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Search results

1000 results found for “VEGF Protein”

Name

Description

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  • View Data Sheet

    Name :

    TINAGL1 Human

    Description:

    Tubulointerstitial Nephritis Antigen Like 1 Human Recombinant

    Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.

    Product # :

    PRO-1675

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    800x600 TINAGL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 469 amino acids (22-467) and having a molecular mass of 52.5 kDa.TINAGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TINAGL1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tubulointerstitial Nephritis Antigen Like 1 also known as TINAGL1 is similar in sequence to tubulointerstitial nephritis antigen, a secreted glycoprotein which is identified by antibodies in several types of immune-related tubulointerstitial nephritis. Three transcript variants encoding different isoforms are known for TINAGL1.

    • Synonyms

      Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.

    • 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 MGSAQQGRGR RELAPGLHLR GIRDAGGRYC QEQDLCCRGR ADDCALPYLG AICYCDLFCN RTVSDCCPDF WDFCLGVPPP FPPIQGCMHG GRIYPVLGTY WDNCNRCTCQ ENRQWQCDQE PCLVDPDMIK AINQGNYGWQ AGNHSAFWGM TLDEGIRYRL GTIRPSSSVM NMHEIYTVLN PGEVLPTAFE ASEKWPNLIH EPLDQGNCAG SWAFSTAAVA SDRVSIHSLG HMTPVLSPQN LLSCDTHQQQ GCRGGRLDGA WWFLRRRGVV SDHCYPFSGR ERDEAGPAPP CMMHSRAMGR GKRQATAHCP NSYVNNNDIY QVTPVYRLGS NDKEIMKELM ENGPVQALME VHEDFFLYKG GIYSHTPVSL GRPERYRRHG THSVKITGWG EETLPDGRTL KYWTAANSWG PAWGERGHFR IVRGVNECDI ESFVLGVWGR VGMEDMGHH.

    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.

    Tinagl1 Human
  • View Data Sheet

    Name :

    LIF Human, Sf9

    Description:

    Leukemia Inhibitory Factor Human Recombinant, Sf9

    Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.

    Product # :

    CYT-1003

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    LIF Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 189 amino acids (23-202a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). LIF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 0.5 ng/ml.

    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

      Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.

    • 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

      ADPSPLPITP VNATCAIRHP CHNNLMNQIR SQLAQLNGSA NALFILYYTA QGEPFPNNLD KLCGPNVTDF PPFHANGTEK AKLVELYRIV VYLGTSLGNI TRDQKILNPS ALSLHSKLNA TADILRGLLS NVLCRLCSKY HVGHVDVTYG PDTSGKDVFQ KKKLGCQLLG KYKQIIAVLA
      QAFHHHHHH.

    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 Human Sf9
  • View Data Sheet

    Name :

    TGFBRAP1 Human

    Description:

    Transforming Growth Factor Beta Receptor Associated Protein 1 Human Recombinant

    TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.

    Product # :

    PRO-1890

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TGFBRAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (601-860 a.a) and having a molecular mass of 33kDa.TGFBRAP1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TGFBRAP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      TGF-beta receptor-associated protein 1 also known as TGFBRAP1 takes part in the TGF-beta/activin signaling pathway. TGFBRAP1 is related with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. TGFBRAP1recruits SMAD4 to the vicinity of the receptor complex and smoothes the progress of its interaction with receptor-regulated Smads, such as SMAD2.

    • Synonyms

      TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSKRLQ KEEYHTHLAV LYLEEVLLQR ASASGKGAEA TETQAKLRRL LQKSDLYRVH FLLERLQGAG LPMESAILHG KLGEHEKALH ILVHELQDFA AAEDYCLWCS EGRDPPHRQQ LFHTLLAIYL HAGPTAHELA VAAVDLLNRH ATEFDAAQVL QMLPDTWSVQ LLCPFLMGAM RDSIHARRTM QVALGLARSE NLIYTYDKMK LKGSSIQLSD KKLCQICQNP FCEPVFVRYP NGGLVHTHCA ASRHTNPSSS SPGTRT

    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.

    Tgfbrap1 Human
  • View Data Sheet

    Name :

    TFF1 Human, His

    Description:

    Trefoil Factor-1 Human Recombinant, His Tag

    TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    Product # :

    CYT-610

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TFF-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids (25-84) which includes a 10 amino acid His Tag and having a total molecular mass of 7.9 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF1 His Tag protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5 and 20mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.

    • Synonyms

      TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF1 His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 His Tag 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 add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS EAQTETCTVA PRERQNCGFP GVTPSQCANK GCCFDDTVRG VPWCFYPNTI DVPPEEECEF.

    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.

    Tff1 Human His
  • View Data Sheet

    Name :

    Tri a 14.0101

    Description:

    Non-Specific Lipid-Transfer Protein Tri a 14 Recombinant

    Non-specific lipid-transfer protein, ltp142.

    Product # :

    ALR-025

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    Description

    Recombinant Non-Specific Lipid-Transfer Protein Tri a 14 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 13kDa. Tri a 14.0101 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Tri a 14.0101 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tri a 14.0101 is a non-specific lipid transfer protein and a major wheat allergen. Those who are sensitive to this allergen may have baker’s asthma, a frequent occupational allergic disease caused mainly by inhalation of cereal flour, especially wheat flour. Tri a 14.0101 consists of 4 helical fragments and irregular C-terminal regions which are highly stable to heat treatment and proteolytic attack.

    • Synonyms

      Non-specific lipid-transfer protein, ltp142.

    • 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 IgE-type human antibodies.2. Immunodot test with positive/negative samples.

    • Applications

      Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.

    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.

    Tri A 140101
  • View Data Sheet

    Name :

    MYLPF Human

    Description:

    Myosin Light chain, Phosphorylatable, Fast Skeletal Muscle Human Recombinant

    Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    Product # :

    PRO-243

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    Description

    MYLPF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a) and having a molecular mass of 21.2kDa.MYLPF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYLPF protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin regulatory light chains, including MRCL3, MYLPF and MYL9, regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of myosin regulatory light chains, catalyzed by MLCK in the presence of calcium and calmodulin, increases the actin-activated myosin ATPase activity, thus regulating the contractile activity. MYLPF is vital for fast and slow skeletal muscle development.

    • Synonyms

      Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    • 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 MAPKRAKRRT VEGGSSSVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKKFL EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE.

    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.

    Mylpf Human
  • View Data Sheet

    Name :

    CCL3L1 Human, His

    Description:

    LD78-beta (CCL3L1) Human Recombinant, His Tag

    C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.

    Product # :

    CHM-251

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    Description

    CCL3L1 Human Recombinant fused with a 22 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 90 amino acids (26-93 a.a.) and having a molecular mass of 10kDa. The CCL3L1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL3L1 solution (0.25 mg/ml) contains Phosphate Buffered Saline pH7.4 containing 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCL3L1 is a small cytokine that belongs to the CC chemokines. The CCL3L1 gene is one of several cytokine genes clustered on the q-arm of chromosome 17. CCL3L1 is involved in immunoregulatory and inflammatory processes. CCL3L1 binds to several chemokine receptors including CCBP2 and CCR5. CCR5 is a co-receptor for HIV, and binding of the CCL3L1 protein to CCR5 inhibits HIV entry.

    • Synonyms

      C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.

    • 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 MSLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.

    • Background

      What is the molecular weight/Mw of CCL3L1 HUMAN, HIS Protein?
      CCL3L1 HUMAN, HIS Protein has a total Mw of 10kDa.

      What is the source or expression system of CCL3L1 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL3L1 HUMAN, HIS Protein?
      CCL3L1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL3L1 HUMAN, HIS Protein?
      The biological functionality of CCL3L1 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL3L1 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MSLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.

      What applications can CCL3L1 HUMAN, HIS Protein be used in?
      CCL3L1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL3L1 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL3L1 HUMAN, HIS Protein was purified using conventional chromatography techniques.


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

    Ccl3L1 Human His
  • View Data Sheet

    Name :

    GDNF Rat

    Description:

    Glial-Derived Neurotrophic Factor Rat Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-403

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    Description

    Glial derived Neurotrophic Factor Rat Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 29.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized from a sterile solution containing 1xPBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by HPLC analysis and by SDS-PAGE.

    Biological Activity

    Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

    • Background

      What is the molecular weight/Mw of GDNF RAT Protein?
      GDNF RAT Protein has a total Mw of 29.8kDa.

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

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

      What is the Biological Activity of GDNF RAT Protein?
      Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

      What is the amino acid sequence of GDNF RAT Protein?
      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

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

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

    Gdnf Rat
  • View Data Sheet

    Name :

    BMP 5 Human

    Description:

    Bone Morphogenetic protein-5 Human Recombinant

    Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    Product # :

    CYT-660

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    • sds-page

    Description

    BMP-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (317-454 a.a.) and having a total molecular mass of 15.7 kDa.BMP-5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BMP-5 solution contains 10mM Sodium Citrate buffer (pH3.5) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    BMP5-sds-page - Product image 1

    More Info

    • Introduction

      BMP5 belongs to the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. This superfamily is comprised of large families of growth and differentiation factors. Bone morphogenetic proteins were initially identified by their ability of demineralizing bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
      BMP5 is an essential signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. It was shown that BMP-5 increases the levels of osteopontin, BMP-2, alkaline phosphatase and core binding factor alpha 1 mRNAs in human periodontal (HPL) ligament cells. The BMP5 protein is expressed in normal synovial tissue and reduced in osteoarthritis and rheumatoid arthritis. BMP5 may have a role in certain cancers given that it is differentially regulated during the formation of different tumors.

    • Synonyms

      Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    • 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

      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

    • Background

      Bone Morphogenetic Protein-5 Human Recombinant: Unleashing the Potential for Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-5 (BMP-5) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, repair, and regeneration. This research paper provides an in-depth analysis of BMP-5, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-5 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine hold great promise for addressing the challenges of tissue repair and regeneration. BMP-5, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the unique features of BMP-5 and presents novel approaches for the production and optimization of BMP-5 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-5 is a secreted growth factor that belongs to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intracellular signaling cascades. BMP-5 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, thereby influencing tissue development and repair.

      Production of BMP-5 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-5 human recombinant. Recombinant protein expression systems, including mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-5. Optimization strategies, such as codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-5 recombinant protein.

      Potential Therapeutic Applications:

      BMP-5 human recombinant holds tremendous potential in the field of tissue engineering and regenerative medicine. It plays a crucial role in bone formation, cartilage regeneration, and wound healing, making it a promising candidate for the treatment of skeletal disorders, osteochondral defects, and tissue injuries. Furthermore, the ability of BMP-5 to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-5 human recombinant emerges as a key regulator in tissue engineering and regenerative medicine, with significant implications for tissue repair and regeneration. Optimizing production methodologies and further elucidating its signaling mechanisms will enhance its therapeutic applications. With its involvement in bone and cartilage formation, as well as wound healing, BMP-5 human recombinant represents a promising tool for promoting tissue regeneration and addressing the challenges of tissue repair in various clinical contexts.

      What is the molecular weight/Mw of BMP5 Protein?
      BMP5 Protein has a total Mw of 15.7kDa.

      What is the source or expression system of BMP5 Protein?
      Escherichia Coli.

      What is the Purity of BMP5 Protein?
      BMP5 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP5 Protein?
      The biological functionality of BMP5 Protein will be determined in the future.

      What is the amino acid sequence of BMP5 Protein?
      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

      What applications can BMP5 Protein be used in?
      BMP5 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP5 Protein?
      The endotoxin level is minimal, BMP5 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.

    Bmp 5 Human
  • View Data Sheet

    Name :

    DPPA4 Human

    Description:

    Developmental Pluripotency Associated 4 Human Recombinant

    Developmental Pluripotency Associated Protein 4, 2410091M23Rik.

    Product # :

    PRO-1546

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    Description

    DPPA4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-304) and having a molecular mass of 35.9kDa.DPPA4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DPPA4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      DPPA4 takes part in the conservation of active epigenetic status of target genes and prevents differentiation of embryonic cells into a primal ectoderm extraction.

    • Synonyms

      Developmental Pluripotency Associated Protein 4, 2410091M23Rik.

    • 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 MGSMLRGSAS STSMEKAKGK EWTSTEKSRE EDQQASNQPN SIALPGTSAK RTKEKMSIKG SKVLCPKKKA EHTDNPRPQK KIPIPPLPSK LPPVNLIHRD ILRAWCQQLK LSSKGQKLDA YKRLCAFAYP NQKDFPSTAK EAKIRKSLQK KLKVEKGETS LQSSETHPPE VALPPVGEPP ALENSTALLE GVNTVVVTTS APEALLASWA RISARARTPE AVESPQEASG VRWCVVHGKS LPADTDGWVH LQFHAGQAWV PEKQEGRVSA LFLLPASNFP PPHLEDNMLC PKCVHRNKVL IKSLQWE

    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.

    Dppa4 Human
  • View Data Sheet

    Name :

    LDOC1L Human

    Description:

    Leucine Zipper, Down-Regulated in Cancer 1-Like Human Recombinant

    Protein LDOC1L, Leucine zipper protein down-regulated in cancer cells-like, Mammalian retrotransposon-derived protein 6, LDOC1L, MAR6, MART6, dJ1033E15.2.

    Product # :

    PRO-1153

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    Description

    LDOC1L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-239 a.a) and having a molecular mass of 28.7kDa.LDOC1L is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LDOC1L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% glycerol, 2mM DTT, 0.1mM PMSF and 1mM EDTA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leucine zipper down-regulated in cancer 1-like (LDOC1L) is a member of the LDOC1 family. LDOC1L is a nuclear protein containing a leucine zipper-like motif and a proline-rich region that shares noticeable similarity with an SH3-binding domain. LDOC1L localizes to the nucleus and is downregulated in certain cancer cell lines. LDOC1L is believed to regulate the transcriptional response mediated by the nuclear factor kB (NFkB).

    • Synonyms

      Protein LDOC1L, Leucine zipper protein down-regulated in cancer cells-like, Mammalian retrotransposon-derived protein 6, LDOC1L, MAR6, MART6, dJ1033E15.2.

    • 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 MGSHMVQPQT SKAESPALAA SPNAQMDDVI DTLTSLRLTN SALRREASTL RAEKANLTNM LESVMAELTL LRTRARIPGA LQITPPISSI TSNGTRPMTT PPTSLPEPFS GDPGRLAGFL MQMDRFMIFQ ASRFPGEAER VAFLVSRLTG EAEKWAIPHM QPDSPLRNNY QGFLAELRRT YKSPLRHARR AQIRKTSASN RAVRERQMLC RQLASAGTGP CPVHPASNGT SPAPALPARA RNL.

    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.

    Ldoc1L Human
  • View Data Sheet

    Name :

    VSNL1 Human, His

    Description:

    Visinin-Like Protein-1 Human Recombinant, His Tag

    VISL1, VISL-1, VIS1, VIS-1, VILIP, HLP3, Hippocalcin-like protein 3, VSNL1, VILIP-1, VILIP1, HLP-3, HPCAL3, HUVISL1, Visinin-like protein 1.

    Product # :

    PRO-602

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    Description

    Visinin-Like Protein-1 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids and having a molecular mass of 23.4 kDa. Visinin-Like Protein-1 is fused to His tag at N-Terminus.The protein‘s amino acid sequence corrssponds toUniProtKB/Swiss-Prot entry P62760.Visinin-Like Protein-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      VSNL1 is a member of the visinin/recoverin subfamily of neuronal calcium sensor proteins. VILIP1 is strongly expressed in granule cells of the cerebellum where it associates with membranes in a calcium-dependent manner and modulates intracellular signaling pathways of the central nervous system by directly or indirectly regulating the activity of adenylyl cyclase. Changes in cellular expression of VSNL1 were found in hipppocampi of schizophrenics, since more interneurons showed immunoreactivity.
      VILIP1 is expressed in pancreatic beta-cells. VILIP1 elevation enhances insulin secretion in cAMP-associated manner. Down-regulation of VILIP-1 decreased cAMP accumulation but increased insulin gene transcription. VILIP-1 interacts with cell membrane and actin-based cytoskeleton. VSNL1 modulates cAMP-accumulation in C6 glioma cells. HLP3 modulates cGMP-accumulation in transfected neural cells and cerebellar granule neurons.

    • Synonyms

      VISL1, VISL-1, VIS1, VIS-1, VILIP, HLP3, Hippocalcin-like protein 3, VSNL1, VILIP-1, VILIP1, HLP-3, HPCAL3, HUVISL1, Visinin-like protein 1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS MGKQNSKLAP EVMEDLVKST EFNEHELKQW YKGFLKDCPS GRLNLEEFQQ LYVKFFPYGD ASKFAQHAFR TFDKNGDGTI DFREFICALS ITSRGSFEQK LNWAFNMYDL DGDGKITRVE MLEIIEAIYK MVGTVIMMKM NEDGLTPEQR VDKIFSKMDK NKDDQITLDE FKEAAKSDPS IVLLLQCDIQK.

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    Vsnl1 Human His
  • View Data Sheet

    Name :

    NHEJ1 Human

    Description:

    Nonhomologous End-Joining Factor 1 Human Recombinant

    Nonhomologous end-joining factor 1, Protein cernunnos, XRCC4-like factor, Cernunnos, XLF, FLJ12610.

    Product # :

    PRO-1193

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    Description

    NHEJ1 Human Recombinant produced in E. coli is a single polypeptide chain containing 247 amino acids (1-224) and having a molecular mass of 27.8 kDa.NHEJ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NHEJ1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Non-homologous end-joining factor 1 (NHEJ1) is a member of the XLF family. NHEJ1 is a DNA repair factor vital for the nonhomologous end-joining pathway, which preferentially mediates repair of double-stranded breaks. NHEJ1 gene mutations cause different kinds of severe combined immunodeficiency disorders. NHEJ1 was initially detected as the protein mutated in five patients with growth retardation, microcephaly, and immunodeficiency. In addition, patients with NHEJ1 mutations have immunodeficiency caused by a defect in V(D)J recombination, which employs NHEJ to promote immune system diversity.

    • Synonyms

      Nonhomologous end-joining factor 1, Protein cernunnos, XRCC4-like factor, Cernunnos, XLF, FLJ12610.

    • 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 MGS MEELEQG LLMQPWAWLQ LAENSLLAKV FITKQGYALL VSDLQQVWHE QVDTSVVSQR AKELNKRLTA PPAAFLCHLD NLLRPLLKDA AHPSEATFSC DCVADALILR VRSELSGLPF YWNFHCMLAS PSLVSQHLIR PLMGMSLALQ CQVRELATLL HMKDLEIQDY QESGATLIRD RLKTEPFEEN SFLEQFMIEK LPEACSIGDG KPFVMNLQDL YMAVTTQ

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    Nhej1 Human
  • View Data Sheet

    Name :

    CFLAR Human

    Description:

    CASP8 and FADD-Like Apoptosis Regulator Human Recombinant

    CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.

    Product # :

    PRO-920

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    Description

    CFLAR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 480 amino acids (1-480) and having a molecular mass of 55.3 kDa.The CFLAR is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      The precise role of CFLAR is not yet revealed but it seems it is vital in apoptosis regulation downstream of all identified death receptors.

    • Synonyms

      CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.

    • 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

      MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG KPKMFFIQNY VVSEGQLENS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD FFWSLCTADM SLLEQSHSSP SLYLQCLSQK LRQERKRPLL DLHIELNGYM YDWNSRVSAK EKYYVWLQHT LRKKLILSYT.

    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.

    Cflar Human
  • View Data Sheet

    Name :

    MMADHC Human

    Description:

    Methylmalonic Aciduria cblD type, with Homocystinuria Human Recombinant

    Chromosome 2 Open Reading Frame 25, Methylmalonic Aciduria (Cobalamin Deficiency) CblD Type With Homocystinuria, Methylmalonic Aciduria And Homocystinuria Type D Protein Mitochondrial, Protein C2orf25 Mitochondrial, CL25022, C2orf25, cblD.

    Product # :

    PRO-1850

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    Description

    MMADHC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (39-296) and having a molecular mass of 31.0 kDa. MMADHC is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMADHC is a mitochondrial protein which takes part in an early step of vitamin B1 2 metabolism. Vitamin B12 (cobalamin) is vital for regular development and existence in humans. Mutations in MMADHC can result in methylmalonic aciduria and homocystinuria type cblD, a cobalamin metabolism syndrome which is characterized by decreased levels of the coenzymes methylcobalamin and adenosylcobalamin.

    • Synonyms

      Chromosome 2 Open Reading Frame 25, Methylmalonic Aciduria (Cobalamin Deficiency) CblD Type With Homocystinuria, Methylmalonic Aciduria And Homocystinuria Type D Protein Mitochondrial, Protein C2orf25 Mitochondrial, CL25022, C2orf25, cblD.

    • 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 MGSSDESHVA AAPPDICSRT VWPDETMGPF GPQDQRFQLP GNIGFDCHLN GTASQKKSLV HKTLPDVLAE PLSSERHEFV MAQYVNEFQG NDAPVEQEIN SAETYFESAR VECAIQTCPE LLRKDFESLF PEVANGKLMI LTVTQKTKND MTVWSEEVEI EREVLLEKFI NGAKEICYAL RAEGYWADFI DPSSGLAFFG PYTNNTLFET DERYRHLGFS VDDLGCCKVI RHSLWGTHVV VGSIFTNATP DSHIMKKLSG N

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    Mmadhc Human
  • View Data Sheet

    Name :

    ACTN1 Human

    Description:

    Actinin Alpha 1 Human Recombinant

    ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.

    Product # :

    PRO-2227

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    Description

    ACTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31.4kDa. ACTN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACTN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

    • Synonyms

      ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFMDHYD SQQTNDYMQP EEDWDRDLLL DPAWEKQQRK TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY LDIPKMLDAE DIVGTARPDE KAIMTYVSSF YHAF.

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    Actn1 Human
  • View Data Sheet

    Name :

    SERPINH1 Human

    Description:

    Heat Shock 47kDa Human Recombinant

    HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.

    Product # :

    HSP-047

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    Description

    Recombinant Human HSP47 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (18-418 a.a.) and having a molecular mass of 48.9 kDa. HSP47 human recombinant is fused to a 38 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINH1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SERPINH1 is part of the serpin superfamily of serine proteinase inhibitors. SEPINH1 expression is induced by heat shock. HSP47 localizes to the endoplasmic reticulum lumen and binds collagen therefore it is a molecular chaperone which takes part in the maturation of collagen molecules, facilitating the folding and assembly of procollagen molecules, retaining unfolded molecules within the ER, and assisting the transport of correctly folded-molecules from the ER to Golgi apparatus. Autoantibodies to HSP47 protein have been found in rheumatoid arthritis. SERPINH1 binds specifically to collagen and acts as a chaperone in the biosynthetic pathway of collagen.

    • Synonyms

      HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.

    • 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 KDRWGSHMAA EVKKPAAAAA PGTAEKLSPK AATLAERSAG LAFSLYQAMA KDQAVENILV SPVVVASSLG LVSLGGKATT ASQAKAVLSA EQLRDEEVHA GLGELLRSLS NSTARNVTWK LGSRLYGPSS VSFADDFVRS SKQHYNCEHS KINFRDKRSA LQSINEWAAQ TTDGKLPEVT KDVERTDGAL LVNAMFFKPH WDEKFHHKMV DNRGFMVTRS YTVGVMMMHR TGLYNYYDDE KEKLQIVEMP LAHKLSSLII LMPHHVEPLE RLEKLLTKEQ LKIWMGKMQK KAVAISLPKG VVEVTHDLQK HLAGLGLTEA IDKNKADLSR MSGKKDLYLA SVFHATAFEL DTDGNPFDQD IYGREELRSP KLFYADHPFI FLVRDTQSGS LLFIGRLVRP KGDKMRDEL.

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    Serpinh1 Human
  • View Data Sheet

    Name :

    DKK3 Human, HEK

    Description:

    Dickkopf-Related Protein 3 Human Recombinant, HEK

    Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    Product # :

    PRO-1638

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    Description

    DKK3 Human Recombinant is a single polypeptide chain containing 337 amino acids (22-350). DKK3 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    DKK3 was lyophilized from a 0.2µM filtered solution of 20mM PB and 150mM NaCl, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.

    • Synonyms

      Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized DKK3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DKK3 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 DKK3 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APAPTATSAPVKPGPALSYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAA
      KASSEVNLANLPPSYHNETNTDTKVGNNTIHVHREIHKITNNQTGQMVFSETVITSVG
      DEEGRRSHECIIDEDCGPSMYCQFASFQYTCQPCRGQRMLCTRDSECCGDQLCVWGHC
      TKMATRGSNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPASRLLDLIT
      WELEPDGALDRCPCASGLLCQPHSHSLVYVCKPTFVGSRDQDGEILLPREVPDEYEVG
      SFMEEVRQELEDLERSLTEEMALGEPAAAAAALLGGEEIVDHHHHHH.

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    Dkk3 Human Hek
  • View Data Sheet

    Name :

    FGF4 Human

    Description:

    Fibroblast Growth Factor-4 Human Recombinant

    HBGF4, FGF-4, FGF4, KFGF, HSTF1.

    Product # :

    CYT-312

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    Description

    FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa. The FGF4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF4 protein was lyophilized with 20mM sodium phosphate and 500mM NaCl pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.

    More Info

    • Introduction

      FGF4 holds s comprehensive mitogenic and cell survival activities and takes part in a range of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF4 possess oncogenic transforming activity. FGF4 and FGF3, oncogenic growth factors are localized on chromosome 11. Co-amplification of both factors was found in several kinds of human tumors. FGF4 functions in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway.

    • Synonyms

      HBGF4, FGF-4, FGF4, KFGF, HSTF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-4 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 FGF4 Human Recombinant sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.

    • Background

      What is the molecular weight/Mw of FGF4 HUMAN Protein?
      FGF4 HUMAN Protein has a total Mw of 19.8kDa.

      What is the source or expression system of FGF4 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FGF4 HUMAN Protein?
      FGF4 HUMAN Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF4 HUMAN Protein?
      The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.

      What is the amino acid sequence of FGF4 HUMAN Protein?
      MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.

      What applications can FGF4 HUMAN Protein be used in?
      FGF4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF4 HUMAN Protein?
      The endotoxin level is minimal, FGF4 HUMAN Protein was purified using conventional chromatography techniques.

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    Fgf4 Human
  • View Data Sheet

    Name :

    TSH Protein

    Description:

    Thyroid Stimulating Hormone Human Recombinant

    Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.

    Product # :

    HOR-050

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    Description

    Thyroid Stimulating Hormone Human Recombinant produced in HEK 293 cells.

    Source

    HEK 293 cells.

    Formulation

    Lyophilized from a concentrated 50mM ammonium bicarbonate.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The protein is biologically active using Siemens Centaur CP is standardized against WHO 3rd IS 81/565.

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    • Synonyms

      Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Recombinant TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant TSH 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 recombinant TSH in sterile 10 mM Sodium Phosphate, 150 mM Sodium Chloride, 1 mg/ml BSA, 0.1% Sodium Azide (optional), pH 7.4.

    • Background

      Thyroid-stimulating hormone (TSH), also known as thyrotropin, is a glycoprotein hormone produced by the anterior pituitary gland. Its primary function is to regulate thyroid gland activity by stimulating the synthesis and secretion of thyroid hormones, thyroxine (T4) and triiodothyronine (T3). Recombinant human TSH (rhTSH) has emerged as a valuable tool in clinical practice, particularly in the management of thyroid disorders and in diagnostic procedures involving the thyroid gland. This paper aims to provide an overview of research on rhTSH, including its mechanism of action, activity, and therapeutic applications.

      The mechanism of action of rhTSH involves binding to the TSH receptor (TSHR) on the surface of thyroid follicular cells. This interaction activates intracellular signalling pathways, including cyclic adenosine monophosphate (cAMP) production and protein kinase A (PKA) activation. These pathways stimulate various cellular processes within thyroid follicular cells, such as iodine uptake, thyroid hormone synthesis, and secretion.

      What is the source or expression system of TSH PROTEIN Protein?
      HEK 293 cells.

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

      What is the Biological Activity of TSH PROTEIN Protein?
      The protein is biologically active using Siemens Centaur CP is standardized against WHO 3rd IS 81/565.

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

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


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    Tsh Recombinant
  • View Data Sheet

    Name :

    ENO2 Protein

    Description:

    Enolase-2 Human

    Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    Product # :

    ENZ-371

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    Description

    Human Neurone Specific Enolase produced in Human CNS having a molecular mass of 45kDa.

    Source

    Human CNS.

    Formulation

    The protein solution is in 10mM NaH2PO4 buffer pH 7.4 containing 150mM NaCl and 5mM MgSO4.

    Purity

    Greater than 96.0%.

    More Info

    • Introduction

      Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.

    • Synonyms

      Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Human NSE although stable at 4°C for 1 week, should be stored at -18°C.

    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.

    Eno2 Human
  • View Data Sheet

    Name :

    OmpA

    Description:

    Outer Membrane Protein-A Bacterial Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-571

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    Description

    The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.

    More Info

    • Introduction

      The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.

    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.

    Outer Membrane Protein A
  • View Data Sheet

    Name :

    Cyclophilin A Mouse

    Description:

    Cyclophilin A Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.

    Product # :

    ENZ-857

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    Description

    Cyclophilin A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.

    • 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 MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL.

    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 A Mouse
  • View Data Sheet

    Name :

    HIF1A Human (85 a.a.)

    Description:

    Hypoxia-Inducible Factor-1 Alpha (85 a.a.) Human Recombinant

    Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

    Product # :

    PRO-258

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    Description

    HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-85 a.a.) and having a molecular mass of 11.8 kDa. The HIF1A is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HIF1A Human (0.25mg/ml) solution containing 20mM Tris buffer(pH 8.0), 20% glycerol, 1mM DTT, 0.2M NaCl and 1mM EDTA.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.

    • Synonyms

      Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

    • 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 MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM RLTISYLRVR KLLDAGDLDI EDDMK.

    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.

    Hif1A Human 85 Aa
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