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Search results

1000 results found for “cyclophilin”

Name

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  • View Data Sheet

    Name :

    Thyroglobulin Human

    Description:

    Thyroglobulin Human Recombinant

    Thyroglobulin, TGN, AITD3, TG.

    Product # :

    PRO-2803

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    • sds-page

    Description

    Thyroglobulin Human produced in a mammalian cell line is a single, non-glycosylated polypeptide chain (1-2768 a.a.) and having a molecular mass of 304640 Dalton. Thyroglobulin Human is fused with GlyAlaProGly4SerHis10-tag at C-terminal and purified by proprietary chromatographic techniques.

    Source

    Mammalian cell line.

    Formulation

    Thyroglobulin was lyophilized from PBS, pH 7.4 and 5.4 % sucrose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    Thyroglobulin Recombinant Human SDS-PAGE - Product image 1

    More Info

    • Synonyms

      Thyroglobulin, TGN, AITD3, TG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Thyroglobulin, a glycoprotein primarily produced in the thyroid gland, stands at the center of thyroid hormone synthesis. Comprising a series of tyrosine residues, thyroglobulin serves as the scaffold upon which thyroid hormones are assembled. Beyond its pivotal role in thyroid physiology, thyroglobulin has garnered significant attention in the realm of thyroid disease diagnostics, offering valuable insights into thyroid function and disorders. This research delves into the intricacies of thyroglobulin human recombinant protein, exploring its biochemical properties, physiological significance, and its crucial applications in both clinical and research settings.

      Structural Complexity of Thyroglobulin:

      Thyroglobulin is a large, dimeric protein boasting an intricate structure composed of multiple domains. Within its structure lie tyrosine residues crucial for iodine incorporation, a process fundamental for thyroid hormone synthesis. Its size and complexity reflect the sophistication of thyroid hormone production, as thyroglobulin acts as a reservoir for thyroid hormones within the thyroid follicles.

      Physiological Significance in Thyroid Function:

      Thyroglobulin plays a central role in the synthesis of triiodothyronine (T3) and thyroxine (T4), the thyroid hormones essential for regulating metabolism and overall body homeostasis. During thyroid hormone synthesis, thyroglobulin is secreted into the follicular lumen, where it undergoes iodination and subsequent proteolysis, releasing T3 and T4. This process highlights the indispensable nature of thyroglobulin in thyroid hormone production, making it a key biomolecule in thyroid physiology.

    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.

    Thyroglobulin Antigen
  • View Data Sheet

    Name :

    Lungkine Mouse

    Description:

    Lungkine (CXCL15) Mouse Recombinant

    C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

    Product # :

    CHM-286

    Price :

    Quantity :

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    Description

    Recombinant Mouse Lungkine produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids and having a molecular mass of 16.4kDa.The CXCL15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Lungkine protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 0.02% Tween-20.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.

    More Info

    • Introduction

      Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.

    • Synonyms

      C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Lungkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL15 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 Lungkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.

    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.

    Lungkine Mouse
  • View Data Sheet

    Name :

    SIGLEC10 Human

    Description:

    Sialic Acid Binding Ig Like Lectin 10 Human Recombinant

    SIGLEC10, PRO940, SLG2, SIGLEC-10, Sialic acid-binding Ig-like lectin 10 isoform 3, Siglec-like protein 2.

    Product # :

    PRO-2610

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    More Info

    • description
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    • More Info

    Description

    SIGLEC10 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 678 amino acids (17-455 a.a.) and having a molecular mass of 75.6kDa. SIGLEC10 is expressed with a 239 hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The SIGLEC10 solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sialic Acid Binding Ig Like Lectin 10(SIGLEC10) is a part of the immunoglobulin superfamily that is expressed on eosinophils, B cells, monocytes and neutrophils. SIGLEC10 is an adhesion molecule that mediates sialic-acid dependent binding to cells.SIGLEC10 is a ligand for CD52, the target of the therapeutic monoclonal antibody Alemtuzumab. Also, it binds to Vascular adhesion protein 1 (VAP-1) and to the co-stimulatory molecule CD24.This binding is modulated by cis interactions of SIGLEC10 with sialated molecules on the same cell.

    • Synonyms

      SIGLEC10, PRO940, SLG2, SIGLEC-10, Sialic acid-binding Ig-like lectin 10 isoform 3, Siglec-like protein 2.

    • 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

      MDGRFWIRVQ ESVMVPEGLC ISVPCSFSYP RQDWTGSTPA YGYWFKAVTE TTKGAPVATN
      HQSREVEMST RGRFQLTGDP AKGNCSLVIR DAQMQDESQY FFRVERGSYV RYNFMNDGFF
      LKVTALTQKP DVYIPETLEP GQPVTVICVF NWAFEECPPP SFSWTGAALS SQGTKPTTSH
      FSVLSFTPRP QDHNTDLTCH VDFSRKGVSA QRTVRLRVAY APRDLVISIS RDNTPALEPQ
      PQGNVPYLEA QKGQFLRLLC AADSQPPATL SWVLQNRVLS SSHPWGPRPL GLELPGVKAG
      DSGRYTCRAE NRLGSQQRAL DLSVQYPPEN LRVMVSQANR TVLENLGNGT SLPVLEGQSL
      CLVCVTHSSP PARLSWTQRG QVLSPSQPSD PGVLELPRVQ VEHEGEFTCH ARHPLGSQHV
      SLSLSVHYKK GLISTAFSNL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR
      TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN
      GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS
      DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

    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.

    Siglec10 Human
  • View Data Sheet

    Name :

    CTGF Human

    Description:

    Connective Tissue Growth Factor Human Recombinant

    CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

    Product # :

    CYT-541

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
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    • More Info

    Description

    CTGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.2 kDa. The CTGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTGF was Lyophilized from a sterile filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

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

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of HUVEC cells. The expected ED50 for this effect is 1-2µg/ml, corresponding to a specific activity of 500-1000units/mg.

    More Info

    • Introduction

      Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
      CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
      Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
      The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the IGFBPs.
      Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
      Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
      Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to binding motifs are also found within this domain.
      Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
      In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
      CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

    • Synonyms

      CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MGKKCIRTPK ISKPIKFELS GCTSMKTYRA KFCGVCTDGR CCTPHRTTTL PVEFKCPDGE VMKKNMMFIK TCACHYNCPG DNDIFESLYY RKMYGDMA.

    • Background

      Title: Connective Tissue Growth Factor Human Recombinant: Insights into Production, Function, and Therapeutic Potential

      Abstract:


      Connective tissue growth factor (CTGF) is a multifunctional protein that plays a critical role in tissue homeostasis and repair. This research paper provides a comprehensive analysis of human recombinant CTGF, focusing on its production, characterization, and potential therapeutic applications. The paper discusses the significance of CTGF in connective tissue development, fibrosis, and wound healing. Furthermore, it explores the ongoing research and clinical trials investigating the therapeutic potential of recombinant CTGF in various pathological conditions. The information presented in this paper aims to deepen our understanding of human recombinant CTGF and its utility as a research tool and a potential therapeutic agent.

      Introduction:


      Connective tissue growth factor (CTGF) is a secreted protein that belongs to the CCN (Cyr61, CTGF, Nov) family. It is involved in diverse cellular processes, including cell proliferation, extracellular matrix synthesis, and angiogenesis. Human recombinant CTGF, produced through genetic engineering techniques, enables researchers to study its biological functions and explore its therapeutic potential.

      Production and Characterization:


      Recombinant CTGF is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and biological activity of the recombinant CTGF.

      Role in Tissue Homeostasis and Repair:


      CTGF plays a critical role in connective tissue development, maintenance, and repair. It promotes the synthesis of extracellular matrix components, such as collagen and fibronectin, and regulates the activity of various growth factors. CTGF is also involved in wound healing and tissue remodeling processes. Understanding the molecular mechanisms underlying CTGF-mediated tissue repair provides insights into potential therapeutic interventions.

      Therapeutic Implications:


      The dysregulation of CTGF expression and signaling has been implicated in several pathological conditions, including fibrosis, arthritis, and cancer. Recombinant CTGF holds promise as a potential therapeutic agent for these diseases. Preclinical and clinical studies are being conducted to evaluate the safety and efficacy of CTGF-based therapies, such as CTGF-targeting antibodies and small-molecule inhibitors.

      Conclusion:


      Human recombinant CTGF is a valuable research tool and a potential therapeutic target in various pathological conditions. Its production, characterization, and applications in connective tissue biology contribute to our understanding of tissue repair mechanisms and the development of novel therapeutic strategies. Continued research and clinical trials exploring the therapeutic potential of recombinant CTGF offer promising avenues for improving patient outcomes.

      What is the molecular weight/Mw of CTGF Protein?
      CTGF Protein has a total Mw of 11.2kDa.

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

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

      What is the Biological Activity of CTGF Protein?
      Determined by the dose-dependent stimulation of the proliferation of HUVEC cells. The expected ED50 for this effect is 1-2µg/ml, corresponding to a specific activity of 500-1000units/mg.

      What is the amino acid sequence of CTGF Protein?
      MGKKCIRTPK ISKPIKFELS GCTSMKTYRA KFCGVCTDGR CCTPHRTTTL PVEFKCPDGE VMKKNMMFIK TCACHYNCPG DNDIFESLYY RKMYGDMA.

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

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

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    Ctgf Human
  • View Data Sheet

    Name :

    LIF Human, His

    Description:

    Leukemia Inhibitory Factor Human Recombinant, His tag

    CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    Product # :

    CYT-1082

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    Description

    LIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 23-202) containing 189 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 20.9kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS PLPITPVNAT CAIRHPCHNN LMNQIRSQLA QLNGSANALF ILYYTAQGEP FPNNLDKLCG PNVTDFPPFH ANGTEKAKLV ELYRIVVYLG TSLGNITRDQ KILNPSALSL HSKLNATADI LRGLLSNVLC RLCSKYHVGH VDVTYGPDTS GKDVFQKKKL GCQLLGKYKQ IIAVLAQAF.

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    Lif Protein
  • View Data Sheet

    Name :

    TFPI2 Human

    Description:

    Tissue Factor Pathway Inhibitor 2 Human Recombinant

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

    Product # :

    PRO-860

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Tfpi2 Human
  • View Data Sheet

    Name :

    TAGLN Human

    Description:

    Transgelin Human Recombinant

    SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.

    Product # :

    PRO-851

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    Description

    TAGLN Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-201 a.a.) and having a molecular mass of 24.8 kDa. The TAGLN is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TAGLN Human solution containing 20mM Tris-HCl pH-7.5, 1mM DTT & 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TAGLN is a transformation and form-change responsive actin cross-linking/gelling protein that is part of the calponin family. TAGLN is expressed abundantly in fibroblasts and smooth muscle. TAGLN participates in calcium interactions and contractile properties of the cell that contribute to replicative senescence. Throughout embryogenesis, TAGLN is expressed in smooth, cardiac and skeletal muscle, but is limited during late fetal growth and adulthood to all vascular and visceral smooth muscle cells and low levels of expression in heart. TAGLN is downregulated in several transformed cell lines, showing that a decrease of TAGLN expression is an premature indicator of the onset of transformation.

    • Synonyms

      SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.

    • 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 MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIIVQCGP DVGRPDRGRL GFQVWLKNGV ILSKLVNSLY PDGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVIKTD MFQTVDLFEG KDMAAVQRTL MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTESQLQE GKHVIGLQMG SNRGASQAGM TGYGRPRQII S.

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    Tagln Human
  • View Data Sheet

    Name :

    CHIKV E2

    Description:

    Chikungunya E2 Recombinant

    Product # :

    CHI-003

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    Description

    Recombinant Chikungunya E2 produced in E.coli having a molecular weight of 38kDa (migrates at 38-40kDa on 10% SDS-PAGE).

    Source

    Escherichia Coli.

    Formulation

    Sterile Filtered solution containing PBS and 25mM K2CO3.

    Purity

    Protein is >95% pure as determined by SDS-PAGE.

    More Info

    • Introduction

      Chikungunya is an infection caused by the chikungunya virus which is passed to humans by two species of mosquito of the genus Aedes: A. albopictus and A. aegypti. Animal reservoirs of the virus include monkeys, birds, cattle, and rodents. The features of the disease are a sudden onset of fever 2-4 days after exposure. The fever typically lasts 2-7 days, while the associated joint pains usually last weeks or months but sometimes years. The mortality rate is a little less than 1 in 1,000. The disease has occurred in outbreaks in Asia, Europe and the Americas since 2004. CHIKV is a single-stranded positive-sense RNA genome, 11,800 nts long which encodes 2 open reading frames. The nucleocapsid is tightly enveloped by a host-derived lipid bilayer (envelope) supporting the virus-encoded envelope proteins. 80 glycoprotein spikes are C- terminally anchored within the viral envelope. The structural polyprotein is translated from a viral sub genomic mRNA, while as the 5 structural proteins (capsid, E3, E2, 6K, E1) are translated as a single polyprotein, from which capsid (C) is cleaved off to encapsidate. The envelope polyprotein precursor E3-E2-6K-E1 is translocated to the endoplasmatic reticulum. Polyprotein is processed by host signalases, resulting in E3, E2 & E1 forming viral hetero-trimeric spikes. The viral spikes majorly contains E2 and E1 facilitate cell receptor recognition, cell entry thru pH-dependent endocytosis and support viral budding.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CHIKV E2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Rapid test and Immunoassay.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    Chikv E2
  • View Data Sheet

    Name :

    ZNF32 Human

    Description:

    Zinc Finger Protein 32 Human Recombinant

    KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.

    Product # :

    PRO-1983

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    Description

    ZNF32 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273 a.a) and having a molecular mass of 33.4kDa. ZNF32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ZNF32 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Zinc Finger Protein 32 (ZNF32) is a part of the krueppel C2H2-type zinc-finger protein family. ZNF32 which contains seven C2H2-type zinc fingers takes part in transcriptional regulation.

    • Synonyms

      KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.

    • 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 MGSMFGFPTA TLLDCHGRYA QNVAFFNVMT EAHHKYDHSE ATGSSSWDIQ NSFRREKLEQ KSPDSKTLQE DSPGVRQRVY ECQECGKSFR QKGSLTLHER IHTGQKPFEC THCGKSFRAK GNLVTHQRIH TGEKPYQCKE CGKSFSQRGS LAVHERLHTG QKPYECAICQ RSFRNQSNLA VHRRVHSGEK PYRCDQCGKA FSQKGSLIVH IRVHTGLKPY ACTQCRKSFH TRGNCILHGK IHTGETPYLC GQCGKSFTQR GSLAVHQRSC SQRLTL.

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    Znf32 Human
  • View Data Sheet

    Name :

    KGF 2 Mouse

    Description:

    Keratinocyte Growth Factor-2 Mouse Recombinant

    FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.

    Product # :

    CYT-126

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    Description

    KGF 2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids and having a molecular mass of 19.5kDa. The KGF 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 containing 5% trehalose.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF receptors is <0.5ng/ml.

    More Info

    • Introduction

      KGF-2 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7. Studies of the mouse homolog of suggested that this gene is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of lim bud formation. This gene is also implicated to be a primary factor in the process of wound healing.

    • Synonyms

      FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KGF 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KGF 2 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 KGF 2 Mouse Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QALGQDMVSQ EATNCSSSSS SFSSPSSAGR HVRSYNHLQG DVRWRRLFSF TKYFLTIEKN GKVSGTKNED CPYSVLEITS VEIGVVAVKA INSNYYLAMN KKGKLYGSKE FNNDCKLKER IEENGYNTYA SFNWQHNGRQ MYVALNGKGA PRRGQKTRRK NTSAHFLPMT IQT

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    Kgf 2 Mouse
  • View Data Sheet

    Name :

    F3 Mouse

    Description:

    Coagulation Factor III Mouse Recombinant

    Tissue factor, TF, Coagulation factor III, CD142.

    Product # :

    PRO-2316

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    Description

    F3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (29-251 a.a.) and having a molecular mass of 26.4kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). F3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    F3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tissue factor is well-known as the main cellular initiator of blood coagulation. The Tissue factor gene encodes coagulation factor III which is a cell surface glycoprotein that enables cells to initiate the blood coagulation cascades, and functions as the high-affinity receptor for the coagulation factor VII. Following vessel injury, the Tissue Factor and Factor VIIa complex activates the coagulation protease cascade, which leads to fibrin deposition and activation of platelets. The ensuing complex presents a catalytic event, which is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Therefore, Tissue factor has a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Tissue Factor can also be stimulated by the inflammatory mediators interleukin 1 and TNF, as well as by endotoxin, to appear on monocytes and vascular endothelial cells as a component of cellular immune response.
      Tissue factor is the only one in the coagulation pathway for which a congenital deficiency has not been described. Certain levels of Tissue Factor are essential for the maintained viability and growth of endothelium and Tissue Factor-expressing tumor cells. Additionally, abnormal Tissue Factor expression inside the vasculature initiates life threatening thrombosis in various diseases, for example sepsis, atherosclerosis, and cancer. Alternative spliced Tissue Factor expression advances tumor growth, and is linked to increased tumor cell proliferation and angiogenesis in pancreatic cancer.

    • Synonyms

      Tissue factor, TF, Coagulation factor III, CD142.

    • 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

      ADPAGIPEKA FNLTWISTDF KTILEWQPKP TNYTYTVQIS DRSRNWKNKC FSTTDTECDL TDEIVKDVTW AYEAKVLSVP RRNSVHGDGD QLVIHGEEPP FTNAPKFLPY RDTNLGQPVI QQFEQDGRKL NVVVKDSLTL VRKNGTFLTL RQVFGKDLGY IITYRKGSST GKKTNITNTN EFSIDVEEGV SYCFFVQAMI FSRKTNQNSP GSSTVCTEQW KSFLGEHHHH HH.

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

    Tissue Factor Human, Active
  • View Data Sheet

    Name :

    COA4 Human

    Description:

    Cytochrome C Oxidase Assembly Factor 4 Human Recombinant

    CHCHD8, CMC3, E2IG2, Cytochrome c oxidase assembly factor 4 homolog, mitochondrial, Coiled-coil-helix-coiled-coil-helix domain-containing protein 8, E2-induced gene 2 protein, COA4.

    Product # :

    PRO-1988

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    Description

    COA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87 a.a) and having a molecular mass of 12.5kDa. COA4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COA4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytochrome c oxidase assembly factor 4 (COA4) is the last enzyme of the mitochondrial respiratory chain which needs a great number of accessory factors. COA4 is vital for oxidative phosphorylation and comprises multiple complexes including cytochrome c oxidase, assembled in macromolecular supercomplexes. COX4 is a protein-coding gene which defect in it causes an acute human encephalomyopathies.

    • Synonyms

      CHCHD8, CMC3, E2IG2, Cytochrome c oxidase assembly factor 4 homolog, mitochondrial, Coiled-coil-helix-coiled-coil-helix domain-containing protein 8, E2-induced gene 2 protein, COA4.

    • 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 MGSMSTSVPQ GHTWTQRVKK DDEEEDPLDQ LISRSGCAAS HFAVQECMAQ HQDWRQCQPQ VQAFKDCMSE QQARRQEELQ RRQEQAGAHH.

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    Coa4 Human
  • View Data Sheet

    Name :

    S100A8 Mouse

    Description:

    S100 Calcium Binding Protein A8 Mouse Recombinant

    Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    Product # :

    PRO-233

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    Description

    S100A8 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89a.a) and having a molecular mass of 12.4kDa.S100A8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A8 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

    • Synonyms

      Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    • 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 MPSELEKALS NLIDVYHNYS NIQGNHHALY KNDFKKMVTT ECPQFVQNIN IENLFRELDI NSDNAINFEE FLAMVIKVGV ASHKDSHKE

    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.

    S100A8 Mouse
  • View Data Sheet

    Name :

    PSPN Mouse

    Description:

    Persephin Mouse Recombinant

    Persephin, PSPN.

    Product # :

    CYT-802

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    Description

    PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg. 

    More Info

    • Introduction

      Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.

    • Synonyms

      Persephin, PSPN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG

    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.

    Pspn Mouse
  • View Data Sheet

    Name :

    CMV gB

    Description:

    Cytomegalo Virus gB Recombinant

    Product # :

    CMV-211

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    Description

    The E.Coli derived recombinant artificial mosaic protein contains the CMV gB immunodominant regions 11-67 amino acids, fused with a 26 kDa GST Tag, the protein weight is 6.5kDa, having a total weight of 32.5 kDa.

    Source

    Escherichia Coli.

    Formulation

    50mM Tris pH 7.2, 1mM EDTA and 50% glycerol.

    Purity

    CMV gB protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      MV belongs to the Beta herpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods.CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.

    • Stability

      CMV gB protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Specificity

      Immunoreactive with sera of CMV-infected individuals.

    • Purification Method

      CMV gB was purified by proprietary chromatographic technique.

    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.

    Cmv Gb
  • View Data Sheet

    Name :

    CCL19 Human

    Description:

    Macrophage Inflammatory Protein-3 Beta Human Recombinant (CCL19)

    Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433.

    Product # :

    CHM-287

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    Description

    Macrophage Inflammatory Protein-3 beta Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8.8kDa. The MIP-3b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized without any additives.

    Purity

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

    Biological Activity

    The Activity of CCL19 is calculated by the ability to chemoattract Human T cells using a concentration of 7-40ng/ml corresponding to a Specific Activity of 25,000-143,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). CCL19 is expressed abundantly in thymus and lymph nodes, with moderate levels in trachea and colon and low levels in stomach, small intestine, lung, kidney and spleen. The gene for CCL19 is located on human chromosome 9. This chemokine elicits its effects on its target cells by binding to the chemokine receptor chemokine receptor CCR7. It attracts certain cells of the immune system, including dendritic cells and antigen-engaged B cells.

    • Synonyms

      Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-3b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL19 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 Macrophage Inflammatory Protein-3b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GTNDAEDCCL SVTQKPIPGY IVRNFHYLLI KDGCRVPAVV FTTLRGRQLC APPDQPWVER IIQRLQRTSA KMKRRSS.

    • Background

      What is the molecular weight/Mw of CCL19 HUMAN Protein?
      CCL19 HUMAN Protein has a total Mw of 8.8kDa.

      What is the source or expression system of CCL19 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL19 HUMAN Protein?
      CCL19 HUMAN Protein is > 98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL19 HUMAN Protein?
      The Activity of CCL19 is calculated by the ability to chemoattract Human T cells using a concentration of 7-40ng/ml corresponding to a Specific Activity of 25,000-143,000IU/mg.

      What is the amino acid sequence of CCL19 HUMAN Protein?
      GTNDAEDCCL SVTQKPIPGY IVRNFHYLLI KDGCRVPAVV FTTLRGRQLC APPDQPWVER IIQRLQRTSA KMKRRSS.

      What applications can CCL19 HUMAN Protein be used in?
      CCL19 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL19 HUMAN Protein?
      The endotoxin level is minimal, CCL19 HUMAN Protein was purified using conventional chromatography techniques.


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    Mip 3B Human
  • View Data Sheet

    Name :

    TNFRSF17 Human, His

    Description:

    B-Cell Maturation Antigen Human Recombinant, His Tag

    BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.

    Product # :

    CYT-190

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    Description

    TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (78-184 a.a) and having a molecular mass of 14.1kDa.TNFRSF17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFRSF17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.

    • Synonyms

      BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.

    • Physical Appearance

      Sterile Filtered colorless liquid.

    • 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 MGSRKINSEP LKDEFKNTGS GLLGMANIDL EKSRTGDEII LPRGLEYTVE ECTCEDCIKS KPKVDSDHCF PLPAMEEGAT ILVTTKTNDY CKSLPAALSA TEIEKSISAR.

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    Tnfrsf17 Human His
  • View Data Sheet

    Name :

    SPIN1 Human

    Description:

    Spindlin-1 Human Recombinant

    Ovarian cancer-related protein, spindlin 1, SPIN, OCR.

    Product # :

    PRO-1184

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    Description

    SPIN1 Human Recombinant produced E. coli is a single polypeptide chain containing 285 amino acids (1-262) and having a molecular mass of 32.0kDa.SPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SPIN1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SPIN1 is a member of the SPIN/STSY family. SPIN1 is localized to nucleus, and expressed in several tissues and cells. SPIN1 takes part in cell-cycle regulation in the course of the transition from gamete to embryo.

    • Synonyms

      Ovarian cancer-related protein, spindlin 1, SPIN, OCR.

    • 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 MGSMKTPFGK TPGQRSRADA GHAGVSANMM KKRTSHKKHR SSVGPSKPVS QPRRNIVGCR IQHGWKEGNG PVTQWKGTVL DQVPVNPSLY LIKYDGFDCV YGLELNKDER VSALEVLPDR VATSRISDAH LADTMIGKAV EHMFETEDGS KDEWRGMVLA RAPVMNTWFY ITYEKDPVLY MYQLLDDYKE GDLRIMPDSN DSPPAEREPG EVVDSLVGKQ VEYAKEDGSK RTGMVIHQVE AKPSVYFIKF DDDFHIYVYD LVKTS

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    Spin1 Human
  • View Data Sheet

    Name :

    CPE Human

    Description:

    Carboxypeptidase-E Human Recombinant

    Carboxypeptidase E, Carboxypeptidase H, CPH, CPE, CPE Human, Enkephalin convertase, Prohormone-processing carboxypeptidase.

    Product # :

    ENZ-687

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    Description

    CPE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (43-476 a.a.) and having a molecular mass of 51.4kDa. CPE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CPE protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carboxypeptidase-E (CPE ) is a carboxypeptidase that cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters. CPE is a peripheral membrane protein. CPE specifically connects regulated secretory pathway proteins, including prohormones, but constitutively secreted proteins. Mutations in CPE are implicated in type II diabetes.

    • Synonyms

      Carboxypeptidase E, Carboxypeptidase H, CPH, CPE, CPE Human, Enkephalin convertase, Prohormone-processing carboxypeptidase.

    • 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 MGSLQQEDGI SFEYHRYPEL REALVSVWLQ CTAISRIYTV GRSFEGRELL VIELSDNPGV HEPGEPEFKY IGNMHGNEAV GRELLIFLAQ YLCNEYQKGN ETIVNLIHST RIHIMPSLNP DGFEKAASQP GELKDWFVGR SNAQGIDLNR NFPDLDRIVY VNEKEGGPNN HLLKNMKKIV DQNTKLAPET KAVIHWIMDI PFVLSANLHG GDLVANYPYD ETRSGSAHEY SSSPDDAIFQ SLARAYSSFN PAMSDPNRPP CRKNDDDSSF VDGTTNGGAW YSVPGGMQDF NYLSSNCFEI TVELSCEKFP PEETLKTYWE DNKNSLISYL EQIHRGVKGF VRDLQGNPIA NATISVEGID HDVTSAKDGD YWRLLIPGNY KLTASAPGYL AITKKVAVPY SPAAGVDFEL ESFSERKEEE KEELMEWWKM MSETLNF.

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    Cpe Human
  • View Data Sheet

    Name :

    Protein-A/G/L

    Description:

    Protein A/G/L Recombinant

    Product # :

    PRO-1936

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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 805 amino acids in total and having a molecular mass of 89.2kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein- A/G/L was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG.

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    Protein A G L
  • View Data Sheet

    Name :

    GroEL E.Coli

    Description:

    GroEL (HSP60) E.Coli Recombinant

    CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.

    Product # :

    HSP-004

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    Description

    Recombinant GroEL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 548 amino acids (1-548) and having a molecular mass of 57.3kDa. GroEL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The groEL protein contains 25mM Tris buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GroEL protein is the major heat shock protein of E.coli and belongs to the chaperonin (HSP60) family. GroEL protein prevents misfolding of proteins and promotes the refolding and proper assembly of unfolded polypeptiedes generated under stress condition.

    • Synonyms

      CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.

    • 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

      MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREIELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGIDKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDGTGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAVAKAGKPLLII AEDVEGEALA TAVVNTIRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTVISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDYDREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALIRVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNAATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM.

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    Groel Ecoli
  • View Data Sheet

    Name :

    C12ORF5 Human, His

    Description:

    Chromosome 12 Open Reading Frame 5 Human Recombinant, His Tag

    Probable fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    Product # :

    PRO-051

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    Description

    C12ORF5 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids (1-270 a.a.) and having a molecular mass of 32.6kDa. The C12ORF5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C12ORF5 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TP53-induced glycolysis and apoptosis regulator (TIGAR or C12ORF5), is a 270 amino acid protein induced by the p53 tumor suppressor pathway that functions to protect against oxidative stress. C12ORF5 specifically functions to block glycolysis, leading the pathway to the pentose phosphate shunt and decreasing the intracellular concentration of reactive oxygen species. Therefore, it is thought that C12ORF5 may act to modulate the apoptotic response to p53, thus allowing cells to survive mild or transient stresses.

    • Synonyms

      Probable fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    • 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 MGSHMARFAL TVVRHGETRF NKEKIIQGQG VDEPLSETGF KQAAAAGIFL NNVKFTHAFS SDLMRTKQTM HGILERSKFC KDMTVKYDSR LRERKYGVVE GKALSELRAM AKAAREECPV FTPPGGETLD QVKMRGIDFF EFLCQLILKE ADQKEQFSQG SPSNCLETSL AEIFPLGKNH SSKVNSDSGI PGLAASVLVV SHGAYMRSLF DYFLTDLKCS LPATLSRSEL MSVTPNTGMS LFIINFEEGR EVKPTVQCIC MNLQDHLNGL TETR.

    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.

    C12Orf5 Human
  • View Data Sheet

    Name :

    CNRIP1 Human

    Description:

    Cannabinoid Receptor Interacting Protein 1 Human Recombinant

    Cannabinoid Receptor Interacting Protein 1, Cannabinoid Receptor CB1-Interacting Protein 1, Chromosome 2 Open Reading Frame 32, C2orf32, CRIP1, CRIP1a, CRIP1b, DKFZP566K1924.

    Product # :

    PRO-1214

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    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CNRIP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 187 amino acids (1-164) and having a molecular mass of 21.0 kDa.CNRIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CNRIP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.

    • Synonyms

      Cannabinoid Receptor Interacting Protein 1, Cannabinoid Receptor CB1-Interacting Protein 1, Chromosome 2 Open Reading Frame 32, C2orf32, CRIP1, CRIP1a, CRIP1b, DKFZP566K1924.

    • 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 MGSMGDLPGL VRLSIALRIQ PNDGPVFYKV DGQRFGQNRT IKLLTGSSYK VEVKIKPSTL QVENISIGGV LVPLELKSKE PDGDRVVYTG TYDTEGVTPT KSGERQPIQI TMPFTDIGTF ETVWQVKFYN YHKRDHCQWG SPFSVIEYEC KPNETRSLMW VNKESFL

    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.

    Cnrip1 Human
  • View Data Sheet

    Name :

    Activin-A Human Active

    Description:

    Activin-A Human Recombinant, Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-145

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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

    Description

    Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

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

      Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential

      Introduction:

      Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.

      Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.

      Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.

      Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.

      The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.

      In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.

    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.

    Inhba Human
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