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Search results

1000 results found for “hemopexin”

Name

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  • View Data Sheet

    Name :

    PTMS Human

    Description:

    Prothymosin Human Recombinant

    ParaT, parathymosin.

    Product # :

    PRO-1735

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    Description

    PTMS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-102aa) and having a molecular mass of 13.9kDa.PTMS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTMS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Parathymosin, also known as PTMS is a member of the pro/parathymosin family. PTMS may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to particular opportunistic infections. Among the diseases associated with PTMS are hepatitis b, and alzheimer's disease.

    • Synonyms

      ParaT, parathymosin.

    • 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 MGSMSEKSVE AAAELSAKDL KEKKEKVEEK ASRKERKKEV VEEEENGAEE EEEETAEDGE EEDEGEEEDE EEEEEDDEGP ALKRAAEEED EADPKRQKTE NGASA

    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.

    Ptms Human
  • View Data Sheet

    Name :

    Adiponectin Protein

    Description:

    Adiponectin Human Recombinant

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

    Product # :

    CYT-280

    Price :

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    • sds-page

    Description

    The Adiponectin Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 25.1 kDa and containing 231 amino acids (15-244).

    Source

    Escherichia Coli.

    Formulation

    Acrp30 protein solution contains Phosphate buffered saline pH 7.4 and 1mM DTT.

    Purity

    Acrp30 purity is greater than 90% as determined by SDS-PAGE.

    sds-page

    Adiponectin-sds-page - Product image 1

    More Info

    • Introduction

      The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
      Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
      The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
      Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

    • Synonyms

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

    • 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

      MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
      KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
      GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
      VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
      RNGLYADNDNDSTFTGFLLYHDTN.

    • Background

      Adiponectin Human Recombinant: Unraveling its Potential in Therapeutic Applications

      1. Abstract

      This paper aims to deliver an extensive exploration into Adiponectin Human Recombinant, a vital adipokine implicated in a multitude of metabolic processes. By delving into the structure, biological roles, and signaling pathways of adiponectin, we elucidate its contribution to pathophysiological conditions. Moreover, we examine the potential therapeutic application of adiponectin in metabolic and cardiovascular diseases.

      2. Introduction

      Adiponectin, a protein predominantly secreted by adipose tissue, plays an integral part in regulating metabolic processes such as glucose regulation and fatty acid oxidation. Understanding the intricacies of adiponectin's actions could pave the way for innovative therapeutic interventions in diseases like obesity, diabetes, and cardiovascular disease.

      3. Structure and Signaling of Adiponectin

      Adiponectin is a 30kDa protein consisting of a collagen-like domain and a C-terminal globular domain. It signals through adiponectin receptors AdipoR1 and AdipoR2, which then activate several intracellular signaling pathways, including AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-alpha (PPAR-α), regulating various metabolic processes.

      4. Biological Functions of Adiponectin

      Adiponectin has been shown to enhance insulin sensitivity, stimulate fatty acid oxidation, and exert anti-inflammatory effects. Additionally, it is involved in regulating energy homeostasis and has been linked to the regulation of food intake and body weight.

      5. Adiponectin in Disease Pathology

      Reduced levels of adiponectin have been associated with obesity, insulin resistance, type 2 diabetes, and cardiovascular disease. Moreover, adiponectin deficiency has been observed in metabolic syndrome, emphasizing the adipokine's crucial role in metabolic health.

      6. Therapeutic Potential of Adiponectin

      Given adiponectin's role in metabolic regulation, its potential as a therapeutic target is of considerable interest. Approaches to increase circulating adiponectin levels or enhance adiponectin signaling could offer potential therapeutic strategies for managing metabolic diseases and cardiovascular conditions.

      7. Conclusion and Future Perspectives

      While our understanding of adiponectin and its role in health and disease has greatly advanced in recent years, there is still much to uncover. Further research on the precise molecular mechanisms of adiponectin could pave the way for novel therapeutic approaches.

      What is the molecular weight / Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 25.1kDa.
      What is the source or expression system of ADIPONECTIN Protein?
      Escherichia Coli.

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >90% 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 is the amino acid sequence of ADIPONECTIN Protein?
      MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
      KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
      GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
      VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
      RNGLYADNDNDSTFTGFLLYHDTN..

      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 Human
  • View Data Sheet

    Name :

    PEDF Human, HEK

    Description:

    Pigment Epithelium-Derived Factor Human Recombinant, HEK

    Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    Product # :

    CYT-553

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    PEDF Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 410 amino acids, having a molecular mass of 45.6 kDa and fused to an 11 aa FLAG tag at C-Terminus.The Human PEDF is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    The filtered (0.4µm) concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
      Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
      Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
      PEDF & VEGF genes contribute to the development of diabetic retinopathy.
      PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
      PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
      SerpinF1 is a new promising approach for the treatment of osteosarcoma.
      Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
      VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
      Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
      PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.

    • Synonyms

      Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recomnded to add deionized water to a working concentration of 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

      QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGPAAADYKDDDDK.

    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.

    Serpinf1 Human Hek
  • View Data Sheet

    Name :

    CX3CL1 Human, Sf9

    Description:

    Fractalkine (CX3CL1) Human Recombinant, Sf9

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

    Product # :

    CHM-042

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    • SDS-PAGE

    Description

    Fractalkine Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 323 amino acids (25-339aa) and having a molecular mass of 34.3kDa.Fractalkine is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Fractalkine solution (1 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    CX3CL1 Human, Sf9-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered 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

      QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
      AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
      QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
      PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
      MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

    • Background

      What is the molecular weight/Mw of CX3CL1 HUMAN, SF9 Protein?
      CX3CL1 HUMAN, SF9 Protein has a total Mw of 34.3kDa.

      What is the source or expression system of CX3CL1 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CX3CL1 HUMAN, SF9 Protein?
      CX3CL1 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 HUMAN, SF9 Protein?
      The biological functionality of CX3CL1 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of CX3CL1 HUMAN, SF9 Protein?
      QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
      AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
      QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
      PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
      MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

      What applications can CX3CL1 HUMAN, SF9 Protein be used in?
      CX3CL1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 HUMAN, SF9 Protein?
      The endotoxin level is minimal, CX3CL1 HUMAN, SF9 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.

    Cx3Cl1 Human
  • View Data Sheet

    Name :

    hchA E.Coli

    Description:

    Chaperone Protein hchA E.Coli Recombinant

    Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950.

    Product # :

    HSP-043

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    Description

    hchA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-283 a.a.) and having a molecular mass of 33.3kDa.hchA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The hchA contains (1mg/ml) 20mM Tris-HCl buffer (pH8.0), 20% glycerol 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Escherichia coli Hsp31 (HchA) is a homodimeric member of the ThiI/DJ-1/PfpI superfamily which combines molecular chaperone and aminopeptidase activities. HchA uses temperature-induced exposure of structured hydrophobic domains to capture and stabilize early unfolding protein intermediates under severe thermal stress.

    • Synonyms

      Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK ILVIAADERY LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL MTKFEYWAMP HKDEKVMPFF EQHKSLFRNP KKLADVVASL NADSEYAAIF VPGGHGALIG LPESQDVAAA LQWAIKNDRF VISLCHGPAA FLALRHGDNP LNGYSICAFP DAADKQTPEI GYMPGHLTWY FGEELKKMGM NIINDDITGR VHKDRKLLTG DSPFAANALG KLAAQEMLAA YAG.

    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.

    Hcha Ecoli
  • View Data Sheet

    Name :

    HPGDS Human

    Description:

    Hematopoietic Prostaglandin D Synthase Human Recombinant

    Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.

    Product # :

    ENZ-616

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    Description

    HPGDS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-199 a.a.) and having a molecular mass of 25.9kDa.HPGDS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the sigma class glutathione-S-transferase family. The HPGDS enzyme catalyzes the conversion of PGH2 to PGD2 and has a role in the production of prostanoids in the immune system and mast cells. The presence of the HPGDS enzyme can be utilized to identify the differentiation stage of human megakaryocytes. Furthermore, HPGDS is a prostaglandin involved in smooth muscle contraction/relaxation and an effective inhibitor of platelet aggregation, and the conjugation of glutathione with a extensive range of aryl halides and organic isothiocyanates. In addition, HPGDS displays low glutathione-peroxidase activity towards cumene hydroperoxide. HPGDS is expressed in a number of megakaryocytic cell lines but not in platelets. HPGDS is highly expressed in the adipose tissue, macrophages and placenta; however it is expressed at lower levels in the lung, heart, lymph nodes, appendix, bone marrow and fetal liver.

    • Synonyms

      Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMPNYKL TYFNMRGRAE IIRYIFAYLD IQYEDHRIEQ ADWPEIKSTL PFGKIPILEV DGLTLHQSLA IARYLTKNTD LAGNTEMEQC HVDAIVDTLD DFMSCFPWAE KKQDVKEQMF NELLTYNAPH LMQDLDTYLG GREWLIGNSV TWADFYWEIC
      STTLLVFKPD LLDNHPRLVT LRKKVQAIPA VANWIKRRPQ TKL.

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    Hpgds Human
  • View Data Sheet

    Name :

    ENSA Human

    Description:

    Endosulfine Alpha Human Recombinant

    ARPP-19e, Alpha endosulfine isoform 3, Alpha-endosulfine, ENSA, MGC4319, MGC8394, MGC78563.

    Product # :

    PRO-772

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    Description

    ENSA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (1-121 a.a.) and having a molecular weight of 15.5kDa. The ENSA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Endosulfine Alpha protein solution contains 20mM Tris, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ENSA is an endogenous ligand for sulfonylurea receptor. ENSA reduces K(ATP) channel currents by inhibiting sulfonylurea from binding to the receptor and thus stimulates insulin secretion. Endosulfine Alpha is part of a conserved cAMP-regulated phosphoprotein (ARPP) family. Endosulfine Alpha is an endogenous ligand for the sulfonylurea receptor, ABCC8/SUR1. Endosulfine Alpha is an endogenous regulator of KATP channels. ENSA modulates insulin secretion through the interaction with KATP channel. ENSA is a candidate gene for type 2 diabetes. ENSA is expressed in a wide range of tissues including muscle, brain, and endocrine tissues.

    • Synonyms

      ARPP-19e, Alpha endosulfine isoform 3, Alpha-endosulfine, ENSA, MGC4319, MGC8394, MGC78563.

    • 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 MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV E.

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    Ensa Human
  • View Data Sheet

    Name :

    Periostin Human

    Description:

    Periostin Human Recombinant

    OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    Product # :

    CYT-452

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    Description

    The OSF2 His-Tagged Fusion Protein Human is produced in E. coli, and its molecular weight is 75 kDa protein containing 648 amino acid residues of the human OSF-2 and 23 additional amino acid residues - HisTag, Xa - cleavage site.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
      Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart.

    • Synonyms

      OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MGHHHHHHHH HHSSGHIEGR HMRNNHYDKI LAHSRIRGRD QGPNVCALQQ ILGTKKKYFS TCKNWYKKSI CGQKTTVLYE CCPGYMRMEG MKGCPAVLPI DHVYGTLGIV GATTTQRYSD ASKLREEIEG KGSFTYFAPS NEAWDNLDSD IRRGLESNVN VELLNALHSH MINKRMLTKD LKNGMIIPSM YNNLGLFINH YPNGVVTVNC ARIIHGNQIA TNGVVHVIDR VLTQIGTSIQ DFIEAEDDLS SFRAAAITSD ILEALGRDGH FTLFAPTNEA FEKLPRGVLE RFMGDKVASEALMKYHILNT LQCSESIMGG AVFETLEGNT IEIGCDGDSI TVNGIKMVNK KDIVTNNGVI HLIDQVLIPD SAKQVIELAG KQQTTFTDLV AQLGLASALR PDGEYTLLAP VNNAFSDDTL SMVQRLLKLI LQNHILKVKV GLNELYNGQI LETIGGKQLR VFVYRTAVCI ENSCMEKGSK QGRNGAIHIF REIIKPAEKS LHEKLKQDKR FSTFLSLLEA ADLKELLTQP GDWTLFVPTN DAFKGMTSEE KEILIRDKNA LQNIILYHLT PGVFIGKGFE PGVTNILKTT QGSKIFLKEV NDTLLVNELK SKESDIMTTN GVIHVVDKLL YPADTPVGND QLLEILNKLI KYIQIKFVRG STFKEIPVTV Y.

    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.

    Periostin Human
  • View Data Sheet

    Name :

    GLRX2 Human

    Description:

    Glutaredoxin 2 Human Recombinant

    Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2, CGI133.

    Product # :

    ENZ-466

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    Description

    Glutaredoxin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 154 amino acids (20-164 a.a.) and having a molecular mass of 17 kDa. The GRX2 is fused to 9 amino acid His tag at C-Terminus.

    Source

    Escherichia Coli.

    Formulation

    Glutaredoxin-2 solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 0.1mM PMSF and 10% glycerol.

    Purity

    Purity of GRX2 is greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLRX2 is a multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. Glutaredoxins are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.

    • Synonyms

      Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2, CGI133.

    • Physical Appearance

      Sterile Filtered clear 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

      MSAGWLDRAA GAAGAAAAAA SGMESNTSSS LENLATAPVN QIQETISDNC VVIFSKTSCS YCTMAKKLFH DMNVNYKVVE LDLLEYGNQF QDALYKMTGE RTVPRIFVNG TFIGGATDTH RLHKEGKLLP LVHQCYLKKS KRKEFQLEHH HHHH.

    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.

    Glrx2 Human
  • View Data Sheet

    Name :

    Leptin tA Rat, PEG

    Description:

    Leptin Antagonist Triple Mutant Pegylated Rat Recombinant

    Product # :

    CYT-567

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    Description

    Leptin Antagonist Triple Mutant Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Rat Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Rat Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Antagonist Triple Mutant Rat Recombinant half-life in circulation after SC injection was over 20 hours.
    Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Rat Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 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 Rat Peg
  • View Data Sheet

    Name :

    GLRX3 Human

    Description:

    Glutaredoxin-3 Human Recombinant

    Glutaredoxin-3, Thioredoxin-like protein 2, PKC-interacting cousin of thioredoxin, PKC-theta-interacting protein, PKCq-interacting protein, GLRX3, PICOT, TXNL2, GRX3, GRX4, GLRX4, TXNL3, FLJ11864, bA500G10.4.

    Product # :

    ENZ-482

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    Description

    GLRX3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (1-335 a.a.) and having a molecular mass of 39.6kDa. GLRX3 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLRX3 solution containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutaredoxin belongs to the thiol-disulfide oxidoreductase family. Glutraredoxins catalyze the reversible reduction of protein-glutathionyl mixed disulfides to free sulfhydryl groups though a monothiol mechanism. Glutaredoxin-3 (GRX3) is an important protein involved in the regulation of signal transduction, for example during immune cell activation and development of cardiac hypertrophy, apparently in response to redox signals. GRX3 interacts with PRKCQ. GRX3 may have a role in the regulation the function of the thioredoxin system. GRX3 is expressed in the heart, spleen, testis and, to a lower extent, in the thymus and peripheral blood leukocytes. GRX3 is weakly expressed in lung, placenta, colon and small intestine.

    • Synonyms

      Glutaredoxin-3, Thioredoxin-like protein 2, PKC-interacting cousin of thioredoxin, PKC-theta-interacting protein, PKCq-interacting protein, GLRX3, PICOT, TXNL2, GRX3, GRX4, GLRX4, TXNL3, FLJ11864, bA500G10.4.

    • 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 MAAGAAEAAV AAVEEVGSAG QFEELLRLKA KSLLVVHFWA PWAPQCAQMN EVMAELAKEL PQVSFVKLEA EGVPEVSEKY EISSVPTFLF FKNSQKIDRL DGAHAPELTK KVQRHASSGS FLPSANEHLK EDLNLRLKKL THAAPCMLFM KGTPQEPRCG FSKQMVEILH KHNIQFSSFD IFSDEEVRQG LKAYSSWPTY PQLYVSGELI GGLDIIKELE ASEELDTICP KAPKLEERLK VLTNKASVML FMKGNKQEAK CGFSKQILEI LNSTGVEYET FDILEDEEVR QGLKAYSNWP TYPQLYVKGE LVGGLDIVKE LKENGELLPI LRGEN.

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    Glrx3 Human
  • View Data Sheet

    Name :

    GRHPR Human

    Description:

    Glyoxylate Reductase/Hydroxypyruvate Reductase Human Recombinant

    EC 1.1.1.79, GLXR, GLYD, GRHPR, PH2.

    Product # :

    ENZ-521

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    Description

    GRHPR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-328 a.a.) and having a molecular mass of 37.8 kDa. The GRHPR is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GRHPR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 5mM DTT and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GRHPR located in the cytosol, belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family of proteins. GRHPR is widely expressed in liver. GRHPR has widespread tissue expression and is involved in metabolism. GRHPR is an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities.

    • Synonyms

      EC 1.1.1.79, GLXR, GLYD, GRHPR, PH2.

    • 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 MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA GAHGLLCLLS DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV GYTPDVLTDT TAELAVSLLL TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF LYTGRQPRPE EAAEFQAEFV STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF INISRGDVVN QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR TRNTMSLLAA NNLLAGLRGE PMPSELKL.

    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.

    Grhpr Human
  • View Data Sheet

    Name :

    EREG Human

    Description:

    Epiregulin Human Recombinant

    EREG, Epiregulin, ER.

    Product # :

    CYT-609

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    Description

    Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

    More Info

    • Introduction

      Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

    • Synonyms

      EREG, Epiregulin, ER.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 5.6kDa.

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

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

      What is the Biological Activity of EREG Protein?
      The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

      What is the amino acid sequence of EREG Protein?
      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

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

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

    Epiregulin Human
  • View Data Sheet

    Name :

    ARTN Human

    Description:

    Artemin Human Recombinant

    ART, ARTN , EVN, NBN.

    Product # :

    CYT-306

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    Description

    Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

    More Info

    • Introduction

      The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.

    • Synonyms

      ART, ARTN , EVN, NBN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

    • Background

      Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications

      Abstract:

      Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.

      Introduction:

      Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.

      Artemin Signaling and Mechanisms:

      Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.

      Artemin in Neurological Disorders:

      Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.

      Therapeutic Potential of Artemin Human Recombinant:

      Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.

      Challenges and Future Directions:

      While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.

      Conclusion:

      Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.

      What is the molecular weight/Mw of ARTN Protein?
      ARTN Protein has a total Mw of 24.2kDa.

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

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

      What is the Biological Activity of ARTN Protein?
      The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

      What is the amino acid sequence of ARTN Protein?
      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

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

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

    Artemin Human
  • View Data Sheet

    Name :

    CRMP1 Mouse

    Description:

    Collapsin Response Mediator Protein-1 Mouse Recombinant

    Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.

    Product # :

    PRO-2521

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    Description

    CRMP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (1-572 a.a) and having a molecular mass of 64.8kDa.CRMP1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CRMP1 protein solution (0.25mg/ml) contains 40% glycerol, 20mM Tris-HCl (pH 8.5), 0.2M NaCl & 0.1mM PMSF.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation as well as axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The X-ray crystal structure of murine CRMP1 was determined at 2.1 resolution and demonstrates that CRMP1 is a bilobed ‘lung-shaped’ protein forming a tetrameric assembly.

    • Synonyms

      Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.

    • 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 MGSEFMSHQG KKSIPHITSD RLLIRGGRII NDDQSFYADV YLEDGLIKQI GENLIVPGGV KTIEANGRMV IPGGIDVNTY LQKPSQGMTS ADDFFQGTKA ALAGGTTMII DHVVPEPGSS LLTSFEKWHE AADTKSCCDY SLHVDITSWY DGVREELEVL VQDKGVNSFQ VYMAYKDLYQ MSDSQLYEAF TFLKGLGAVI LVHAENGDLI AQEQKRILEM GITGPEGHAL SRPEELEAEA VFRAIAIAGR INCPVYITKV MSKSAADIIA LARKKGPLVF GEPIAASLGT DGTHYWSKNW AKAAAFVTSP PLSPDPTTPD YLTSLLACGD LQVTGSGHCP YSTAQKAVGK DNFTLIPEGV NGIEERMTVV WDKAVATGKM DENQFVAVTS TNAAKIFNLY PRKGRIAVGS DADVVIWDPD KMKTITAKSH KSTVEYNIFE GMECHGSPLV VISQGKIVFE DGNISVSKGM GRFIPRKPFP EHLYQRVRIR SKVFGLHSVS RGMYDGPVYE VPATPKHAAP APSAKSSPSK HQPPPIRNLH QSNFSLSGAQ IDDNNPRRTG HRIVAPPGGR SNITSLG.

    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.

    CRMP1 Mouse
  • View Data Sheet

    Name :

    Adiponectin Human, Sf9

    Description:

    Adiponectin Human Recombinant, Sf9

    Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

    Product # :

    CYT-1002

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    • sds-page

    Description

    Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Acrp30 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.

    sds-page

    Adiponectin-sds-page - Product image 1

    More Info

    • Introduction

      The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
      Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
      The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
      Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

    • Synonyms

      Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16.9kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      Sf9, Baculovirus cells.

      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 is the amino acid sequence of ADIPONECTIN Protein?
      ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

      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.

    Acrp30 Human Sf9
  • View Data Sheet

    Name :

    AMELX Human

    Description:

    Amelogenin, X-Linked Human Recombinant

    Amelogenin X isoform, AMELX, AMG, AMGX, AI1E, AIH1, ALGN, AMGL.

    Product # :

    PRO-1324

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    Description

    AMELX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (17-191 a.a) and having a molecular mass of 22kDa.AMELX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AMELX protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Amelogenin, X-Linked (AMELX) belongs to the amelogenin family of extracellular matrix proteins. Amelogenins have a role biomineralization during tooth enamel development. AMELX gene mutations cause X-linked amelogenesis imperfecta. AMELX regulates the formation of crystallites during the secretory stage of tooth enamel development. AMELX is transiently but amply expressed by ameloblasts during tooth development. Amelogenin is the principal protein in developing dental enamel.

    • Synonyms

      Amelogenin X isoform, AMELX, AMG, AMGX, AI1E, AIH1, ALGN, AMGL.

    • 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 MGSMPLPPHP GHPGYINFSY EVLTPLKWYQ SIRPPYPSYG YEPMGGWLHH QIIPVLSQQH PPTHTLQPHH HIPVVPAQQP VIPQQPMMPV PGQHSMTPIQ HHQPNLPPPA QQPYQPQPVQ PQPHQPMQPQ PPVHPMQPLP PQPPLPPMFP MQPLPPMLPD LTLEAWPSTD KTKREEVD.

    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.

    Amelx Human
  • View Data Sheet

    Name :

    HPD Mouse

    Description:

    4-Hydroxyphenylpyruvate Dioxygenase Mouse Recombinant

    4-hydroxyphenylpyruvate dioxygenase, 4-hydroxyphenylpyruvic acid oxidase, 4HPPD, HPD, HPPDase, F Alloantigen, F protein.

    Product # :

    ENZ-1067

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    Description

    HPD Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 416 amino acids (1-393 a.a) and having a molecular mass of 47.4kDa.HPD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HPD protein solution (0.5mg/ml) contains 10% glycerol & 20mM Tris-HCl (pH 8.0).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      HPGD is the essential enzyme of prostaglandin degradation. 15-PGDH protein strongly decreases the biologic activity of these molecules by catalyzing the oxidation of the 15-hydroxyl group of prostaglandins to a keto group. GDH1 is involved in numerous physiologic and cellular processes, for instance inflammation.

    • Synonyms

      4-hydroxyphenylpyruvate dioxygenase, 4-hydroxyphenylpyruvic acid oxidase, 4HPPD, HPD, HPPDase, F Alloantigen, F protein.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTTYNNK GPKPERGRFL HFHSVTFWVG NAKQAASFYC NKMGFEPLAY RGLETGSREV VSHVIKQGKI VFVLCSALNP WNKEMGDHLV KHGDGVKDIA FEVEDCDHIV QKARERGAKI VREPWVEQDK FGKVKFAVLQ TYGDTTHTLV EKINYTGRFL PGFEAPTYKD TLLPKLPRCN LEIIDHIVGN QPDQEMQSAS EWYLKNLQFH RFWSVDDTQV HTEYSSLRSI VVTNYEESIK MPINEPAPGR KKSQIQEYVD YNGGAGVQHI ALKTEDIITA IRHLRERGTE FLAAPSSYYK LLRENLKSAK IQVKESMDVL EELHILVDYD EKGYLLQIFT KPMQDRPTLF LEVIQRHNHQ GFGAGNFNSL FKAFEEEQAL RGNLTDLEPN GVRSGM.

    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.

    Hpd Mouse
  • View Data Sheet

    Name :

    Vimentin Human

    Description:

    Vimentin Human Recombinant

    Vimentin, Vim, FLJ36605.

    Product # :

    PRO-309

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    Description

    Vimentin Human Recombinant produced in E.coli cells is a single non-glycosylated protein containing 465 amino acids chain and having a molecular mass of 53.5kDa. The Vimentin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Vimentin was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    More Info

    • Introduction

      Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.

    • Synonyms

      Vimentin, Vim, FLJ36605.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      STRSVSSSSY RRMFGGPGTA SRPSSSRSYV TTSTRTYSLG SALRPSTSRS LYASSPGGVY ATRSSAVRLR SSVPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED IMRLREKLQE EMLQREEAEN TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHEEE IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA ANRNNDALRQ AKQESTEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF AVEAANYQDT IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL NLRETNLDSL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE.

    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.

    Vimentin Human
  • View Data Sheet

    Name :

    TXN1 E.Coli

    Description:

    Thioredoxin E.Coli Recombinant

    Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    Product # :

    PRO-334

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    • More Info

    Description

    Recombinant Thioredoxin was purified from E. coli harboring its gene.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 20mM phosphate buffer pH 7.4.

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    TRX activity is assayed by measuring the change in absorbance at 650 nm at 25°C using 0.13µM bovine insulin containing 0.33mM DTT (pH 6.5).
    The specific activity was found to be 3IU/mg.

    More Info

    • Introduction

      Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. 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. This could be especially useful in refolding proteins expressed in E. coli. To this end, thioredoxin has been shown to act as a protein disulfide isomerase.Its Molecular Weight is 11.9kDa. and the pI is 4.67.

    • Synonyms

      Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    • Physical Appearance

      Sterile Lyophilized Powder.

    • Stability

      TRX although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TRX in sterile 18MΩ-cm H2O.

    • Amino Acid Sequence

      HMSDKIIHL TDDSFDTDVLKADGAIL VDFW AEWCGPCKMIAPILDEI GKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGAL DANLA.

    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 1
  • View Data Sheet

    Name :

    NPPA Human

    Description:

    Natriuretic Peptide A Human Recombinant

    Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND. 

    Product # :

    CYT-1028

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    Description

    NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.

    • Synonyms

      Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.

    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.

    Nppa Human
  • View Data Sheet

    Name :

    Leptin Pufferfish

    Description:

    Leptin Pufferfish Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-530

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    Description

    Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.

    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 Pufferfish 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 Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE

      GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE

      QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 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 Pufferfish
  • View Data Sheet

    Name :

    Staphylokinase

    Description:

    Staphylokinase Recombinant

    Staphylokinase, SakSTAR, Neutral proteinase, Protease III, SAK.

    Product # :

    ENZ-288

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    • sds-page

    Description

    Staphylokinase Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 136 amino acids and having a molecular weight of 16kDa.The Staphylokinase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The biological activity measured by the ability of fibrin lysis in agarose plate was found to be 50,000IU/mg.

    sds-page

    Staphylokinase sds-page - Product image 1

    More Info

    • Introduction

      Staphylokinase (SAK) is a 136-amino acidenzymefrom Staphylococcus aureus. It is positively regulated by the "agr" gene regulator. It activates plasminogen, which in turn can degrade various host proteins during infection.

    • Synonyms

      Staphylokinase, SakSTAR, Neutral proteinase, Protease III, SAK.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SAK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SAK 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 SAKin 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.

    Staphylokinase
  • View Data Sheet

    Name :

    DHH (C23II) Mouse

    Description:

    Desert Hedgehog (C23II) Mouse Recombinant

    Desert hedgehog protein, DHH, HHG-3, C78960.

    Product # :

    CYT-773

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    Description

    DHH (C23II) Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 20kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4, 1mM DTT and 0.05% Tween-80.

    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 its ability to induce alkaline phosphatase production by murine MC3T3-E1 cells is 5-20 µg/ml.

    More Info

    • Introduction

      DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
      DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.

    • Synonyms

      Desert hedgehog protein, DHH, HHG-3, C78960.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IIGPGRGPVG RRRYVRKQLV PLLYKQFVPS MPERTLGASG PAEGRVTRGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH IHVSVKADNS LAVRAGG.

    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.

    Dhh C23Ii Mouse
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