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Search results

1000 results found for “Leptin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    UCN3 Human

    Description:

    Urocortin 3 Human Recombinant

    Stresscopin, urocortin-iii.

    Product # :

    HOR-056

    Price :

    Quantity :

    Shipping Method :

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    • source
    • formulation
    • purity
    • More Info

    Description

    The UCN3Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCN3His-Tagged Fusion Protein, produced in E. coli, is a 20kDa protein containing 161 amino acid residues of the UCN3Human, 1-161 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Stresscopin, urocortin-iii.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized UCN3at -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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      Urocortin 3 also known as UCN3 is a part of the corticotropin-releasing factor (CRF) family of peptides, which are involved in metabolism, stress response and neuroendocrine regulation. UCN3 exerts its biological effects through interactions with CRFR2. UCN3 takes a main part in mediating few important biological processes, specially those associated with energy metabolism, stress response and the regulation of the hypothalamic-pituitary-adrenal (HPA) axis. UCN3 expressed mainly in the brain in areas such as the hypothalamus, as well as in peripheral tissues, including the heart and adipose tissue.

      What is the molecular weight/Mw of UCN3 HUMAN Protein?
      UCN3 HUMAN Protein has a total Mw of 20kDa.

      What is the source or expression system of UCN3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of UCN3 HUMAN Protein?
      UCN3 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of UCN3 HUMAN Protein?
      The biological functionality of UCN3 HUMAN Protein will be determined in the future.

      What applications can UCN3 HUMAN Protein be used in?
      UCN3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for UCN3 HUMAN Protein?
      The endotoxin level is minimal, UCN3 HUMAN Protein was purified using conventional chromatography techniques.

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

    Ucn3 Human
  • View Data Sheet

    Name :

    WIF1 Mouse

    Description:

    WNT Inhibitory Factor 1 Mouse Recombinant

    Wnt inhibitory factor 1, WIF-1, Wif1.

    Product # :

    PRO-2248

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    WIF1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 359 amino acids (29-379a.a.) and having a molecular mass of 39.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).WIF1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    WIF1 protein solution (1mg/ml) contains 20mM MES (pH5.5), 1mM DTT, 1mM PMSF and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.

    • Synonyms

      Wnt inhibitory factor 1, WIF-1, Wif1.

    • 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

      GQPPEESLYL WIDAHQARVL IGFEEDILIV SEGKMAPFTH DFRKAQQRMP AIPVNIHSMN FTWQAAGQAE YFYEFLSLRS LDKGIMADPT VNVPLLGTVP HKASVVQVGF PCLGKQDGVA AFEVNVIVMN SEGNTILRTP QNAIFFKTCQ QAECPGGCRN GGFCNERRVC ECPDGFYGPH
      CEKALCIPRC MNGGLCVTPG FCICPPGFYG VNCDKANCST TCFNGGTCFY PGKCICPPGL EGEQCELSKC PQPCRNGGKC IGKSKCKCPK GYQGDLCSKP VCEPGCGAHG TCHEPNKCQC REGWHGRHCN KRYGASLMHA PRPAGAGLER HTPSLKKAED RRDPPESNYI WVEHHHHHH.

    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.

    Wif1 Mouse
  • View Data Sheet

    Name :

    CRHBP Human

    Description:

    Corticotropin Releasing Hormone Binding Protein Human Recombinant

    Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.

    Product # :

    HOR-267

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • More Info

    Description

    CRHBP Human Recombinant is a 34.58 kDa protein containing 308 aa and fused to a 10 aa N-Terminal His-tag. CRHBP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CRHBP Human was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.

    More Info

    • Introduction

      CRH is a powerful stimulator of synthesis and secretion of preopiomelanocortin-derived peptides. CRH concentration in the human peripheral circulation is usually low. The concentration rises during pregnancy and fall back quickly after parturition. Maternal plasma CRH most likely originates from the placenta. Human plasma has a CRH-binding protein that inactivates CRH and can inhibit inappropriate pituitary-adrenal stimulation in pregnancy.

    • Synonyms

      Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.

    • Physical Appearance

      Filtered white lyophilized powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS YLELREAADY DPFLLFSANL KRELAGEQPY RRALRCLDML SLQGQFTFTA DRPQLHCAAF FISEPEEFIT IHYDQVSIDC QGGDFLKVFD GWILKGEKFP SSQDHPLPSA ERYIDFCESG LSRRSIRSSQ NVAMIFFRVH EPGNGFTLTI KTDPNLFPCN VISQTPNGKF TLVVPHQHRN CSFSIIYPVV IKISDLTLGH VNGLQLKKSS AGCEGIGDFV ELLGGTGLDP SKMTPLADLC YPFHGPAQMK VGCDNTVVRM VSSGKHVNRV TFEYRQLEPY ELENPNGNSI GEFCLSGL YLELREAADY DPFLLFSANL KRELAGEQPY RRALRCLDML SLQGQFTFTA DRPQLHCAAF FISEPEEFIT IHYDQVSIDC QGGDFLKVFD GWILKGEKFP SSQDHPLPSA ERYIDFCESG LSRRSIRSSQ NVAMIFFRVH EPGNGFTLTI KTDPNLFPCN VISQTPNGKF TLVVPHQHRN CSFSIIYPVV IKISDLTLGH VNGLQLKKSS AGCEGIGDFV ELLGGTGLDP SKMTPLADLC YPFHGPAQMK VGCDNTVVRM VSSGKHVNRV TFEYRQLEPY ELENPNGNSI GEFCLSGL

    • Applications

      ELISA, Western blotting

    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.

    Crhbp Human
  • View Data Sheet

    Name :

    Periostin Human, HEK

    Description:

    Periostin Human Recombinant, HEK

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

    Product # :

    CYT-835

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Periostin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn22-Gln836) containing a total of 821 amino acids, having a calculated molecular mass of 91.8kDa and fused to a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    Periostin was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% trehalose.

    Purity

    Greater than 38.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      NNHYDKILAH SRIRGRDQGP NVCALQQILG TKKKYFSTCK NWYKKSICGQ KTTVLYECCP GYMRMEGMKG CPAVLPIDHV YGTLGIVGAT TTQRYSDASK LREEIEGKGS FTYFAPSNEA WDNLDSDIRR GLESNVNVEL LNALHSHMIN KRMLTKDLKN GMIIPSMYNN LGLFINHYPN GVVTVNCARI IHGNQIATNG VVHVIDRVLT QIGTSIQDFI EAEDDLSSFR AAAITSDILE ALGRDGHFTL FAPTNEAFEK LPRGVLERIM GDKVASEALM KYHILNTLQC SESIMGGAVF ETLEGNTIEI GCDGDSITVN GIKMVNKKDI VTNNGVIHLI DQVLIPDSAK QVIELAGKQQ TTFTDLVAQL GLASALRPDG EYTLLAPVNN AFSDDTLSMD QRLLKLILQN HILKVKVGLN ELYNGQILET IGGKQLRVFV YRTAVCIENS CMEKGSKQGR NGAIHIFREI IKPAEKSLHE KLKQDKRFST FLSLLEAADL KELLTQPGDW TLFVPTNDAF KGMTSEEKEI LIRDKNALQN IILYHLTPGV FIGKGFEPGV TNILKTTQGS KIFLKEVNDT LLVNELKSKE SDIMTTNGVI HVVDKLLYPA DTPVGNDQLL EILNKLIKYI QIKFVRGSTF KEIPVTVYTT KIITKVVEPK IKVIEGSLQP IIKTEGPTLT KVKIEGEPEF RLIKEGETIT EVIHGEPIIK KYTKIIDGVP VEITEKETRE ERIITGPEIK YTRISTGGGE TEETLKKLLQ EEVTKVTKFI EGGDGHLFED EEIKRLLQGD TPVRKLQANK KVQGSRRRLR EGRSQHHHHH 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.

    Periostin Human Hek
  • View Data Sheet

    Name :

    Cagrilintide

    Description:

    Cagrilintide

    Product # :

    HOR-059

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    Description

    Cagrilintide is a synthetic single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 4409 Dalton and a Molecular formula of C194H312N54O59.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      (Eicosanedioic acid-γ-Glu)-Lys-CysAsn-Thr-Ala-Thr-Cys-Ala-Thr-Gln-Arg-Leu-Ala-Glu-Phe-Leu-Arg-HisSer-Ser-Asn-Asn-Phe-Gly-Pro-Ile-Leu-Pro-Pro-Thr-Asn-Val-Gly-SerAsn-Thr-Pro-NH2 (Disulfide bridge:Cys3-Cys8).

    • Background

      Cagrilintide plays a role as a pioneering long-acting amylin analogue and integrates into the fixed-dose combination CagriSema (Cagrilintide + Semaglutide). Unlike GLP-1 agonists, Cagrilintide mimics amylin, a hormone co-secreted with insulin takes part in regulating satiety and slows gastric emptying through brainstem pathways.

    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.

    Cagrilintide
  • View Data Sheet

    Name :

    METRN Mouse

    Description:

    Meteorin Mouse Recombinant

    Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.

    Product # :

    PRO-2241

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    Description

    METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.

    • Synonyms

      Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.

    • 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

      GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD HHHHHH.

    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.

    Metrn Mouse
  • View Data Sheet

    Name :

    RELM b Human

    Description:

    RELM-Beta Human Recombinant

    Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    Product # :

    CYT-780

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    Description

    RELM-b Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 19kDa. RELM-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RELM-b was lyophilized from a solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
      RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
      The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.

    • Synonyms

      Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized RELM-b in sterile 0.1% TFA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQCSLDSVMD KKIKDVLNSL EYSPSPISKK LSCASVKSQG RPSSCPAGMA VTGCACGYGC GSWDVQLETT CHCQCSVVDW TTARCCHLT.

    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.

    Relm B Human
  • View Data Sheet

    Name :

    NEFL Bovine

    Description:

    Neurofilament Light Bovine

    Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    Product # :

    PRO-2786

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    Description

    NEFL Bovine having a calculated molecular mass of 68 kDa, pI-5.0.

    Source

    Bovine spinal cord.

    Formulation

    NEFL was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized NEFL between 2-8°C, do not freeze. Upon reconstitution NEFL should be stored at -20°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Background

      Neurofilament light chain (NEFL) is a critical component of the neuronal cytoskeleton, primarily found in neurons of the central and peripheral nervous systems. While extensive research has been conducted on NEFL in human and rodent models, the study of NEFL in bovine nervous tissues is an emerging area with potential for advancing our understanding of neuronal biology in larger mammals and its applications in veterinary medicine and neurobiology.

      Bovine nervous tissues, such as the brain and spinal cord, are of particular interest due to their relevance in cattle health and the food industry. This research aims to provide a comprehensive exploration of NEFL in bovine nervous tissues, elucidating its functions, structural significance, and potential applications.

      The primary objective of this research is to elucidate the role of NEFL in bovine nervous tissues, particularly in maintaining the structural integrity of neurons and axons. In vitro and ex vivo experiments, utilizing bovine neuronal cell cultures and tissue specimens, will be conducted to investigate how NEFL contributes to neuronal morphology, axonal transport, and neuronal resilience. Understanding these mechanisms is fundamental for deciphering the complexities of neuronal biology in bovine species.

      The second objective is to assess the relevance of bovine NEFL in veterinary medicine. Studies involving bovine models will be conducted to evaluate the impact of NEFL mutations or variations on neuronal health, disease susceptibility, and neurodegenerative conditions. These investigations may provide valuable insights into potential applications in cattle health and the development of diagnostic tools for neurological disorders.

      The third objective is to explore the potential applications of bovine NEFL in neurobiology and biotechnology. Research will investigate the use of bovine NEFL-expressing cells as models for studying neuronal-related diseases and for developing tissue engineering approaches for veterinary medicine and biotechnology.

      By delving into the functions and roles of NEFL in bovine nervous tissues, this research aims to expand our knowledge of neuronal biology, its implications for veterinary medicine, and its potential applications in neurobiology and cattle health

    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.

    Nefl Bovine
  • View Data Sheet

    Name :

    KRT18 Bovine

    Description:

    Cytokeratin-18 Bovine

    Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    Product # :

    PRO-2785

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    Description

    KRT18 Bovine having a calculated molecular mass of 45 kDa, pI-5.4.

    Source

    Bovine liver.

    Formulation

    KRT18 was lyophilized from a 1mg/ml solution containing 30mM Tris/HCI pH 8, 9M urea, 2mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized KRT18 between 2-8°C, do not freeze. Upon reconstitution KRT18 should be stored at -20°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized KRT18 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Keratin-18 (K18) is an intermediate filament protein that plays a vital role in maintaining the structural integrity of epithelial cells. Extensive research has been conducted on K18 in human and murine models, shedding light on its functions and implications for various epithelial tissues.

      However, the study of K18 in bovine tissues is an emerging area with potential for advancing our understanding of epithelial cell biology and its applications in veterinary medicine and biotechnology. Bovine tissues, such as the liver and gastrointestinal tract, are of particular interest due to their relevance in cattle production and food safety.

      This research aims to provide a comprehensive exploration of K18 in bovine tissues, elucidating its functions, structural significance, and potential applications.
      The primary objective of this research is to elucidate the role of K18 in bovine tissues, particularly in maintaining the structural integrity of epithelial cells.

      In vitro and ex vivo experiments, utilizing bovine epithelial cell cultures and tissue specimens, will be conducted to investigate how K18 contributes to cellular morphology, cytoskeletal organization, and tissue resilience. Understanding these mechanisms is fundamental for deciphering the complexities of epithelial cell biology in bovine species.
      The second objective is to assess the relevance of bovine K18 in veterinary medicine and cattle production. Studies involving bovine models will be conducted to evaluate the impact of K18 mutations or variations on tissue health, disease susceptibility, and meat quality. These investigations may provide valuable insights into potential applications in cattle breeding and food safety.


      The third objective is to explore the potential biotechnological applications of bovine K18. Research will investigate the use of K18-expressing bovine cells as models for studying epithelial-related diseases and for developing tissue engineering approaches for veterinary medicine and biotechnology.
      By delving into the functions and roles of K18 in bovine tissues, this research aims to expand our knowledge of epithelial cell biology, its implications for veterinary medicine, and its potential applications in biotechnology and cattle production.

    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.

    Keratin 18 Bovine
  • View Data Sheet

    Name :

    GH Antagonist Ovine

    Description:

    Growth Hormone Antagonist Ovine Recombinant

    GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-215

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    Description

    Somatotropin Ovine Antagonist Recombinant G119R produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 22 kDa. The Somatotropin Ovine Antagonist Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045M NaHCO3, pH 9.

    Purity

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

    Biological Activity

    GH G119R acts as antagonist using an in vitro bioassay in PDF-P1 3B9 cells stably transfected with rabbit GH receptors. It is capable of forming a 1:1 complex with the recombinant ovine growth hormone receptor extracellular domain (ECD) and binds to this ECD with affinity similar the the wild type oGH.

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH G119R although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 GH G119R in 0.4% NaHCO3 or water adjusted to pH 9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

    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.

    Gh Antagonist Ovine
  • View Data Sheet

    Name :

    LGALS14 Human

    Description:

    Galectin-14 Human Recombinant

    Placental protein 13-like, Charcot-Leyden crystal protein 2, CLC2, Galectin-14, Gal-14, LGALS14, PPL13, MGC22235.

    Product # :

    CYT-003

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    Description

    LGALS14 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids (1-139 a.a.) and having a molecular mass of 18.5kDa. The LGALS14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LGALS14 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Galectin14, aka LGALS14, is a member of the galectin family of carbohydrate binding proteins. Galectin family members contain one or two carbohydrate recognition domains, which can bind beta-galactoside. The LGALS14 gene is predominantly expressed in the placenta. LGALS14 is expressed intracellularly in the placenta and eosinophils and is released by eosinophils following allergen stimulation. LGALS14 may be involved in the development of allergic inflammation.

    • Synonyms

      Placental protein 13-like, Charcot-Leyden crystal protein 2, CLC2, Galectin-14, Gal-14, LGALS14, PPL13, MGC22235.

    • 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 MGSMSSLPVP YTLPVSLPVG SCVIITGTPI LTFVKDPQLE VNFYTGMDED SDIAFQFRLH FGHPAIMNSR VFGIWRYEEK CYYLPFEDGK PFELCIYVRH KEYKVMVNGQ RIYNFAHRFP PASVKMLQVL RDISLTRVLI SD.

    • Background

      What is the molecular weight/Mw of LGALS14 HUMAN Protein?
      LGALS14 HUMAN Protein has a total Mw of 18.5kDa.

      What is the source or expression system of LGALS14 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS14 HUMAN Protein?
      LGALS14 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS14 HUMAN Protein?
      The biological functionality of LGALS14 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of LGALS14 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMSSLPVP YTLPVSLPVG SCVIITGTPI LTFVKDPQLE VNFYTGMDED SDIAFQFRLH FGHPAIMNSR VFGIWRYEEK CYYLPFEDGK PFELCIYVRH KEYKVMVNGQ RIYNFAHRFP PASVKMLQVL RDISLTRVLI SD.
      What applications can LGALS14 HUMAN Protein be used in?
      LGALS14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS14 HUMAN Protein?
      The endotoxin level is minimal, LGALS14 HUMAN Protein was purified using conventional chromatography techniques.


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

    Lgals14 Human
  • View Data Sheet

    Name :

    Activin-A Mouse

    Description:

    Activin-A Mouse Recombinant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-146

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    Description

    Active form Activin-A Murine 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

    Mouse Activin-A 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 cytoxicity of MPC-11 cells and was found to be 8.8ng/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

      Murine 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

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 26.2 kDa.

      What is the source or expression system of Activin A Protein?
      Ecoli

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

      What is the Biological Activity of Activin A Protein?
      Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000 units/mg.

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

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

    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 Mouse
  • View Data Sheet

    Name :

    SOSTDC1 Human

    Description:

    Sclerostin Domain Containing 1 Human Recombinant

    Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    Product # :

    PRO-426

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    Description

    SOSTDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (24-206 a.a) and having a molecular mass of 23kDa.SOSTDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOSTDC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sclerostin Domain Containing 1 (SOSTDC1) belongs to the sclerostin family and an N-glycosylated, secreted protein with a C-terminal cystine knot-like domain. The SOSTDC1 protein acts as a bone morphogenetic protein (BMP) antagonist. Specifically, SOSTDC1 directly associates with BMPs, prohibiting them from binding their receptors, thus regulating BMP signaling throughout cellular proliferation, differentiation, and programmed cell death. SOSTDC1 may also be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and hinders TGF-beta signaling. In addition, SOSTDC1 directly antagonizes the activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner.

    • Synonyms

      Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    • 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 MGSFKNDATE ILYSHVVKPV PAHPSSNSTL NQARNGGRHF SNTGLDRNTR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLPVL PNWIGGGYGT KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE SMSPAKPVQH HRERKRASKS SKHSMS.

    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.

    Sostdc1 Human
  • View Data Sheet

    Name :

    SRI Human

    Description:

    Sorcin Human Recombinant

    Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.

    Product # :

    PRO-166

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    Description

    SRI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 221 amino acids (1-198 a.a.) and having a molecular mass of 24.1kDa. The SRI is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SRI solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.2M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sorcin (SRI) which is a 22kDa calcium-binding protein was originally identified in multidrug-resistant cells. Sorcin, which modulates excitation-contraction coupling in the heart, contributes to calcium homeostasis in the heart sarcoplasmic reticulum.

    • Synonyms

      Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.

    • 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 MGSMAYPGHP GAGGGYYPGG YGGAPGGPAF PGQTQDPLYG YFAAVAGQDG QIDADELQRC LTQSGIAGGY KPFNLETCRL MVSMLDRDMS GTMGFNEFKE LWAVLNGWRQ HFISFDTDRS GTVDPQELQK ALTTMGFRLS PQAVNSIAKR YSTNGKITFD DYIACCVKLR ALTDSFRRRD TAQQGVVNFP YDDFIQCVMS V.

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

    Sri Human
  • View Data Sheet

    Name :

    OCM Human

    Description:

    Oncomodulin-1 Human Recombinant

    Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.

    Product # :

    PRO-143

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    Description

    The Recombinant Human Oncomodulin-1 produced in E.coli has a molecular mass of 13.21kDa containing 117 amino acid residues of the human Oncomodulin-1 and fused to a 9 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    Oncomodulin-1 was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    More Info

    • Introduction

      Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.

    • Synonyms

      Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.

    • Applications

      Western blotting.

    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.

    Ocm Human
  • View Data Sheet

    Name :

    OTOR Human

    Description:

    Otoraplin Human Recombinant

    Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.

    Product # :

    CYT-582

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    Description

    Otoraplin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.7 kDa.The OTOR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OTOR protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM NaCl.

    Purity

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

    More Info

    • Introduction

      OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
      Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness.

    • Synonyms

      Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VHGIFMDRLASKKLCADDECVYTISLASAQEDYNAPDCRFINVKKGQQIYVYS
      KLVKENGAGEFWAGSVYGDGQDEMGVVGYFPRNLVKEQRVYQEATKEVPTT
      DIDFFCE.

    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.

    Otoraplin Human
  • View Data Sheet

    Name :

    BTC Human, HEK

    Description:

    Betacellulin Human Recombinant, HEK

    Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC

    Product # :

    CYT-1188

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    Description

    BTC Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (32-111 a.a) containing 86 amino acids and having a molecular mass of 9.8kDa.BTC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.

    More Info

    • Introduction

      BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are mediated by the EGF receptor and other related receptors.

    • Synonyms

      Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC

    • 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

      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 9.8kDa.

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

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

      What is the Biological Activity of BETACELLULIN Protein?
      ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.

      What is the amino acid sequence of BETACELLULIN Protein?
      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH

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

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

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

    Betacellulin Protein
  • View Data Sheet

    Name :

    CHGB Human

    Description:

    Chromogranin B Human Recombinant

    SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.

    Product # :

    PRO-824

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    Description

    CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.

    • Synonyms

      SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.

    • 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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.

    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.

    Chgb Human
  • View Data Sheet

    Name :

    RELM b Mouse

    Description:

    RELM-Beta Mouse Recombinant

    Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    Product # :

    CYT-413

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    Description

    Mouse RELM-b Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 8.9kDa. The Mouse RETNLB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) protein solution containing 10mM Acetic Acid with 2:1 mannitol to protein.

    Purity

    Greater than 97% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
      RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
      The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.

    • Synonyms

      Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    • Physical Appearance

      Brownish lyophilized powder.

    • Stability

      Lyophilized RETNLB is stable at -20°C. After reconstitution the protein should be kept at all times at -20°C. It is recommended to add a carrier protein (0.1% HSA or BSA) for long term storage.

    • Solubility

      Reconstitute at 0.1 mg/ml with sterile pyrogen free water.

    • Amino Acid Sequence

      MQCSFESLVD QRIKEALSRQ EPKTISCTSV TSSGRLASCP AGMVVTGCAC GYGCGSWDIR NGNTCHCQCS VMDWASARCC RMA.

    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.

    Relm Beta Mouse
  • View Data Sheet

    Name :

    CRHBP (22-322), Human

    Description:

    Corticotropin Releasing Hormone Binding Protein (22-322 a.a.) Human Recombinant

    Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.

    Product # :

    HOR-025

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    Description

    CRHBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (22-322 a.a) and having a molecular mass of 36.1kDa.CRHBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Corticotropin Releasing Hormone Binding Protein or CRHBP is a hormone that stimulates the preopiomelanocortin-derived peptides secretion & synthesis. In general, the levels of CRHBP in the human plasma are relatively low. There are times when we can find high levels of the hormone, mainly in pregnancy, after parturition the levels drop back, the high levels are thought to be derived from the placenta. CRH-binding protein can be found in the plasma, this protein inactivates CRH, in order to avoid inappropriate pituitary-adrenal stimulation during gestation.

    • Synonyms

      Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.

    • 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 MGSESRYLEL REAADYDPFL LFSANLKREL AGEQPYRRAL RCLDMLSLQG QFTFTADRPQ LHCAAFFISE PEEFITIHYD QVSIDCQGGD FLKVFDGWIL KGEKFPSSQD HPLPSAERYI DFCESGLSRR SIRSSQNVAM IFFRVHEPGN GFTLTIKTDP NLFPCNVISQ TPNGKFTLVV PHQHRNCSFS IIYPVVIKIS DLTLGHVNGL QLKKSSAGCE GIGDFVELLG GTGLDPSKMT PLADLCYPFH GPAQMKVGCD NTVVRMVSSG KHVNRVTFEY RQLEPYELEN PNGNSIGEFC LSGL

    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.

    Crhbp Protein
  • View Data Sheet

    Name :

    GHRP5

    Description:

    Growth Hormone Releasing Peptide-5

    GHRP-5, GHRP5.

    Product # :

    HOR-023

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    Description

    Growth Hormone Releasing Peptide-5 Synthetic is a single, non-glycosylated polypeptide chain containing 5 amino acids, having a molecular mass of 770.91 Dalton and a Molecular formula of C43H46N8O6.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH effect on pituitary somatotrophs to stimulate GH release. The GHRP5 is one of several synthetic met-enkephalin analogs that owns unnatural D-amino acids. They were developed for their growth hormone (GH) releasing activity and called GH secretatogues. They lack opioid activity but are potent stimulators of GH release. These secretatogues are distinct from the growth hormone releasing hormone (GHRH or GHRF) as they share no sequence relation and derive their function through action at a completely different receptor, the ghrelin receptor.

    • Synonyms

      GHRP-5, GHRP5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth Hormone Releasing Peptide-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP5 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 GHRP5 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Tyr-(D-Trp)-Ala-Trp-(D-Phe)-NH2.

    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.

    Ghrp5
  • View Data Sheet

    Name :

    CUTA Human

    Description:

    CutA Divalent Cation Tolerance Homolog Human Recombinant

    ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.

    Product # :

    PRO-812

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    Description

    CUTA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids (33-179 a.a.) and having a molecular mass of 17.1 kDa. CUTA protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CUTA Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUTA is the 179 amino acid mammalian homolog of the cutA E. coli protein and is ubiquitously expressed, particularly in brain tissue. CUTA participates in cellular tolerance to a broad range of divalent cations other than copper. The CUTA protein is a cytoplasmic protein, encoded by the single-gene operon and has been related to divalent cation tolerance.

    • Synonyms

      ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.

    • 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). Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MRLLLLPRVL LTMASGSPPT QPSPASDSGS GYVPGSVSAA FVTCPNEKVA KEIARAVVEK RLAACVNLIP QITSIYEWKG KIEEDSEVLM MIKTQSSLVP ALTDFVRSVH PYEVAEVIAL PVEQGNFPYL QWVRQVTESV SDSITVLPLE HHHHHH.

    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.

    Cuta Human
  • View Data Sheet

    Name :

    LGALS3 Human, His

    Description:

    Galectin-3 Human Recombinant, His Tag

    Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.

    Product # :

    CYT-693

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    • sds-page

    Description

    LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 270 amino acids (1-250 a.a.) and having a molecular mass of 28.3 kDa. The LGALS3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Galectin-3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is < 15ug/ml as measured by its ability to agglutinate human red blood cells.

    sds-page

    LGALS3 Human, His-sds-page - Product image 1

    More Info

    • Introduction

      Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.

    • Synonyms

      Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.

    • 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 MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.

    • Background

      What is the molecular weight/Mw of LGALS3 HUMAN, HIS Protein?
      LGALS3 HUMAN, HIS Protein has a total Mw of 28.3kDa.

      What is the source or expression system of LGALS3 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of LGALS3 HUMAN, HIS Protein?
      LGALS3 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS3 HUMAN, HIS Protein?
      The ED50 for this effect is < 2.5ug/ml as measured by its ability to agglutinate human red blood cells.

      What is the amino acid sequence of LGALS3 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.

      What applications can LGALS3 HUMAN, HIS Protein be used in?
      LGALS3 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS3 HUMAN, HIS Protein?
      The endotoxin level is minimal, LGALS3 HUMAN, HIS Protein was purified using conventional chromatography techniques.


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

    Lgals3 Human His
  • View Data Sheet

    Name :

    Procalcitonin Mouse

    Description:

    Procalcitonin Mouse Recombinant

    Calcitonin, Calca, Calc.

    Product # :

    HOR-014

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Procalcitonin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val26-Ser136) containing 121 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 13.6kDa.

    Source

    Escherichia Coli.

    Formulation

    Procalcitonin was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 94.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Calcitonin, Calca, Calc.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASVPLRSILESS PGMATLSEEE VRLLAALVQD YMQMKARELE QEEEQEAEGS SLDSPRSKRC GNLSTCMLGT YTQDLNKFHT FPQTSIGVEA PGKKRDVAKD LETNHQSHFG N.

    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.

    Procalcitonin Mouse
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