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Search results

1000 results found for “Chromogranin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    VAMP5 Human

    Description:

    Vesicle-associated membrane protein 5 Human Recombinant

    VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.

    Product # :

    PRO-681

    Price :

    Quantity :

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    • source
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    Description

    VAMP5 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 109 amino acids (1-72 a.a.) and having a molecular mass of 12.7 kDa.VAMP5 is fused to 37 amino acids His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VAMP5 (0.5mg/ml) protein solution contains 20mM Tris-HCl (pH 8.0), 0.2M NaCl, 5mM DTT, 0.5mM EDTA and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      VAMP5 is part of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily. VAMP5 is involved is vesicle trafficking events that are associated with myogenesis.

    • Synonyms

      VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.

    • 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 KDRWGSHMAG IELERCQQQA NEVTEIMRNN FGKVLERGVK LAELQQRSDQ LLDMSSTFNK TTQNLAQKKC WENIRYRIC.

    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.

    Vamp5 Human
  • View Data Sheet

    Name :

    NCK2 Human

    Description:

    NCK Adaptor Protein 2 Human Recombinant

    NCK Adaptor Protein 2, Growth Factor Receptor-Bound Protein 4, SH2/SH3 Adaptor Protein NCK-Beta, Noncatalytic Region Of Tyrosine Kinase Beta,  Cytoplasmic Protein NCK2, GRB4, NCKbeta, Nck-2.

    Product # :

    PRO-1621

    Price :

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    Description

    NCK2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-380) and having a molecular mass of 45.3kDa.NCK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NCK2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NCK2 belongs to the NCK family of adaptor proteins. NCK2 holds one SH2 domain and three SH3 domains. NCK2 bind and recruit several proteins that take part in the regulation of receptor protein tyrosine kinases even though it has no known catalytic function. That indicates that NCK2 takes part in cytoskeletal reorganization. Alternate transcription splice variants, encoding diverse isoforms, were characterized.

    • Synonyms

      NCK Adaptor Protein 2, Growth Factor Receptor-Bound Protein 4, SH2/SH3 Adaptor Protein NCK-Beta, Noncatalytic Region Of Tyrosine Kinase Beta, Cytoplasmic Protein NCK2, GRB4, NCKbeta, Nck-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 MGSMTEEVIV IAKWDYTAQQ DQELDIKKNE RLWLLDDSKT WWRVRNAANR TGYVPSNYVE RKNSLKKGSL VKNLKDTLGL GKTRRKTSAR DASPTPSTDA EYPANGSGAD RIYDLNIPAF VKFAYVAERE DELSLVKGSR VTVMEKCSDG WWRGSYNGQI GWFPSNYVLE EVDEAAAESP SFLSLRKGAS LSNGQGSRVL HVVQTLYPFS SVTEEELNFE KGETMEVIEK PENDPEWWKC KNARGQVGLV PKNYVVVLSD GPALHPAHAP QISYTGPSSS GRFAGREWYY GNVTRHQAEC ALNERGVEGD FLIRDSESSP SDFSVSLKAS GKNKHFKVQL VDNVYCIGQR RFHTMDELVE HYKKAPIFTS EHGEKLYLVR ALQ

    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.

    Nck2 Human
  • View Data Sheet

    Name :

    TXN1, His

    Description:

    Thioredoxin Recombinant, His Tag

    Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    Product # :

    PRO-784

    Price :

    Quantity :

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    Description

    Recombinant Thioredoxin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (2-109 a.a.) and having a molecular mass of 12.8kDa. TRX contains 9 amino acid His Tag N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TRX His Tag protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >70 A650/cm/min/mg, detected by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.

    Citations

    More Info

    • Introduction

      Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in

    • Synonyms

      Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    • 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

      MHHHHHHMGS DKIIHLTDDS FDTDVLKADG AILVDFWAEW CGPCKMIAPI LDEIADEYQG KLTVAKLNID QNPGTAPKYG IRGIPTLLLF KNGEVAATKV GALSKGQLKE FLDANLAGS.

    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.

    Thioredoxin 1 His
  • View Data Sheet

    Name :

    VEGF Human

    Description:

    Vascular Endothelial Growth Factor Human Recombinant

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-241

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    • description
    • source
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    • Citations

    Description

    Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38.2kDa.The VEGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VEGF protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

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

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 3.7-5.6 ng/ml, corresponding to a Specific Activity of 178,570-270,270IU/mg.

    Citations

    More Info

    • Introduction

      Vascular endothelial growth factor (VEGF) is an important signaling protein involved in vessel formation As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces vasculogenesis and endothelial cell production, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. VEGF is located in normal cartilage though only osteoarthritic cartilage expresses the VEGF receptors, NP1, VEGFR1 and VEGFR2. The VEGF level in the culture media from OA chondrocytes was more than 3 folds higher than in media from normal chondrocytes

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR

    • Protein content

      VEGF protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.2875 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of VEGF as a Reference Standard.

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

    Vegf Human
  • View Data Sheet

    Name :

    FGF23 Human

    Description:

    Fibroblast Growth Factor-23 Human Recombinant

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

    Product # :

    CYT-020

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    • purity
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    • More Info
    • Citations

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    Citations

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    • Introduction

      FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FGF-23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

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

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

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

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

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

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

    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.

    Fgf23 Human
  • View Data Sheet

    Name :

    FCER1A Human 201 a.a

    Description:

    IgE Receptor Subunit A Human Recombinant

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

    Product # :

    PRO-2357

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      The Recombinant FCER1A protein although stable at 4°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

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

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    Fcer1A Human 201 Aa
  • View Data Sheet

    Name :

    GDF6 Human

    Description:

    Bone Morphogenetic protein-13 Human Recombinant

    Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    Product # :

    CYT-938

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    Description

    BMP13 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.1kDa.The BMP-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-13 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

    Citations

    More Info

    • Introduction

      Growth/differentiation factors (GDF1-GDF15) belong to the BMP family of TGF-beta superfamily proteins. These factors are produced as inactive preproproteins which are subsequently cleaved and assembled into active secreted homodimers. BMP13 is a growth factor which controls proliferation and cellular differentiation in the retina and bone formation. BMP13 has a central role in regulating apoptosis during retinal development. GDF proteins are vital during embryonic development, particularly in the skeletal, nervous, and muscular systems. BMP13 gene mutations result in colobomata, which are congenital abnormalities in ocular development, and in Klippel-Feil syndrome (KFS), which is a congenital disorder of spinal segmentation.

    • Synonyms

      Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-13 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 BMP13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

    • Background

      Bone Morphogenetic Protein-13 Human Recombinant: Unraveling its Potential in Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-13 (BMP-13) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-13, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-13 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 in addressing tissue repair and regeneration challenges. BMP-13, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-13 and presents novel approaches for the production and optimization of BMP-13 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-13 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling cascades. BMP-13 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.

      Production of BMP-13 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-13 human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-13. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-13 recombinant protein.

      Potential Therapeutic Applications:

      BMP-13 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its involvement in cartilage formation, osteogenesis, and tissue repair makes it a potential candidate for the treatment of musculoskeletal disorders, joint injuries, and cartilage defects. Furthermore, the ability of BMP-13 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-13 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in cartilage and bone formation, as well as tissue repair, BMP-13 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.

      What is the molecular weight/Mw of GDF6 Protein?
      GDF6 Protein has a total Mw of 27.1kDa.

      What is the source or expression system of GDF6 Protein?
      Escherichia Coli.

      What is the Purity of GDF6 Protein?
      GDF6 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF6 Protein?
      The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

      What is the amino acid sequence of GDF6 Protein?
      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

      What applications can GDF6 Protein be used in?
      GDF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF6 Protein?

      The endotoxin level is minimal, GDF6 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.

    Bmp13 Human
  • View Data Sheet

    Name :

    FCGR2B Human

    Description:

    CD32 Human Recombinant

    CD32, CD32B, FCG2, FCGR2, IGFR2, Low affinity immunoglobulin gamma Fc region receptor II-b, CDw32, Fc-gamma-RIIb, FcRII-b.

    Product # :

    PRO-1295

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    Description

    FCGR2B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (46-217a.a.) and having a molecular mass of 22.0kDa. FCGR2Bis fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FCGR2B protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      FCGR2B is a low affinity receptor for the Fc region of immunoglobulin gamma complexes. FCGR2B participates in the phagocytosis of immune complexes and in the regulation of antibody production by B-cells. FCGR2B Expressed in monocyte, neutrophils, macrophages, basophils, eosinophils, Langerhans cells, B-cells, platelets cells and placenta (endothelial cells). Variants in FCGR2B may increase susceptibilty to systemic lupus erythematosus (SLE).

    • Synonyms

      CD32, CD32B, FCG2, FCGR2, IGFR2, Low affinity immunoglobulin gamma Fc region receptor II-b, CDw32, Fc-gamma-RIIb, FcRII-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. 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 MGSHMAPPKA VLKLEPQWIN VLQEDSVTLT CRGTHSPESD SIQWFHNGNL IPTHTQPSYR FKANNNDSGE YTCQTGQTSL SDPVHLTVLS EWLVLQTPHL EFQEGETIVL RCHSWKDKPL VKVTFFQNGK SKKFSRSDPN FSIPQANHSH SGDYHCTGNI GYTLYSSKPV TITVQAP.

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    Fcgr2B Human
  • View Data Sheet

    Name :

    KLK7 Human, sf9

    Description:

    Kallikrein-7 Human Recombinant, sf9

    Kallikrein Related Peptidase 7, Kallikrein 7 (Chymotryptic, Stratum Corneum), Stratum Corneum Chymotryptic Enzyme, Serine Protease 6, PRSS6, SCCE, HK7, Kallikrein-Related Peptidase 7, Signal Protein, EC 3.4.21.117, EC 3.4.21, HSCCE.

    Product # :

    ENZ-962

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    Description

    KLK7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (1-181 a.a.) and having a molecular mass of 20.9kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). KLK7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK7 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 cleaves insulin B chain at ''6-Leu- -Cys-7'', ''16-Tyr- -Leu-17'', ''25-Phe- -Tyr-26'' and ''26-Tyr--Thr-27''. KLK7 is involved in the activation of precursors to inflammatory cytokines.

    • Synonyms

      Kallikrein Related Peptidase 7, Kallikrein 7 (Chymotryptic, Stratum Corneum), Stratum Corneum Chymotryptic Enzyme, Serine Protease 6, PRSS6, SCCE, HK7, Kallikrein-Related Peptidase 7, Signal Protein, EC 3.4.21.117, EC 3.4.21, HSCCE.

    • 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

      ADPMNEYTVH LGSDTLGDRR AQRIKASKSF RHPGYSTQTH VNDLMLVKLN SQARLSSMVK KVRLPSRCEP PGTTCTVSGW GTTTSPDVTF PSDLMCVDVK LISPQDCTKV YKDLLENSML CAGIPDSKKN ACNGDSGGPL VCRGTLQGLV SWGTFPCGQP NDPGVYTQVC KFTKWINDTM KKHRHHHHHH.

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    Klk7 Human Sf9
  • View Data Sheet

    Name :

    CREB3L2 Human

    Description:

    CAMP Responsive Element Binding Protein 3-Like 2 Human Recombinant

    CAMP Responsive Element Binding Protein 3-Like 2, BBF2H7, CAMP-Responsive Element-Binding Protein 3-Like Protein 2, BBF2 Human Homolog On Chromosome 7, Cyclic AMP-Responsive Element-Binding Protein 3-Like Protein 2, Basic Transcription Factor 2, B-ZIB Transcription Factor, FUS/BBF2H7 Protein, TCAG_1951439, Cyclic AMP-responsive element-binding protein 3-like protein 2, cAMP-responsive element-binding protein 3-like protein 2.

    Product # :

    PRO-2153

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    Description

    CREB3L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-378 a.a) and having a molecular mass of 44kDa. CREB3L2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CREB3L2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CAMP Responsive Element Binding Protein 3-Like 2, also known as CREB3L2 belongs to the oasis bZIP transcription factor family. Members of this family are able to dimerize however from homodimers only. CREB3L2 is a transcriptional activator. Translocations between CREB3L2 on chromosome 7 and the gene fused in sarcoma on chromosome 16 can be found in some tumors. One disease which is associated with CREB3L2 is myxofibrosarcoma.

    • Synonyms

      CAMP Responsive Element Binding Protein 3-Like 2, BBF2H7, CAMP-Responsive Element-Binding Protein 3-Like Protein 2, BBF2 Human Homolog On Chromosome 7, Cyclic AMP-Responsive Element-Binding Protein 3-Like Protein 2, Basic Transcription Factor 2, B-ZIB Transcription Factor, FUS/BBF2H7 Protein, TCAG_1951439, Cyclic AMP-responsive element-binding protein 3-like protein 2, cAMP-responsive element-binding protein 3-like protein 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 MGSMEVLESG EQGVLQWDRK LSELSEPGDG EALMYHTHFS ELLDEFSQNV LGQLLNDPFL SEKSVSMEVE PSPTSPAPLI QAEHSYSLCE EPRAQSPFTH ITSDSFNDDE VESEKWYLST DFPSTSIKTE PITDEPPPGL VPSVTLTITA ISTPLEKEEP PLEMNTGVDS SCQTIIPKIK LEPHEVDQFL NFSPKEAPVD HLHLPPTPPS SHGSDSEGSL SPNPRLHPFS LPQTHSPSRA APRAPSALSS SPLLTAPHKL QGSGPLVLTE EEKRTLIAEG YPIPTKLPLS KSEEKALKKI RRKIKNKISA QESRRKKKEY MDSLEKKVES CSTENLELRK KVEVLENTNR TLLQQLQKLQ TLVMGKVSRT CKLAGTQTGT C.

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    Creb3L2 Human
  • View Data Sheet

    Name :

    SNCA Human

    Description:

    Alpha Synuclein Human Recombinant

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

    Product # :

    PRO-393

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    Description

    a-Synuclein Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (Real molecular weight on SDS-PAGE will be shift up). The Recombinant Human a-Synuclein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl and 1mM MgCl2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.

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

    Snca Human
  • View Data Sheet

    Name :

    Vimentin Bovine

    Description:

    Bovine Vimentin

    Vimentin, Vim, FLJ36605.

    Product # :

    PRO-525

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    Description

    Bovine Vimentin protein produced in Bovine Lens, having a molecular weight of 57 kDa.

    Source

    Bovine Lens.

    Formulation

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

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.

    • Synonyms

      Vimentin, Vim, FLJ36605.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Reconstitution to filaments

      After vimentin is dissolved in 6M urea buffer (see above), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Sodium Phosphate, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco''s PBS).- Hatzfeld M. and Franke W.W. (1985). J. Cell Biol. 101, 1826-1841.- Hatzfeld M. et al. (1987). J. Mol. Biol. 197, 237-255.

    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.

    Vimentin Bovine
  • View Data Sheet

    Name :

    HDGFL1 Human

    Description:

    Hepatoma Derived Growth Factor-Like 1 Human Recombinant

    Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.

    Product # :

    CYT-850

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    Description

    HDGFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-251 a.a) and having a molecular mass of 29.6kDa.HDGFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HDGFL1 protein solution (0.25mg/ml) containing Phosphate buffered saline, (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Hepatoma Derived Growth Factor-Like 1 (HDGFL1) is a member of the HDGF family and contains 1 PWWP domain.

    • Synonyms

      Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing 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).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.

    • Background

      What is the molecular weight/Mw of HDGFL1 HUMAN Protein?
      HDGFL1 HUMAN Protein has a total Mw of 29.6kDa.

      What is the source or expression system of HDGFL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of HDGFL1 HUMAN Protein?
      HDGFL1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of HDGFL1 HUMAN Protein?
      The biological functionality of HDGFL1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of HDGFL1 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.

      What applications can HDGFL1 HUMAN Protein be used in?
      HDGFL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HDGFL1 HUMAN Protein?
      The endotoxin level is minimal, HDGFL1 HUMAN Protein was purified using conventional chromatography techniques.


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

    Hdgfl1 Human
  • View Data Sheet

    Name :

    NEUROG3 Human

    Description:

    Neurogenin 3 Human Recombinant

    Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.

    Product # :

    CYT-811

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    Description

    NEUROG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-214) and having a molecular mass of 25.1 kDa. NEUROG3 is fused to a 20 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The NEUROG3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NEUROG3 is a common helix-loop-helix (bHLH) transcription factor which takes part in neurogenesis. NEUROG3 functions as a heterodimer with another bHLH protein. Mutations in this gene can result in congenital malabsorptive diarrhea 4 (DIAR4).

    • Synonyms

      Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.

    • 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 MTPQPSGAPT VQVTRETERS FPRASEDEVT CPTSAPPSPT RTRGNCAEAE EGGCRGAPRK LRARRGGRSR PKSELALSKQ RRSRRKKAND RERNRMHNLN SALDALRGVL PTFPDDAKLT KIETLRFAHN YIWALTQTLR IADHSLYALE PPAPHCGELG SPGGSPGDWG SLYSPVSQAG SLSPAASLEE RPGLLGATSS ACLSPGSLAF SDFL

    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.

    Neurog3 Human
  • View Data Sheet

    Name :

    Ostreolysin

    Description:

    Ostreolysin Pleurotus Ostreatus Recombinant

    Product # :

    PRO-2600

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    Description

    Pleurotus Ostreatus Ostreolysin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15 kDa. The Ostreolysin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Ostreolysin 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 analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Ostreolysin has potent anti-carcinogenic activity in several colon cancer cell lines. 

    Citations

    More Info

    • Introduction

      Ostreolysin is extracted from Pleurotus ostreatus (oyster mushroom). It is a pore forming protein, which contains a lytic part to both cholesterol and sphingomyelin containing membranes. Because of their cholesterol content and the appearance of ostreolysin in the detergent resistant membranes, ostreolysin is cytotoxic towards the ovary cells of Chinese hamster. It seems that Ostreolysin spots a rich lipid cholesterol phase, presumably the liquid ordered phase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pleurotus Ostreatus Ostreolysin 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 Ostreolysin should be stored at 4°C 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 Ostreolysin in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AYAQWVIILI HNVGQQNVKI KNLNASWGKL YADGDKDTEV PASKYEGMVI APGDQVQINA
      CGREDAAEGT TGTFDLVDPN DSDKQVRHIS WDCPWGTKAN SWVVGGSNSK WMIEYTGQNL
      DSGALGTITV NTLKIGN

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 2.64 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNA-man computer analysis program.

    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.

    Ostreolysin
  • View Data Sheet

    Name :

    C7ORF49 Human

    Description:

    Chromosome 7 Open Reading Frame 49 Human Recombinant

    MRI, Modulator of retrovirus infection homolog, C7orf49.

    Product # :

    PRO-1415

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    Description

    C7ORF49 Human Recombinant produced in E. coli is a single polypeptide chain containing 180 amino acids (1-157) and having a molecular mass of 19.2kDa. C7ORF49 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The C7ORF49 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Chromosome 7 Open Reading Frame 49 (C7ORF49) is affiliated with the lncRNA class. C7ORF49 characterizes the hamster ortholog and suggests that it may modulate the ability of the proteasome to degrade retroviral cores upon cellular infection.

    • Synonyms

      MRI, Modulator of retrovirus infection homolog, C7orf49.

    • 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 MGSMETLQSE TKTRVLPSWL TAQVATKNVA PMKAPKRMRM AAVPVAAARL PATRTVYCMN EAEIVDVALG ILIESRKQEK ACEQPALAGA DNPEHSPPCS VSPHTSSGSS SEEEDSGKQA LAPGLSPSQR PGGSSSACSR SPEEEEEEDV LKYVREIFFS.

    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.

    C7Orf49 Human
  • View Data Sheet

    Name :

    PRKACA Human, sf9

    Description:

    c-AMP dependant Protein Kinase A catalytic subunit alpha Human Recombinant, Sf9

    cAMP-dependent protein kinase alpha-catalytic subunit, EC 2.7.11.11, PKA C-alpha, PKACA, PRKACA,  MGC48865, MGC102831.

    Product # :

    PKA-093

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    Description

    PRKACA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 578 amino acids (1-351 a.a.) and having a molecular mass of 67kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). PRKACA is expressed with a 227 amino acid GST Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      cAMP-dependent protein kinase catalytic subunit alpha isoform Calpha1 (PRKACA) belongs to the Ser/Thr protein kinase family. PRKACA is responsible for phosphorylating other proteins and substrates, changing their activity. The PRKACA protein is a member of the AGC kinase family, and contributes to the regulation of cellular processes which include glucose metabolism, cell division, and contextual memory.

    • Synonyms

      cAMP-dependent protein kinase alpha-catalytic subunit, EC 2.7.11.11, PKA C-alpha, PKACA, PRKACA, MGC48865, MGC102831.

    • 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

      MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSHMGN AAAAKKGSEQ ESVKEFLAKA KEDFLKKWES PAQNTAHLDQ FERIKTLGTG SFGRVMLVKH KETGNHYAMK ILDKQKVVKL KQIEHTLNEK RILQAVNFPF LVKLEFSFKD NSNLYMVMEY VPGGEMFSHL RRIGRFSEPH ARFYAAQIVL TFEYLHSLDL IYRDLKPENL LIDQQGYIQV TDFGFAKRVK GRTWTLCGTP EYLAPEIILS KGYNKAVDWW ALGVLIYEMA AGYPPFFADQ PIQIYEKIVS GKVRFPSHFS SDLKDLLRNL LQVDLTKRFG NLKNGVNDIK NHKWFATTDW IAIYQRKVEA PFIPKFKGPG DTSNFDDYEE EEIRVSINEK CGKEFSEF.

    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.

    Prkaca Human Sf9
  • View Data Sheet

    Name :

    TXNDC12 Human

    Description:

    Thioredoxin Domain Containing 12 Human Recombinant

    Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.

    Product # :

    PRO-1133

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    Description

    TXNDC12 Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (27-172) and having a molecular mass of 20.8 kDa.TXNDC12 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TXNDC12 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TXNDC12 is a member of the thioredoxin super family. This Family members have a thioredoxin fold with a consensus active-site sequence (CxxC) and take part in redox regulation, protection against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors.

    • Synonyms

      Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMHN GLGKGFGDHI HWRTLEDGKK EAAASGLPLM VIIHKSWCGA CKALKPKFAE STEISELSHN FVMVNLEDEE EPKDEDFSPD GGYIPRILFL DPSGKVHPEI INENGNPSYK YFYVSAEQVV QGMKEAQERL TGDAFRKKHL EDEL

    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.

    Txndc12 Human
  • View Data Sheet

    Name :

    CFI Human

    Description:

    Complement Factor I Human

    Complement factor I, C3B/C4B inactivator, CFI, IF.

    Product # :

    PRO-2701

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    Description

    Human Complement Factor I produced in Human plasma is glycosylated polypeptide composed of 2 disulfide-linked chains having a total molecular mass of 88kDa.

    Source

    Human Plasma.

    Formulation

    CFI protein solution contains Sodium phosphate, pH 7.2.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CFI cleaves and inactivates C3b and C4b. CFI is inactive without a cofactor such as the soluble factor H and C4b binding protein. CFI cleaves the alpha-peptide chain of C3b and C4b when these binds1 of the cofactors. This cleavage inactivates all of the complement activating functions of these proteins producing iC3b and iC4b.CFI cleaves the alpha chain of C3b twice and this releases a small fragment called C3f. CFI can cleave iC3b releasing C3c from C3dg in the presence of CR1.C4b is cleaved rapidly at 2 sites separating C4c from C4d.

    • Synonyms

      Complement factor I, C3B/C4B inactivator, CFI, IF.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFI Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

    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.

    Cfi Human
  • View Data Sheet

    Name :

    SYT1 Human

    Description:

    Synaptotagmin I Human Recombinant

    Synaptotagmin-1, Synaptotagmin I, SytI, p65, SYT1, SVP65, SYT.

    Product # :

    PRO-239

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    Description

    SYT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (136-382 a.a) and having a molecular mass of 29.5kDa.SYT1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SYT1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synaptotagmin-1(SYT1) is a member of the synaptotagmin family, which contains two C2 domains. The synaptotagmins are integral membrane proteins of synaptic vesicles assumed to function as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SYT1 is the principal regulator responsible for allowing the human brain to release neurotransmitters. SYT1 may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. SYT1 binds acidic phospholipids with a specificity which entails the presence of both an acidic head group and a diacyl backbone. SYT1 can also bind to at least 3 additional proteins in a Ca2+-independent manner; these being neurexins, syntaxin and AP2.

    • Synonyms

      Synaptotagmin-1, Synaptotagmin I, SytI, p65, SYT1, SVP65, SYT.

    • 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

      MEPKEEEKLG KLQYSLDYDF QNNQLLVGII QAAELPALDM GGTSDPYVKV FLLPDKKKKF ETKVHRKTLN PVFNEQFTFK VPYSELGGKT LVMAVYDFDR FSKHDIIGEF KVPMNTVDFG HVTEEWRDLQ SAEKEEQEKL GDICFSLRYV PTAGKLTVVI LEAKNLKKMD VGGLSDPYVK IHLMQNGKRL KKKKTTIKKN TLNPYYNESF SFEVPFEQIQ KVQVVVTVLD YDKIGKNDAI GKVFVGYNLE HHHHHH.

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

    Syt1 Human
  • View Data Sheet

    Name :

    ARHGDIB Human

    Description:

    Rho GDP Dissociation Inhibitor (GDI) Beta Human Recombinant

    Rho GDP dissociation inhibitor (GDI) beta, Rho GDI 2, Rho-GDI beta, GDIA2, GDID4, Ly-GDI, RAP1GN1.

    Product # :

    PRO-1067

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    Description

    ARHGDIB Human Recombinant produced in E. coli is a single polypeptide chain containing 428 amino acids (1-201) and having a molecular mass of 49.4kDa.ARHGDIB is fused to a 227 amino acid GST-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ARHGDIB solution (1mg/1ml) contains phosphate-buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Members of the Rho (or ARH) protein family and other Ras-related small GTP-binding proteins are involved in various cellular procedures, such as cell cytoskeletal organization, secretion, proliferation, and signaling. The GTPBPs are active only in the GTP-bound state. At least 3 types of proteins firmly regulate cycling between the GTP-bound and GDP-bound states: GDP-dissociation inhibitors (GDIs), GTPase-activating proteins (GAPs) and guanine nucleotide-releasing factors (GRFs). ARHGDIB and the other GDIs lower the level of GDP dissociation from Ras-like GTPases.

    • Synonyms

      Rho GDP dissociation inhibitor (GDI) beta, Rho GDI 2, Rho-GDI beta, GDIA2, GDID4, Ly-GDI, RAP1GN1.

    • 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

      MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSHMTE KAPEPHVEED DDDELDSKLN YKPPPQKSLK ELQEMDKDDE SLIKYKKTLL GDGPVVTDPK APNVVVTRLT LVCESAPGPI TMDLTGDLEA LKKETIVLKE GSEYRVKIHF KVNRDIVSGL KYVQHTYRTG VKVDKATFMV GSYGPRPEEY EFLTPVEEAP KGMLARGTYH NKSFFTDDDK QDHLSWEWNL SIKKEWTE

    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.

    Arhgdib Human
  • View Data Sheet

    Name :

    ANXA5 Human

    Description:

    Annexin A5 Human Recombinant

    PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.

    Product # :

    PRO-732

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    • Citations

    Description

    ANXA5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-320 a.a.) and having a molecular mass of 35.9 kDa.ANXA5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA5 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.

    • Synonyms

      PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.

    • 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

      MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI KGDTSGDYKK ALLLLCGEDD.

    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.

    Anxa5 Human
  • View Data Sheet

    Name :

    CCNH Human

    Description:

    Cyclin-H Human Recombinant

    CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    Product # :

    PKA-364

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    Description

    CCNH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 39.8 kDa. The CCNH is fused to a 20 amino acid His Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCNH solution contains 20mM Tris-HCl pH-8, 2mM DTT, 2mM EDTA, 0.1M NaCl and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.

    • Synonyms

      CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    • 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 MYHNSSQKRH WTFSSEEQLA RLRADANRKF RCKAVANGKV LPNDPVFLEP HEEMTLCKYY EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV SSPQFVGNLR ESPLGQEKAL EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDLKTRYPI LENPEILRKT ADDFLNRIAL TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLKE NRTCLSQLLD IMKSMRNLVK KYEPPRSEEV AVLKQKLERC HSAELALNVI TKKRKGYEDD DYVSKKSKHE EEEWTDDDLV ESL.

    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.

    Ccnh Human
  • View Data Sheet

    Name :

    SELE Human, HEK

    Description:

    E-Selectin Human Recombinant, HEK

    E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    Product # :

    PRO-1645

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    Description

    SELE Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 543 amino acids (22-556). SELE is fused to an 8 amino acid His-tag at C-terminus is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    SELE was lyophilized from a 0.2 µM filtered solution of PBS and 4% Mannitol, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.

    • Synonyms

      E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVW
      VWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTA
      ACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSY
      NSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPW
      NTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHSPAGEFT
      FKSSCNFTCEEGFMLQGPAQVECTTQGQWTQQIPVCEAFQCTALSNPERGYMNCLPSASGSFR
      YGSSCEFSCEQGFVLKGSKRLQCGPTGEWDNEKPTCEAVRCDAVHQPPKGLVRCAHSPIGEFTY
      KSSCAFSCEEGFELHGSTQLECTSQGQWTEEVPSCQVVKCSSLAVPGKINMSCSGEPVFGTVCKF
      ACPEGWTLNGSAARTCGATGHWSGLLPTCEAPTESNIPVDHHHHHH.

    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.

    Sele Human Hek
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