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Search results

1000 results found for “Calcyphosine”

Name

Description

Product #

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  • View Data Sheet

    Name :

    sRANKL Human

    Description:

    RANK Ligand Soluble Human Recombinant

    Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    Product # :

    CYT-334

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • HPLC, SDS-PAGE

    Description

    sRANKL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19.7kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Sodium phosphate, pH-7.5.

    Purity

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

    Biological Activity

    The activity of RAW-Blue was measured to be 46.96 ng/ml, corresponding to a specific activity of 2.1x104 units/mg.

    HPLC, SDS-PAGE

    sRANKL Human HPLC - Product image 1
    sRANKL Human SDS PAGE - Product image 2

    More Info

    • Introduction

      RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

    • Synonyms

      Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANKL 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 sRANKL in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EKAMVDGSW LDLAKRSKLE AQPFAHLTIN ATDIPSGSHK VSLSSWYHDR GWAKISNMTF SNGKLIVNQD GFYYLYANIC FRHHETSGDL ATEYLQLMVY VTKTSIKIPS SHTLMKGGST KYWSGNSEFH FYSINVGGFF KLRSGEEISI EVSNPSLLDP DQDATYFGAF KVRDID.

    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.

    Rankl Human
  • View Data Sheet

    Name :

    S100A1 Human

    Description:

    S100 Calcium Binding Protein A1 Human Recombinant

    Protein S100-A1, S100 calcium-binding protein A1, S-100 protein alpha subunit, S-100 protein alpha chain, S100A1, S100A, S100, S100-alpha, S100-A1.

    Product # :

    PRO-364

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
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    • More Info

    Description

    S100A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 103 amino acids which include a 10 amino acid His Tag fused at N-terminus and having a total molecular mass of 11.66 kDa. S100A1 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A1 protein was lyophilized from 0.4µm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5 and 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A1 is a member of the S100 family of calcium binding proteins with EF-hand type Ca+2 binding motive. S100A1 (Calcium Binding Protein A1) is involved in the activation of sarcoplasmatic calcium release and the regulation of intermediate filament polymerization. S100A1 may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of S100A1 has been implicated in cardiomyopathies.
      S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.

    • Synonyms

      Protein S100-A1, S100 calcium-binding protein A1, S-100 protein alpha subunit, S-100 protein alpha chain, S100A1, S100A, S100, S100-alpha, S100-A1.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized S100A1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution S100A1 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

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

    • Amino Acid Sequence

      MKHHHHHHAS GSELETAMET LINVFHAHSG KEGDKYKLSK KELKELLQTE LSGFLDAQKD VDAVDKVMKE LDENGDGEVD FQEYVVLVAA LTVACNNFFW ENS.

    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.

    S100A1 Human
  • View Data Sheet

    Name :

    Activin A Human Plant

    Description:

    Activin A Human Recombinant, Plant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-052

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). 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

      Sterile Filtered White 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

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

    • Amino Acid Sequence

      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 27.4 kDa.
      What is the source or expression system of Activin A Protein?
      Nicotinia

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

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

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

      What is the amino acid sequence of ACTIVIN A Protein?
      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

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

    • Serological Identification

      The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin A.

    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.

    Activin A Human Plant
  • View Data Sheet

    Name :

    PODXL Mouse

    Description:

    Podocalyxin-Like Mouse Recombinant

    Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.

    Product # :

    PRO-2310

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PODXL Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 391 amino acids (22-404a.a.) and having a molecular mass of 41.0kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). PODXL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Podocalyxin (PODXL) is a greatly glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein is involved in the regulation of both adhesion and cell morphology and cancer progression. PODXL functions as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Moreover, PODXL serves as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner.

    • Synonyms

      Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      HNGNETSTSA IKSSTVQSHQ SATTSTEVTT GHPVASTLAS TQPSNPTPFT TSTQSPSMPT STPNPTSNQS GGNLTSSVSE VDKTKTSSPS STAFTSSSGQ TASSGGKSGD SFTTAPTTTL GLINVSSQPT DLNTTSKLLS TPTTDNTTSP QQPVDSSPST ASHPVGQHTP AAVPSSSGST PSTDNSTLTW KPTTHKPLGT SEATQPLTSQ TPGITTLPVS TLQQSMASTV GTTTEEFTHL ISNGTPVAPP GPSTPSPIWA FGNYQLNCEP PIRPDEELLI LNLTRASLCE RSPLDEKEKL VELLCHSVKA SFKPAEDLCT LHVAPILDNQ AVAVKRIIIE TKLSPKAVYE LLKDRWDDLT EAGVSDMKLG KEGPPEVNED RFSLEHHHHH H.

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

    Podxl Mouse
  • View Data Sheet

    Name :

    SCGN Rat

    Description:

    Secretagogin Rat Recombinant

    SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.

    Product # :

    PRO-657

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    Description

    Secretagogin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 286 amino acids and having a molecular mass of 33.3 kDa. The Rat SCGN is fused to a 10 a.a. His tag at N-Terminus.The protein’s amino acids sequence is identical to UniProtKB/Swiss-Prot entry Q6R556.The Rat SCGN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
      Secretagogin plays a role in human non-functional pituitary adenomas.

    • Synonyms

      SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.

    • Physical Appearance

      Sterile 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

      Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKHHHHHHAS MDNAHRQTQA HLDAACFWQI WQRFDKDEKG YIKETELDAF FDDLLAKFGI EDTLMEENVQ KMKEQLMVGH DISKEGRILM KELASMFLSE DENFLLFFRL ETPLDNSVEF MQIWRKYDAD SSGFISAAEL SNFLRDLFLH HKKVISEAEL EEYTSTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DASSTEERKR DFEKIFAHYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCLGLKINP.

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    Scgn Rat
  • View Data Sheet

    Name :

    CYTH1 Human

    Description:

    Cytohesin 1 Human Recombinant

    Cytohesin 1, D17S811E, PH, SEC7 And Coiled-Coil Domain-Containing Protein 1, Pleckstrin Homology, Sec7 And Coiled-Coil Domains 1, SEC7 Homolog B2-1, PSCD1, SEC7, Homolog Of Secretory Protein SEC7, Cytoadhesin 1, CYTOHESIN-1, B2-1, Cytohesin-1.

    Product # :

    PRO-2215

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    Description

    CYTH1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (1-398 a.a) and having a molecular mass of 48.8kDa. CYTH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CYTH1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytohesin 1 also known as CYTH1 belongs to the PSCD family. CYTH1 is responsible for promoting guanine-nucleotide exchange on ARF1 and ARF5 and also promotes the activation of ARF factors by the replacement of GDP with GTP.

    • Synonyms

      Cytohesin 1, D17S811E, PH, SEC7 And Coiled-Coil Domain-Containing Protein 1, Pleckstrin Homology, Sec7 And Coiled-Coil Domains 1, SEC7 Homolog B2-1, PSCD1, SEC7, Homolog Of Secretory Protein SEC7, Cytoadhesin 1, CYTOHESIN-1, B2-1, Cytohesin-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 MGSMEEDDSY VPSDLTAEER QELENIRRRK QELLADIQRL KDEIAEVANE IENLGSTEER KNMQRNKQVA MGRKKFNMDP KKGIQFLIEN DLLKNTCEDI AQFLYKGEGL NKTAIGDYLG ERDEFNIQVL HAFVELHEFT DLNLVQALRQ FLWSFRLPGE AQKIDRMMEA FAQRYCQCNN GVFQSTDTCY VLSFAIIMLN TSLHNPNVKD KPTVERFIAM NRGINDGGDL PEELLRNLYE SIKNEPFKIP EDDGNDLTHT FFNPDREGWL LKLGGGRVKT WKRRWFILTD NCLYYFEYTT DKEPRGIIPL ENLSIREVED SKKPNCFELY IPDNKDQVIK ACKTEADGRV VEGNHTVYRI SAPTPEEKEE WIKCIKAAIS RDPFYEMLAA RKKKVSSTKR H.

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

    Cyth1 Human
  • View Data Sheet

    Name :

    SNCA 1-60 Human

    Description:

    Alpha Synuclein 1-60 Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-165

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    Description

    A-Synuclein 1-60 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 1-60 and contains the N-terminal amphipathic domain, produced in E.Coli is a single, non-glycosylated polypeptide chain of 60 amino acids having a molecular mass of 6.1kDa. The Recombinant Human a-Synuclein 1-60 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA 1-60 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK.

    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.

    Snca 1 60 Human
  • View Data Sheet

    Name :

    IP 10 Mouse

    Description:

    IP-10 Mouse Recombinant (CXCL10)

    Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.

    Product # :

    CHM-336

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    • sds-page

    Description

    IP-10 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8701 Dalton. The IP-10 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IP-10 was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 100.0-500.0 ng/ml.

    sds-page

    cxcl10 mouse sds-page - Product image 1

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.

    • Synonyms

      Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IP-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL10 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 IP-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IP-10 as a Reference Standard.

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    Ip 10 Mouse
  • View Data Sheet

    Name :

    Latexin Human

    Description:

    Latexin Human Recombinant

    LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    Product # :

    ENZ-407

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    Description

    Recombinant Human Latexin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids and having a molecular mass of 25.7kDa. Latexin is purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Latexin protein solution contains 20mM Tris-HCl, pH-7.5, 50mM NaCl and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.

    • Synonyms

      LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    • 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

      MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYRLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFTFEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDYTILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE.

    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.

    Latexin Human
  • View Data Sheet

    Name :

    CFL2 Human

    Description:

    Cofilin-2 Human Recombinant

    Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    Product # :

    PRO-912

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    Description

    CFL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-166 a.a.) and having a molecular mass of 20.9kDa.CFL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CFL2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CFL2 protein is a member of the actin-binding proteins ADF family which contains 1 ADF-H domain. Cofilin is a broadly distributed intracellular actin-modulating protein which binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Defects in the CFL2 gene are the cause of nemaline myopathy type 7 (NEM7).

    • Synonyms

      Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    • 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 MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL.

    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.

    Cfl2 Human
  • View Data Sheet

    Name :

    S100B Human, His

    Description:

    S100 Calcium Binding Protein B Human Recombinant, His Tag

    Protein S100-B, S100 calcium-binding protein B, S-100 protein subunit beta, S-100 protein beta chain, S100B, NEF, S100, S100beta.

    Product # :

    PRO-306

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    Description

    S100B Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 112 amino acids fragment (1-92) with a 20 amino acids N-terminal His tag and having a total molecular mass of 12.8kDa. The S100B is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100B (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100b is a member of the S100 family of proteins which are a family of EF-hand calcium binding proteins that exist mostly as dimers of the 20 currently identified individual S100 monomers. The S100B homodimer is expressed in cells of the central nervous system, glial cells and in certain peripheral cells e.g. Schwann cells, melanocytes, adipocytes and chondrocytes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21; however, S100b is located at 21q22.3. The determination of S100B in serum levels may be used to monitor the extent of brain injury and malignant melanoma. S100b proteins may have a role in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of the S100b gene are implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.

    • Synonyms

      Protein S100-B, S100 calcium-binding protein B, S-100 protein subunit beta, S-100 protein beta chain, S100B, NEF, S100, S100beta.

    • 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 MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE.

    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.

    S100B Human
  • View Data Sheet

    Name :

    GM-CSF Mouse

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Mouse Recombinant

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

    Product # :

    CYT-222

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14285.35 Dalton.GM-CSF Mouse is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GM-CSF Mouse was lyophilized with no additives.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GM-CSF 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 Granulocyte Macrophage Colony Stimulating Factor in sterile 20mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

      What is the molecular weight/Mw of GM-CSF MOUSE Protein?
      GM-CSF MOUSE Protein has a total Mw of 14.28kDa.

      What is the source or expression system of GM-CSF MOUSE Protein?
      Escherichia Coli.

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

      What is the Biological Activity of GM-CSF MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

      What is the amino acid sequence of GM-CSF MOUSE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.

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

      What is the endotoxin level for GM-CSF MOUSE Protein?
      The endotoxin level is minimal, GM-CSF MOUSE Protein was purified using conventional chromatography techniques.


    • Protein content

      GM-CSF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.765 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GM-CSF as a Reference Standard.

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

    Gm Csf Mouse
  • View Data Sheet

    Name :

    SERPINE1 Human

    Description:

    Plasminogen Activator Inhibitor-1 Human Recombinant

    PAI-1, PAI1, PLANH1, SERPINE1, PAIE, PLASMINOGEN ACTIVATOR INHIBITOR, BETA-MIGRATING ENDOTHELIAL-CELL-DERIVED TYPE.

    Product # :

    ENZ-357

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    Description

    SERPINE1 Human Recombinant fused to an N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 400 amino acids (24-402) and having a molecular mass of 45kDa.SERPINE1 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    50mM NaAc (pH 5.5), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The IC50 for this effect is less than 3nM, measured by its ability to inhibit uPA cleavage of the substrate Z-GGRAMC.

    More Info

    • Introduction

      Plasminogen activator inhibitor-1 is the principal inhibitor of tissue plasminogen activator(tPA) and uPA, the activators of plasminogenand hence fibrinolysis(the physiological breakdown of blood clots). It is a serine protease inhibitor(serpin) protein (SERPINE1). The other PAI, plasminogen activator inhibitor-2(PAI-2) is secreted by the placentaand only present in significant amounts during pregnancy. In addition, protease nexinacts as an inhibitor of tPA. SERPINE1, however, is the main inhibitor of the plasminogen activators.

    • Synonyms

      PAI-1, PAI1, PLANH1, SERPINE1, PAIE, PLASMINOGEN ACTIVATOR INHIBITOR, BETA-MIGRATING ENDOTHELIAL-CELL-DERIVED TYPE.

    • 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

      MGSSHHHHHH SSGLVPRGSH MVHHPPSYVA HLASDFGVRV FQQVAQASKD RNVVFSPYGVASVLAMLQLT TGGETQQQIQ AAMGFKIDDK GMAPALRHLY KELMGPWNKD EISTTDAIFVQRDLKLVQGF MPHFFRLFRS TVKQVDFSEV ERARFIINDW VKTHTKGMIS NLLGKGAVDQLTRLVLVNAL YFNGQWKTPF PDSSTHRRLF HKSDGSTVSV PMMAQTNKFN YTEFTTPDGHYYDILELPYH GDTLSMFIAA PYEKEVPLSA LTNILSAQLI SHWKGNMTRL PRLLVLPKFSLETEVDLRKP LENLGMTDMF RQFQADFTSL SDQEPLHVAQ ALQKVKIEVN ESGTVASSSTAVIVSARMAP EEIIMDRPFL FVVRHNPTGT VLFMGQVMEP.

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    Serpine1 Human Recombinant
  • View Data Sheet

    Name :

    PTPN7 Human

    Description:

    Protein Tyrosine Phosphatase Non Receptor Type-7 Human Recombinant

    Protein tyrosine phosphatase non-receptor type 7, HEPTP, LC-PTP, Hematopoietic protein-tyrosine phosphatase, Protein-tyrosine phosphatase LC-PTP, PTPNI, LPTP, BPTP-4, dual specificity phosphatase 1, protein-tyrosine phosphatase non-receptor-type, stress induced, EC 3.1.3.48.

    Product # :

    PKA-025

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    Description

    PTPN7 Human Recombinant produced in E. coli is a single polypeptide chain containing 384 amino acids (1-360) and having a molecular mass of 43.1kDa.PTPN7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PTPN7 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PTPN7 performs specifically on tyrosine-phosphorylated MAPK1. PTPN7 takes part in the regulation of signal transduction and T and B-lymphocyte development.

    • Synonyms

      Protein tyrosine phosphatase non-receptor type 7, HEPTP, LC-PTP, Hematopoietic protein-tyrosine phosphatase, Protein-tyrosine phosphatase LC-PTP, PTPNI, LPTP, BPTP-4, dual specificity phosphatase 1, protein-tyrosine phosphatase non-receptor-type, stress induced, EC 3.1.3.48.

    • 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 MGSHMVQAHG GRSRAQPLTL SLGAAMTQPP PEKTPAKKHV RLQERRGSNV ALMLDVRSLG AVEPICSVNT PREVTLHFLR TAGHPLTRWA LQRQPPSPKQ LEEEFLKIPS NFVSPEDLDI PGHASKDRYK TILPNPQSRV CLGRAQSQED GDYINANYIR GYDGKEKVYI ATQGPMPNTV SDFWEMVWQE EVSLIVMLTQ LREGKEKCVH YWPTEEETYG PFQIRIQDMK ECPEYTVRQL TIQYQEERRS VKHILFSAWP DHQTPESAGP LLRLVAEVEE SPETAAHPGP IVVHCSAGIG RTGCFIATRI GCQQLKARGE VDILGIVCQL RLDRGGMIQT AEQYQFLHHT LALYAGQLPE EPSP

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    Ptpn7 Human
  • View Data Sheet

    Name :

    S100P Human

    Description:

    S100 Calcium Binding Protein P Human Recombinant

    Protein S100-P, S100 calcium-binding protein P, S100P, S100E, MIG9.

    Product # :

    PRO-425

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    Description

    The Recombinant Human S100P has a molecular mass of 10.4 kDa containing 95 amino acid residues of the human S100P.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Phosphate buffer pH7.2, 0.1M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100P was originally described as a placental protein of 95 amino acid residues shares about 50% sequence identity with the brain S100 proteins alpha and beta.
      S100 proteins are small dimeric members of the EF-hand superfamily of Ca(2+) binding proteins thought to participate in mediating intracellular Ca(2+) signals by binding to and thereby regulating target proteins in a Ca(2+)-dependent manner. S100P in addition to binding Ca2+, also binds Zn2+ and Mg2+. S100P gene is located on chromosome 4p16.
      S100P is dysregulated in the androgen-independent prostate cancer cell lines LNCaP-R, DU145, and PC3 and may play a role in the etiology of prostate cancer.
      In ductal hyperplasias, in situ and invasive ductal carcinoma, but not in the normal tissues, S100P overexpression is an early event that might play an important role in the immortalization of human breast epithelial cells in vitro and tumor progression in vivo.
      In NIH3T3 cells, the expression of S100P led to the presence of S100P in the culture medium, increased cellular proliferation, and enhanced survival following detachment from the culture substrate or after exposure to the chemotherapeutic agent 5-flurouracil. The proliferation and survival effects of S100P expression were duplicated in a time- and concentration-dependent manner by extracellular addition of purified S100P to wild-type NIH3T3 cells and correlated with the activation of Erks and NFB.
      To determine the mechanisms involved in these effects, we tested the hypothesis that S100P activated RAGE (Receptor for Activated Glycation End-Products). It was found that S100P coimmunoprecipitated with RAGE. Furthermore, the effects of S100P on cell signaling, proliferation and survival were blocked by agents that interfere with RAGE including administration of an amphoterin derived peptide known to antagonize RAGE activation, anti-RAGE antibodies and by expression of a dominant negative RAGE. These data suggest that S100P can act in an autocrine manner via RAGE to stimulate cell proliferation and survival.

    • Synonyms

      Protein S100-P, S100 calcium-binding protein P, S100P, S100E, MIG9.

    • 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

      Add deionized H2O and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MTELEAAMGM IIDVFSRYSG SEGSTQTLTK GELKVLMEKE LPGFLQSGKD KDAVDKLLKD LDANGDAQVD FSEFIVFVAA ITSACHKYFE KAGLK.

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    S100P Human
  • View Data Sheet

    Name :

    FGF23 Human

    Description:

    Fibroblast Growth Factor-23 Human Recombinant

    Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    Product # :

    CYT-020

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    Description

    Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa. The FGF-23 is and purified by chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF-23 protein (0.5mg/ml) was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

    More Info

    • Introduction

      FGF-23 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-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.

    • Synonyms

      Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 FGF-23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.

    • Background

      Before it was discovered in 2000, there was a hypothesis that a similar type of protein existed that performed many of the functions we see in FGF23. This was originally referred to as phosphatonin. Various effects were described and noted by researchers including inhibition of production and inhibition of secretion of parathyroid hormone. Derived from the bone Fibroblast Growth Factor 23 is a phosphaturic hormone. It increases phosphate excretion when acting on the kidney and also suppresses the biosynthesis of 1,25(OH)2D3.

      Mechanism
      Despite various research studies into the topic, many of the mechanisms for the regulations of FGF23 production remain a mystery to the scientific community. While we know that mutations in PHEX, ENPP1 and DMP1 result in the increased expression of FGF23, it is unclear why this occurs. This also means that currently, it is not possible to regulate the production of FGF23 either. We also do not know how signals from FGF23 regulate vitamin D metabolism. However, understanding these types of mechanisms could offer information needed to provide better treatment for deranged bone and mineral metabolism.

      Interactions
      Molecular interactions involving FGF-23, vitamin D and klotho do provide the solution needed to regulate phosphate levels within the body. Furthermore, an interaction between Vitamin D and FGF3 can have an impact on renal phosphate balance. As well as this, when in the presence of klotho, FGF3 does actually increase bioactivity and begins to change systemic phosphate homeostasis.

      Function
      Based on research it seems that the main function for FGF23 is the regulation of phosphate concentration in plasma. It seems to be secreted from the osteocytes due to elevated levels . When acting upon the kidneys, the hormone reduces the expression of NPT2. This is a sodium-phosphate cotransporter found in the proximal tube.
      As such, it appears as though FGF23 is able to reduce the reabsorption, all the while maxing the excretion of phosphate. It has also been suggested that the hormone is able to suppress 1-alpha-hydroxylase. If this is the case, it can limit its potential to activate vitamin D and thus impair the ability for calcium absorption.

      Structure
      FGF243 is located on the chromosome 12. It is composed of three exons. The crystal structure of FGF23 is completely different from the common conformation typically adopted by paracrine-acting FGFs. Instead, there is a conformation of the HPR region between beta strands 10 and 12. As well as this, there is a cleft between the other HPR-binding region, the beta1-beta12 loop and this one. This comes before a direct interaction between HPR sulfate and FGF23s backbone atoms. Due to this, endocrine function is benefitted and HPR-binding affinity is reduced for the lipangs.
      Certain mutations that cause the protein to be completely resistant to proteolytic cleavage does trigger a surge in activity of the protein and the renal phosphate loss typically found in certain human diseases including hypophosphatemic rickets.
      Studies have also revealed that FGF23 is overproduced in certain tumors including phosphaturic mesenchymal tumors. Furthermore a reduced level of activity for this protein is believed to lead to higher phosphate levels and familial tumor calcinosis clinical syndrome.

      What is the molecular weight/Mw of FGF23 HUMAN Protein?
      FGF23 HUMAN Protein has a total Mw of 22.5kDa.

      What is the source or expression system of FGF23 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FGF23 HUMAN Protein?
      FGF23 HUMAN Protein is >95X% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF23 HUMAN Protein?
      The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

      What is the amino acid sequence of FGF23 HUMAN Protein?
      MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.

      What applications can FGF23 HUMAN Protein be used in?
      FGF23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF23 HUMAN Protein?
      The endotoxin level is minimal, FGF23 HUMAN Protein was purified using conventional chromatography techniques.

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    Fgf23 Human
  • View Data Sheet

    Name :

    PHOSPHO2 Human

    Description:

    Phosphatase Orphan-2 Human Recombinant

    Pyridoxal phosphate phosphatase PHOSPHO2, PHOSPHO2.

    Product # :

    ENZ-231

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    Description

    PHOSPHO2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (1-241) and having a molecular mass of 30.3kDa.PHOSPHO2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHOSPHO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pyridoxal phosphate phosphatase PHOSPHO2, orphan 2 (PHOSPHO2) is a member of the haloacid dehalogenase (HAD) superfamily. Phosphatase has an elevated activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). PHOSPHO 1, a phosphoethanolamine/phosphocholine phosphatase, is upregulated in mineralizing cells and is believed to be implicated in the production of inorganic phosphate for bone mineralization. PHOSPHO2 is a recognized phosphatase sharing a 42% sequence identity with PHOSPHO1. PHOSPHO1 and PHOSPHO2 are especially similar, however surprisingly recombinant PHOSPHO2 hydrolyses phosphoethanolamine and phosphocholine comparatively inadequately.

    • Synonyms

      Pyridoxal phosphate phosphatase PHOSPHO2, PHOSPHO2.

    • 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 MGSHMKILLV FDFDNTIIDD NSDTWIVQCA PNKKLPIELR DSYRKGFWTE FMGRVFKYLG DKGVREHEMK RAVTSLPFTP GMVELFNFIR KNKDKFDCII ISDSNSVFID WVLEAASFHD IFDKVFTNPA AFNSNGHLTV ENYHTHSCNR CPKNLCKKVV
      LIEFVDKQLQ QGVNYTQIVY IGDGGNDVCP VTFLKNDDVA MPRKGYTLQK TLSRMSQNLE PMEYSVVVWS SGVDIISHLQ FLIKD.

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    Phospho2 Human
  • View Data Sheet

    Name :

    S100A15 Mouse

    Description:

    S100 Calcium Binding Protein A15 Mouse Recombinant

    Protein S100-A7A, S100 calcium-binding protein A15A, S100 calcium-binding protein A7A.

    Product # :

    PRO-1145

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    Description

    S100A15 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (1-108) and having a molecular mass of 15.0 kDa.S100A15 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The S100A15 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mouse S100A15 is a protein of 104 amino acids with an expected molecular weight of 12,870 Dalton having 2 EF-hand calcium binding sites. The S100A15 expression is upregulated in cultured keratinocytes stimulated to differentiate by calcium or phorbol esters. S100A15 is expressed in the skin and keratinocytes.

    • Synonyms

      Protein S100-A7A, S100 calcium-binding protein A15A, S100 calcium-binding protein A7A.

    • 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 MGSHMPDTPV EDSLFQIIHC FHHYAAREGD KETLSLEELK ALLLDSVPRF MDTLGRRQPY YITELFRAAD KNKDNQICFD EFLYILGKLV KDYHLQFHRQ LCAHYCTEHS LY.

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    S100A15 Mouse
  • View Data Sheet

    Name :

    S100A14 Human

    Description:

    S100 Calcium Binding Protein A14 Human Recombinant

    Protein S100-A14, S100 calcium-binding protein A14, S114, S100A14, S100A15, BCMP84.

    Product # :

    PRO-154

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    Description

    S100A14 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids (1-104 a.a.) and having a molecular mass of 13.8kDa. The S100A14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A14 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A14 belongs to a subfamily of proteins related by EF-hand Ca2+ binding protein superfamily. The extracellular functions of the S100 family include the ability to boost neurite outgrowth, involvement in inflammation, and motility of tumor cells. S100A14 contains 2 EF-hand Ca2+-binding domains, a myristoylation motif, a glycosylation site, and a number of potential protein kinase phosphorylation sites. S100A14 is expressed at high levels in the colon and at moderate levels in the thymus, kidney, liver, small intestine, and lung.

    • Synonyms

      Protein S100-A14, S100 calcium-binding protein A14, S114, S100A14, S100A15, BCMP84.

    • 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 MGQCRSANAE DAQEFSDVER AIETLIKNFH QYSVEGGKET LTPSELRDLV TQQLPHLMPS NCGLEEKIAN LGSCNDSKLE FRSFWELIGE AAKSVKLERP VRGH.

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    S100A14 Human
  • View Data Sheet

    Name :

    TACSTD2 Human

    Description:

    Tumor-Associated Calcium Signal Transducer 2 Human Recombinant

    EGP-1, EGP1, GA733-1, GA7331, GP50, M1S1, TROP2, Cell surface glycoprotein Trop-2, Membrane component chromosome 1 surface marker 1, Pancreatic carcinoma marker protein GA733-1.

    Product # :

    PRO-157

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    Description

    TACSTD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (31-274a.a.) and having a molecular mass of 29.9kDa. TACSTD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TACSTD2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor-associated calcium signal transducer 2 (TACSTD2), is a member of to the EPCAM family. TACSTD2 is an intronless gene which encodes a carcinoma-associated antigen. TACSTD2 may act as a growth factor receptor and as a cell surface receptor that transduces calcium signals. Mutations of TACSTD2 have been associated with gelatinous drop-like corneal dystrophy.

    • Synonyms

      EGP-1, EGP1, GA733-1, GA7331, GP50, M1S1, TROP2, Cell surface glycoprotein Trop-2, Membrane component chromosome 1 surface marker 1, Pancreatic carcinoma marker protein GA733-1.

    • 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 MGSQDNCTCP TNKMTVCSPD GPGGRCQCRA LGSGMAVDCS TLTSKCLLLK ARMSAPKNAR TLVRPSEHAL VDNDGLYDPD CDPEGRFKAR QCNQTSVCWC VNSVGVRRTD KGDLSLRCDE LVRTHHILID LRHRPTAGAF NHSDLDAELR RLFRERYRLH PKFVAAVHYE QPTIQIELRQ NTSQKAAGDV DIGDAAYYFE RDIKGESLFQ GRGGLDLRVR GEPLQVERTL IYYLDEIPPK FSMKRLT.

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    Tacstd2 Human
  • View Data Sheet

    Name :

    SNCA NACP112 Human

    Description:

    Alpha Synuclein NACP112 Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-162

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    Description

    A-Synuclein NACP112 Human Recombinant which is an alternatively spliced (103-129) form of a-Synuclein, produced in E.Coli is a single, non-glycosylated polypeptide chain of 112 amino acids having a molecular mass of 11.3kDa. The Recombinant Human a-Synuclein NACP112 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA NACP112 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKEGYQDYEP EA.

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    Snca Nacp112 Human
  • View Data Sheet

    Name :

    Hexarelin

    Description:

    Hexarelin

    Product # :

    HOR-288

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    • More Info

    Description

    Hexarelin has 7 amino acids H-His-D-2-Methyl-Trp-Ala-Trp-D-Phe-Lys-NH2 and having a molecular weight of 887 Dalton. The Molecular Formula is C47H58N12O6.

    Formulation

    The Hexarelin peptide was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Hexarelin stimulates GH secretion. Hexarelin is more resistant to proteolytic degradation than GHRP-6.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) powder.

    • Stability

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

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

    Hexarelin
  • View Data Sheet

    Name :

    Anaplasma p44

    Description:

    Anaplasma phagocytophilum p44 Recombinant

    Product # :

    PRO-2566

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Recombinant Anaplasma p44 produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 49kDa. Anaplasma p44 is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Anaplasma p44 is supplied at a 20mM HEPES buffer pH-8.0, 250mM NaCl and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Anaplasma p44 which belongs to the outer membrane antigen superfamily (OMP1/Msp2/p44), is a serodiagnostic antigen for HGA. Anaplasma p44 allows the bacterium to adhere to the host cell and prevents host immune surveillance.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgG- and IgM-type human antibodies. 2. Immunodot test with positive/negative samples.

    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.

    Anaplasma Phagocytophilum P44
  • View Data Sheet

    Name :

    Atosiban

    Description:

    Atosiban

    Product # :

    HOR-239

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • formulation
    • purity
    • More Info
    • HPLC, MS

    Description

    Atosiban also called ADH (Anti-Diuretic Hormone) has a molecular formula of C43H67N11O12S2, 3-Mercaptopropionyl-D-Tyr(ET)-Ile-Thr-Asn-Cys-Pro-Orn-Gly-NH2 having a Mw of 994.2 Dalton.

    Formulation

    The Atosiban peptide was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by analysis by RP-HPLC.

    HPLC, MS

    atosiban hplc - Product image 1
    atosiban hplc - Product image 2

    More Info

    • Introduction

      Atosiban is the first oxytocin antagonist to be specifically developed for the treatment of preterm labor. Atosiban has a specific mode of action, inhibiting oxytocin-induced uterine contractions by blocking oxytocin receptors in the uterus. Extensive clinical investigations have shown Atosiban to be at least as effective as current tocolytic agents. In addition, due to its novel and specific mode of action, Atosiban has a markedly improved maternal side effects profile compared with conventional therapies.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Atosiban
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