute to various disease states. Mutations in the POR gene have been linked to disorders such as Antley-Bixler syndrome and disordered steroidogenesis, highlighting the critical role of POR in development and endocrine function. Moreover, altered POR expression and activity have been implicated in drug resistance and toxicity, as well as in the pathogenesis of certain cancers.

      Conclusion:

      The investigation of P450 Oxidoreductase (POR) protein in human cells provides valuable insights into its function, regulation, and significance in various physiological and pathological processes. Understanding the interplay between POR and CYP enzymes is essential for deciphering drug metabolism pathways, predicting drug interactions, and developing personalized therapeutic strategies. Further research is warranted to unravel the intricate mechanisms governing POR activity and its potential as a therapeutic target.

    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.

    Por 43 677 Human
  • View Data Sheet

    Name :

    Leptin tA Human

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant

    Product # :

    CYT-352

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    Description

    Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin 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 Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, 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-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Ta Human
  • View Data Sheet

    Name :

    TXN Mouse

    Description:

    Thioredoxin Mouse Recombinant

    TRX1, TRX2, Thioredoxin-1, Thioredoxin I, TR-I, Thioredoxin-2, Thioredoxin-1, ADF, Surface associated sulphydryl protein, TXN protein, ATL derived factor, DKFZp686B1993, MGC61975, SASP, Thioredoxin, TRDX, TRX, TRX 1, TXN.

    Product # :

    PRO-2607

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    Description

    TXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-105 a.a.) and having a molecular mass of 14.1kDa. TXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >60 A650/cm/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.

    More Info

    • Introduction

      Thioredoxin or TRX contains a single disulfide active site and serves as a general protein disulphide oxidoreductase.Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that are found in all the kingdoms of living organisms. The proteinis involved in the first unique step in DNA synthesis; It interacts with a wide range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, along with the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant.

    • Synonyms

      TRX1, TRX2, Thioredoxin-1, Thioredoxin I, TR-I, Thioredoxin-2, Thioredoxin-1, ADF, Surface associated sulphydryl protein, TXN protein, ATL derived factor, DKFZp686B1993, MGC61975, SASP, Thioredoxin, TRDX, TRX, TRX 1, TXN.

    • 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 MGSMVKLIES KEAFQEALAA AGDKLVVVDF SATWCGPCKM IKPFFHSLCD KYSNVVFLEV DVDDCQDVAA DCEVKCMPTF QFYKKGQKVG EFSGANKEKL EASITEYA.

    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.

    Thioredoxin Mouse
  • View Data Sheet

    Name :

    Tamm Horsfall

    Description:

    Recombinant Human Tamm Horsfall Glycoprotein

    Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.


    Product # :

    ENZ-1206

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    • SDS-PAGE

    Description

    Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.

    Source

    HEK293

    Formulation

    The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE analysis.

    SDS-PAGE

    Tamm Horsfall-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
      Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
      Reduced Uromodulin levels is associated with chronic kidney disease.
      UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.

    • Synonyms

      Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH

    • Background

      Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

      What is the molecular weight/Mw of UMOD Protein?
      UMOD Protein has a total Mw of 65kDa.

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

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

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

      What is the amino acid sequence of UMOD Protein?
      UMOD Protein is composed from 595 amino acids.

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

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

    Tamm Horsfall
  • View Data Sheet

    Name :

    LRPAP1 Antibody

    Description:

    Low Density Lipoprotein Receptor-Related Protein Associated Protein 1, Mouse Anti Human

    Low density lipoprotein-related protein-associated protein 1 (alpha-2-macroglobulin receptor-associated protein 1), A2MRAP, HBP44, RAP, A2RAP, Alpha-2-MRAP, LRPAP1.

    Product # :

    ANT-547

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    • More Info

    Formulation

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

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    • Introduction

      LRPAP1 is a member of the alpha-2-MRAP family. LRPAP1 cooperates with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330. LRPAP1, located on the cell surface, creates a complex with the alpha 2 macroglobulin receptor light and heavy chains and has part in the pathogenesis of membrane glomerular nephritis.

    • Synonyms

      Low density lipoprotein-related protein-associated protein 1 (alpha-2-macroglobulin receptor-associated protein 1), A2MRAP, HBP44, RAP, A2RAP, Alpha-2-MRAP, LRPAP1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human LRPAP1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human LRPAP1 protein 35-357 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT8G8AT.

    • Applications

      LRPAP1 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:500.

    • 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

      LRPAP1 antibody was purified from mouse ascitic fluids by protein-A 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.

    Lrpap1 Antibody
  • View Data Sheet

    Name :

    MT II

    Description:

    Melanotan-II

    Melanotan-II, MT-II, Melanotan.

    Product # :

    HOR-289

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    Description

    The molecular formula of Melanotan-II is C50H69N15O9. It has the amino acid sequence of Ac-Nle-cyclo [Asp-His-D-Phe-Arg-Trp-Lys]-NH2 and a molecular weight of 1024.2 Dalton. The CAS Number is 121062-08-6.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 99% as determined by by RP-HPLC.

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    • Introduction

      Melanotan and Melanotan-II are both analogs of the peptide hormone alpha melanocyte stimulating hormone (a-MSH) that tend to induce skin tanning. Unlike Melanotan, Melanotan-II has the additional effect of increasing libido. Melanotan II has aphrodisiac properties.

    • Synonyms

      Melanotan-II, MT-II, Melanotan.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Melanotan Ii
  • View Data Sheet

    Name :

    Acrp30 Antibody

    Description:

    Adiponectin, Mouse Anti Human

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

    Product # :

    ANT-232

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    Formulation

    containing PBS, pH-7.4, & 0.1% Sodium Azide

    More Info

    • Introduction

      Human Adiponectin is a secreted protein expressed exclusively in differentiated adipocyte (adipokine). Adiponectin contains a modular structure comprising an N-terminal collagenous domain followed by a C-terminal globular domain. APM-1 plays a role in various physiological processes such as energy homeostasis and obesity. Plasma levels of adiponectin are reduced in obese humans, and decreased levels are associated with insulin resistance and hyperinsulinemia.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered solution.

    • Immunogen

      Anti-human adiponectin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human adiponectin amino acids 15-244 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      P1G12AT.

    • Applications

      Adiponectin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Recommended dilution range for Western blot analysis is 1:250 ~ 1:1,000. The antibody has the specificity against globular domain of adiponectin. Recommended starting dilution is 1:500.

    • 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

      Adiponectin 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.

    Acrp30 Antibody
  • View Data Sheet

    Name :

    Kisspeptin-10

    Description:

    Kisspeptin-10

    Product # :

    HOR-044

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • formulation
    • purity
    • More Info

    Description

    Kisspeptin-10 Synthetic is a single, non-glycosylated polypeptide chain containing 10 amino acids, having a molecular mass of 1302 Dalton and a Molecular formula of C63H83N17O14 .

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Kisspeptin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kisspeptin-10 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 Kisspeptin-10 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2.

    • Background

      Kisspeptin-10, a peptide derived from the Kisspeptin gene (KISS1), has emerged as a key player in the regulation of reproductive physiology. The peptide is known for its potent ability to stimulate the release of gonadotropin-releasing hormone (GnRH), a crucial factor in the control of the hypothalamic-pituitary-gonadal axis. The pivotal role of kisspeptin-10 in orchestrating the onset of puberty and the regulation of the menstrual cycle highlights its significance in reproductive health. This research aims to delve into the multifaceted functions of kisspeptin-10, shedding light on its physiological roles and potential applications in reproductive disorders.

      The primary objective of this study is to comprehensively explore the effects of kisspeptin-10 on the reproductive system. In vitro and in vivo assays will be conducted to investigate the impact of kisspeptin-10 on GnRH release and subsequent gonadotropin secretion. The interactions between kisspeptin-10 and its receptor, G protein-coupled receptor 54 (GPR54), will be explored using binding assays, potentially unraveling novel signaling pathways activated by this interaction.

      The second objective is to investigate the potential therapeutic applications of kisspeptin-10 in reproductive disorders. Clinical studies and animal models will be utilized to assess the efficacy of kisspeptin-10 in stimulating ovulation, particularly in cases of infertility caused by hypothalamic dysfunction. Furthermore, the potential of kisspeptin-10 in regulating conditions like polycystic ovary syndrome (PCOS) and hypogonadotropic hypogonadism will be explored.

      The third objective is to elucidate the molecular mechanisms underlying the actions of kisspeptin-10. Transcriptomic and proteomic analyses will be employed to identify genes and proteins regulated by kisspeptin-10 stimulation. This information could reveal novel downstream effectors of kisspeptin-10 signaling, contributing to a more comprehensive understanding of its role in reproductive physiology.

      By delving into the complexities of kisspeptin-10, this research aims to provide insights into its multifunctional roles in reproductive health and expand its potential therapeutic applications. The findings from this study may pave the way for the development of targeted interventions for reproductive disorders, potentially improving the quality of life for individuals affected by these conditions.

    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.

    Kisspeptin 10
  • View Data Sheet

    Name :

    Leptin Protein

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

    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

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile water or 0.4% NaHCO3 pH-8-9, 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-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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).

    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.

    Leptin Human
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