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  • MEC (CCL28)

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Search results

1000 results found for “prolactin prl”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    Leptin Bovine

    Description:

    Leptin Bovine Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-502

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Leptin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 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).

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

    Leptin Bovine
  • View Data Sheet

    Name :

    Thromboplastin Bovine

    Description:

    Thromboplastin Bovine

    Tissue factor, Coagulation factor III, Thromboplastin, CD142, TF, F3, TFA.

    Product # :

    PRO-2760

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • More Info

    Description

    Thromboplastin bovine native

    Source

    Bovine Lung.

    Formulation

    The bovine thromboplastin was lyophilized with no additives.

    More Info

    • Introduction

      Tissue factor is well-known as the main cellular initiator of blood coagulation. The Tissue factor gene encodes coagulation factor III which is a cell surface glycoprotein that enables cells to initiate the blood coagulation cascades, and functions as the high-affinity receptor for the coagulation factor VII. Following vessel injury, the Tissue Factor and Factor VIIa complex activates the coagulation protease cascade, which leads to fibrin deposition and activation of platelets. The ensuing complex presents a catalytic event, which is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Therefore, Tissue factor has a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Tissue Factor can also be stimulated by the inflammatory mediators interleukin 1 and TNF, as well as by endotoxin, to appear on monocytes and vascular endothelial cells as a component of cellular immune response.
      Tissue factor is the only one in the coagulation pathway for which a congenital deficiency has not been described. Certain levels of Tissue Factor are essential for the maintained viability and growth of endothelium and Tissue Factor-expressing tumor cells. Additionally, abnormal Tissue Factor expression inside the vasculature initiates life threatening thrombosis in various diseases, for example sepsis, atherosclerosis, and cancer. Alternative spliced Tissue Factor expression advances tumor growth, and is linked to increased tumor cell proliferation and angiogenesis in pancreatic cancer.

    • Synonyms

      Tissue factor, Coagulation factor III, Thromboplastin, CD142, TF, F3, TFA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bovine Thromboplastin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Prothrombin should be stored at 4C between 2-7 days and for future use below -18C.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 Bovine Thromboplastin in sterile 0.9% NaCl

    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.

    Thromboplastin Bovine
  • View Data Sheet

    Name :

    Thyroglobulin Human, Biotin

    Description:

    Thyroglobulin Human, Biotinylated

    Thyroglobulin, TGN, AITD3, TG.

    Product # :

    PRO-2563

    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

    Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).

    Source

    Native, Isolated from human thyroid glands.

    Formulation

    Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
      Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease.

    • Synonyms

      Thyroglobulin, TGN, AITD3, TG.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

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

    Thyroglobulin Protein
  • View Data Sheet

    Name :

    IL 1 alpha Rat

    Description:

    Interleukin-1 alpha Rat Recombinant

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    Product # :

    CYT-381

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Interleukin-1A Rat Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17703 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Tris-HCl, pH=8.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.

    More Info

    • Introduction

      Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.

    • Synonyms

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 Interleukin 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    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.

    Il 1 Alpha Rat
  • View Data Sheet

    Name :

    TSLPR Human, Sf9

    Description:

    Thymic Stromal Lymphopoietin Receptor Human Recombinant, Sf9

    Cytokine receptor-like factor 2, CRLF2, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, Thymic stromal lymphopoietin protein receptor, TSLP receptor, CRL2, ILXR, TSLPR, Cytokine receptor-like factor 2 isoform 1, CRLF2Y.

    Product # :

    CYT-995

    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

    TSLPR Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 218 amino acids (23-231) and having a molecular mass of 25.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).TSLPR is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TSLPR protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymic Stromal Lymphopoietin Receptor (TSLPR) is a member of the type I cytokine receptor family. TSLPR alongside the interleukin 7 receptor (IL7R) activate STAT3, STAT5, and JAK2 pathways, which is regulated processes such as cell proliferation and development of the hematopoietic system. Two transcript variants encoding dissimilar isoforms have been found for this gene. TSLPR is expressed in heart, skeletal muscle, kidney and adult and fetal liver.

    • Synonyms

      Cytokine receptor-like factor 2, CRLF2, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, Thymic stromal lymphopoietin protein receptor, TSLP receptor, CRL2, ILXR, TSLPR, Cytokine receptor-like factor 2 isoform 1, CRLF2Y.

    • 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

      ADPQGGAAEG VQIQIIYFNL ETVQVTWNAS KYSRTNLTFH YRFNGDEAYD QCTNYLLQEG HTSGCLLDAE QRDDILYFSI RNGTHPVFTA SRWMVYYLKP SSPKHVRFSW HQDAVTVTCS DLSYGDLLYE VQYRSPFDTE WQSKQENTCN VTIEGLDAEK CYSFWVRVKA MEDVYGPDTY PSDWSEVTCW QRGEIRDACA ETPTPPKPKL SKHHHHHH.

    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.

    Tslpr Human Sf9
  • View Data Sheet

    Name :

    LIF Human, Yeast

    Description:

    LIF Human Recombinant, Yeast

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

    Product # :

    CYT-191

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    Description

    LIF Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 58.5 kDa. The LIF is purified by proprietary chromatographic techniques.

    Source

    Pichia pastoris.

    Formulation

    The protein was lyophilized from a 0.2 µm filtered PBS.

    Purity

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

    Biological Activity

    The biological activity of recombinant human LIF was measured by the ability to induce differentiation of murine M1 myeloid leukemic cells. The minimal detectable concentration of human LIF in this assay is <0.05 ng/mL. The specific activity is > 1 x 108 units/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      S P L P I T P V N A T C A I R H P C H N N L M N Q I R S Q L A Q L N G S A N A L F I L Y Y T A Q G E P F P N N L D K L C G P N V T D F P P F H A N G T E K A K L V E L Y R I V V Y L G T S L G N I T R D Q K I L N P S A L S L H S K L N A T A D I L R G L L S N V L C R L C S K Y H V G H V D V T Y G P D T S G K D V F Q K K K L G C Q L L G K Y K Q I I A V L A Q A F.

    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 Yeast
  • View Data Sheet

    Name :

    TPO Human, CHO

    Description:

    Thrombopoietin Human Recombinant, CHO

    MPL Ligand, THCYT1, MPLLG, TPO, ML, Thrombopoietin Nirs Variant 1, MKCSF, Thrombopoietin, Myeloproliferative Leukemia Virus Oncogene Ligand, Megakaryocyte Growth and Development Factor, Megakaryocyte Colony-Stimulating Factor, C-Mpl Ligand, MGDF, Megakaryocyte Stimulating Factor, Prepro-Thrombopoietin.

    Product # :

    CYT-1070

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    Description

    Thrombopoietin Human Recombinant produced in CHO cells has a molecular weight range of 80-90kDa due to glycosylation. The TPO is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells.

    Formulation

    TPO protein solution contains phosphate buffered saline (pH7.4) and 2% albumin.

    Purity

    Greater than 98% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of MO7e cells corresponding to a specific activity of 3x105 units/mg.

    More Info

    • Introduction

      Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets.

    • Synonyms

      MPL Ligand, THCYT1, MPLLG, TPO, ML, Thrombopoietin Nirs Variant 1, MKCSF, Thrombopoietin, Myeloproliferative Leukemia Virus Oncogene Ligand, Megakaryocyte Growth and Development Factor, Megakaryocyte Colony-Stimulating Factor, C-Mpl Ligand, MGDF, Megakaryocyte Stimulating Factor, Prepro-Thrombopoietin.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Thrombopoietin although stable at room temperature for 1 week, should be stored between 2-8°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.

    Thrombopoietin
  • View Data Sheet

    Name :

    Resistin Rat

    Description:

    Resistin Rat Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-1129

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    Description

    Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.

    Purity

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

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.

    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.

    Rat Resistin Protein
  • View Data Sheet

    Name :

    IMPACT Human

    Description:

    Impact RWD Domain Protein Human Recombinant

    RWDD5, Protein IMPACT, Imprinted and ancient gene protein homolog, IMPACT.

    Product # :

    PRO-1653

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    Description

    IMPACT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a.) and having a molecular mass of 38.9kDa.IMPACT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Impact RWD Domain Protein (IMPACT) is a member of the IMPACT family which is comprised of 1 RWD domain. IMPACT is a translational regulator which certifies constant high levels of translation under amino acid starvation. IMPACT interacts with GCN1/GCN1L1, thus preventing activation of GCN2 protein kinases (EIF2AK1 to 4) and subsequent down-regulation of protein synthesis. IMPACT is highly expressed especially in brain.

    • Synonyms

      RWDD5, Protein IMPACT, Imprinted and ancient gene protein homolog, IMPACT.

    • 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 MGSMAEGDAG SDQRQNEEIE AMAAIYGEEW CVIDDCAKIF CIRISDDIDD PKWTLCLQVM LPNEYPGTAP PIYQLNAPWL KGQERADLSN SLEEIYIQNI GESILYLWVE KIRDVLIQKS QMTEPGPDVK KKTEEEDVEC EDDLILACQP ESSVKALDFD ISETRTEVEV EELPPIDHGI PITDRRSTFQ AHLAPVVCPK QVKMVLSKLY ENKKIASATH NIYAYRIYCE DKQTFLQDCE DDGETAAGGR LLHLMEILNV KNVMVVVSRW YGGILLGPDR FKHINNCARN ILVEKNYTNS PEESSKALGK NKKVRKDKKR NEH.

    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.

    Impact Human
  • View Data Sheet

    Name :

    EDN3

    Description:

    Human Endothelin-3

    EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.

    Product # :

    HOR-309

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    Description

    EDN3 contains 21 amino acids having a molecular mass of 2643.08 Dalton, and the molecular formula is: C121H168N26O33S4. Disulfide bonds between cys-1 and cys-15 + cys-3 and cys-11.

    Formulation

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

    Purity

    Greater than 97.0% as determined by RP-HPLC.

    More Info

    • Introduction

      EDN3 interacts with endothelin receptor B, on the surface of cells. Throughout embryonic development, EDN3 takes part in neural crest cells that migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. EDN3 and EDN3R are necessary for the formation of nerves in the large intestine (enteric nerves) and melanocytes (produce melanin). Mutations in the EDN3 gene is linked with Waardenburg syndrome, type IV that is characterized by changes in skin, hair, and eye coloring. Mutations in the EDN3 gene is linked with Hirschsprung disease that causes severe constipation or intestinal blockage.

    • Synonyms

      EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EDN3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EDN3 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 EDN3 in sterile Acetic Acid not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Cys-Thr-Cys-Phe-Thr-Tyr-Lys-Asp-Lys-Glu-Cys-Val-Tyr-Tyr-Cys-His-Leu-Asp-Ile-Ile-Trp-OH.

    • Peptide Content

      88%.

    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.

    Edn3 Human
  • View Data Sheet

    Name :

    PRDX1 Antibody

    Description:

    Peroxiredoxin-1, Mouse Anti Human

    Peroxiredoxin-1, EC 1.11.1.15, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Proliferation-associated gene protein, Natural killer cell-enhancing factor A, NKEF-A, PRDX1, TDPX2, PRDX-1, PAG, PAGA, PRX1, PAGB, PRXI, MSP23, NKEFA.

    Product # :

    ANT-394

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      PRDX1 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX1 is an important protector of red blood cells against reactive oxygen species and in tumor prevention. PRDX1 is antioxidant protective in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX1 has a proliferative effect and is involved in cancer development or progression. Peroxiredoxin-1 is plays a role in redox regulation of the cell. Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. Peroxiredoxin is involved in eliminating peroxides generated during metabolism. Peroxiredoxin participates in the signaling cascades of growth factors and TNF-alpha by regulating the intracellular concentrations of h(2)o(2).

    • Synonyms

      Peroxiredoxin-1, EC 1.11.1.15, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Proliferation-associated gene protein, Natural killer cell-enhancing factor A, NKEF-A, PRDX1, TDPX2, PRDX-1, PAG, PAGA, PRX1, PAGB, PRXI, MSP23, NKEFA.

    • Immunogen

      Anti-human PRDX1 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PRDX1 amino acids 1-199 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT1D8AT.

    • Applications

      PRDX1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1000 ~ 2000. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      PRDX1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Prdx1 Antibody
  • View Data Sheet

    Name :

    CXCL6 Bovine

    Description:

    Granulocyte Chemotactic Protein 2 (CXCL6) Bovine Recombinant

    C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.

    Product # :

    CHM-040

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    Description

    Granulocyte Chemotactic Protein 2 (CXCL6) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of approximately 8.0kDa.GCP2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-50 ng/ml.

    More Info

    • Introduction

      Granulocyte Chemotactic Protein 2 (CXCL6), also known as GCP-2, is a Chemotactic for neutrophil granulocytes. GCP-2 signals through binding and activation of its receptors (CXCR1 and CXCR2). GCP-2 has strong antibacterial activity against Gram-positive and Gram-negative bacteria in addition to its chemotactic and angiogenic property.

    • Synonyms

      C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GCP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulocyte Chemotactic Protein 2 (CXCL6) 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 Granulocyte Chemotactic Protein 2 (CXCL6) in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPVAAVVREL RCVCLTTTPG IHPKTVSDLQ VIAAGPQCSK VEVIATLKNG REVCLDPEAP LIKKIVQKIL DSGKNN.

    • Background

      What is the molecular weight/Mw of CXCL6 BOVINE Protein?
      CXCL6 BOVINE Protein has a total Mw of 8.0kDa.

      What is the source or expression system of CXCL6 BOVINE Protein?
      Escherichia Coli.

      What is the Purity of CXCL6 BOVINE Protein?
      CXCL6 BOVINE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL6 BOVINE Protein?
      The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-50 ng/ml.

      What is the amino acid sequence of CXCL6 BOVINE Protein?
      GPVAAVVREL RCVCLTTTPG IHPKTVSDLQ VIAAGPQCSK VEVIATLKNG REVCLDPEAP LIKKIVQKIL DSGKNN.

      What applications can CXCL6 BOVINE Protein be used in?
      CXCL6 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL6 BOVINE Protein?
      The endotoxin level is minimal, CXCL6 BOVINE 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.

    Gcp2 Bovine
  • View Data Sheet

    Name :

    Leptin tA Human

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant

    Product # :

    CYT-352

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    Description

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

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ta Human
  • View Data Sheet

    Name :

    Thrombopoietin Human

    Description:

    Thrombopoietin Human Recombinant

    Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO

    Product # :

    CYT-1178

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    Description

    TPO Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 343 amino acids (22-353 a.a) and having a molecular mass of 36.8kDa.TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤10ng/ml. It is measured by cell proliferation assay using MO7e human megakaryocytic leukemic cells.

    More Info

    • Introduction

      Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets.

    • Synonyms

      Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO

    • 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

      DGSHMSPAPP ACDLRVLSKL LRDSHVLHSR LSQCPEVHPL PTPVLLPAVD FSLGEWKTQM EETKAQDILG AVTLLLEGVM AARGQLGPTC LSSLLGQLSG QVRLLLGALQ SLLGTQLPPQ GRTTAHKDPN AIFLSFQHLL RGKVRFLMLV GGSTLCVRRA PPTTAVPSRT SLVLTLNELP NRTSGLLETN FTASARTTGS GLLKWQQGFR AKIPGLLNQT SRSLDQIPGY LNRIHELLNG TRGLFPGPSR RTLGAPDISS GTSDTGSLPP NLQPGYSPSP THPPTGQYTL FPLPPTLPTP VVQLHPLLPD PSAPTPTPTS PLLNTSYTHS QNLSQEGHHH HHH

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

    Thrombopoietin Protein
  • View Data Sheet

    Name :

    Leptin tA Ovine

    Description:

    Leptin Antagonist Triple Mutant Ovine Recombinant

    Product # :

    CYT-356

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    • More Info

    Description

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

    Source

    Escherichia coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

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

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

    Leptin Ta Ovine
  • View Data Sheet

    Name :

    IGF1 Human

    Description:

    IGF-1 Human Recombinant

    Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.

    Product # :

    CYT-216

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    Description

    IGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.6kDa.IGF-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated solution in PBS, pH 7.0.

    Purity

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

    Biological Activity

    The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 105IU/mg.

    More Info

    • Introduction

      The somatomedins, IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B.

    • Synonyms

      Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

    • Background

      IGF stands for INS like growth factors, which are proteins that have a high similarity to INS. They are part of a complicated process that uses cells to communication with the physiologic environment around them. IGF’s complex system is often called the ‘axis’. This consists of:
      ● Two cell-surface receptors (IGF1R and IGF2R)
      ● Two ligands (IGF-1 and IGF-2)
      ● A family of six high-affinity IGF-binding proteins.
      ● Proteases.

      The Effect IGF Has On The Body
      Many unique tissue types express the IGF-1 receptor, and the effects can vary. It induces the survival of neurons, may catalyse skeletal muscle hypertrophy by inducing protein synthesis, and by blocking muscle atrophy. It works as a protector for cartilage cells, and may work to be an anabolic factor for the bones. When used in high concentrations, it can activate the INS receptor, and can even complement the effects that INS has on the body.

      Diseases And IGF
      Diseases and IGF are closely related, and a number of them can be affected. The INS IGF axis is thought to have an effect on aging, with an increased life span shown in fruit flies when used in studies.
      It is also important to note the crucial role that IGF plays in cancer and diabetes - IGF- 1 has been shown to stimulate growth in both prostate and breast cancer cells. The degree of risk that IGF-1 poses is up for debate, and many scientists are not in agreement. IGF has also shown to have the ability to decrease blood glucose levels, although not quite as effective as INS.

      How Was IGF Discovered?
      Investigators began studying the effects of biological substances on cells and tissues outside the body when IGFs were discovered. The name is self explanatory in the fact that IGF performs INS actions in some tissues, but is less potent than INS at decreasing blood sugar. Its fundamental action is to stimulate growth, whether that be within the epidermal growth factor or the nerve growth factor.

      What’s The Difference Between IGF-1 And IGF-2?
      The two types of IGF are IGF-1 and IGF-2. Although the names are similar, the specific actions that they take are different - they bind and activate completely difference receptors. The major actor in them both is the effect that they have on cell growth. Most of the actions of the pituitary GH are mediated by IGFs, but predominantly IGF-1. GH works to stimulate many tissues within the body, especially the liver which then secretes IGF-1. This then causes hypertrophy, or in layman's terms, an increase in cell size, as well as hyperplasia which is an increase in the number of cells.
      The IGF-1 concentration will increase during childhood and hit peak during puberty, but will then decrease afterwards, as does the hormone secretion itself. It has been proven that children and adults with a deficiency of the GH have low serum IGF-1 concentrations when put in comparison with others in the same age range. Patients who have conditions like acromegaly have been shown to have increased serum IGF-1 concentrations. The production of IGF-2 is less dependent on the secretion of GH than IGF-1, and is much less important for stimulating linear growth.

    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.

    Igf 1 Human
  • View Data Sheet

    Name :

    RXRA Human

    Description:

    Retinoid X Receptor Alpha Human Recombinant

    Retinoic acid receptor RXR-alpha, Retinoid X receptor alpha, Nuclear receptor subfamily 2 group B member 1, RXRA, NR2B1, FLJ00280, FLJ00318, FLJ16020, FLJ16733, MGC102720, RXR Alpha, RXR-a.

    Product # :

    PRO-437

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    Description

    RXRA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (111-228) & having a molecular mass of 13.6 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) containing 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM ?-Mercaptoethanol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The retinoid X receptor (RXR) is a pleiotropic nuclear receptor transcription factor that interacts with a variety of nuclear receptor dimeric partner. RXR binds cognate response elements as a homodimer in the presence of its ligand, 9-cis retinoic acid, or as a heterodimer with other members of the nuclear hormone receptor superfamily including retinoic acid receptors (RAR), thyroid hormone receptors (TR), vitamin D receptors and peroxisome proliferators-activated receptors (PPAR). The RXR family includes three different isoforms; RXR a, b, g . Human RXR a gene is localized on 9q34.9 and encodes two major isoforms (RXR a1, RXR a2). The DNA binding domain of RXR (111-228aa) was purified by using conventional column chromatography techniques.

    • Synonyms

      Retinoic acid receptor RXR-alpha, Retinoid X receptor alpha, Nuclear receptor subfamily 2 group B member 1, RXRA, NR2B1, FLJ00280, FLJ00318, FLJ16020, FLJ16733, MGC102720, RXR Alpha, RXR-a.

    • 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

      MLGLNGVLKV PAHPSGNMAS FTKHICAICG DRSSGKHYGV YSCEGCKGFF KRTVRKDLTY TCRDNKDCLI DKRQRNRCQY CRYQKCLAMG MKREAVQEER QRGKDRNENE VESTSSANE.

    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.

    Rxra Human
  • View Data Sheet

    Name :

    IPP-POZ Human

    Description:

    IPP-POZ Human Recombinant

    Intracisternal A Particle-Promoted Polypeptide, Actin-binding protein IPP, MIPP protein, Kelch-like protein 27, IPP, KLHL27, IPP-POZ.

    Product # :

    PRO-436

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    Description

    IPP-POZ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids & having a molecular mass of 17.3 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) containing 10mM HEPES (pH7.4) and 25mM NaCl.

    Purity

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

    More Info

    • Introduction

      Intracisternal A particle-promoted polypeptide (IPP) is a 66kDa protein (584 amino acids), which contains an N-terminal POZ protein-protein interaction domain and a C-terminal kelch repeat domain consisting of six tandem arranged repeats. The POZ domain (also called BTB domain) is present near the N-terminus of a fraction of zinc finger proteins and in protein that contain the pfam01344 motif such as kelch and pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-coR and SMRT.

    • Synonyms

      Intracisternal A Particle-Promoted Polypeptide, Actin-binding protein IPP, MIPP protein, Kelch-like protein 27, IPP, KLHL27, IPP-POZ.

    • 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

      MANEDCPKAA DSPFSSDKHA QLILAQINKM RNGQHFCDVQ LQVGQESFKA HRLVLAASSPYFAALFTGGM KESSKDVVPI LGIEAGIFQI LLDFIYTGIV NIGVNNVQEL IIAADMLQLTEVVHLCCEFL KGQIDPLNCI GIFQFSEQIA CHDLLEF.

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    Ipp Poz Human
  • View Data Sheet

    Name :

    GLC8 Yeast

    Description:

    GLC8 Yeast Recombinant

    Protein GLC8, GLC8, YMR311C, YM9924.03C.

    Product # :

    PRO-540

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    Description

    GLC8 Yeast (Saccharomyces cerevisiae) Recombinant produced in E.coli is a single, glycosylated polypeptide chain containing 265 amino acids (1-229) and having a molecular mass of 30.7 kDa (molecular size on SDS-PAGE will appear higher). The GLC8 is fused to a 35 amino acid His Tag at N-Terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLC8 is a regulatory subunit of protein phosphatase 1 (Glc7p). GLC8 plays a role in glycogen metabolism and chromosome segregation, and regulates Glc7p activity through conformational alteration; ortholog of the mammalian protein phosphatase inhibitor 2. Under regular conditions, GLC8 triggers GLC7, but when GLC8 is over epxressed, it inhibits Glc7p function. GLC8 is activated upon phosphoylation by Pho85p complexed with four cyclins (Pcl6p, Pcl7p, Pcl8p, or Pcl10p).

    • Synonyms

      Protein GLC8, GLC8, YMR311C, YM9924.03C.

    • 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 KDRWGSMGGI LKNPLALSPE QLAQQDPETL EEFRRQVYEN TQKNAKLTSH KRNIPGLDNT KEEGEIIGTS STFLPKDTLS LKHEQDMLAK MTPEERVQWN QRNLAENEIT KKQFQDIHID EPKTPYQGAV DPHGEYYRVD DDEDEDNSDK KPCQVANDDI DDLSLGEPEF EIKENKQPDF ETNDENDEDS PEARHKKFEE MRKKHYDVRA IFNKKSREAL KDEDEDEDDS TTKEP.

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    Glc8
  • View Data Sheet

    Name :

    Leptin Ovine, MTS

    Description:

    Leptin Ovine Recombinant, MTS tag

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-531

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    Description

    Leptin Ovine MTS tagged Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.5 kDa.The Leptin is purified by proprietary chromatographic techniques. The membrane translocating sequence Tag is composed of 10 amino acids Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro located at the N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Ovine MTS tagged although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.02% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ovine Mts
  • View Data Sheet

    Name :

    Prealbumin Human

    Description:

    Transthyretin Human

    TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.

    Product # :

    PRO-2740

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    Description

    Human Transthyretin dimer protein produced in Human plasma having a molecular mass of 30kD. Under certain conditions it may be shown as a monomer (15kD) or a tetramer (60kD).

    Source

    Human serum.

    Formulation

    The protein was lyophilized (0.2 µm filtered) from 20mM NH4HCO3.

    Purity

    Greater than 96.0%.

    More Info

    • Introduction

      Prealbumin is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. Prealbumin is a carrier protein which transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. Transthyretin consists of a tetramer of identical subunits and is dominantly produced in the liver. Mutations in Prealbumin are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, and carpal tunnel syndrome. Prealbumin is an indicator of protein-energy malnutrition since it has a circulating half life of 2 days and reacts swiftly to changes in nutritional status.

    • Synonyms

      TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Prealbumin Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.

    • Solubility

      It is recommended to reconstitute the lyophilized Prealbumin Human in phosphate buffer pH > 7 containing 0.15M NaCl.

    • Human Virus Test

      Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG, Parvovirus B19, Syphilis and HIV/HBV/HCV (PCR).

    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.

    Prealbumin Protein
  • View Data Sheet

    Name :

    SLAMF1 Human

    Description:

    SLAMF1 Human Recombinant

    Signaling lymphocytic activation molecule, CDw150, IPO-3, CD150, SLAMF1, SLAM.

    Product # :

    PRO-1342

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    Description

    SLAMF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (21-237 a.a) and having a molecular mass of 26.7kDa.SLAMF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SLAMF1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SLAMF1 is a member of the immunoglobulin gene superfamily and is involved in T-cell stimulation. The SLAMF1 protein is constitutively expressed on peripheral blood memory T cells, T-cell clones, immature thymocytes, and a fraction of B cells, and is swiftly induced on naive T cells after activation. There are probably 2 modes of SLAM signaling: one in which the inhibitor SH2D1A serves as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction functions.

    • Synonyms

      Signaling lymphocytic activation molecule, CDw150, IPO-3, CD150, SLAMF1, SLAM.

    • 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 MGSASYGTGG RMMNCPKILR QLGSKVLLPL TYERINKSMN KSIHIVVTMA KSLENSVENK IVSLDPSEAG PPRYLGDRYK FYLENLTLGI RESRKEDEGW YLMTLEKNVS VQRFCLQLRL YEQVSTPEIK VLNKTQENGT CTLILGCTVE KGDHVAYSWS EKAGTHPLNP ANSSHLLSLT LGPQHADNIY ICTVSNPISN NSQTFSPWPG CRTDPSETKP.

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    Slamf1 Human
  • View Data Sheet

    Name :

    SNRPC Human

    Description:

    Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant

    U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    Product # :

    PRO-1004

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    Description

    SNRPC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-159 a.a.) and having a molecular mass of 19.8kDa (Molecular weight on SDS-PAGE will appear higher).SNRPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNRPC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.3M NaCl, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNRPC is a member of the U1 small nuclear ribonucleoprotein C family. The SNRPC protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle required for the formation of the spliceosome. SNRPC participates in the processing of nuclear precursor messenger RNA splicing. snRNP particles are tackled by autoantibodies frequently produced by patients with connective tissue diseases.

    • Synonyms

      U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    • 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 MGSMPKFYCD YCDTYLTHDS PSVRKTHCSG RKHKENVKDY YQKWMEEQAQ SLIDKTTAAF QQGKIPPTPF SAPPPAGAMI PPPPSLPGPP RPGMMPAPHM GGPPMMPMMG PPPPGMMPVG PAPGMRPPMG GHMPMMPGPP MMRPPARPMM VPTRPGMTRP DR.

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    Snrpc Human
  • View Data Sheet

    Name :

    BMP 7 Human, HEK

    Description:

    Bone Morphogenetic protein-7 Human Recombinant, HEK

    Osteogenic Protein 1, BMP-7.

    Product # :

    CYT-082

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    Description

    BMP-7 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 30-38kDa due to glycosylation.The BMP7 corresponds to amino acid residues 315 to 431 of the full-length BMP-7 precursor and is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The BMP7 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

    More Info

    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

    • Synonyms

      Osteogenic Protein 1, BMP-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-7 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 BMP-7 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.

    • Background

      BMP-7 Bone Morphogenetic Protein-7 Human Recombinant: A Key Regulator of Osteogenesis and Beyond

      Abstract:

      BMP-7 (Bone Morphogenetic Protein-7), also known as Osteogenic Protein 1 or BMP-7, is a potent growth factor that plays a crucial role in various biological processes, particularly in osteogenesis and tissue regeneration.

      This research paper aims to comprehensively explore the molecular characteristics, signaling pathways, and diverse physiological functions of BMP-7.

      Additionally, it investigates the therapeutic implications of BMP-7 in different disorders. Synonyms such as Osteogenic Protein 1 and BMP-7 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a growth factor with multifaceted roles in osteogenesis, tissue regeneration, and disease. This section introduces BMP-7 and its synonyms, highlighting their significance and relevance in scientific research.

      Molecular Characteristics of BMP-7:

      This section explores the molecular characteristics of BMP-7, including its primary amino acid sequence, protein structure, post-translational modifications, and binding partners. The importance of these factors in determining BMP-7's biological activity and receptor specificity is discussed.

      Signaling Pathways Activated by BMP-7 :

      BMP-7 activates specific signaling pathways upon binding to its receptors, leading to diverse cellular responses. This section focuses on the canonical BMP signaling pathway, highlighting the activation of Smad-dependent and Smad-independent pathways. The downstream effectors and transcriptional regulators involved in mediating BMP-7's cellular responses are also discussed.

      Physiological Functions of BMP-7 :

      BMP-7 plays critical roles in various physiological processes, particularly in osteogenesis and tissue regeneration. This section provides an in-depth analysis of BMP-7's contributions to these processes, emphasizing its role in promoting bone formation, cartilage development, renal function, and wound healing.

      Therapeutic Implications of BMP-7 :

      The unique properties of BMP-7 make it a promising therapeutic candidate for various disorders. This section discusses the potential applications of BMP-7 in bone regeneration, cartilage repair, kidney disease, and tissue engineering. The challenges and future directions in utilizing BMP-7 as a therapeutic agent are also explored.

      BMP-7 in Disease Progression:

      BMP-7 is implicated in the progression of certain diseases, including fibrosis, cancer, and cardiovascular disorders. This section examines the role of BMP-7 in tissue fibrosis, tumor progression, angiogenesis, and cardiac remodeling. The therapeutic implications and targeting of BMP-7 in disease management are also discussed.

      Conclusion:

      BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a critical growth factor involved in osteogenesis, tissue regeneration, and disease progression. Understanding the molecular characteristics, signaling pathways, and physiological functions of BMP-7 contributes to the exploration of its therapeutic potential in various disorders.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 38kDa.

      What is the source or expression system of BMP7 Protein?
      HEK.

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

      What is the amino acid sequence of BMP7 Protein?
      DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.


      What applications can BMP7 Protein be used in?
      BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP7 Protein?
      The endotoxin level is minimal, BMP7 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.

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