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  • Aprotinin

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Search results

1000 results found for “Avidin”

Name

Description

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  • View Data Sheet

    Name :

    EFNA5 Human, Active

    Description:

    Ephrin A5 Human Recombinant, Active

    EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.

    Product # :

    PRO-2816

    Price :

    Quantity :

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    Description

    EFNA5 Human Recombinant is a single, glycosylated, polypeptide chain (21-203 a.a) containing a total of 422 amino acids and having a molecular mass of 48.1 kDa. EFNA5 is fused to a 239 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The EFNA5 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 60 ng/ml measured by its binding ability in a functional ELISA with Mouse EphA3 (CAT# pro-2817).

    Citations

    More Info

    • Synonyms

      EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.

    • 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

      QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

    • Background

      EFNA5 functions through contact-mediated signaling, which can result in either forward signaling (through Eph receptors) or reverse signaling (through ephrins themselves). These signaling pathways regulate various cellular processes such as migration, adhesion, and proliferation. Disruptions or alterations in EFNA5 signaling have been implicated in neurodevelopmental disorders, cancer metastasis, and angiogenesis, highlighting the importance of understanding this protein's roles at a molecular level.

    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.

    Efna5 Protein
  • View Data Sheet

    Name :

    VEGF Human, HEK

    Description:

    Vascular Endothelial Growth Factor Human Recombinant, HEK

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

    Product # :

    CYT-225

    Price :

    Quantity :

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    Description

    Vascular Endothelial Growth Factor Human Recombinant produced in HEK293 cells is a double, glycosylated, polypeptide chain containing 165 amino acids (27-191) and having a molecular mass of 40 kDa. The VEGF is purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

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

    Purity

    Greater than 95.0% as determined 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 4.0ng/ml, corresponding to a specific activity of 2.5 x 105 Units/mg.

    Citations

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

    • Amino Acid Sequence

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

    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 Hek
  • View Data Sheet

    Name :

    Insulin Human, His

    Description:

    Insulin Human Recombinant, His Tag

    Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.    

    Product # :

    CYT-1076

    Price :

    Quantity :

    Shipping Method :

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    • source
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    Description

    Insulin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (25-110 a.a) and having a molecular mass of 11.8kDa. Insulin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Insulin protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using MCF7 human breast cancer cell. The ED50 for this effect is less or equal to 4 ug/ml.

    Citations

    More Info

    • Introduction

      Insulin decreases blood glucose concentration. it increases cell permeability to monosaccharides, amino acids and fatty acids. it accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

    • Synonyms

      Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

    • 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 MGSFVNQHLC GSHLVEALYL VCGERGFFYT PKTRREAEDL QVGQVELGGG PGAGSLQPLA LEGSLQKRGI VEQCCTSICS LYQLENYCN

    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.

    Insulin 2
  • View Data Sheet

    Name :

    DCN Human, Sf9

    Description:

    Decorin Human Recombinant, Sf9

    Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.

    Product # :

    PRO-2232

    Price :

    Quantity :

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    • description
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    Description

    DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 335 amino acids (31-359a.a.) and having a molecular mass of 37.1kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). DCN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.

    • 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

      DEASGIGPEV PDDRDFEPSL GPVCPFRCQC HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHAL ILVNNKISKV SPGAFTPLVK LERLYLSKNQ LKELPEKMPK TLQELRAHEN EITKVRKVTF NGLNQMIVIE LGTNPLKSSG IENGAFQGMK KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS LKGLNNLAKL GLSFNSISAV DNGSLANTPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR SAIQLGNYKH 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.

    Dcn Human Sf9
  • View Data Sheet

    Name :

    VEGF C Rat

    Description:

    Vascular Endothelial Growth Factor Related Protein Rat Recombinant

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

    Product # :

    CYT-262

    Price :

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    Description

    Vascular Endothelial Growth Factor C Rat Recombinant contains 127 amino acids residues and was fused to a His- tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 15-20 kDa protein in SDS-PAGE under reducing conditions.

    Source

    Sf9, Insect Cells.

    Formulation

    Each mg of VEGF-C Rat contains 50mg BSA and PBS as buffer.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to stimulate phosphorylation of the VEGFR-3/FLT-4 receptor in porcine aortic endothelial cells. The ED50 for this effect is typically 200-300ng/ml corresponding to a Specific Activity of 3,334-5,000IU/mg.

    Citations

    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. The rat VEGFC 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 rat 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 rat 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.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      DTVKLAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGAATNTFFKP PCVSVYRCGGCCNSEGLQCMNTSTGYLSKTLFEITVPLSQGPKPVTISFA NHTSCRCMSKLDVYRQVHSIIHHHHHH.

    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 Rat
  • View Data Sheet

    Name :

    Leptin Receptor Chicken

    Description:

    Leptin Receptor Chicken Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    Product # :

    CYT-509

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    Description

    Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    • Physical Appearance

      Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.

    • Stability

      Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of Leptin Binding Domain as a Reference Standard.

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

    Leptin Receptor Chicken
  • View Data Sheet

    Name :

    APOE4 Human

    Description:

    Apolipoprotein E4 Human Recombinant

    Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.

    Product # :

    CYT-968

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    Description

    Apolipoprotein E4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 299 amino acids and having a molecular mass of 34.4kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 20mM PBS, pH7.8 and 5% trehalose.

    Purity

    Greater than 95% as determined by:

    (a) Analysis by RP-HPLC.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.

    Citations

    More Info

    • Introduction

      Apolipoprotein E (APOE) is a chylomicron lipoprotein which is essential for the metabolism of lipoproteins and lipid transport. The APOE gene has 3 alleles, designated APOE2, APOE3, and APOE4. The APOE allelic proteins differ by only one or two amino acids, however have different biological structures and functions. APOE3 is the most common and neutral allele. The APOE4 allele is linked with an increased risk for Alzheimer's Disease (AD) and coronary artery disease (CAD). The APOE4 protein morphology decreases the ability of APOE4 to clear beta-amyloid protein from the brain, resulting in AD progression. The APOE2 allele is linked with type III hyperlipoproteinemia, which is characterized by defects in the clearance of plasma lipoproteins, however APOE2 may have a protective effect against AD.

    • Synonyms

      Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized APOE4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOE4 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 APOE4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.

    • Background

      What is the molecular weight/Mw of APOE4 Protein?
      APOE4 Protein has a total Mw of 34.4kDa.

      What is the source or expression system of APOE4 Protein?
      Escherichia Coli.

      What is the Purity of APOE4 Protein?
      APOE4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOE4 Protein?
      When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.

      What is the amino acid sequence of APOE4 Protein?
      KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.

      What applications can APOE4 Protein be used in?
      APOE4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOE4 Protein?
      The endotoxin level is minimal, APOE4 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.

    Apoe4 Human
  • View Data Sheet

    Name :

    HNRNPAB Human

    Description:

    Heterogeneous Nuclear Ribonucleoprotein A/B Human Recombinant

    Heterogeneous Nuclear Ribonucleoprotein A/B, ABBP-1, ABBP1, APOBEC1-Binding Protein 1, HnRNP A/B, Apobec-1 Binding Protein 1, Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide 1-Binding Protein 1, HnRNP Type A/B Protein.

    Product # :

    PRO-1731

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    Description

    HNRNPAB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285 a.a) and having a molecular mass of 33kDa.HNRNPAB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HNRNPAB protein solution (0.25mg/ml) containing 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Heterogeneous Nuclear Ribonucleoprotein A/B (HNRNPAB) is a member of the subfamily of ubiquitously expressed heterogeneous nuclearribonucleoproteins (hnRNPs). The hnRNPs are produced by RNA polymerase II and are components of theheterogeneous nuclear RNA (hnRNA) complexes. They are linked with pre-mRNAs in the nucleus and seem to influence pre-mRNA processing and further aspects of mRNA metabolism and transport. Whereas all of the hnRNPsare present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. HNRNPAB, which binds to one of the components of the multiproteineditosome complex, has two repeats of quasi-RRM (RNA recognition motif) domains that bind to RNAs. Among the diseases associated with HNRNPAB are wells syndrome, and cystic fibrosis.

    • Synonyms

      Heterogeneous Nuclear Ribonucleoprotein A/B, ABBP-1, ABBP1, APOBEC1-Binding Protein 1, HnRNP A/B, Apobec-1 Binding Protein 1, Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide 1-Binding Protein 1, HnRNP Type A/B Protein.

    • 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 MGSMSEAGEE QPMETTGATE NGHEAVPEGE SPAGAGTGAA AGAGGATAAP PSGNQNGAEG DQINASKNEE DAGKMFVGGL SWDTSKKDLK DYFTKFGEVV DCTIKMDPNT GRSRGFGFIL FKDAASVEKV LDQKEHRLDG RVIDPKKAMA MKKDPVKKIF VGGLNPEATE EKIREYFGEF GEIEAIELPM DPKLNKRRGF VFITFKEEEP VKKVLEKKFH TVSGSKCEIK VAQPKEVYQQ QQYGSGGRGN RNRGNRGSGG GGGGGGQGST NYGKSQRRGG HQNNYKPY

    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.

    Hnrnpab Human
  • View Data Sheet

    Name :

    NECTIN2 Human

    Description:

    Nectin Cell Adhesion Molecule 2 Human Recombinant

    Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.

    Product # :

    PRO-2461

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    Description

    NECTIN2 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 337 amino acids (32-360a.a.) and having a molecular mass of 36.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN2 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    NECTIN2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Nectin Cell Adhesion Molecule 2, also known as NECTIN2, is a Ca(2+)-independent cell-cell adhesion molecule which is one of the plasma membrane components of adherens junctions. NECTIN2 takes a vital part in the establishment of homotypic as well as heterotypic cell to cell contacts. NECTIN2 is essential for resisting herpes simplex virus type 2 infection in transfected cells. NECTIN2 is also a possible target for antibody therapy of breast & ovarian cancers. NECTIN2 might be related with human longevity. Two diseases which have been associated with NECTIN2 are Herpes Simplex and Ovarian Cystic Teratoma.

    • Synonyms

      Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.

    • 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

      QDVRVQVLPE VRGQLGGTVE LPCHLLPPVP GLYISLVTWQ RPDAPANHQN VAAFHPKMGP SFPSPKPGSE RLSFVSAKQS TGQDTEAELQ DATLALHGLT VEDEGNYTCE FATFPKGSVR GMTWLRVIAK PKNQAEAQKV TFSQDPTTVA LCISKEGRPP ARISWLSSLD WEAKETQVSG TLAGTVTVTS RFTLVPSGRA DGVTVTCKVE HESFEEPALI PVTLSVRYPP EVSISGYDDN WYLGRTDATL SCDVRSNPEP TGYDWSTTSG TFPTSAVAQG SQLVIHAVDS LFNTTFVCTV TNAVGMGRAE QVIFVRETPN TAGAGATGGL EHHHHHH.

    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.

    Nectin2 Human
  • View Data Sheet

    Name :

    IFAN1 Porcine

    Description:

    Interferon-alpha 1 Porcine Recombinant

    Interferon alpha-1, Interferon-alpha, IFN-alpha-1, IFNA1, IFN-ALPHA-1, IFN1

    Product # :

    CYT-1197

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    Description

    IFA1 porcine Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-189) containing 176 amino acids and having a molecular mass of 20.2kDa.IFA1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    IFA1 protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      IFNs are cytokines that are widely known to induce potent anti-viral activity. IFN-a exerts a variety of other biological effects, including antitumor and immunomodulatory activities and are increasingly used clinically to treat a range of malignancies, myelodysplasias and autoimmune diseases.

    • Synonyms

      Interferon alpha-1, Interferon-alpha, IFN-alpha-1, IFNA1, IFN-ALPHA-1, IFN1

    • 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

      DGSMCDLPQT HSLAHTRALR LLAQMRRISP FSCLDHRRDF GSPHEAFGGN QVQKAQAMAL VHEMLQQTFQ LFSTEGSAAA WNESLLHQFC TGLDQQLRDL EACVMQEAGL EGTPLLEEDS ILAVRKYFHR LTLYLQEKSY SPCAWEIVRA EVMRSFSSSR NLQDRLRKKE HHHHHH

    • Background

      What is the molecular weight/Mw of IFNA1 PORCINE Protein?
      IFNA1 PORCINE Protein has a total Mw of 20.2kDa.

      What is the source or expression system of IFNA1 PORCINE Protein?
      HEK293 cells.

      What is the Purity of IFNA1 PORCINE Protein?
      IFNA1 PORCINE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNA1 PORCINE Protein?
      The biological functionality of IFNA1 PORCINE Protein will be determined in the future.

      What is the amino acid sequence of IFNA1 PORCINE Protein?
      DGSMCDLPQT HSLAHTRALR LLAQMRRISP FSCLDHRRDF GSPHEAFGGN QVQKAQAMAL VHEMLQQTFQ LFSTEGSAAA WNESLLHQFC TGLDQQLRDL EACVMQEAGL EGTPLLEEDS ILAVRKYFHR LTLYLQEKSY SPCAWEIVRA EVMRSFSSSR NLQDRLRKKE HHHHHH

      What applications can IFNA1 PORCINE Protein be used in?
      IFNA1 PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNA1 PORCINE Protein?
      The endotoxin level is minimal, IFNA1 PORCINE 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.

    Ifna1 Porcine
  • View Data Sheet

    Name :

    IL11 Mouse

    Description:

    Interleukin-11 Mouse Recombinant

    AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.

    Product # :

    CYT-646

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    Description

    Interleukin-11 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19.1kDa. The Mouse IL-11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% 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 the proliferation of murine T11 was found to be less than 2.0 ng/ml, corresponding to a specific activity of 500,000IU/mg.

    Citations

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL.

    • Background

      What is the molecular weight/Mw of IL11 MOUSE Protein?
      IL11 MOUSE Protein has a total Mw of 19.1kDa.

      What is the source or expression system of IL11 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL11 MOUSE Protein?
      IL11 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL11 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of murine T11 was found to be less than 2.0 ng/ml, corresponding to a specific activity of 500,000IU/mg.

      What is the amino acid sequence of IL11 MOUSE Protein?
      MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL.
      What applications can IL11 MOUSE Protein be used in?
      IL11 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL11 MOUSE Protein?
      The endotoxin level is minimal, IL11 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL11 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL11 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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 11 Mouse
  • View Data Sheet

    Name :

    PFDN2 Human

    Description:

    Prefoldin Subunit 2 Human Recombinant

    Prefoldin subunit 2, PFDN2, PFD2.

    Product # :

    PRO-001

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    Description

    PFDN2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-154 a.a.) and having a molecular mass of 18.8kDa. The PFDN2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PFDN2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Prefoldin subunit 2 (PFDN2) belongs to the prefoldin beta subunit family. The PFDN2 protein is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold correctly. PFDN2 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. PFDN2 also binds to a nascent polypeptide chain and promotes folding in an setting in which there are many competing pathways for nonnative proteins.

    • Synonyms

      Prefoldin subunit 2, PFDN2, PFD2.

    • 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 MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS.

    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.

    Pfdn2 Human
  • View Data Sheet

    Name :

    FLT1 D7 Human

    Description:

    Vascular Endothelial Growth Factor Receptor-1 D1-7 Human Recombinant

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-241

    Price :

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    Description

    Soluble FLT1 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric, glycosylated, polypeptide containing 751 amino acids and having a molecular mass of 130 kDa. The soluble receptor protein contains only the first 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. The FLT1 fc/Chimera is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT1 D1-7 was lyophilized from a concentrated (1 mg/ml) sterile solution containing PBS Buffer, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity of FLT1/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells. The ED50 for this effect is typically 10-30 ng/ml, corresponding to a specific activity of 33,333.33-100,000 units/mg.

    Citations

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    • Introduction

      Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution FLT1 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 FLT1 Fc/Chimera in PBS not less than 50µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG TAASDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI S.

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    Flt1 D7 Human
  • View Data Sheet

    Name :

    PLDN Human

    Description:

    Pallidin Homolog Human Recombinant

    Pallidin protein homolog (mouse), PA, HPS9, PALLID, syntaxin 13-interacting protein pallid.

    Product # :

    PRO-1068

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    Description

    PLDN Human Recombinant produced in E. coli is a single polypeptide chain containing 192 amino acids (1-172) and having a molecular mass of 21.9kDa.PLDN is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PLDN solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Pallidin is involved in intracellular vesicle trafficking. PLDN cooperates with Syntaxin 13 that facilitates intracellular membrane fusion. A Few alternatively spliced transcript variations of this gene have been discovered however the full-length nature of several of these variants has not been determined. PLDN takes part in the creation of lysosome-related organelles, for example melanosomes and platelet-dense granules. PLDN is known to cooperate with Dysbindin, BLOC1S1, STX12, CNO, MUTED, SNAPAP and BLOC1S2.

    • Synonyms

      Pallidin protein homolog (mouse), PA, HPS9, PALLID, syntaxin 13-interacting protein pallid.

    • 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 MSVPGPSSPD GALTRPPYCL EAGEPTPGLS DTSPDEGLIE DLTIEDKAVE QLAEGLLSHY LPDLQRSKQA LQELTQNQVV LLDTLEQEIS KFKECHSMLD INALFAEAKH YHAKLVNIRK EMLMLHEKTS KLKKRALKLQ QKRQKEELER EQQREKEFER EKQLTARPAK RM

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    Pldn Human
  • View Data Sheet

    Name :

    PODXL Mouse

    Description:

    Podocalyxin-Like Mouse Recombinant

    Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.

    Product # :

    PRO-2310

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    Description

    PODXL Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 391 amino acids (22-404a.a.) and having a molecular mass of 41.0kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). PODXL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Podocalyxin (PODXL) is a greatly glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein is involved in the regulation of both adhesion and cell morphology and cancer progression. PODXL functions as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Moreover, PODXL serves as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner.

    • Synonyms

      Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      HNGNETSTSA IKSSTVQSHQ SATTSTEVTT GHPVASTLAS TQPSNPTPFT TSTQSPSMPT STPNPTSNQS GGNLTSSVSE VDKTKTSSPS STAFTSSSGQ TASSGGKSGD SFTTAPTTTL GLINVSSQPT DLNTTSKLLS TPTTDNTTSP QQPVDSSPST ASHPVGQHTP AAVPSSSGST PSTDNSTLTW KPTTHKPLGT SEATQPLTSQ TPGITTLPVS TLQQSMASTV GTTTEEFTHL ISNGTPVAPP GPSTPSPIWA FGNYQLNCEP PIRPDEELLI LNLTRASLCE RSPLDEKEKL VELLCHSVKA SFKPAEDLCT LHVAPILDNQ AVAVKRIIIE TKLSPKAVYE LLKDRWDDLT EAGVSDMKLG KEGPPEVNED RFSLEHHHHH H.

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    Podxl Mouse
  • View Data Sheet

    Name :

    H2AFZ Human

    Description:

    H2A Histone Family, Member Z Human Recombinant

    H2A Histone Family, Member Z, H2AZ, H2A/z, H2A.Z-1, H2A.z, H2AZ Histone, Histone H2A.Z.

    Product # :

    PRO-1908

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    Description

    H2AFZ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (1-128 a.a) and having a molecular mass of 15.9kDa.H2AFZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    H2AFZ protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Histone H2A.Z (H2AFZ) belongs to the histone H2A family. Histones are basic nuclear proteins which are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). H2AFZ is implicated in the formation of constitutive heterochromatin and vital for chromosome segregation during cell division. Moreover, variant Histone H2A, which takes the place of conventional H2A in a subset of nucleosomes. Studies in mice have demonstrated that this particular histone is essential for embryonic development and show that lack of functional histone H2A leads to embryonic lethality.

    • Synonyms

      H2A Histone Family, Member Z, H2AZ, H2A/z, H2A.Z-1, H2A.z, H2AZ Histone, Histone H2A.Z.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAGGKAG KDSGKAKTKA VSRSQRAGLQ FPVGRIHRHL KSRTTSHGRV GATAAVYSAA ILEYLTAEVL ELAGNASKDL KVKRITPRHL QLAIRGDEEL DSLIKATIAG GGVIPHIHKS LIGKKGQQKT V

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    H2Afz Human
  • View Data Sheet

    Name :

    Resistin Human, HEK

    Description:

    Resistin Human Recombinant, HEK

    RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.

    Product # :

    CYT-1183

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    Description

    Resistin Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (19-108 a.a) containing 96 amino acids and having a molecular mass of 10.3 kDa.Resistin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    Resistin protein (1mg/ml) contains 20% glycerol and 20mM Sodium citrate (pH3.0).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis.Resistin blocks insulinstimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of lowdensity lipoprotein (LDL), increasing the risk of heart disease.

    • Synonyms

      RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.

    • 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

      KTLCSMEEAI NERIQEVAGS LIFRAISSIG LECQSVTSRG DLATCPRGFA VTGCTCGSAC GSWDVRAETT CHCQCAGMDW TGARCCRVQP HHHHHH

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    Resistin Protein
  • View Data Sheet

    Name :

    Omentin Human

    Description:

    Omentin Human Recombinant

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

    Product # :

    CYT-301

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    Description

    Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 313 amino acids and having a molecular mass of 35 kDa. Intelectin is purified by proprietary chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Each mg of lyophilized powder contains 10mM NaP, pH-7.5 and 5:1 mannitol to protein.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MNQLSFLLFL IATTRGWSTD EANTYFKEWTCSSSPSLPRS CKEIKDECPS AFDGLYFLRT ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKADY PEGDGNWANY NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS REITEAAVLLFYR.

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

    Omentin Human
  • View Data Sheet

    Name :

    TK1 Human

    Description:

    Thymidine Kinase 1 Human Recombinant

    Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    Product # :

    PKA-036

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    Description

    TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TK1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.

    • Synonyms

      Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    • 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 MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.

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    Tk1 Human
  • View Data Sheet

    Name :

    AITRL Human

    Description:

    AITRL Human Recombinant

    Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

    Product # :

    CYT-076

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    Description

    AITRL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (72-199) and having a molecular mass of 14.6 kDa.AITRL is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The AITRL solution (0.5mg/ml) contains 10mM sodium citrate (pH 3.5), 1mMDTT and 10% glycerol

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    AITRL-sds-page - Product image 1

    Citations

    More Info

    • Synonyms

      Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

    • 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

      MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LLANPQFIS

    • Background

      AITRL Human Recombinant: Unraveling its Significance in Immune Modulation and Therapeutic Implications

      1. Abstract

      This research paper provides a comprehensive examination of AITRL Human Recombinant, an essential protein involved in immune modulation. By exploring its structure, signaling mechanisms, biological functions, and implications in disease pathology, we shed light on the potential therapeutic applications of AITRL in immune-related disorders.

      2. Introduction

      AITRL, also known as TNFSF18, is a receptor protein belonging to the tumor necrosis factor superfamily. It plays a crucial role in immune regulation and has emerged as an intriguing target for therapeutic interventions in various immune-mediated conditions.

      3. Structure and Signaling of AITRL

      AITRL is a transmembrane protein with a conserved TNF domain. It interacts with its receptor, AITR (TNFRSF18), leading to downstream signaling events that modulate immune cell function. The binding of AITRL to AITR promotes immune cell activation and cytokine production.

      4. Biological Functions of AITRL

      AITRL is involved in the regulation of immune responses by influencing T-cell activation, proliferation, and differentiation. It can stimulate effector T-cell responses while also promoting the development and function of regulatory T cells, thus maintaining immune homeostasis.

      5. AITRL in Disease Pathology

      Dysregulation of AITRL signaling has been implicated in various immune-related disorders, including autoimmune diseases, allergic reactions, and cancer. AITRL's involvement in disease pathology highlights its significance as a potential therapeutic target.

      6. Therapeutic Potential of AITRL

      The unique role of AITRL in immune modulation presents opportunities for therapeutic interventions. Modulating AITRL signaling holds promise for manipulating immune responses in the context of autoimmune diseases, allergic disorders, and cancer immunotherapy.

      7. Conclusion and Future Perspectives

      While our understanding of AITRL and its functions has advanced significantly, further research is needed to unravel its complex signaling pathways and therapeutic potential fully. Continued investigations into AITRL biology will pave the way for the development of targeted therapies for immune-related disorders.

      What is the molecular weight/Mw of AITRL Protein?
      AITRL Protein has a total Mw of 15.6kDa.

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

      What is the Purity of AITRL Protein?
      AITRL Protein is >85% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of AITRL Protein?
      MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH.

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

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

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    Tnfsf18 Human
  • View Data Sheet

    Name :

    DEFB118 Human

    Description:

    Beta Defensin 118 Human Recombinant

    Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    Product # :

    CYT-714

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    Description

    DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    DEFB118-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.

    • Synonyms

      Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    • 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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

    • Background

      Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications

      Abstract:


      Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.

      Production and Characterization:


      Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD118.

      Role in Innate Immunity:


      BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.

      Therapeutic Implications:


      Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.

      Conclusion:


      Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.

      What is the molecular weight/Mw of DEFB118 Protein?
      DEFB118 Protein has a total Mw of 13.8kDa.

      What is the source or expression system of DEFB118 Protein?
      Escherichia Coli.

      What is the Purity of DEFB118 Protein?
      DEFB118 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of DEFB118 Protein?
      The biological functionality of DEFB118 Protein will be determined in the future.

      What is the amino acid sequence of DEFB118 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

      What applications can DEFB118 Protein be used in?
      DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for DEFB118 Protein?
      The endotoxin level is minimal, DEFB118 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.

    Defb118 Human
  • View Data Sheet

    Name :

    ANXA7 Human

    Description:

    Annexin A7 Human Recombinant

    Annexin A7, Annexin-7, Annexin VII, Synexin, ANXA7, ANX7, SNX.

    Product # :

    PRO-449

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    Description

    ANXA7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 490 amino acids (1-466 a.a.) and having a molecular mass of 52.9kDa.ANXA7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ANXA7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 150mM NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Annexin VII is a member of the annexin family of calcium-dependent phospholipid binding proteins. Annexin VII has molecular weight of approximately 51 kDa with a unique, highly hydrophobic N-terminal domain of 167 amino acids and a conserved C-terminal region of 299 amino acids. The latter domain is composed of alternating hydrophobic and hydrophilic segments. Structural analysis of the protein suggests that Annexin VII is a membrane binding protein with diverse properties including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion.

    • Synonyms

      Annexin A7, Annexin-7, Annexin VII, Synexin, ANXA7, ANX7, SNX.

    • 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 MGSHMSYPGY PPTGYPPFPG YPPAGQESSF PPSGQYPYPS GFPPMGGGAY PQVPSSGYPG AGGYPAPGGY PAPGGYPGAP QPGGAPSYPG VPPGQGFGVP PGGAGFSGYP QPPSQSYGGG PAQVPLPGGF PGGQMPSQYP GGQPTYPSQP ATVTQVTQGT IRPAANFDAI RDAEILRKAM KGFGTDEQAI VDVVANRSND QRQKIKAAFK TSYGKDLIKD LKSELSGNME ELILALFMPP TYYDAWSLRK AMQGAGTQER VLIEILCTRT NQEIREIVRC YQSEFGRDLE KDIRSDTSGH FERLLVSMCQ GNRDENQSIN HQMAQEDAQR LYQAGEGRLG TDESCFNMIL ATRSFPQLRA TMEAYSRMAN RDLLSSVSRE FSGYVESGLK TILQCALNRP AFFAERLYYA MKGAGTDDST LVRIVVTRSE IDLVQIKQMF AQMYQKTLGT MIAGDTSGDY RRLLLAIVGQ

    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.

    Anxa7 Human
  • View Data Sheet

    Name :

    ARF1 Human

    Description:

    ADP-Ribosylation Factor 1 Human Recombinant

    ARF-1, ADP-ribosylation factor 1.

    Product # :

    PRO-867

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    Description

    ARF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8 kDa. The ARF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARF1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARF1 is a small guanine nucleotide-binding protein that increases the enzymatic activities of cholera toxin. ARF1 is necessary and ubiquitous in eukaryotes. ARF1 takes part in vesicular transport and functioning via phospholipase D activation. ARF1 is involved in membrane traffic and organelle integrity which are closely tied to their reversible association with membranes and distinct interactions with membrane phospholipids.

    • Synonyms

      ARF-1, ADP-ribosylation factor 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K.

    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.

    Arf1 Human
  • View Data Sheet

    Name :

    SNTN Human

    Description:

    Sentan Cilia Apical Structure Protein Human Recombinant

    Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-like.

    Product # :

    PRO-216

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    Description

    SNTN Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 18.6kDa. The SNTN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.15M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SNTN is a member of to the S-100 family. SNTN is localized solely to the bridging structure between the cell membrane and peripheral singlet microtubules that specifically exists in the narrowed distal portion of cilia. Exogenously expressed sentan displayed affinity for the membrane protrusions, and a protein-lipid binding assay discovered that sentan bounds to phosphatidylserine which indicate that sentan is the leading molecular component of the ciliary tip to link the cell membrane and peripheral singlet microtubules, making the distal portion of the cilia narrow and stiff to permit better airway approval or ovum transport.

    • Synonyms

      Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-like.

    • 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 MGGCMHSTQD KSLHLEGDPN PSAAPTSTCA PRKMPKRISI SKQLASVKAL RKCSDLEKAI ATTALIFRNS SDSDGKLEKA IAKDLLQTQF RNFAEGQETK PKYREILSEL DEHTENKLDF EDFMILLLSI TVMSDLLQNI RNVKIMK

    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.

    Sntn Human
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