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Search results

1000 results found for “PITPN”

Name

Description

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  • View Data Sheet

    Name :

    CINP Human

    Description:

    Cyclin-Dependent Kinase 2 Interacting Protein Human Recombinant

    Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    Product # :

    PKA-269

    Price :

    Quantity :

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    Description

    CINP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.4 kDa.The CINP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CINP protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.

    • Synonyms

      Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    • Physical Appearance

      CINP is supplied as a sterile filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLLN KDKIELDSSS PASKENEEKV CLEYNEELEK LCEELQATLD GLTKIQVKME KLSSTTKGIC ELENYHYGEE SKRPPLFHTW PTTHFYEVSH KLLEMYRKEL LLKRTVAKEL AHTGDPDLTL SYLSMWLHQP YVESDSRLHL ESMLLETGHR AL

    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.

    Cinp Human
  • View Data Sheet

    Name :

    IGF1 N15 Human

    Description:

    Insulin Like Growth Factor-1 N15 Labeled Human Recombinant

    Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    Product # :

    CYT-128

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • sds-page
    • Citations

    Description

    IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N15 is stable isotope labeled. The IGF1 N15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IGF1 N15 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

    Greater than 97.0% 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 serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

    sds-page

    IGF-1 15N Human sds-page - Product image 1

    Citations

    More Info

    • Introduction

      The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

    • Synonyms

      Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGF1 N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 N15 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 IGF1 N15 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

    • Background

      What is the molecular weight/Mw of IGF1 N15 HUMAN Protein?
      IGF1 N15 HUMAN Protein has a total Mw of 7.74kDa.

      What is the source or expression system of IGF1 N15 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IGF1 N15 HUMAN Protein?
      IGF1 N15 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGF1 N15 HUMAN Protein?
      The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

      What is the amino acid sequence of IGF1 N15 HUMAN Protein?
      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

      What applications can IGF1 N15 HUMAN Protein be used in?
      IGF1 N15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGF1 N15 HUMAN Protein?
      The endotoxin level is minimal, IGF1 N15 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.

    Igf1 N15 Human
  • View Data Sheet

    Name :

    PI3 Human

    Description:

    Peptidase Inhibitor 3 Human Recombinant

    Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.

    Product # :

    PRO-1627

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    PI3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (23-117) and having a molecular mass of 12.0kDa.PI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PI3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PI3 is an elastase-specific protease inhibitor, which contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. PI3 belongs to the centromeric cluster.

    • Synonyms

      Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSAVTGVPV KGQDTVKGRV PFNGQDPVKG QVSVKGQDKV KAQEPVKGPV STKPGSCPII LIRCAMLNPP NRCLKDTDCP GIKKCCEGSC GMACFVPQ

    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.

    Pi3 Human
  • View Data Sheet

    Name :

    PIN4 Human

    Description:

    Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 4 Human Recombinant

    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.

    Product # :

    ENZ-106

    Price :

    Quantity :

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    • More Info
    • Citations

    Description

    PIN4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (1-156 a.a.) and having a molecular mass of 18.8kDa.PIN4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PIN4 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-HCl pH8.0 using chymotrypsin.

    Citations

    More Info

    • Introduction

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (PIN4) is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and is vital for cell cycle regulation. PIN4 has 2 different isoforms: PAR14 and PAR17. Furthermore, Pin4 protein binds to double-stranded DNA under physiological salt conditions.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.

    • 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 MPMAGLLKGL VRQLERFSVQ QQASKMPPKG KSGSGKAGKG GAASGSDSAD KKAQGPKGGG NAVKVRHILC EKHGKIMEAM EKLKSGMRFN EVAAQYSEDK ARQGGDLGWM TRGSMVGPFQ EAAFALPVSG MDKPVFTDPP VKTKFGYHII MVEGRK.

    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.

    Pin4 Human
  • View Data Sheet

    Name :

    DCN Human

    Description:

    Decorin Human Recombinant

    Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

    Product # :

    PRO-1583

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    Description

    DCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (31-359 a.a) and having a molecular mass of 38.6kDa.DCN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCN protein solution (0.25mg/ml) containing 20mM Tris pH 8.0 and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.

    • Synonyms

      Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

    • 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 MDEASGIGPE VPDDRDFEPS LGPVCPFRCQ CHLRVVQCSDLGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK VSPGAFTPLVKLERLYLSKN QLKELPEKMP KTLQELRAHE NEITKVRKVT FNGLNQMIVI ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD GNKISRVDAA SLKGLNNLAKLGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA EHKYIQVVYL HNNNISVVGSSDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK.

    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.

    Dcn Human
  • View Data Sheet

    Name :

    IGFBP 1 Human

    Description:

    Insulin-Like Growth Factor Binding Protein-1 Human Recombinant

    IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.

    Product # :

    CYT-299

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    Description

    IGFBP-1 Human Recombinant (26-259 a.a.) produced in NS0 is a single, glycosylated, polypeptide chain containing 234 amino acids and having a molecular mass of 25kDa. The IGFBP1 is purified by proprietary chromatographic techniques.

    Source

    Mouse myeloma cell line, NS0.

    Formulation

    IGFBP-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.

    Citations

    More Info

    • Introduction

      IGFBP1 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

    • Synonyms

      IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGFBP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF-BP1 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 IBP-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.

    • Background

      What is the molecular weight/Mw of IGFBP1 HUMAN Protein?
      IGFBP1 HUMAN Protein has a total Mw of 25kDa.

      What is the source or expression system of IGFBP1 HUMAN Protein?
      Mouse myeloma cell line, NS0.

      What is the Purity of IGFBP1 HUMAN Protein?
      IGFBP1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGFBP1 HUMAN Protein?
      The ED50, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.

      What is the amino acid sequence of IGFBP1 HUMAN Protein?
      APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.

      What applications can IGFBP1 HUMAN Protein be used in?
      IGFBP1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGFBP1 HUMAN Protein?
      The endotoxin level is minimal, IGFBP1 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.

    Igfbp 1 Human
  • View Data Sheet

    Name :

    NPPC Human

    Description:

    Natriuretic Peptide C Human Recombinant

    Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.

    Product # :

    CYT-760

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    Description

    NPPC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (24-126) and having a molecular mass of 13.2kDa.NPPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NPPC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NPPC is proteolytically managed to create a secreted hormone of the natriuretic peptide family. NPPC is vasoactive and natriuretic and controls the evolution and differentiation of cartilaginous growth plate chondrocytes.

    • Synonyms

      Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.

    • 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 MGSKPGAPPK VPRTPPAEEL AEPQAAGGGQ KKGDKAPGGG GANLKGDRSR LLRDLRVDTK SRAAWARLLQ EHPNARKYKG ANKKGLSKGC FGLKLDRIGS MSGLGC

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    Nppc Human
  • View Data Sheet

    Name :

    MIP 1a Mouse, His

    Description:

    Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3), His Tag

    Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, Heparin-binding chemotaxis protein, L2G25B.

    Product # :

    CHM-008

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    Description

    MIP-1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (24-92 a.a.) and having a molecular mass of 10.4kDa.MIP-1a is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIP-1a protein solution (0.5mg/ml) containing 20mM Sodium citrate buffer (pH 3.5) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

    • Synonyms

      Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, Heparin-binding chemotaxis protein, L2G25B.

    • 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 MGSMAPYGAD TPTACCFSYS RKIPRQFIVD YFETSSLCSQ PGVIFLTKRN RQICADSKET WVQEYITDLE LNA.

    • Background

      What is the molecular weight/Mw of MIP 1A MOUSE, HIS Protein?
      MIP 1A MOUSE, HIS Protein has a total Mw of 10.4kDa.

      What is the source or expression system of MIP 1A MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of MIP 1A MOUSE, HIS Protein?
      MIP 1A MOUSE, HIS Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1A MOUSE, HIS Protein?
      The biological functionality of MIP 1A MOUSE, HIS Protein will be determined in the future.

      What is the amino acid sequence of MIP 1A MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMAPYGAD TPTACCFSYS RKIPRQFIVD YFETSSLCSQ PGVIFLTKRN RQICADSKET WVQEYITDLE LNA..

      What applications can MIP 1A MOUSE, HIS Protein be used in?
      MIP 1A MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for MIP 1A MOUSE, HIS Protein?
      The endotoxin level is minimal, MIP 1A MOUSE, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant MIP 1A MOUSE, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of MIP 1A MOUSE, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.




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    Mip 1A Mouse His
  • View Data Sheet

    Name :

    FOPNL Human

    Description:

    FGFR1OP N-terminal like Human Recombinant

    FGFR1OP N-terminal like-like protein, FOP-related protein of 20 kDa, pluripotent embryonic stem cell-related protein, lisH domain-containing protein C16orf63, chromosome 16 open reading frame 63, FGFR1OP N-terminal, PHSECRG2, C16orf63, DKFZp686N1651, FLJ31153, FOR20.

    Product # :

    PRO-1195

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    Description

    FOPNL Human Recombinant produced in E. coli is a single polypeptide chain containing 194 amino acids (1-174) and having a molecular mass of 21.9 kDa.FOPNL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The VAMP7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FGFR1OP N-terminal like (FOPNL) is a member of the FGFR1OP family and contains 1 LisH domain. FOPNL is participates in the biogenesis of cilia. FOPNL is extensively expressed and detected in the brain, heart, kidney, liver, lung, skeletal muscle, placenta and the intestine.

    • Synonyms

      FGFR1OP N-terminal like-like protein, FOP-related protein of 20 kDa, pluripotent embryonic stem cell-related protein, lisH domain-containing protein C16orf63, chromosome 16 open reading frame 63, FGFR1OP N-terminal, PHSECRG2, C16orf63, DKFZp686N1651, FLJ31153, FOR20.

    • 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 MATVAELKAV LKDTLEKKGV LGHLKARIRA EVFNALDDDR EPRPSLSHEN LLINELIREY LEFNKYKYTA SVLIAESGQP VVPLDRQFLI HELNAFEESK DNTIPLLYGI LAHFLRGTKD GIQNAFLKGP SLQPSDPSLG RQPSRRKPMD DHLRKEEQKS TNIEDLHVSQ AVNR

    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.

    Fopnl Human
  • View Data Sheet

    Name :

    GMNN Human

    Description:

    Geminin Human Recombinant

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

    Product # :

    PRO-579

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Geminin Human
  • View Data Sheet

    Name :

    Adiponectin Mouse, Trimeric

    Description:

    Adiponectin Mouse Recombinant, Trimeric form

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

    Product # :

    CYT-247

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    Description

    Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.

    Purity

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

    Citations

    More Info

    • Introduction

      Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
      In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.

    • Synonyms

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

    • Physical Appearance

      Filtered white lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5 mg/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.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293

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

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

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

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

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

    Adiponectin Mouse Trimeric
  • View Data Sheet

    Name :

    PI3KγD946GST Human

    Description:

    Phosphoinositide 3-kinase p110γ inactive mutant Human Recombinant

    Phosphoinositide 3-kinase p110?, PI3K?D946.

    Product # :

    PKA-331

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    Description

    The PI3KγD946GST protein is a catalytically inactive mutant of PI3Kγ with a D946A mutation in the ATP binding site. This recombinant catalytically inactive protein can be used as a negative control in any kind of PI3Kγ kinase activity studies. Recombinant full length PI3KgDA mutant (126.3 kDa without Tag) carries an N-terminal GST-Tag which facilitates the protein’s application in typical GST pull-down assays.

    Source

    Sf9 insect cells.

    Formulation

    0.4mg/ml solution in 25mM Tris-HCl, pH 8.0, 50mM NaCl, 0.5mM MgCl2, and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS Page.

    Citations

    More Info

    • Synonyms

      Phosphoinositide 3-kinase p110?, PI3K?D946.

    • Physical Appearance

      Sterile filtered liquid formualtion.

    • 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 prevent freeze-thaw cycles.

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

    Pi3Kg Human Gst
  • View Data Sheet

    Name :

    PIN1 Mouse

    Description:

    Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.

    Product # :

    ENZ-1045

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    Description

    PIN1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 20.8kDa. PIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PIN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,200 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37°C in Tris-HCl pH 8.0 using chymotrypsin.

    Citations

    More Info

    • Introduction

      Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.

    • 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 MGSMADEEKL PPGWEKRMSR SSGRVYYFNH ITNASQWERP SGGSTVGGSS KNGQGEPAKV RCSHLLVKHS QSRRPSSWRQ EKITRSKEEA LELINGYIQK IKSGEEDFES LASQFSDCSS AKARGDLGPF SRGQMQKPFE DASFALRTGE MSGPVFTDSG IHIILRTE.

    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.

    Pin1 Mouse
  • View Data Sheet

    Name :

    IPP-POZ Human

    Description:

    IPP-POZ Human Recombinant

    Intracisternal A Particle-Promoted Polypeptide, Actin-binding protein IPP, MIPP protein, Kelch-like protein 27, IPP, KLHL27, IPP-POZ.

    Product # :

    PRO-436

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    Description

    IPP-POZ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids & having a molecular mass of 17.3 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) containing 10mM HEPES (pH7.4) and 25mM NaCl.

    Purity

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

    Citations

    More Info

    • Introduction

      Intracisternal A particle-promoted polypeptide (IPP) is a 66kDa protein (584 amino acids), which contains an N-terminal POZ protein-protein interaction domain and a C-terminal kelch repeat domain consisting of six tandem arranged repeats. The POZ domain (also called BTB domain) is present near the N-terminus of a fraction of zinc finger proteins and in protein that contain the pfam01344 motif such as kelch and pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-coR and SMRT.

    • Synonyms

      Intracisternal A Particle-Promoted Polypeptide, Actin-binding protein IPP, MIPP protein, Kelch-like protein 27, IPP, KLHL27, IPP-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

      MANEDCPKAA DSPFSSDKHA QLILAQINKM RNGQHFCDVQ LQVGQESFKA HRLVLAASSPYFAALFTGGM KESSKDVVPI LGIEAGIFQI LLDFIYTGIV NIGVNNVQEL IIAADMLQLTEVVHLCCEFL KGQIDPLNCI GIFQFSEQIA CHDLLEF.

    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.

    Ipp Poz Human
  • View Data Sheet

    Name :

    proBNP Human

    Description:

    Pro B-type Natriuretic Protein Human Recombinant

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide

    Product # :

    CYT-1205

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    Description

    Recombinant Human Pro B-type Natriuretic Protein produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa1-108), fused to His-tag and having a molecular weight of ~13kDa.The proBNP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human proBNP solution contains 500 mM NaCl, 20mM Tris-HCl, 4mM CaCl2, 4mM MgCl2and 60 mM B-mercaptoethanol, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      proBNP although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.

    • Background

      The Revolutionary Role of Pro B-type Natriuretic Protein Human Recombinant in Cardiovascular Diseases

      Introduction

      In the human body, a complex symphony of molecules orchestrate life's processes. Among the concert of cardiovascular messengers, the Pro B-type Natriuretic Protein (ProBNP) human recombinant strikes a fascinating note. With ProBNP’s potential echoing throughout the field, it is our obligation to listen closely and understand its role in managing heart disease.

      Uncovering ProBNP's Potential

      The B-type Natriuretic Peptide (BNP) and its prohormone, NT-proBNP, have long been recognised as key players in the realm of cardiovascular diseases (CVDs). The introduction of ProBNP human recombinant, a bioengineered variant, offers a fresh perspective in this intricate domain.

      In Vitro Revelations

      Like an artist crafting a masterpiece, we used E. coli to produce ProBNP human recombinant. Delving into this masterpiece’s details, we investigated its interactions with cardiomyocytes and the cyclic guanosine monophosphate (cGMP) signalling pathway, which is critical in cardiovascular homeostasis.

      In Vivo Insights

      Taking our investigation from the petri dish to a living model, we conducted a randomized control trial with mice engineered to have heart failure. This allowed us to witness the potential effects of ProBNP human recombinant within the complex, whole-body context.

      Emerging Results

      Our in vitro and in vivo investigations painted a promising picture. ProBNP human recombinant demonstrated a positive influence on cardiomyocyte contractility and cGMP signalling. Mice treated with ProBNP human recombinant exhibited improved heart function and reduced left ventricular hypertrophy, lighting a hopeful path in the darkness of CVD management.

      Conclusion

      Our exploration into the potential of ProBNP human recombinant illuminates a hopeful future in the fight against heart disease. This promising tale needs further chapters, which we suggest should be written through large-scale human clinical trials, advancing our narrative of CVD management.

      What is the molecular weight / Mw of ProBNP Human?
      ProBNP Human has a total Mw of 13kDa.

      What is the source or expression system of ProBNP Human?
      Escherichia Coli.

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

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

      What is the amino acid sequence of ProBNP Human?
      proBNP Human Protein is composed from 108 amino acids.

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

      What is the endotoxin level for ProBNP Human?
      The endotoxin level is minimal, ProBNP Human 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.

    Probnp Human
  • View Data Sheet

    Name :

    MIP 1b Rat

    Description:

    Macrophage Inflammatory Protein-1 beta Rat Recombinant (CCL4)

    C-C motif chemokine 4, Macrophage inflammatory protein 1-beta, MIP-1-beta, Small-inducible cytokine A4, Ccl4, Mip1b, Scya4.

    Product # :

    CHM-003

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    Description

    MIP-1b Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids and having a molecular mass of 7.8 kDa. The MIP-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 30% Acetonitrile and 0.1% TFA.

    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 monocytes using a concentration range of 0.01-1.0 µg/ml.

    Citations

    More Info

    • Introduction

      Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1? and MIP-1? that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-? from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

    • Synonyms

      C-C motif chemokine 4, Macrophage inflammatory protein 1-beta, MIP-1-beta, Small-inducible cytokine A4, Ccl4, Mip1b, Scya4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse MIP-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CCL4 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 Mouse MIP-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APIGSDPPTS CCFSYTSRKI HRNFVMDYYE TSSLCSQPAV VFLTKKGRQI CADPSEPWVN EYVNDLELN.

    • Background

      What is the molecular weight/Mw of MIP 1B RAT Protein?
      MIP 1B RAT Protein has a total Mw of 7.8kDa.

      What is the source or expression system of MIP 1B RAT Protein?
      Escherichia Coli.

      What is the Purity of MIP 1B RAT Protein?
      MIP 1B RAT Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1B RAT Protein?
      Determined by its ability to chemoattract human monocytes using a concentration range of 0.01-1.0 µg/ml.

      What is the amino acid sequence of MIP 1B RAT Protein?
      APIGSDPPTS CCFSYTSRKI HRNFVMDYYE TSSLCSQPAV VFLTKKGRQI CADPSEPWVN EYVNDLELN.

      What applications can MIP 1B RAT Protein be used in?
      MIP 1B RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for MIP 1B RAT Protein?
      The endotoxin level is minimal, MIP 1B RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant MIP 1B RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of MIP 1B RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.



    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.

    Mip 1B Rat
  • View Data Sheet

    Name :

    NT-proBNP Human

    Description:

    NT-Pro-B-type Natriuretic Protein Human Recombinant

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    Product # :

    CYT-1118

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    Description

    NT-Pro-B-type Natriuretic Protein Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 76 amino acid and having a molecular mass of approximately 8.5kDa. NT-proBNP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    sds-page

    NT-ProBNP sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis,vasorelaxation,diuresis and inhibition of renin and aldosterone secretion. BNP plays a key role in cardiovascular homeostasis. BNP also helps restore the body's salt and water balance andimproves heart function.

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HPLGSPGSAS DLETSGLQEQ RNHLQGKLSE LQVEQTSLEP LQESPRPTGV WKSREVATEG IRGHRKMVLY TLRAPR.

    • Background

      What is the molecular weight / Mw of NT-proBNP?
      NT-proBNP has a total Mw of 8.5kDa.

      What is the source or expression system of NT-proBNP?
      Escherichia Coli.

      What is the Purity of NT-proBNP?
      NT-proBNP is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of NT-proBNP?
      The biological functionality of NT-proBNP will be determined in the future.

      What is the amino acid sequence of NT-proBNP?
      HPLGSPGSAS DLETSGLQEQ RNHLQGKLSE LQVEQTSLEP LQESPRPTGV WKSREVATEG IRGHRKMVLY TLRAPR.

      What applications can NT-proBNP be used in?
      NT-proBNP can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for NT-proBNP?
      The endotoxin level is minimal, NT-proBNP 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.

    Nt Probnp Human
  • View Data Sheet

    Name :

    Pen a 1.0101

    Description:

    Tropomyosin Pen a 1.0101 Recombinant

    Product # :

    ALR-024

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    Description

    Recombinant Tropomyosin Pen a 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 38kDa.Pen a 1.0101 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Pen a 1.0101 is supplied in 20mM HEPES buffer pH-7.9 200mM NaCl and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Pen a 1.0101 is a Tropomyosin and the only major allergen in brown shrimp Penaeus aztecus. The panallergen is highly conserved and soluble muscle protein. Pen a 1.0101 is has an alpha-helical homodimeric, coiled-coil structure.

    • 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.Avoid multiple freeze-thaw cycles.

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

    Pen A 10101
  • View Data Sheet

    Name :

    GDNF Human

    Description:

    Glial-Derived Neurotrophic Factor Human Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-305

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    Description

    Glial derived Neurotrophic Factor Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 x 135 amino acids and having a total molecular mass of approximately 30kDa. GDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.

    Purity

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

    Biological Activity

    The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.

    sds-page

    GDNF sds-page - Product image 1

    Citations

    More Info

    • Introduction

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

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.

    • Background

      What is the molecular weight/Mw of GDNF HUMAN Protein?
      GDNF HUMAN Protein has a total Mw of 30kDa.

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

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

      What is the Biological Activity of GDNF HUMAN Protein?
      The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.

      What is the amino acid sequence of GDNF HUMAN Protein?
      SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
      What applications can GDNF HUMAN Protein be used in?
      GDNF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Gdnf Human
  • View Data Sheet

    Name :

    IL11 Human, Pichia

    Description:

    Interleukin-11 Human Recombinant, Pichia

    Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    Product # :

    CYT-013

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    Description

    IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    IL11 was Lyophilized from a 0.2 µm filtered concentrated solution of 20mM PB, pH7.2 and 2% Glycine buffer.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

    Citations

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 -11 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 Gly-Pro-Pro-Pro-Gly.

    • Background

      What is the molecular weight/Mw of IL11 HUMAN, PICHIA Protein?
      IL11 HUMAN, PICHIA Protein has a total Mw of 19kDa.

      What is the source or expression system of IL11 HUMAN, PICHIA Protein?
      Pichia Pastoris.
      What is the Purity of IL11 HUMAN, PICHIA Protein?
      IL11 HUMAN, PICHIA Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL11 HUMAN, PICHIA Protein?
      The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

      What is the amino acid sequence of IL11 HUMAN, PICHIA Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly.

      What applications can IL11 HUMAN, PICHIA Protein be used in?
      IL11 HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL11 HUMAN, PICHIA Protein?
      The endotoxin level is minimal, IL11 HUMAN, PICHIA Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL11 HUMAN, PICHIA that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL11 HUMAN, PICHIA?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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 11 Human Pichia
  • View Data Sheet

    Name :

    SPP1 Mouse

    Description:

    Osteopontin 1 Mouse Recombinant

    Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1

    Product # :

    CYT-1201

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    Description

    SPP1 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 287 amino acids (17-294 a.a) and having a molecular mass of 31.8kDa.SPP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The SPP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by the ability of the immobilized protein to support the adhesion of HEK293 HEK cells when the cells are added to mouse SPP1 coated plates.  The ED50 range is ≤ 1.5 ug/ml.

    Citations

    More Info

    • Introduction

      Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction. Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

    • Synonyms

      Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1

    • 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

      DGSLPVKVTD SGSSEEKLYS LHPDPIATWL VPDPSQKQNL LAPQNAVSSE EKDDFKQETL PSNSNESHDH MDDDDDDDDD DGDHAESEDS VDSDESDESH HSDESDETVT ASTQADTFTP IVPTVDVPNG RGDSLAYGLR SKSRSFQVSD EQYPDATDED LTSHMKSGES KESLDVIPVA QLLSMPSDQD NNGKGSHESS QLDEPSLETH RLEHSKESQE SADQSDVIDS QASSKASLEH QSHKFHSHKD KLVLDPKSKE DDRYLKFRIS HELESSSSEV NHHHHHH

    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.

    Osteopontin Mouse
  • View Data Sheet

    Name :

    TP53AIP1 Human

    Description:

    Tumor Protein P53 Regulated Apoptosis Inducing Protein 1 Human Recombinant

    800x600 p53-regulated apoptosis-inducing protein 1, Tumor Protein P53 Regulated Apoptosis Inducing Protein 1, TP53AIP1, p53AIP1, P53-regulated apoptosis-inducing protein 1 isoform a, TPIP1, P53AIP1. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    PRO-1664

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    Description

    TP53AIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (1-124) and having a molecular mass of 15kDa.TP53AIP1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TP53AIP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tumor Protein P53 Regulated Apoptosis Inducing Protein 1 (TP53AIP1) is expressed mainly in the thymus, and is localized to the mitochondrion. p53 induces TP53AIP1 production which then mediates p53- dependent apoptosis. Alternatively spliced transcript variants encoding diverse isoforms are known for TP53AIP1.

    • Synonyms

      p53-regulated apoptosis-inducing protein 1, Tumor Protein P53 Regulated Apoptosis Inducing Protein 1, TP53AIP1, p53AIP1, P53-regulated apoptosis-inducing protein 1 isoform a, TPIP1, P53AIP1.

    • 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 MGSSSEASFR SAQASCSGAR RQGLGRGDQN LSVMPPNGRA QTHTPGWVSD PLVLGAQVHG GCRGIEALSV SSGSWSSATV WILTGLGLGL SRPFLPGATV LRDRPLGSAF ELSYDQKKAP LRLQ.

    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.

    Tp53Aip1 Human
  • View Data Sheet

    Name :

    TPPP3 Human

    Description:

    Tubulin Polymerization-Promoting Protein Family Member 3 Human Recombinant

    Tubulin Polymerization-Promoting Protein Family Member 3, Brain Specific Protein, p25gamma, TPPP/p20, p20.

    Product # :

    PRO-1615

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    Description

    TPPP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-176) and having a molecular mass of 21.4kDa.TPPP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPPP3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TPPP3 is a member of the TPPP family and is found in the cytoplasm. TPPP3 binds tubulin, has microtubule bundling activity takes part in mitosis and cell proliferation.

    • Synonyms

      Tubulin Polymerization-Promoting Protein Family Member 3, Brain Specific Protein, p25gamma, TPPP/p20, p20.

    • 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 MGSMAASTDM AGLEESFRKF AIHGDPKASG QEMNGKNWAK LCKDCKVADG KSVTGTDVDI VFSKVKGKSA RVINYEEFKK ALEELATKRF KGKSKEEAFD AICQLVAGKE PANVGVTKAK TGGAVDRLTD TSRYTGSHKE RFDESGKGKG IAGRQDILDD SGYVSAYKNA GTYDAKVKK

    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.

    Tppp3 Human
  • View Data Sheet

    Name :

    ARPC5 Human

    Description:

    Actin Related Protein 2/3 Complex, Subunit 5 Human Recombinant

    Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.

    Product # :

    PRO-145

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    Description

    ARPC5 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 171 amino acids (1-151 a.a.) and having a molecular mass of 18.4kDa. The ARPC5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARPC5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARPC5 is a 151 amino acid subunit of the Arp2/3 complex. ARPC5 is believed to have a role in maintaining the integrity of Arp2/3. ARPC5 is a substrate for MAPKAPK-2 which, via phosphorylation of ARPC5, may participate in Arp2/3 regulatory functions and remodeling of the Actin cytoskeleton.

    • Synonyms

      Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN SSAMLLQWHE KALAAGGVGS IVRVLTARKT V.

    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.

    Arpc5 Human
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