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Search results

1000 results found for “Visinin-Like Protein”

Name

Description

Product #

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  • View Data Sheet

    Name :

    ARL11 Human

    Description:

    ADP-Ribosylation Factor-Like 11 Human Recombinant

    ADP-ribosylation factor-like protein 11, ADP-ribosylation factor-like tumor suppressor protein 1, ARL11, ARLTS1.

    Product # :

    PRO-884

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    Description

    ARL11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-196 a.a.) and having a molecular mass of 23.6kDa.ARL11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARL11 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT,30% glycerol, 100mM NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARL11 (ADP-ribosylation factor-like protein 11) belongs to the ARF family of the Ras superfamily of small GTPases which are known to be involved in multiple regulatory pathways altered in human carcinogenesis. ARFs are highly conserved guanine nucleotide binding proteins which enhance the ADP-ribosyltransferase activity of choleratoxin. ARFs are important in eukaryotic vesicular trafficking pathways and they have a vital role in the activation of phospholipase D (PC-PLD). ARL11 is assumed to act as a tumor suppressor which may have a role in the regulation of apoptosis.

    • Synonyms

      ADP-ribosylation factor-like protein 11, ADP-ribosylation factor-like tumor suppressor protein 1, ARL11, ARLTS1.

    • 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 MGSVNSRGHK AEAQVVMMGL DSAGKTTLLY KLKGHQLVET LPTVGFNVEP LKAPGHVSLT LWDVGGQAPL RASWKDYLEG TDILVYVLDS TDEARLPESA AELTEVLNDP NMAGVPFLVL ANKQEAPDAL PLLKIRNRLS LERFQDHCWE LRGCSALTGE GLPEALQSLW SLLKSRSCMC LQARAHGAER GDSKRS.

    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.

    Arl11 Human
  • View Data Sheet

    Name :

    VEGFC Human, Sf9

    Description:

    Vascular Endothelial Growth Factor C Human Recombinant, Sf9

    Vascular Endothelial Growth Factor C, Vascular Endothelial Growth Factor-Related Protein, Flt4-L, VRP, FLT4 Ligand DHM, Flt4 Ligand, LMPH1D, VEGF-C, Vascular endothelial growth factor C, VEGF-C, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein.

    Product # :

    CYT-948

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    Description

    VEGFC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 125 amino acids (112-227a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). VEGFC is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    VEGFC protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. Human VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant human VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT-4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant human VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.

    • Synonyms

      Vascular Endothelial Growth Factor C, Vascular Endothelial Growth Factor-Related Protein, Flt4-L, VRP, FLT4 Ligand DHM, Flt4 Ligand, LMPH1D, VEGF-C, Vascular endothelial growth factor C, VEGF-C, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein.

    • 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

      ADPAHYNTEI LKSIDNEWRK TQCMPREVCI DVGKEFGVAT NTFFKPPCVS VYRCGGCCNS EGLQCMNTST SYLSKTLFEI TVPLSQGPKP VTISFANHTS CRCMSKLDVY RQVHSIIRRH HHHHH.

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

    Vegfc Human Sf9
  • View Data Sheet

    Name :

    C3d Human

    Description:

    Complement C3d Human

    Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    Product # :

    PRO-2687

    Price :

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    Description

    Human Complement C3d produced in Human plasma having a molecular mass of 33.8kDa.

    Source

    Human Plasma.

    Formulation

    C3d solution contains phosphate buffered saline, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C3d is derived from human C3 after a series of proteolytic cleavages.C3d is prepared from purified human C3. The C3 is converted to C3b by treatment with the natural human C3 convertase and this C3b is converted to iC3b. Finally, this iC3b is cleaved with trypsin to yield C3d.If the C3b precursor was attached to a surface (as occurs during complement activation) the iC3b, C3dg and C3d fragments would remain covalently attached to that surface.C3d is able to attach to a surfaceonly during complement activation on a surface. Surface-bound C3d is linked to the target through an ester or an amide covalent bond. Ester bonds are unstable, thusC3d releasesfrom the particle.

    • Synonyms

      Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C3d 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.

    C3D Human
  • View Data Sheet

    Name :

    VEGF Human, Baculovirus

    Description:

    Vascular Endothelial Growth Factor Human Recombinant, Baculovirus

    Vascular Endothelial Growth Factor A, VEGF, Vascular Permeability Factor, MVCD1, VPF, Vascular Endothelial Growth Factor, VEGF-A, Vascular endothelial growth factor A.

    Product # :

    CYT-849

    Price :

    Quantity :

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    Description

    VEGF produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 171 amino acids (27-191 a.a.) and having a molecular mass of 19.9 kDa. VEGF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    VEGF protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. 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/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular Endothelial Growth Factor A, VEGF, Vascular Permeability Factor, MVCD1, VPF, Vascular Endothelial Growth Factor, VEGF-A, Vascular endothelial growth factor 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

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

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

    Vegf Human Baculovirus
  • View Data Sheet

    Name :

    CPPED1 Human

    Description:

    Calcineurin-Like Phosphoesterase Domain Containing 1 Human Recombinant

    CSTP1, Calcineurin-like phosphoesterase domain-containing protein 1, Complete S-transactivated protein 1, CPPED1.

    Product # :

    PRO-1500

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    Description

    CPPED1 Human Recombinant produced in E. coli is a single polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 37.9kDa. CPPED1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CPPED1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CPPED1 which is a part of the metallophosphoesterase superfamily takes part in glucose uptake by adipocytes. CPPED1 binds two divalent metal cations and is transactivated by the great envelope protein of the hepatitis B virus.

    • Synonyms

      CSTP1, Calcineurin-like phosphoesterase domain-containing protein 1, Complete S-transactivated protein 1, CPPED1.

    • 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 MGSMSAAEAG GVFHRARGRT LAAFPAEKES EWKGPFYFIL GADPQFGLIK AWSTGDCDNG GDEWEQEIRL TEQAVQAINK LNPKPKFFVL CGDLIHAMPG KPWRTEQTED LKRVLRAVDR AIPLVLVSGN HDIGNTPTAE TVEEFCRTWG DDYFSFWVGG VLFLVLNSQF YENPSKCPSL KQAQDQWLDE QLSIARQRHC QHAIVFQHIP LFLESIDEDD DYYFNLSKST RKKLADKFIH AGVKVVFSGH YHRNAGGTYQ NLDMVVSSAI GCQLGRDPHG LRVVVVTAEK IVHRYYSLDE LSEKGIEDDL MDLIKKK.

    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.

    Cpped1 Human
  • View Data Sheet

    Name :

    HSA Protein

    Description:

    HSA Human Protein

    HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    Product # :

    PRO-354

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    Description

    HSA contains 584 amino acid residues derived from the prototypicalHSA sequence.

    Source

    Human Serum.

    Formulation

    0.2gr/ml solution containing no additives.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSA is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted HSA. HSA is a soluble, monomeric protein which comprises about one-half of the blood serum protein. HSA functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. HSA is a globular unglycosylated serum protein of molecular weight 65,000. The human HSA gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
      Suitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications.

    • Synonyms

      HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    • Physical Appearance

      Sterile Filtered clear yellowish solution.

    • Stability

      HSA although stable at room temperature for 2 weeks should be stored at 4°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.

    Human Serum Albumin
  • View Data Sheet

    Name :

    CST7 Human

    Description:

    Cystatin 7 Human Recombinant

    Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.

    Product # :

    PRO-2222

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    Description

    CST7 Human Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (20-145) and having a molecular mass of 15.3kDa.CST7 is fused to a 7 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CST7 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatin 7 (CST7) is a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system. Cystatin-7 is comprised of multiple cystatin-like sequences. The superfamily is comprised of 3 inhibitory families: the type 1 cystatins (stefins), type 2 cystatins and the kininogens. Some members are active cysteine protease inhibitors, while others have lost or possibly never had this inhibitory activity. Type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in various human fluids and secretions. CST7 protein expression has been observed in numerous human cancer cell lines established from malignant tumors.

    • Synonyms

      Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.

    • 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

      GPSPDTCSQD LNSRVKPGFP KTIKTNDPGV LQAARYSVEK FNNCTNDMFL FKESRITRAL VQIVKGLKYM LEVEIGRTTC KKNQHLRLDD CDFQTNHTLK QTLSCYSEVW VVPWLQHFEV PVLRCHHHHH HH.

    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.

    Cst7 Human
  • View Data Sheet

    Name :

    Avidin Recombinant

    Description:

    Avidin Recombinant

    Avidin, AVD, AVID.

    Product # :

    PRO-2597

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    Description

    Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit. The Recombinant Avidin is purified by affinity chromatographic techniques.

    Source

    Corn (Zea Mays).

    Purity

    Greater than 90% as visualized by SDS-PAGE.

    Biological Activity

    13.5 units/mg protein, 1 unit binds 1µg biotin.

    More Info

    • Introduction

      Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.

    • Synonyms

      Avidin, AVD, AVID.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Recombinant Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.

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

    Avidin Recombinant
  • View Data Sheet

    Name :

    VEGF Rat

    Description:

    Vascular Endothelial Growth Factor Rat Recombinant

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

    Product # :

    CYT-392

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    Description

    Vascular Endothelial Growth Factor Rat Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38,750 Dalton. The VEGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 10mM NaP, pH 7.5.

    Purity

    Greater than 97.0% 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 4.0-8.0 ng/ml.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. 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/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • 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 Vascular Endothelial Growth Factor 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 Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAPTTEGEQK AHEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNVTMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

    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 Rat
  • View Data Sheet

    Name :

    MIS12 Human

    Description:

    MIS12 Human Recombinant

    hMis12, KNTC2AP, MTW1, Protein MIS12 homolog.

    Product # :

    PRO-022

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    Description

    MIS12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-205 a.a.) and having a molecular mass of 26.5kDa. MIS12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIS12 protein solution (1mg/ml) containing 20mM Tris-HCl buffer, (pH 8.0) ,2M Urea and10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein MIS12 Belongs to the mis12 family. MIS12 is an element of the MIS12 complex, which is necessary for kinetochore formation during mitosis and normal chromosome alignment and segregation. The MIS12 complex which comprised of MIS12,DSN1 , NSL1 and PMF-1. MIS12 is section of a network of complexes that supply microtubule attachment and generates pulling forces from depolymerization.

    • Synonyms

      hMis12, KNTC2AP, MTW1, Protein MIS12 homolog.

    • 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 MGSMSVDPMT YEAQFFGFTP QTCMLRIYIA FQDYLFEVMQ AVEQVILKKL DGIPDCDISP VQIRKCTEKF LCFMKGHFDN LFSKMEQLFL QLILRIPSNI LLPEDKCKET PYSEEDFQHL QKEIEQLQEK YKTELCTKQA LLAELEEQKI VQAKLKQTLT FFDELHNVGR DHGTSDFRES LVSLVQNSRK LQNIRDNVEK ESKRLKIS.

    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.

    Mis12 Human
  • View Data Sheet

    Name :

    MORF4L1 Human

    Description:

    Mortality Factor 4 Like 1 Human Recombinant

    Mortality factor 4-like protein 1, MORF-related gene 15 protein, Protein MSL3-1, Transcription factor-like protein MRG15, MORF4L1, MRG15, FWP006, HSPC008, HSPC061, PP368, Eaf3, MEAF3, S863-6, HsT17725, MORFRG15.

    Product # :

    PRO-1078

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    Description

    MORF4L1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 347 amino acids (1-323 a.a) and having a molecular mass of 39.8kDa.MORF4L1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MORF4L1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mortality factor 4-like protein 1 (MORF4L1) is a member of the MRG family. MORF4L1 is a component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes mostly by acetylation of nucleosomal histones H4 and H2A. MORF4L1 is a transcription factor expressed in various human tissues, and its orthologs have been found in many other eukaryotes which comprise the MRG protein family. The C-terminal part of MORF4L1 forms a conserved MRG domain that is involved in interactions with the tumor suppressor protein retinoblastoma and a nucleoprotein.

    • Synonyms

      Mortality factor 4-like protein 1, MORF-related gene 15 protein, Protein MSL3-1, Transcription factor-like protein MRG15, MORF4L1, MRG15, FWP006, HSPC008, HSPC061, PP368, Eaf3, MEAF3, S863-6, HsT17725, MORFRG15.

    • 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 MGSHMAPKQD PKPKFQEGER VLCFHGPLLY EAKCVKVAIK DKQVKYFIHY SGWNKNWDEW VPESRVLKYV DTNLQKQREL QKANQEQYAE GKMRGAAPGK KTSGLQQKNV EVKTKKNKQK TPGNGDGGST SETPQPPRKK RARVDPTVEN EETFMNRVEV KVKIPEELKP WLVDDWDLIT RQKQLFYLPA KKNVDSILED YANYKKSRGN TDNKEYAVNE VVAGIKEYFN VMLGTQLLYK FERPQYAEIL ADHPDAPMSQ VYGAPHLLRL FVRIGAMLAY TPLDEKSLAL LLNYLHDFLK YLAKNSATLF SASDYEVAPP EYHRKAV.

    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.

    Morf4L1 Human
  • View Data Sheet

    Name :

    Leptin Protein

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

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    Description

    Leptin Human 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 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological Activity is 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 water or 0.4% NaHCO3 pH-8-9, 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 0.87 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 Human
  • View Data Sheet

    Name :

    Protein-L Cys, His

    Description:

    Protein-L Cys Recombinant, His Tag

    Product # :

    PRO-1932

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    Description

    Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at N-terminus and a Cys on C-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 373 amino acids in total and having a molecular mass of 41.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-L was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MHHHHHHKEE TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AGC.

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

    Protein L Cys His
  • View Data Sheet

    Name :

    LIF Human, His

    Description:

    Leukemia Inhibitory Factor Human Recombinant, His tag

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

    Product # :

    CYT-1082

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    Description

    LIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 23-202) containing 189 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 20.9kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    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

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKHHHHHHAS PLPITPVNAT CAIRHPCHNN LMNQIRSQLA QLNGSANALF ILYYTAQGEP FPNNLDKLCG PNVTDFPPFH ANGTEKAKLV ELYRIVVYLG TSLGNITRDQ KILNPSALSL HSKLNATADI LRGLLSNVLC RLCSKYHVGH VDVTYGPDTS GKDVFQKKKL GCQLLGKYKQ IIAVLAQAF.

    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 Protein
  • View Data Sheet

    Name :

    HSA Fatty Acid free

    Description:

    Human Serum Albumin Recombinant, Fatty Acid Free

    Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42,   PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    Product # :

    PRO-1917

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    Description

    HSA Human Recombinant Fatty Acid reduced produced in Plant contains 585 amino acids having a molecular mass of 67 kDa. The recombinant Albumin is purified by proprietary chromatographic techniques.

    Source

    Rice Grain.

    Formulation

    solution containing no additives.

    Purity

    Greater than 97% as determined by SDS-PAGE.

    More Info

    • Introduction

      Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize

    • Synonyms

      Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    • Physical Appearance

      Sterile Filtered clear yellowish solution.

    • Stability

      Recombinant Albumin stable at room temperature for 2 weeks should be stored at 4°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.

    Hsa Lipid Free
  • View Data Sheet

    Name :

    FAM107B Human

    Description:

    Family with Sequence Similarity 107, Member B Human Recombinant

    FAM107B protein, FLJ45505, MGC11034, Protein FAM107B, Family with Sequence Similarity 107, Member B, FAM107B, C10orf45.

    Product # :

    PRO-1691

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    Description

    FAM107B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-131) and having a molecular mass of 17.9kDa.FAM107B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FAM107B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Family with Sequence Similarity 107, Member B (FAM107B) which is a part of the FAM107 family, is expressed in most tissues in the human body. FAM107B exists in all stages of human development.

    • Synonyms

      FAM107B protein, FLJ45505, MGC11034, Protein FAM107B, Family with Sequence Similarity 107, Member B, FAM107B, C10orf45.

    • 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 MGSMAEPDYI EDDNPELIRP QKLINPVKTS RNHQDLHREL LMNQKRGLAP QNKPELQKVM EKRKRDQVIK QKEEEAQKKK SDLEIELLKR QQKLEQLELE KQKLQEEQEN APEFVKVKGN LRRTGQEVAQ AQES.

    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.

    Fam107B Human
  • View Data Sheet

    Name :

    TIPIN Human

    Description:

    TIMELESS Interacting Protein Human Recombinant

    TIMELESS Interacting Protein, CSM3 Homolog.

    Product # :

    PRO-1710

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    Description

    TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.

    • Synonyms

      TIMELESS Interacting Protein, CSM3 Homolog.

    • 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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR

    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.

    Tipin Human
  • View Data Sheet

    Name :

    Resistin Human (64-110)

    Description:

    Resistin (64-110) Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    Product # :

    CYT-1232

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    Description

    The Resistin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Resistin His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 47 amino acid residues of the Resistin Human, 64-110 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Background

      Human resistin is an adipokine primarily secreted by adipose tissue, mainly in response to obesity and inflammatory conditions.

      Resistin Function

      Resistin takes part in insulin resistance, which can be the cause of the development of type 2 diabetes. Resistin can also affect glucose metabolism and insulin signalling.

      Regulation

      Levels of resistin are influenced by factors such as inflammation, obesity and certain hormones. It tends to increase in conditions associated with obesity and metabolic syndrome.

      Clinical Relevance

      Elevated levels of resistin have been associated with obesity-related conditions, cardiovascular diseases, and metabolic disorders. Resisting is considered as a potential biomarker for these conditions.

      Resistin Mechanism

      Resistin promotes insulin resistance through different pathways such as the modulation of inflammatory processes and the inhibition of insulin signaling in target tissues like liver and muscle.

      Research

      Ongoing studies are exploring resistin’s role in metabolic regulation, the exact mechanisms of action of resistin and its potential as a therapeutic target for treating metabolic diseases.

      Overall, resistin is a critical factor in metabolic health, mainly in the context of diabetes and obesity.

    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.

    Resistin Human Protein
  • View Data Sheet

    Name :

    VEGF Mouse

    Description:

    Vascular Endothelial Growth Factor Mouse Recombinant

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

    Product # :

    CYT-336

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    Description

    Vascular Endothelial Growth Factor Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, double polypeptide chains containing 165 amino acids and having a molecular mass of 38.8kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered solution with PBS, pH 7.4.

    Purity

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

    Biological Activity

    The biological activity is determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 5.0 ng/ml corresponding to a specific activity of 200,000IU/mg.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. 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/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • 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 Vascular Endothelial Growth Factor 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 Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

    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 Mouse
  • View Data Sheet

    Name :

    Adiponectin Protein

    Description:

    Adiponectin Human Recombinant

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

    Product # :

    CYT-280

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    • sds-page

    Description

    The Adiponectin Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 25.1 kDa and containing 231 amino acids (15-244).

    Source

    Escherichia Coli.

    Formulation

    Acrp30 protein solution contains Phosphate buffered saline pH 7.4 and 1mM DTT.

    Purity

    Acrp30 purity is greater than 90% as determined by SDS-PAGE.

    sds-page

    Adiponectin-sds-page - Product image 1

    More Info

    • Introduction

      The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
      Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
      The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
      Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

    • Synonyms

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

    • 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

      MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
      KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
      GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
      VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
      RNGLYADNDNDSTFTGFLLYHDTN.

    • Background

      Adiponectin Human Recombinant: Unraveling its Potential in Therapeutic Applications

      1. Abstract

      This paper aims to deliver an extensive exploration into Adiponectin Human Recombinant, a vital adipokine implicated in a multitude of metabolic processes. By delving into the structure, biological roles, and signaling pathways of adiponectin, we elucidate its contribution to pathophysiological conditions. Moreover, we examine the potential therapeutic application of adiponectin in metabolic and cardiovascular diseases.

      2. Introduction

      Adiponectin, a protein predominantly secreted by adipose tissue, plays an integral part in regulating metabolic processes such as glucose regulation and fatty acid oxidation. Understanding the intricacies of adiponectin's actions could pave the way for innovative therapeutic interventions in diseases like obesity, diabetes, and cardiovascular disease.

      3. Structure and Signaling of Adiponectin

      Adiponectin is a 30kDa protein consisting of a collagen-like domain and a C-terminal globular domain. It signals through adiponectin receptors AdipoR1 and AdipoR2, which then activate several intracellular signaling pathways, including AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-alpha (PPAR-α), regulating various metabolic processes.

      4. Biological Functions of Adiponectin

      Adiponectin has been shown to enhance insulin sensitivity, stimulate fatty acid oxidation, and exert anti-inflammatory effects. Additionally, it is involved in regulating energy homeostasis and has been linked to the regulation of food intake and body weight.

      5. Adiponectin in Disease Pathology

      Reduced levels of adiponectin have been associated with obesity, insulin resistance, type 2 diabetes, and cardiovascular disease. Moreover, adiponectin deficiency has been observed in metabolic syndrome, emphasizing the adipokine's crucial role in metabolic health.

      6. Therapeutic Potential of Adiponectin

      Given adiponectin's role in metabolic regulation, its potential as a therapeutic target is of considerable interest. Approaches to increase circulating adiponectin levels or enhance adiponectin signaling could offer potential therapeutic strategies for managing metabolic diseases and cardiovascular conditions.

      7. Conclusion and Future Perspectives

      While our understanding of adiponectin and its role in health and disease has greatly advanced in recent years, there is still much to uncover. Further research on the precise molecular mechanisms of adiponectin could pave the way for novel therapeutic approaches.

      What is the molecular weight / Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 25.1kDa.
      What is the source or expression system of ADIPONECTIN Protein?
      Escherichia Coli.

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
      KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
      GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
      VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
      RNGLYADNDNDSTFTGFLLYHDTN..

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

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

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

    Adiponectin Human
  • View Data Sheet

    Name :

    VEGF Mouse, Sf9

    Description:

    Vascular Endothelial Growth Factor Mouse Recombinant, Sf9

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

    Product # :

    CYT-226

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    Description

    Vascular Endothelial Growth Factor Mouse Recombinant produced in Sf9 insect cells is a double, glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 48 kDa.The VEGF is purified by proprietary chromatographic techniques.

    Source

    Baculovirus Sf9 cells.

    Formulation

    The 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

    The ED50 range, determined by the dose-dependent proliferation of human umbilical vein endothelial cells (HUVEC) (measured by 3H-thymidine uptake) is 1-2 ng/ml, corresponding to a specific activity of 1x106 Units/mg.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. 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/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • 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 Vascular Endothelial Growth Factor Sf9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-Sf9 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 Vascular Endothelial Growth Factor-Sf9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Vegf Mouse Sf9
  • View Data Sheet

    Name :

    VEGF C Human

    Description:

    Vascular Endothelial Growth Factor C Human Recombinant

    VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein, VEGFC.

    Product # :

    CYT-527

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    Description

    VEGF-C Human Recombinant- contains 121 amino acids residues including 6 amino acid His-tag fused at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 18-24 kDa protein in SDS-PAGE under reducing conditions.

    Source

    Sf9, Insect Cells.

    Formulation

    Each mg of VEGF-C Human contains 50mg BSA and 1xPBS as buffer.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to induce to the VEGFR-3/FLT-4 receptor phosphorylation inPAEC/VEGFR3 cells and VEGFC induced proliferation of primary HDLEC cells.

    More Info

    • Introduction

      VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. Human VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant human VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT-4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant human VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.

    • Synonyms

      VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein, VEGFC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Vegf C Human
  • View Data Sheet

    Name :

    Desmin Chicken

    Description:

    Desmin Chicken Gizzard

    Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    Product # :

    PRO-2783

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    Description

    Desmin Chicken having a calculated molecular mass of 53 kDa, pI-5.4.

    Source

    Chicken gizzard.

    Formulation

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

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.

    • Solubility

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

    • Background

      Desmin, an intermediate filament protein, plays a fundamental role in maintaining the structural integrity and function of muscle cells. While extensive research has been conducted on desmin in mammals, the study of desmin in chickens is an emerging area with considerable potential for advancing our understanding of muscle biology. Chickens are valuable model organisms for studying muscle development, growth, and regeneration due to their relatively simple muscular system and economic significance in poultry production. This research aims to provide a comprehensive exploration of desmin in chickens, shedding light on its functions and implications for muscle structure and function.

      The primary objective of this research is to elucidate the role of desmin in chicken muscle structure and development. In vitro and in vivo experiments, utilizing chicken cell cultures and embryonic models, will be conducted to investigate how desmin contributes to the organization of muscle fibers, sarcomere assembly, and myofibrillogenesis. Understanding these mechanisms is fundamental for deciphering the complexities of muscle development in chickens.

      The second objective is to assess the clinical and economic relevance of desmin in poultry production. Studies involving broiler chickens will be conducted to evaluate the impact of desmin mutations or variations on muscle growth, meat quality, and disease susceptibility. These investigations may provide valuable insights into potential strategies for enhancing poultry production efficiency and meat quality.

      The third objective is to explore the potential applications of desmin in biotechnology and tissue engineering. Research will investigate the use of desmin-expressing chicken cells as models for studying muscle-related diseases and for developing tissue engineering approaches for muscle repair and regeneration.

      By delving into the functions and roles of desmin in chickens, this research aims to expand our knowledge of muscle biology, its implications for poultry production, and its potential applications in biotechnology and regenerative medicine.

    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.

    Desmin Chicken
  • View Data Sheet

    Name :

    SVIP Human

    Description:

    Small VCP/P97-Interacting Protein Human Recombinant

    Small VCP/P97-Interacting Protein, SVIP.

    Product # :

    PRO-472

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    Description

    SVIP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77) and having a molecular mass of 10.8 kDa.SVIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SVIP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Small VCP/p97-interacting protein (SVIP) is involved in various cellular processes, including membrane fusion and ubiquitin-dependent protein degradation. SVIP functions as an inhibitor of the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. On the other hand, SVIP overexpression increased the levels of p62 protein and enhanced starvation-activated autophagy as well as stimulated sequestration of polyubiquitinated proteins and p62 in autophagosomes.

    • Synonyms

      Small VCP/P97-Interacting Protein, SVIP.

    • 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 MGSMGLCFPC PGESAPPTPD LEEKRAKLAE AAERRQKEAA SRGILDVQSV QEKRKKKEKI EKQIATSGPP PEGGLRWTVS.

    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.

    Svip Human
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