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Search results

1000 results found for “oncostatin-m”

Name

Description

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  • 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%.

    More Info

    • 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 :

    MECR Human

    Description:

    Mitochondrial Trans-2-Enoyl-CoA Reductase Human Recombinant

    NRBF1, CGI-63, FASN2B, EC 1.3.1.38, MECR, Mitochondrial Trans-2-Enoyl-CoA Reductase.

    Product # :

    ENZ-533

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    Description

    MECR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (54-373 a.a.) and having a molecular mass of 49.8 kDa. The MECR is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MECR Human solution containing 20mM Trsi pH-8, 0.2M NaCl, 5mM DTT & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MECR catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH dependent manner with preference to medium chain length substrate. MECR protein takes part in the mitochondrial synthesis of fatty acids.

    • Synonyms

      NRBF1, CGI-63, FASN2B, EC 1.3.1.38, MECR, Mitochondrial Trans-2-Enoyl-CoA Reductase.

    • 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 MPAKVVELKN LELAAVRGSD VRVKMLAAPI NPSDINMIQG NYGLLPELPA VGGNEGVAQV VAVGSNVTGL KPGDWVIPAN AGLGTWRTEA VFSEEALIQV PSDIPLQSAA TLGVNPCTAY RMLMDFEQLQ PGDSVIQNAS NSGVGQAVIQ IAAALGLRTI NVVRDRPDIQ KLSDRLKSLG AEHVITEEEL RRPEMKNFFK DMPQPRLALN CVGGKSSTEL LRQLARGGTM VTYGGMAKQP VVASVSLLIF KDLKLRGFWL SQWKKDHSPD QFKELILTLC DLIRRGQLTA PACSQVPLQD YQSALEASMK PFISSKQILT M.

    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.

    Mecr Human
  • View Data Sheet

    Name :

    GM-CSF Rat

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Rat Recombinant

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    Product # :

    CYT-395

    Price :

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    • description
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    Description

    Granulocyte Macrophage Colony Stimulating Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14590.65 Dalton. GM-CSF Rat Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GM-CSF Rat was lyophilized with no additives.

    Purity

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

    Biological Activity

    The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.

    More Info

    • Introduction

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

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI

      QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE

      VTTFEDFIKN LKGFLFDIPF DCWKPVQK.

    • Background

      What is the molecular weight/Mw of GM-CSF RAT Protein?
      GM-CSF RAT Protein has a total Mw of 14.59kDa.

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

      What is the Purity of GM-CSF RAT Protein?
      GM-CSF RAT Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF RAT Protein?
      The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.

      What is the amino acid sequence of GM-CSF RAT Protein?
      MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
      QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
      VTTFEDFIKN LKGFLFDIPF DCWKPVQK.

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

      What is the endotoxin level for GM-CSF RAT Protein?
      The endotoxin level is minimal, GM-CSF RAT 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.

    Gm Csf Rat
  • View Data Sheet

    Name :

    CES1D Mouse

    Description:

    Carboxylesterase 1D Mouse Recombinant

    Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.

    Product # :

    ENZ-1007

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    Description

    CES1D Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 555 amino acids (19-565 a.a) and having a molecular mass of 60.9kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1D is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1D protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 80,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of p-nitrophenyl acetate to pnitrophenol per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      Carboxylesterase 1D, also known as CES1D is part of a big family of carboxylesterases which are responsible for the hydrolysis of ester in addition to amide bonds. CES1D is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity in addition to lesser but detectable neutral cholesteryl ester hydrolase activity. CES1D demonstrates low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics.

    • Synonyms

      Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.

    • 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

      YPSSPPVVNT VKGKVLGKYV NLEGFTQPVA VFLGVPFAKP PLGSLRFAPP QPAEPWSFVK NTTSYPPMCS QDAVGGQVLS ELFTNRKENI PLQFSEDCLY LNIYTPADLT KNSRLPVMVW IHGGGLVVGG ASTYDGLALS AHENVVVVTI QYRLGIWGFF STGDEHSRGN WGHLDQVAALRWVQDNIANF GGNPGSVTIF GESAGGFSVS VLVLSPLAKN LFHRAISESG VSLTAALITT DVKPIAGLVA TLSGCKTTTS AVMVHCLRQK TEDELLETSL KLNLFKLDLL GNPKESYPFL PTVIDGVVLP KAPEEILAEK SFSTVPYIVG INKQEFGWII PTLMGYPLAE GKLDQKTANSLLWKSYPTLK ISENMIPVVA EKYLGGTDDL TKKKDLFQDL MADVVFGVPS VIVSRSHRDA GASTYMYEFE YRPSFVSAMR PKAVIGDHGD EIFSVFGSPF LKDGASEEET NLSKMVMKFW ANFARNGNPN GGGLPHWPEY DQKEGYLKIG ASTQAAQRLK DKEVSFWAEL RAKESAQRPSHREHVELLEH HHHHH.

    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.

    Ces1D Mouse
  • View Data Sheet

    Name :

    SPP1 Human, HEK

    Description:

    Osteopontin Human Recombinant, HEK

    Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    Product # :

    CYT-047

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    Description

    Osteopontin Human Recombinant is a single, glycosylated, polypeptide chain produced in HEK293 cells, is a full length protein (amino acids 17-314) fused with a polyhistidine tag at the C-terminus, having a total calculated molecular mass of 34.5kDa (The actual molecular mass may be approximately 60-65kDa in SDS-PAGE under reducing conditions due to glycosylation).Osteopontin is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    Osteopontin was lyophilized from a 0.2µM filtered solution of 20mM PBS and 150mM NaCl, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly 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 via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

    • Synonyms

      Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.Please avoid freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized SPP1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETL
      PSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDEL
      VTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDIT
      SHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRK
      ANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDS
      ASSEVNVDHHHHHH.

    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.

    Spp1 Human Hek
  • View Data Sheet

    Name :

    MHC Class II, I-A Antibody, Biotin

    Description:

    MHC Class II, (I-A) Mouse Antibody, Biotin

    Product # :

    ANT-269

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    Formulation

    1mg/ml in PBS (after reconstitution).

    More Info

    • Introduction

      MHC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.

    • Solubility

      Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Purified mouse LN B cells (C3H anti-C57Bl6).

    • Ig Subclass

      Mouse IgG2a.

    • Clone

      NYRmI-A.

    • Applications

      Cytotoxic and staining antibody. For staining, use 10ml/1,000,000 cells. Titer for cytotoxicity should be determined by the investigator.

    • Specificity

      Recognizes most MHC class II haplotypes (b,f,p,q,r,s,u,v), but weak against I-Ak.

    • Available Conjugates

      This antibody is also available unconjugated and conjugated to FITC.

    • Type

      Mouse Antibody Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Ion exchange column.

    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.

    Mhc Class Ii I A Antibody Biotin
  • View Data Sheet

    Name :

    Omentin Human, His

    Description:

    Omentin Human Recombinant, His Tag

    Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    Product # :

    CYT-551

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    Description

    Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.

    Purity

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

    More Info

    • Introduction

      Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

    • Synonyms

      Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.

    • Applications

      Elisa
      Western blot.

    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.

    Omentin Human His
  • View Data Sheet

    Name :

    LA/SS-B Human, Biotin

    Description:

    LA / SS-B Human Recombinant, Biotinylated

    Lupus La protein, Sjoegren syndrome type B antigen, SS-B, La ribonucleoprotein, La autoantigen, SSB, La, LARP3, LA/SS-B, La(SS-B).

    Product # :

    PRO-2562

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    Description

    LA/SS-B Human Recombinant produced in SF9 is a single, glycosylated, polypeptide chain having a calculated molecular mass of 48 kDa. The LA/SS-B is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    The protein solution contains 20mM HEPES, pH 7.5, 400mM NaCl, 20% Glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The La protein is a 47 kDa polypeptide that frequently acts as an autoantigen in systemic lupus erythematosus and Sjogren's syndrome patients. La is involved in various aspects of RNA metabolism, including binding and protecting 3-prime UUU(OH) elements of newly RNA polymerase III - transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs linked to hepatitis C virus. It occurs in both the nucleus and the cytoplasm, where it assumes different roles. In the nucleus, La protein facilitates the production of tRNAs, acting as an RNA polymerase III (RNAP III) transcription factor by attaching to the U-rich 3'UTR of nascent transcripts, aiding in their folding and maturation. In the cytoplasm, La protein facilitates the translation of specific mRNAs, acting as a translation factor. As an RNA binding protein (RBP), La protein associates with subsets of mRNAs which contain a 5'-terminal oligopyrimidine (5'TOP) motif known to direct protein synthesis. The binding of La protein to particular classes of RNA molecules regulates their downstream processing, guards them from endonuclease digestion, and organizes their export from the nucleus. La/SS-B appears to be readily disposed to proteolysis, which results in many smaller (42kD, 320, and 270) nevertheless still immunoreactive polypeptides. La/SS-B antigen is strongly conserved across species. Anti-La/SS-B autoantibodies were originally found as precipitating autoantibodies in sera of Sjogren's Syndrome patients and referred to as SjT. Anti-La/SS-B precipitins are most frequently found in Sjogren's Syndrome, Systemic Lupus Erythematosus (SLE) and Subacute Cutaneous Lupus. Also, there seems to be a correlation between anti-La/SS-B and the absence of nephritis in SLE patients.

    • Synonyms

      Lupus La protein, Sjoegren syndrome type B antigen, SS-B, La ribonucleoprotein, La autoantigen, SSB, La, LARP3, LA/SS-B, La(SS-B).

    • 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 type human auto antibodies.2. Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

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

    Ssb Protein
  • View Data Sheet

    Name :

    Ang K1-3 Human

    Description:

    Angiostatin Kringles 1-3 Human Recombinant

    Angiostatin, Angiostatin Kringles 1-3, Ang K1-3.

    Product # :

    PRO-284

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    Description

    Angiostatin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 259 amino acids and having a molecular mass of approximately 29.7 kDa. The Ang K1-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated (1.0mg/ml) solution in 20mM NaAc, pH5.5, 4% mannitol.

    Purity

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

    Biological Activity

    The activity is assayed on anti-proliferation and anti-migration of endothelial cells in vitro and anti-angiogenesis in vivo. The specific activity of anti-migration of endothelial cells in vitro is 550,000 Units/mg.

    More Info

    • Introduction

      Ang K1-3 is a proteolytic fragment of plasminogen containing the first three kringle structures. A specific inhibitor of endothelial cell growth and angiogenesis. More active relative to kringles 1-4. Ang K1-3 reduces endothelial cell proliferation and acts as a potent inhibitor of angiogenesis and tumor growth.

    • Synonyms

      Angiostatin, Angiostatin Kringles 1-3, Ang K1-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      The lyophilized Angiostatin K1-3 is stable for several weeks at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.

    • Solubility

      We recommend to briefly centrifuge the vial prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      VYLSECKTGN GKNYRGTMSK TKNGITCQKW SSTSPHRPRF SPATHPSEGL EENYCRNPDN DPQGPWCYTT DPEKRYDYCD ILECEEECMH CSGENYDGKI SKTMSGLECQ AWDSQSPHAH GYIPSKFPNK NLKKNYCRNP DRELRPWCFT TDPNKRWELC DIPRCTTPPP SSGPTYQCLKGTGENYRGNV AVTVSGHTCQ HWSAQTPHTH NRTPENFPCK NLDENYCRNP DGKRAPWCHT TNSQVRWEYC KIPSCDSSP.

    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.

    Angiostatin K1 3 Human
  • View Data Sheet

    Name :

    METAP1D Human

    Description:

    Methionyl Aminopeptidase 1D Human Recombinant

    MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.

    Product # :

    ENZ-759

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    Description

    METAP1D Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (20-335a.a) and having a molecular mass of 37.4kDa. METAP1D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The METAP1D solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Methionyl Aminopeptidase 1D (METAP1D) is a part of the peptidase M24A family. METAP1D which is overexpressed in colon cancer cell lines participates in tumorigenesis. METAP1D eliminates methionine from the N-terminus of nascent proteins.

    • Synonyms

      MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.

    • 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 MGSSSPLNHI YLHKQSSSQQ RRNFFFRRQR DISHSIVLPA AVSSAHPVPK HIKKPDYVTT GIVPDWGDSI EVKNEDQIQG LHQACQLARH VLLLAGKSLK VDMTTEEIDA LVHREIISHN AYPSPLGYGG FPKSVCTSVN NVLCHGIPDS RPLQDGDIIN IDVTVYYNGY HGDTSETFLV GNVDECGKKL VEVARRCRDE AIAACRAGAP FSVIGNTISH ITHQNGFQVC PHFVGHGIGS YFHGHPEIWH HANDSDLPME EGMAFTIEPI ITEGSPEFKV LEDAWTVVSL DNQRSAQFEH TVLITSRGAQ ILTKLPHEA.

    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.

    Metap1D Human
  • View Data Sheet

    Name :

    Leptin tA Ovine

    Description:

    Leptin Antagonist Triple Mutant Ovine Recombinant

    Product # :

    CYT-356

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    Description

    Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin-Antagonist Triple Mutant Ovine Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of mouse leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, 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 Ala-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ta Ovine
  • View Data Sheet

    Name :

    NPPA Human

    Description:

    Natriuretic Peptide A Human Recombinant

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

    Product # :

    CYT-1028

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

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

    Nppa Human
  • View Data Sheet

    Name :

    CRKL Human

    Description:

    V-crk Sarcoma Virus CT10 Oncogene Homolog (Avian)-Like Human Recombinant

    Crk-like protein, CRKL.

    Product # :

    PRO-063

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    Description

    CRKL Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 323 amino acids (1-303 a.a.) and having a molecular mass of 35.9kDa (Molecular size on SDS-PAGE will appear higher). The CRKL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRKL solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Crk-like protein (CRKL) is a protein kinase containing SH2 and SH3 (src homology) domains which activates the RAS and JUN kinase signaling pathways and transforms fibroblasts in a RAS-dependent manner. CRKL is a substitute of the BCR-ABL tyrosine kinase, it also has a role in fibroblast transformation by BCR-ABL, and has oncogenic potential.

    • Synonyms

      Crk-like protein, CRKL.

    • 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 MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRDSSTCPGDYVL SVSENSRVSH YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPM GSVSAPNLPT AEDNLEYVRT LYDFPGNDAE DLPFKKGEIL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPAVS GSPGAAITPL PSTQNGPVFA KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD ENE.

    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.

    CRKL Human
  • View Data Sheet

    Name :

    ACOT11 Human

    Description:

    Acyl-CoA Thioesterase 11 Human Recombinant

    Acyl-CoA Thioesterase 11, StAR-Related Lipid Transfer (START) Domain Containing 14, Thioesterase, Adipose Associated, Acyl-CoA Thioester Hydrolase 11, Adipose-Associated Thioesterase, Brown Fat-Inducible Thioesterase, Thioesterase Superfamily Member 1, START Domain Containing 14, Acyl-Coenzyme A Thioesterase 11, STARD14, THEM1, THEA, BFIT, BFIT1, BFIT2, KIAA0707, EC 3.1.2.1.

    Product # :

    ENZ-756

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    Description

    ACOT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 268 amino acids (19-250 a.a) and having a molecular mass of 29.9kDa. ACOT11 is fused to a 36 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    ACOT11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACOT11 belongs to the acyl-CoA thioesterase family which catalyses the transformation of activated fatty acids to the equivalent non-esterified fatty acid and coenzyme A. Expression of a mouse homolog in brown adipose tissue is induced by low temperatures and inhibited by high temperatures. Obesity-resistant mice demonstrated High levels of expression compared with obesity-prone mice, indicating BFIT takes part in acyl-CoA thioesterase 11 in obesity. BFIT has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.

    • Synonyms

      Acyl-CoA Thioesterase 11, StAR-Related Lipid Transfer (START) Domain Containing 14, Thioesterase, Adipose Associated, Acyl-CoA Thioester Hydrolase 11, Adipose-Associated Thioesterase, Brown Fat-Inducible Thioesterase, Thioesterase Superfamily Member 1, START Domain Containing 14, Acyl-Coenzyme A Thioesterase 11, STARD14, THEM1, THEA, BFIT, BFIT1, BFIT2, KIAA0707, EC 3.1.2.1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSNRTS RKSALRAGND SAMADGEGYR NPTEVQMSQL VLPCHTNQRG ELSVGQLLKW IDTTACLSAE RHAGCPCVTA SMDDIYFEHT ISVGQVVNIK AKVNRAFNSS MEVGIQVASE DLCSEKQWNV CKALATFVAR REITKVKLKQ ITPRTEEEKM EHSVAAERRR MRLVYADTIK DLLANCAIQG DLESRDCSRM VPAEKTRVES VELVLPPHAN HQGNTFGGQI MAWMENVA

    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.

    Acot11 Human
  • View Data Sheet

    Name :

    ACOT7 Human

    Description:

    Acyl-CoA Thioesterase 7 Human Recombinant

    Cytosolic acyl coenzyme A thioester hydrolase, Acyl-CoA thioesterase 7, Brain acyl-CoA hydrolase, BACH, CTE-IIa, CTE-II, Long chain acyl-CoA thioester hydrolase, ACOT7, ACT, ACH1, LACH, LACH1, hBACH, RP1-120G22.10.

    Product # :

    ENZ-214

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    Description

    ACOT7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-370) and having a molecular mass of 42.6kDa.ACOT7 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACOT7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acyl-CoA Thioesterase 7 (ACOT7) belongs to the acyl coenzyme family. ACOT7 hydrolyzes the CoA thioester of palmitoyl-CoA and other long-chain fatty acids. Decreased expression of the ACOT7 protein may be linked to mesial temporal lobe epilepsy.

    • Synonyms

      Cytosolic acyl coenzyme A thioester hydrolase, Acyl-CoA thioesterase 7, Brain acyl-CoA hydrolase, BACH, CTE-IIa, CTE-II, Long chain acyl-CoA thioester hydrolase, ACOT7, ACT, ACH1, LACH, LACH1, hBACH, RP1-120G22.10.

    • 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 MARPGLIHSA PGLPDTCALL QPPAASAAAA PSMSGPDVET PSAIQICRIM RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC VAALARVERT DFLSPMCIGE VAHVSAEITY TSKHSVEVQV NVMSENILTG AKKLTNKATL WYVPLSLKNV DKVLEVPPVV YSRQEQEEEG RKRYEAQKLE RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT LHGFVHGGVT MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE GKGRYLQMKA KRQGHAEPQP.

    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.

    Acot7 Human
  • View Data Sheet

    Name :

    CXCL9 Mouse

    Description:

    MIG Mouse Recombinant (CXCL9)

    Small inducible cytokine B9, CXCL9, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, M119.

    Product # :

    CHM-337

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    Description

    MIG (CXCK9) Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 12208 Dalton. The MIG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH7.4 and 100mM NaCl.

    Purity

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

    Biological Activity

    The Activity is calculated by the ability to chemoattract Human lymphocytes using a concentration of 0.1-1 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belonging to the CXC chemokine family that is also known as Monokine induced by MIG. CXCL9 is a T-cell chemoattractant. It is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.

    • Synonyms

      Small inducible cytokine B9, CXCL9, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, M119.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL9 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 MIG in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TLVIRNARCS CISTSRGTIH YKSLKDLKQF APSPNCNKTE IIATLKNGDQ TCLDPDSANV KKLMKEWEKK INQKKKQKRG KKHQKNMKNR KPKTPQSRRR SRKTT.

    • Background

      What is the molecular weight/Mw of CXCL9 MOUSE Protein?
      CXCL9 MOUSE Protein has a total Mw of 12.2kDa.

      What is the source or expression system of CXCL9 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL9 MOUSE Protein?
      CXCL9 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL9 MOUSE Protein?
      The Activity is calculated by the ability to chemoattract Human lymphocytes using a concentration of 0.1-1 ng/ml.

      What is the amino acid sequence of CXCL9 MOUSE Protein?
      TLVIRNARCS CISTSRGTIH YKSLKDLKQF APSPNCNKTE IIATLKNGDQ TCLDPDSANV KKLMKEWEKK INQKKKQKRG KKHQKNMKNR KPKTPQSRRR SRKTT.

      What applications can CXCL9 MOUSE Protein be used in?
      CXCL9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL9 MOUSE Protein?
      The endotoxin level is minimal, CXCL9 MOUSE 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.

    Mig Mouse
  • View Data Sheet

    Name :

    MLLT11 Human

    Description:

    Myeloid/Lymphoid Leukemia Translocated To 11 Human Recombinant

    AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    Product # :

    PRO-1991

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    Description

    MLLT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids (1-90 a.a) and having a molecular mass of 12.4kDa. MLLT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MLLT11 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myeloid/Lymphoid Leukemia Translocated To 11 (MLLT11) is a part of the Mixed-Lineage Leukemia protein family. MLLT11 which takes part in leukemogenesis and in the progression of severe monocytic leukemia (AML) is located on chromosome 11q23. MLLT11 which is also expressed in embryonic brain cortex is upregulated during neuronal differentiation and is taking part in the evolution of the central nervous system.

    • Synonyms

      AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    • 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 MGSMRDPVSS QYSSFLFWRM PIPELDLSEL EGLGLSDTAT YKVKDSSVGK MIGQATAADQ EKNPEGDGLL EYSTFNFWRA PIASIHSFEL DLL.

    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.

    Mllt11 Human
  • View Data Sheet

    Name :

    CTSB Mouse

    Description:

    Cathepsin-B Mouse Recombinant

    Cathepsin B, Cathepsin B1, CTSB.

    Product # :

    PRO-2304

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    Description

    CTSB Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 330 amino acids (18-339a.a.) and having a molecular mass of 36.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTSB is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cathepsin B preproprotein (CTSB) is a papain-family cysteine protease which is normally located in lysosomes. CTSB is able to degrade several extracellular matrix components at both neutral and acidic pH and has been implicated in the progression of some human and rodent tumors progression and arthritis.

    • Synonyms

      Cathepsin B, Cathepsin B1, CTSB.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      HDKPSFHPLS DDLINYINKQ NTTWQAGRNF YNVDISYLKK LCGTVLGGPK LPGRVAFGED IDLPETFDAR EQWSNCPTIG QIRDQGSCGS CWAFGAVEAI SDRTCIHTNG RVNVEVSAED LLTCCGIQCG DGCNGGYPSG AWSFWTKKGL VSGGVYNSHV GCLPYTIPPC EHHVNGSRPP CTGEGDTPRC NKSCEAGYSP SYKEDKHFGY TSYSVSNSVK EIMAEIYKNG PVEGAFTVFS DFLTYKSGVY KHEAGDMMGG HAIRILGWGV ENGVPYWLAA NSWNLDWGDN GFFKILRGEN HCGIESEIVA GIPRTDQYWG RFLEHHHHHH.

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    Ctsb Mouse
  • View Data Sheet

    Name :

    Adipsin Human, Sf9

    Description:

    Complement Factor D Human Recombinant, Sf9

    Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.

    Product # :

    PRO-2213

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    Description

    Adipsin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 241 amino acids (21-253a.a.) and having a molecular mass of 26.01kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). Adipsin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Adipsin protein solution (1mg/ml) contains phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.

    • Synonyms

      Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.

    • 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

      PPRGRILGGR EAEAHARPYM ASVQLNGAHL CGGVLVAEQW VLSAAHCLED AADGKVQVLL GAHSLSQPEP SKRLYDVLRA VPHPDSQPDT IDHDLLLLQL SEKATLGPAV RPLPWQRVDR DVAPGTLCDV AGWGIVNHAG RRPDSLQHVL LPVLDRATCN RRTHHDGAIT ERLMCAESNR RDSCKGDSGG PLVCGGVLEG VVTSGSRVCG NRKKPGIYTR VASYAAWIDS VLAVEHHHHH 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.

    Adipsin Human Sf9
  • View Data Sheet

    Name :

    MMP-2 Human, HEK

    Description:

    Matrix Metalloproteinase-2 Human Recombinant, HEK

    72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    Product # :

    ENZ-100

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    • sds-page

    Description

    MMP-2 Human Recombinant produced in HEK293 cells is a proform of the Human MMP-2 (Ala30-Cys660) and fused with a ployhistide tag at the C-terminus, having an Mw of 71kDa. MMP-2 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The MMP-2 is supplied as a 0.2µm filtered solution in 20mM Tris-HCl, 150mM NaCl and 0.05% Brij 35, pH 7.4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The activity was measured by its ability to cleave fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (RND,Catalog # ES001)., The specific activity is > 1,000 pmoles/min/µg.
    Recombinant Human MMP-2 protein pro form needs to be activated with p-aminophenylmercuric acetate (APMA).
    Activation Protocol:
    1. Dilute MMP2 to 100µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
    2. Activate MMP2 by adding APMA to a final concentration of 1mM. (Sigma, Catalog # A9563) and 100mM stock in DMSO.
    3. Incubate at 37°C for 1 hour.

    sds-page

    mmp-2 human hek sds-page - Product image 1

    More Info

    • Introduction

      Matrix metalloproteinase-2 (MMP-2) is a type IV collagenase, which is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).

    • Synonyms

      72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    • Physical Appearance

      The MMP-2 is supplied as a sterile Filtered colorless solution.

    • Stability

      Store MMP-2 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.

    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.

    Mmp 2 Human
  • View Data Sheet

    Name :

    CXCL16 Mouse

    Description:

    CXCL16 Mouse Recombinant

    C-X-C motif chemokine 16, Small-inducible cytokine B16, Transmembrane chemokine CXCL16, Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein, SR-PSOX, Cxcl16, Srpsox, Zmynd15, AV290116, BB024863, 0910001K24Rik.

    Product # :

    CHM-363

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    Description

    CXCL16 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 9.9kDa. The CXCL16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract murine lymphocytes using a concentration range of 100-1000ng/ml corresponding to a Specific Activity of 1,000-10,000IU/mg.

    More Info

    • Introduction

      Mouse CXCL16 is a nonELR motif including CXC chemokine with a transmembrane domain. Mouse CXCL16 cDNA encodes a 246 a.a. precursor protein with a putative 26 a.a. residue signal peptide, an 88 a.a. residue chemokine domain, an 87 a.a. residue mucinlike spacer region, a 22 a.a. residue transmembrane domain, and a 23 a.a. residue cytoplasmic tail.
      CXCL16 induces a strong chemotactic response and calcium mobilization. Furthermore, CXCL16 acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis.
      Mouse CXCL16 is generated by dendritic cells in lymphoid organ T cell zones as well as by cells in the splenic red pulp both as membranebound and soluble forms. CXCR6/Bonzo (STRL33 and TYMSTR) is the receptor for CXCL16. CXCL16 is expressed in the spleen, lymph nodes, and Peyer patches. It is also expressed in non-lymphoid tissues such as lung, kidney, small intestine, and thymus, with weak expression in heart and liver and no expression in brain and purified B- and T-cells.
      CXCL16 deficiency is linked to breast cancer progression. In addition, CXCL16 is involved in immunological liver injury by regulating T lymphocyte infiltration in liver tissue. Furtheremore, CXCL16 has a distinctive role in the maintenance of cardiac allograft tolerance mediated by natural killer T cells. Moreover, CXCL16 has a significant role in not only the production of IFN-gamma by NKT cells, but also promotion of Th1-inclined immune responses mediated by NKT cells.

    • Synonyms

      C-X-C motif chemokine 16, Small-inducible cytokine B16, Transmembrane chemokine CXCL16, Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein, SR-PSOX, Cxcl16, Srpsox, Zmynd15, AV290116, BB024863, 0910001K24Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL16 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 CXCL16 Mouse in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NQGSVAGSCS CDRTISSGTQ IPQGTLDHIR KYLKAFHRCP FFIRFQLQSK SVCGGSQDQW VRELVDCFER KECGTGHGKS FHHQKHLP.

    • Background

      What is the molecular weight/Mw of CXCL16 MOUSE Protein?
      CXCL16 MOUSE Protein has a total Mw of 9.9kDa.

      What is the source or expression system of CXCL16 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL16 MOUSE Protein?
      CXCL16 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL16 MOUSE Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 100-1000ng/ml corresponding to a Specific Activity of 1,000-10,000IU/mg.

      What is the amino acid sequence of CXCL16 MOUSE Protein?
      NQGSVAGSCS CDRTISSGTQ IPQGTLDHIR KYLKAFHRCP FFIRFQLQSK SVCGGSQDQW VRELVDCFER KECGTGHGKS FHHQKHLP.

      What applications can CXCL16 MOUSE Protein be used in?
      CXCL16 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL16 MOUSE Protein?
      The endotoxin level is minimal, CXCL16 MOUSE 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.

    Cxcl16 Mouse
  • View Data Sheet

    Name :

    CXCL17 Rat

    Description:

    VEGF Co-regulated Chemokine 1 Rat Recombinant

    Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.

    Product # :

    CHM-281

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    Description

    CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.

    Purity

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

    Biological Activity

    Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.

    More Info

    • Introduction

      Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.

    • Synonyms

      Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.

    • Background

      What is the molecular weight/Mw of CXCL17 RAT Protein?
      CXCL17 RAT Protein has a total Mw of 11.5kDa.

      What is the source or expression system of CXCL17 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL17 RAT Protein?
      CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL17 RAT Protein?
      Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.

      What is the amino acid sequence of CXCL17 RAT Protein?
      SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.

      What applications can CXCL17 RAT Protein be used in?
      CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL17 RAT Protein?
      The endotoxin level is minimal, CXCL17 RAT 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.

    Cxcl17 Rat
  • View Data Sheet

    Name :

    Cyclophilin B Mouse

    Description:

    Cyclophilin-B Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.

    Product # :

    ENZ-1039

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

    Description

    Cyclophilin B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (34-216 a.a) and having a molecular mass of 22.7kDa.Cyclophilin B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cyclophilin B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.

    More Info

    • Introduction

      Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.

    • 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 MGSMNDKKKG PKVTVKVYFD LQIGDESVGR VVFGLFGKTV PKTVDNFVAL ATGEKGFGYK NSKFHRVIKD FMIQGGDFTR GDGTGGKSIY GERFPDENFK LKHYGPGWVS MANAGKDTNG SQFFITTVKT SWLDGKHVVF GKVLEGMDVV RKVESTKTDS
      RDKPLKDVII VDSGKIEVEK PFAIAKE.

    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.

    Cyclophilin B Mouse
  • View Data Sheet

    Name :

    DCN Human

    Description:

    Decorin Human Recombinant

    Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

    Product # :

    PRO-1583

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    Description

    DCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (31-359 a.a) and having a molecular mass of 38.6kDa.DCN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCN protein solution (0.25mg/ml) containing 20mM Tris pH 8.0 and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.

    • Synonyms

      Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

    • 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 MDEASGIGPE VPDDRDFEPS LGPVCPFRCQ CHLRVVQCSDLGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK VSPGAFTPLVKLERLYLSKN QLKELPEKMP KTLQELRAHE NEITKVRKVT FNGLNQMIVI ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD GNKISRVDAA SLKGLNNLAKLGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA EHKYIQVVYL HNNNISVVGSSDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK.

    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.

    Dcn Human
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