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Search results

1000 results found for “Follistatin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    DSTN Human

    Description:

    Destrin Human Recombinant

    Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.

    Product # :

    PRO-1137

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    Description

    DSTN Human Recombinant produced in E. coli is a single polypeptide chain containing 173 amino acids (1-165) and having a molecular mass of 19.5 kDa.DSTN is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DSTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Actin depolymerizing factor (Destrin/DSTN) belongs to the ADF/Cofilin/destrin superfamily which has the ability to swiftly depolymerize F-Actin in a stoichiometric mode. The ADF family of proteins is responsible for enhancing the turnover rate of actin in vivo. Destrin is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. DSTN functions in a pH-independent manner. DSTN is found in a variety of epithelial and endothelial cells, however it is virtually nonexistent in adult mouse heart and skeletal muscle cells. Destrin shares a 71% sequence homology with Cofilin, however the 2 proteins vary in their interaction with Actin.

    • Synonyms

      Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.

    • 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

      MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPVLEHHH HHH

    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.

    Dstn Human
  • View Data Sheet

    Name :

    ID2 Human

    Description:

    Inhibitor of DNA Binding 2 Human Recombinant

    DNA-binding protein inhibitor ID-2, bHLHb26, GIG8, ID2A, ID2H, MGC26389, Class B basic helix-loop-helix protein 26, Inhibitor of DNA binding 2.

    Product # :

    PRO-1383

    Price :

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    Description

    ID2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-134 a.a.) and having a molecular mass of 17kDa. ID2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ID2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Inhibitor of DNA Binding 2 (ID2) is a part of the inhibitor of DNA binding family, whose members are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative way by suppressing their heterodimerization partners through the HLH domains. ID2 play a role in negatively regulating cell differentiation and may be an inhibitor of tissue-specific gene expression.

    • Synonyms

      DNA-binding protein inhibitor ID-2, bHLHb26, GIG8, ID2A, ID2H, MGC26389, Class B basic helix-loop-helix protein 26, Inhibitor of DNA binding 2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKAFSPVRSV RKNSLSDHSL GISRSKTPVD DPMSLLYNMN DCYSKLKELV PSIPQNKKVS KMEILQHVID YILDLQIALD SHPTIVSLHH QRPGQNQASR TPLTTLNTDI SILSLQASEF PSELMSNDSK ALCG.

    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.

    Id2 Human
  • View Data Sheet

    Name :

    Eotaxin Human

    Description:

    Eotaxin Human Recombinant (CCL11)

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    Product # :

    CHM-256

    Price :

    Quantity :

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    Shipped at Room temp

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    • description
    • source
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    • purity
    • biological activity
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    • Citations

    Description

    Eotaxin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8345.9 Dalton. The CCL11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.

    Purity

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

    Biological Activity

    The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.

    Citations

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 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 Eotaxin Human Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD

      SMKYLDQKSP TPKP.

    • Background

      What is the molecular weight/Mw of EOTAXIN HUMAN Protein?
      EOTAXIN HUMAN Protein has a total Mw of 8.3459kDa.

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

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

      What is the Biological Activity of EOTAXIN HUMAN Protein?
      The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.

      What is the amino acid sequence of EOTAXIN HUMAN Protein?
      GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
      SMKYLDQKSP TPKP.

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

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

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

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

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

    Eotaxin Human
  • View Data Sheet

    Name :

    FBL Human

    Description:

    Fibrillarin Human Recombinant

    rRNA 2'-O-methyltransferase fibrillarin, 34 kDa nucleolar scleroderma antigen, FBL, FIB1, FLRN, fibrillarin, FIB, RNU3IP1.

    Product # :

    ENZ-566

    Price :

    Quantity :

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    Description

    FBL Human Recombinant fused with 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 262 amino acids (83-321 a.a.) and having a molecular mass of 28.9kDa. The FBL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FBL solution contains Phosphate buffered saline (pH 7.4), 30% glycerol, and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FBL is a significant small nucleolar protein in eukaryotes, which has an essential role in pre-rRNA processing during ribosomal biogenesis. Fibrillarin is a component of several ribonucleoproteins including a nucleolar small nuclear ribonucleoprotein (SnRNP) and one of the two classes of small nucleolar ribonucleoproteins (snoRNPs). Fibrillarin contains an N-terminal repetitive domain which is rich in glycine and arginine residues, like fibrillarins in other species. Fibrillarin’s central region is similar to an RNA-binding domain and contains an RNP consensus sequence. FBL is linked to the U3, U8, and U13 small nuclear RNAs and is positioned in the dense fibrillar component (DFC) of the nucleolus. Antisera from roughly 8% of humans with the autoimmune disease scleroderma recognize fibrillarin.

    • Synonyms

      rRNA 2'-O-methyltransferase fibrillarin, 34 kDa nucleolar scleroderma antigen, FBL, FIB1, FLRN, fibrillarin, FIB, RNU3IP1.

    • 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 RSMGKNVMVE PHRHEGVFIC RGKEDALVTK NLVPGESVYG EKRVSISEGD DKIEYRAWNP FRSKLAAAIL GGVDQIHIKP GAKVLYLGAA SGTTVSHVSD IVGPDGLVYA VEFSHRSGRD LINLAKKRTN IIPVIEDARH PHKYRMLIAM VDVIFADVAQ PDQTRIVALN AHTFLRNGGH FVISIKANCI DSTASAEAVF ASEVKKMQQE NMKPQEQLTL EPYERDHAVV VGVYRPPPKV KN.

    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.

    Fbl Human
  • View Data Sheet

    Name :

    FIS1 Human

    Description:

    Fission-1 Human Recombinant

    TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).

    Product # :

    PRO-829

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    Description

    FIS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids (1-122 a.a.) and having a molecular mass of 16.3 kDa. FIS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    FIS1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FIS1 is part of the mitochondrial complex that promotes mitochondrial fission. FIS1 induces cytochrome C discharge from the mitochondrion to the cytosol, eventually leading to apoptosis. FIS1 participates in peroxisomal growth and division. The C terminus is required for mitochondrial localisation, while the N teminus is necessary for mitochondrial fission.

    • Synonyms

      TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).

    • 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 MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD IRKGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK DG.

    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.

    Fis1 Human
  • View Data Sheet

    Name :

    PLAC8 Human

    Description:

    Placenta-Specific 8 Human Recombinant

     Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.

    Product # :

    PRO-1725

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    Description

    PLAC8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa.PLAC8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PLAC8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0),0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Placenta-Specific 8 (PLAC8) is a member of the cornifelin family. The PLAC8 protein is expressed at high levels in the plasmacytoid dendritic cells, spleen, lymph nodes, peripheral blood leukocytes, and bone marrow.

    • Synonyms

      Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.

    • 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 MGSMQAQAPV VVVTQPGVGP GPAPQNSNWQ TGMCDCFSDC GVCLCGTFCF PCLGCQVAAD MNECCLCGTS VAMRTLYRTR YGIPGSICDD YMATLCCPHC TLCQIKRDIN RRRAMRTF.

    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.

    Plac8 Human
  • View Data Sheet

    Name :

    PLGF1 Human, Sf9

    Description:

    Placental Growth Factor-1 Human Recombinant, Sf9

    PIGF, PGF, PLGF-1.

    Product # :

    CYT-419

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    Description

    Placenta Growth Factor-1 Human Recombinant produced in insect cells is a homodimer, glycosylated polypeptide chain containing 2 x 131 amino acids and having a total molecular mass of approximately 34 kDa. The PLGF-1 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 50mM acetic acid.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to bind to immobilized rh-sFlt-1 in a functional ELISA. PlGF-1 human Recombinant can bind to immobilized rh-sFlt-1 (100ng/well) with a linear range at 0.5-10ng/ml, corresponding to a Specific Activity of 1x105-2x106units/mg.

    Citations

    More Info

    • Introduction

      PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.

    • Synonyms

      PIGF, PGF, PLGF-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Placenta Growth Factor 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Placenta Growth Factor 1 in sterile 0.1M 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-Leu-Pro-Ala-Val.

    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.

    Pigf Human
  • View Data Sheet

    Name :

    MBL2 Human

    Description:

    Mannose-Binding Lectin 2 Human Recombinant

    COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.

    Product # :

    PRO-1285

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    Description

    MBL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (108-248) and having a molecular mass of 18 kDa. MBL2 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MBL2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 20% glycerol and 0.2M Nacl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Mannose-binding protein C (MBL2),belongs to the collectin family of patternrecognition molecules and is an important component in the innate immune system. MBL2 is a secreted glycoprotein which recognizes mannose and N-acetylglucosamine on various microorganisms, and is capable of activating the classical complement pathway. Lacking MBL2 has been associated with susceptibility to autoimmune and infectious diseases.

    • Synonyms

      COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.

    • 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 MGSAASERKA LQTEMARIKK WLTFSLGKQV GNKFFLTNGE IMTFEKVKAL CVKFQASVAT PRNAAENGAI QNLIKEEAFL GITDEKTEGQ FVDLTGNRLT YTNWNEGEPN NAGSDEDCVL LLKNGQWNDV PCSTSHLAVC EFPI.

    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.

    Mbl2 Human
  • View Data Sheet

    Name :

    REG4 Human

    Description:

    Regenerating Islet-Derived 4 Human Recombinant

    Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.

    Product # :

    PRO-424

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    Description

    The Recombinant Human REG-4 is manufactured with N-terminal fusion of His Tag. The Recombinant Human REG-IV His-Tagged Fusion Protein is 17.4 kDa protein containing 136 amino acid residues of the Human REG 4 and 12 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
      Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system.

    • Synonyms

      Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.

    • 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 water to a working concentration approximately 0.5 mg/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 HMDIIMRPSC APGWFYHKSN CYGYFRKLRN WSDAELECQS YGNGAHLASI LSLKEASTIA EYISGYQRSQ PIWIGLHDPQ KRQQWQWIDG AMYLYRSWSG KSMGGNKHCA EMSSNNNFLT WSSNECNKRQ HFLCKYRP.

    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.

    Reg4 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.

    Citations

    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 :

    Globular Adiponectin Human, His

    Description:

    Adiponectin Globular Recombinant, His Tag

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

    Product # :

    CYT-277

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    Description

    Acrp30 Human has a total of 171 amino acids. N-terminal underlined amino acids are His-tag and the protease cleavage site (31AA-Underlined). The AA sequence of Acrp30 Human is homologous to the 105-244 amino acid sequence of the Human full-length Adiponectin (Swiss-prot entry Q15848).

    Source

    Escherichia Coli.

    Formulation

    Acrp30 Human is a filtered powder, lyophilized from 0.6mg/ml in PBS buffer.

    Purity

    Purity of Acrp30 Human is greater than 95% as determined by SDS PAGE.

    Citations

    More Info

    • Introduction

      Adiponectin is a protein exclusively secreted from adipose tissue. In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (LMW, also called trimer) forms. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.

    • Synonyms

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

    • Stability

      For long term, store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized Acrp30 Human remains stable for 24 months when stored at -20°C.

    • Solubility

      Add deionized water and let the lyophilized pellet of Acrp30 Human dissolve completely.

    • Amino Acid Sequence

      MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.

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

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

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

    Gacrp30 Human His
  • View Data Sheet

    Name :

    Protein-A/G Cys

    Description:

    Protein A/G Cys Recombinant

    Product # :

    PRO-1928

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by HPLC.
    (b) Analysis by SDS-PAGE.

    sds-page, HPLC

    protein a/g cys hplc - Product image 1
    protein a/g cys sds-page - Product image 2

    Citations

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEC.

    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.

    Protein A G Cys
  • View Data Sheet

    Name :

    Lanreotide

    Description:

    Lanreotide

    Product # :

    HOR-282

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    Description

    Lanreotide is an octapeptide, an analogue of a naturally occurring hormone, somatostatin.

    Formulation

    The protein (1mg/ml) was lyophilized with 5mg manntitol and 0.04mg tween-80.

    Purity

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

    Citations

    More Info

    • Introduction

      Lanreotide is a peptide inhibitor of a number of endocrine, neuroendocrine, exocrine and paracrine functions. It shows good affinity for peripheral somatostatin receptors (anterior pituitary and pancreatic). In contrast, its affinity for central receptors is much lower. This profile confers a good specificity of action at the level of growth hormone and digestive hormone secretion. Lanreotide shows a much longer duration of action than natural somatostatin. In addition, its marked selectivity for the secretion of growth hormone, compared to that of insulin, makes it a suitable candidate for the treatment of acromegaly. By inhibiting the synthesis of thyroid stimulating hormone (TSH), lanreotide also normalised thyroid function of patients with thyrotrophin secreting adenomas in 50% (8/16) of the per-protocol population treated for 6 months. There was no significant reduction in the size of the adenoma. Furthermore, the inhibitory action of lanreotide on intestinal exocrine secretion, d

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    Lanreotide
  • View Data Sheet

    Name :

    Adiponectin Rat

    Description:

    Adiponectin Rat Recombinant

    Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-831

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    Description

    ACRP30 Rat Recombinant produced in 293 cell line is a polypeptide chain containing 238 amino acids and having a total molecular mass of 25.7 kDa. ACRP30 contains a C-Terminal linker (3 AA residue) and a C-Terminal Flag- tag (8 AA residue).

    Source

    HEK293 cell line.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

      Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ACRP30 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ACRP30 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 0.5 mg/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

      GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 25.7kDa.

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

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK.

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

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

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

    Acrp30 Rat
  • View Data Sheet

    Name :

    HTF Bovine

    Description:

    Holo Transferrin Bovine

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    Product # :

    PRO-510

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    Description

    Bovine Holo Transferrin is a glycoprotein of approximately 80 kDa.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by Cellulose Acetate.

    Citations

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bovine HTF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bovine HTF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG, HBc, ALT and Syphilis.Viral inactivation by pasteurization (60°C for 10 hours) has been validated using three different test viruses, with removal of 8-14.5 logs of virus documented. The purification process has also been found to remove significant additional quantities of virus.

    • Applications

      Bovine Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    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.

    Holo Transferrin Bovine
  • View Data Sheet

    Name :

    FCER1A Human 201 a.a

    Description:

    IgE Receptor Subunit A Human Recombinant

    Fc Fragment Of IgE, High Affinity I, Receptor For; Alpha Polypeptide, FCE1A, IgE Fc Receptor Subunit Alpha, FcERI, Fc-Epsilon RI-Alpha, Fc Epsilon RI Alpha-Chain, Fc IgE Receptor, Alpha Polypeptide, High Affinity Immunoglobulin Epsilon Receptor Alpha-Subunit, High Affinity Immunoglobulin Epsilon Receptor Subunit Alpha, Immunoglobulin E Receptor, High-Affinity, Of Mast Cells, Alpha Polypeptide.

    Product # :

    PRO-2357

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    Description

    FCER1A Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 201 amino acids.FCER1Ais fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1x PBS, 50mM Arginine and 0.05% NaN3.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide (FCER1A) binds to the Fc region of immunoglobulins epsilon. FCER1A is a high affinity receptor. In addition FCER1A is responsible for starting the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators such as histamine which is responsible for the manifestations of allergy. This receptor is contains of an alpha subunit, a beta subunit, and two gamma subunits. FCER1A stands for the alpha subunit. Among the diseases associated with FCER1A are mast-cell leukemia, and allergic asthma.

    • Synonyms

      Fc Fragment Of IgE, High Affinity I, Receptor For; Alpha Polypeptide, FCE1A, IgE Fc Receptor Subunit Alpha, FcERI, Fc-Epsilon RI-Alpha, Fc Epsilon RI Alpha-Chain, Fc IgE Receptor, Alpha Polypeptide, High Affinity Immunoglobulin Epsilon Receptor Alpha-Subunit, High Affinity Immunoglobulin Epsilon Receptor Subunit Alpha, Immunoglobulin E Receptor, High-Affinity, Of Mast Cells, Alpha Polypeptide.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      The Recombinant FCER1A protein although stable at 4°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      HMAPAMESPTL LCVALLFFAP DGVLAVPQKP KVSLNPPWNR IFKGENVTLT CNGNNFFEVS STKWFHNGSL SEETNSSLNI VNAKFEDSGE YKCQHQQVNE SEPVYLEVFS DWLLLQASAE VVMEGQPLFL RCHGWRNWDV YKVIYYKDGE ALKYWYENHN ISITNATVED SGTYYCTGKV WQLDYESEPL NITVIKAPLEHHHHHH.

    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.

    Fcer1A Human 201 Aa
  • 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.

    Citations

    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.

    • Background

      What is the molecular weight/Mw of GHRP5 Protein?
      GHRP5 Protein has a total Mw of 0,770kDa.

      What is the Purity of GHRP5 Protein?
      GHRP5 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of GHRP5 Protein?
      The biological functionality of GHRP5 Protein will be determined in the future.

      What is the amino acid sequence of GHRP5 Protein?
      Tyr-(D-Trp)-Ala-Trp-(D-Phe)-NH2.

      What applications can GHRP5 Protein be used in?
      GHRP5 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GHRP5 Protein?
      The endotoxin level is minimal, GHRP5 Protein was purified using conventional chromatography techniques.

      Who supplies GHRP5 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of GHRP5?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Ghrp5
  • View Data Sheet

    Name :

    Borrelia Spielmanii DbpA

    Description:

    Borrelia Spielmanii Decorin Binding Protein A Recombinant

    Product # :

    BOR-026

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    Description

    Recombinant Borrelia Spielmanii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 17kDa. Borrelia Spielmanii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Spielmanii DbpA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mostly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The Gram-negative bacterium Borreliella spielmanii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. DbpA, also known as p17 or Osp17, is a heterogeneous protein among the human pathogenic B. burgdorferi sensu lato species.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

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

    • Applications

      Western blot with Lyme positive plasma.

    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.

    Borrelia Spielmanii Dbpa
  • View Data Sheet

    Name :

    hCG Protein

    Description:

    Chorionic Gonadotropin Human

    Chorionic gonadotropin, hCG, CG.

    Product # :

    HOR-250

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    • Citations

    Description

    Human Chorionic Gonadotropin is produced from a sterile preparation of placental glucoprotein urine of pregnant women having a total molecular mass of 36,700 Dalton. The hCG consists of 237 amino acids, a chain-92 amino acids and b chain-145 amino acids. The hCG is purified by proprietary chromatographic techniques.

    Source

    Urine of pregnant women.

    Formulation

    The hCG was lyophilized with no additives.

    Biological Activity

    The activity was found to be 5212IU/mg.

    Activity Assay

    hcg activity assay - Product image 1
    hcg bioactivity assay - Product image 2

    Citations

    More Info

    • Introduction

      Human chorionic gonadotropin (hCG) is a peptide hormone produced in pregnancy, that is made by the embryosoon after conception and later by the syncytiotrophoblast(part of the placenta). Its role is to prevent the disintegration of the corpus luteumof the ovaryand thereby maintain progesterone production that is critical for a pregnancy in humans. hCG may have additional functions, for instance it is thought that it affects the immune tolerance of the pregnancy. Early pregnancy testing generally is based on the detection or measurement of hCG.

    • Synonyms

      Chorionic gonadotropin, hCG, CG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Contaminants

      Free of: HbsAg and antibodies to HIV and HCV.

    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.

    Hcg Human
  • View Data Sheet

    Name :

    Thrombin

    Description:

    Human Thrombin

    Product # :

    PRO-339

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    Description

    Thrombin was purified from human plasma.

    Source

    Human Plasma.

    Formulation

    Lyophilized protein containing mannitol, sodium chloride, calcium chloride.

    Biological Activity

    The specific activity was found to be 116 US Units/mg protein.

    Citations

    More Info

    • Introduction

      Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.

    • Physical Appearance

      lyophilized powder.

    • Stability

      Lyophilized Human Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution human thrombin 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 human thrombin in sterile a 0.9% NaCl solution at 500U/ml.

    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.

    Thrombin Human
  • View Data Sheet

    Name :

    NRG1 A Human

    Description:

    Neuregulin-1/Heregulin Alpha (EGF Domain) Human Recombinant

    Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.

    Product # :

    CYT-736

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    Description

    Recombinant Human Neuregulin-1/Heregulin Alpha (EGF Domain) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 65 amino acids and having a total molecular mass of 7.4kDa. NRG1-A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 6.0 and 150mM NaCl.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 40 ng/ml, corresponding to a specific activity of > 2.5×104 units/mg.

    Citations

    More Info

    • Introduction

      Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. These isoforms contain the heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). All these factors have the Ig and EGF-like domain, and are able to bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. NRG1 isoforms act to induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells.

    • Synonyms

      Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NRG1-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-A should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NRG1-A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCQPGF TGARCTENVP MKVQNQEKAE ELYQK.

    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.

    Nrg1 A Human
  • View Data Sheet

    Name :

    SPP1 Human, Active

    Description:

    Osteopontin Human Recombinant, BioActive

    OPN, SPP-1, BNSP, BSPI, ETA-1, Bone sialoprotein 1, BSP I.Early T lymphocyte activation 1, ETA 1, ETA1, MGC110940, Nephropontin, Secreted phosphoprotein 1, SPP 1, SPP1, urinary stone protein, uropontin.

    Product # :

    CYT-1166

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    Description

    SPP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 321 amino acids (17-314 a.a.) and having a molecular mass of 36.2kDa. SPP1 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 1mM DTT, 10% glycerol and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by the ability of the immobilized protein to support the adhesion of HEK293 human embryonic kidney cells. When cells are added to OPN coated plates 10ug/ml. This effect is more to 40%.

    Citations

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    • Introduction

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

    • Synonyms

      OPN, SPP-1, BNSP, BSPI, ETA-1, Bone sialoprotein 1, BSP I.Early T lymphocyte activation 1, ETA 1, ETA1, MGC110940, Nephropontin, Secreted phosphoprotein 1, SPP 1, SPP1, urinary stone protein, uropontin.

    • 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 RSMIPVKQAD SGSSEEKQLY NKYPDAVATW LNPDPSQKQN LLAPQNAVSS EETNDFKQET LPSKSNESHD HMDDMDDEDD DDHVDSQDSI DSNDSDDVDD TDDSHQSDES HHSDESDELV TDFPTDLPAT EVFTPVVPTV DTYDGRGDSV VYGLRSKSKK FRRPDIQYPD ATDEDITSHM ESEELNGAYK AIPVAQDLNA PSDWDSRGKD SYETSQLDDQ SAETHSHKQS RLYKRKANDE SNEHSDVIDS QELSKVSREF HSHEFHSHED MLVVDPKSKE EDKHLKFRIS HELDSASSEV 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.

    Osteopontin Human
  • View Data Sheet

    Name :

    GLP 2 Human

    Description:

    Human GLP-2

    GLP2, GLP-2, GLP 2.

    Product # :

    HOR-305

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    Description

    GLP-2 contains 34 amino acids having a molecular mass of 3922.35 Dalton.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    Citations

    More Info

    • Introduction

      GLP-2 functions as an intestinal growth factor, which stimulates intestinal epithelial growth. GLP2 is involved in diabetes-associated bowel growth. GLP2 enhances cell differentiation, playing a role as a cytokine and in tissue regeneration, and mediating cytoprotection. GLP2 is invloded numerous therapeutic applications. GLP2 regulates signaling pathways coupled to cell proliferation and cell death by apoptosis.
      GLP-2 is produced by specific post-translational proteolytic cleavage of proGLP. GLP-2 is manufactured by the intestinal endocrine L cell and by several neurons in the central nervous system.

    • Synonyms

      GLP2, GLP-2, GLP 2, Glucagon Like Peptide-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GLP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP2 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 GLP-2 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-Met-Asn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Ala-Arg-Asp-Phe-Ile-Asn-Trp-Leu-Ile-Gln-Thr-Lys-Ile-Thr-Asp-Arg.

    • Background

      What is the molecular weight/Mw of GLP 2 HUMAN Protein?
      GLP 2 HUMAN Protein has a total Mw of 3.92kDa.


      What is the Purity of GLP 2 HUMAN Protein?
      GLP 2 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GLP 2 HUMAN Protein?
      The biological functionality of GLP 2 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GLP 2 HUMAN Protein?
      His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-Met-Asn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Ala-Arg-Asp-Phe-Ile-Asn-Trp-Leu-Ile-Gln-Thr-Lys-Ile-Thr-Asp-Arg.

      What applications can GLP 2 HUMAN Protein be used in?
      GLP 2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GLP 2 HUMAN Protein?
      The endotoxin level is minimal, GLP 2 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.

    Glp 2 Human
  • View Data Sheet

    Name :

    LIF Mouse

    Description:

    Leukemia Inhibitory Factor Mouse Recombinant

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

    Product # :

    CYT-645

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

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

    Description

    Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.02% Tween-20.

    Purity

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

    Biological Activity

    Activity of murine LIF was determined by the M1 cell differentiation assay which was found to be < 0.01 ng/ml, corresponding to a specific activity of 100,000,000 IU/mg.
    A standard of 50 Units is defined as the concentration of mouse LIF in 1.0 mL of tissue culture medium that induces the differentiation of 50% of M1 colonies.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MSPLPITPVNATCAIRHPCHGNLMNQIKNQLAQLNGSANALFISYYTAQGEPFP NNVEKLCAPNMTDFPSFHGNGTEKTKLVELYRMVAYLSASLTNITRDQKVLNP TAVSLQVKLNATIDVMRGLLSNVLCRLCNKYRVGHVDVPPVPDHSDKEAFQR KKLGCQLLGTYKQVISVVVQAF.

    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.

    Lif Mouse
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