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    B-Cell Activating Factor

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    B type Natriuretic Peptide

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    Betacellulin

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    Eotaxin (CCL11,24,26)

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Search results

1000 results found for “Ring Finger Protein”

Name

Description

Product #

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  • View Data Sheet

    Name :

    EIF1 Human

    Description:

    Eukaryotic Translation Initiation Factor 1 Human Recombinant

    A121, EIF-1, EIF1A, ISO1, SUI1, Eukaryotic translation initiation factor 1, eIF1, Protein translation factor SUI1 homolog, Sui1iso1, EIF1.

    Product # :

    PRO-773

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    EIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-113 a.a.) and having a molecular weight of 16.9kDa.The EIF1 is fused to 37 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF1 is important for scanning and plays a role in initiation site selection. EIF1 promotes the assembly of 48S ribosomal at the authentic initiation codon of a conventional capped mRNA.

    • Synonyms

      A121, EIF-1, EIF1A, ISO1, SUI1, Eukaryotic translation initiation factor 1, eIF1, Protein translation factor SUI1 homolog, Sui1iso1, EIF1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWAGSMSA IQNLHSFDPF ADASKGDDLL PAGTEDYIHI RIQQRNGRKT LTTVQGIADD YDKKKLVKAF KKKFACNGTV IEHPEYGEVI QLQGDQRKNI CQFLVEIGLA KDDQLKVHGF.

    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.

    Eif1 Human
  • View Data Sheet

    Name :

    TEK Human Fc

    Description:

    TEK Tyrosine Kinase Endothelial Fc Chimera Human Recombinant

    Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.

    Product # :

    PKA-248

    Price :

    Quantity :

    Shipping Method :

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    • More Info

    Description

    Soluble TEK Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a monomeric, glycosylated, polypeptide containing 730 amino acids and having a total molecular mass of 250 kDa. Human TIE-2/Fc monomer has a calculated molecular mass of approximately 125 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 140 kDa protein in SDS-PAGE under reducing conditions.The TEK Fc Chimera is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    TEK Fc Chimera was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.

    • Synonyms

      Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized sTIE-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TEK 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 TIE-2 Fc Chimera in sterile water 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.

    Tie 2 Human Fc
  • View Data Sheet

    Name :

    Thyroglobulin Human

    Description:

    Thyroglobulin Human

    Thyroglobulin, TGN, AITD3, TG.

    Product # :

    PRO-443

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
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    • More Info
    • sds-page

    Description

    Human Thyroglobulin is a glycosylated, polypeptide chain having a total molecular mass of 660 kDa (330 kDa per subunit).

    Source

    Human thyroid glands.

    Formulation

    Lyophilized from 0.02M NH4HCO3. May contain traces of buffer salts.

    Purity

    Greater than 98.0%.

    sds-page

    Thyroglobulin Human Native SDS-PAGE - Product image 1

    More Info

    • Introduction

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

    • Synonyms

      Thyroglobulin, TGN, AITD3, TG.

    • Physical Appearance

      Sterile Filtered Off-White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Use phosphate buffer, pH>7.0 containing 0.15M NaCl is recommended.

    • Human Virus Test

      Starting material tested and certified negative for HIV I & II antibodies, Hepatitis B surface antigen, Hepatitis C antibodies, Syphilis and HIV-1/HBV/HCV NAT.

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

    Thyroglobulin Human
  • View Data Sheet

    Name :

    Leptin Human, PEG

    Description:

    Leptin Human Recombinant, PEG

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1108

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    Pegylated Leptin Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Leptin Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It’s in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo it has profound weight reducing effect, resulting mainly from reduced food intake.

    More Info

    • Introduction

      Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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 Pegylated leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • 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 at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Mutant
  • View Data Sheet

    Name :

    CRISP1 Human

    Description:

    Cysteine-Rich Secretory Protein 1 Human Recombinant

    Cysteine-rich secretory protein 1, ARP, CRISP-1, AEGL1, Acidic epididymal glycoprotein-like 1, HSCRISP1D, HSCRISP1G, HUMARP, AEG-like protein, cysteine-rich secretory protein-1 delta.

    Product # :

    PRO-473

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
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    • More Info

    Description

    The CRISP1 Protein Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (Lys 22 - Lys 249) having a molecular mass of 27kDa.CRISP1 is fused to 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.5mg/ml solution containing 20mM TRIS, 50mM NaCl, pH 7.5.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Insemination involves of a series of specific cell-cell interactions concluding in the fusion of the sperm and egg plasma membranes. Recognition, binding, and fusion take place through the interface of complementary molecules which are localized to specific domains of the sperm and egg plasma membranes. In the sperm, the postacrosomal region or equatorial segment is involved in sperm-egg plasma membrane fusion. The protein encoded by this gene belongs to the cysteine-rich secretory protein (CRISP) family. CRISP1 is expressed in the epididymis, is secreted into the epididymal lumen, and binds to the postacrosomal region of the sperm head, where it takes part in sperm-egg fusion.

    • Synonyms

      Cysteine-rich secretory protein 1, ARP, CRISP-1, AEGL1, Acidic epididymal glycoprotein-like 1, HSCRISP1D, HSCRISP1G, HUMARP, AEG-like protein, cysteine-rich secretory protein-1 delta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CRISP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CRISP1 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 CRISP1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MKHHHHHHAS KKKSARDQFN KLVTDLPNVQ EEIVNIHNAL RRRVVPPASN MLKMSWSEEA AQNARIFSKY CDMTESNPLE RRLPNTFCGE NMHMTSYPVS WSSVIGVWYS ESTSFKHGEW TTTDDDITTD HYTQIVWATS YLIGCAIASC RQQGSPRYLY VCHYCHEGND PETKNEPYKT GVPCEACPSN CEDKLCTNPC IYYDEYFDCD IQVHYLGCNH STTILFCKAT CLCDTEIK

    • Applications

      Western blotting, ELISA.

    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.

    Crisp1 Human
  • View Data Sheet

    Name :

    Cyclosporin A

    Description:

    Cyclosporin-A

    Product # :

    PRO-408

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    Description

    Cyclosporin is a cyclic polypeptide immunosuppressant agent consisting of 11 amino acids and having a molecular weight of 1202.64. It is produced as a metabolite by the fungus species Beauveria nlyea. Chemically, cyclosporin is designated as [R-[R*,R*-(E)]]-cyclic(L-alanyl-D- alanyl-N-methyl-L-leucyl-N-methyl-L-leucyl-N-methyl-L-valyl-3-hydroxy-N, 4-dimethyl-L-2-amino-6-octenoyl-L-a-amino-butyryl- N-methylglycyl-N- methyl-L-leucyl-L-valyl-N-methyl-L-leucyl). Molecular Formula: C62H111N11O12.

    Source

    Beauveria Nivea.

    Formulation

    The Cyclosporin-A was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

    Greater than 99.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Cyclosporin A is a noncytotoxic, natural, 11 amino acid cyclic peptide used clinically as an immunosuppressant for the treatment of autoimmune and inflammatory disorders and to prevent organ rejection after transplantation. Cyclosporin acts chiefly by inhibiting T lymphocyte function, which is vital for the propagation of inflammation. Cyclosporin A does not suppress the activity of other hematopoietic cells, does not cause bone marrow suppression and has a rapid onset of action as opposed to other immunosuppressive agents. Nevertheless, Cyclosporin A -induced nephrotoxicity remains an important clinical problem, and oxidative stress has been implicated as a potential responsible mechanism.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cyclosporin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cyclosporin A 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 Cyclosporin-A in anhydrous ethanol R at a concentration of 50mg/ml.

    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.

    Cyclosporin A
  • View Data Sheet

    Name :

    ANXA1 Human

    Description:

    Annexin A1 Human Recombinant

    ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

    Product # :

    PRO-679

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    Description

    ANXA1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 346 amino acids (1-346 a.a.) and having a molecular mass of 38.7 kDa.ANXA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.

    • Synonyms

      ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

    • 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

      MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK
      PLDETLKKAL TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL
      LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK VLDLELKGDI EKCLTAIVKCATSKPAFFAE KLHQAMKGVG TRHKALIRIM VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN.

    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.

    Anxa1 Human
  • View Data Sheet

    Name :

    FGB Human

    Description:

    Fibrinogen Beta Chain Human Recombinant

    Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.

    Product # :

    PRO-2210

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    Description

    FGB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 351 amino acids (164-491a.a) and having a molecular mass of 40kDa. FGB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fibrinogen Beta Chain 9 (FGB) is the beta component of fibrinogen, a blood-borne glycoprotein composed of 3 pairs of nonidentical polypeptide chains. When vascular injury accrues, fibrinogen is cleaved by thrombin to form fibrin which is found in abundance in blood clots.

    • Synonyms

      Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.

    • 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 MGSDNENVVN EYSSELEKHQ LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM SMKIRPFFPQ Q.

    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.

    Fgb Human
  • View Data Sheet

    Name :

    NOL3 Human

    Description:

    Nucleolar Protein 3 Human Recombinant

    Nucleolar protein 3 (apoptosis repressor with CARD domain), Muscle-enriched cytoplasmic protein, Nucleolar protein of 30 kDa, Apoptosis repressor with CARD, nucleolar protein 3, NOP30, CARD2, ARC, NOP, MYP, MYC.

    Product # :

    PRO-1178

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    Description

    NOL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 231 amino acids (1-208) and having a molecular mass of 25.0 kDa.NOL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NOL3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT, 1mM EDTA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleolar protein 3 (NOL3) is primarily expressed in the muscle and is appears in the nucleoplasm and concentrated in nucleoli. NOL3 is an anti-apoptotic protein which down-regulates the enzymatic activities of caspase 2, caspase 8 and tumor protein p53. NOL3 is highly expressed in the heart and skeletal muscle. NOL3 is identified at low levels in the placenta, liver, kidney and pancreas. The NOL3 mRNA and protein levels are stimulated by neuronal activity, which is vital in order to promote neuroplasticity, thus indicating a potential role for NOL3 in activity-dependent changes in dendrite function. NOL3 localizes to the cytoskeleton of neuronal cells and seems to colocalize with F-Actin, though it may connect with an actin-associated protein instead of directly with F-Actin.

    • Synonyms

      Nucleolar protein 3 (apoptosis repressor with CARD domain), Muscle-enriched cytoplasmic protein, Nucleolar protein of 30 kDa, Apoptosis repressor with CARD, nucleolar protein 3, NOP30, CARD2, ARC, NOP, MYP, MYC.

    • 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 MGSMGNAQER PSETIDRERK RLVETLQADS GLLLDALLAR GVLTGPEYEA LDALPDAERR VRRLLLLVQG KGEAACQELL RCAQRTAGAP DPAWDWQHVG PGYRDRSYDP PCPGHWTPEA PGSGTTCPGL PRASDPDEAG GPEGSEAVQS GTPEEPEPEL EAEASKEAEP EPEPEPELEP EAEAEPEPEL EPEPDPEPEP DFEERDESED S.

    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.

    Nol3 Human
  • View Data Sheet

    Name :

    MLLT11 Human

    Description:

    Myeloid/Lymphoid Leukemia Translocated To 11 Human Recombinant

    AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    Product # :

    PRO-1991

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    Description

    MLLT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids (1-90 a.a) and having a molecular mass of 12.4kDa. MLLT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MLLT11 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myeloid/Lymphoid Leukemia Translocated To 11 (MLLT11) is a part of the Mixed-Lineage Leukemia protein family. MLLT11 which takes part in leukemogenesis and in the progression of severe monocytic leukemia (AML) is located on chromosome 11q23. MLLT11 which is also expressed in embryonic brain cortex is upregulated during neuronal differentiation and is taking part in the evolution of the central nervous system.

    • Synonyms

      AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    • 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 MGSMRDPVSS QYSSFLFWRM PIPELDLSEL EGLGLSDTAT YKVKDSSVGK MIGQATAADQ EKNPEGDGLL EYSTFNFWRA PIASIHSFEL DLL.

    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.

    Mllt11 Human
  • View Data Sheet

    Name :

    PRRT2 Human

    Description:

    Proline-Rich Transmembrane Protein 2 Human Recombinant

    Proline-Rich Transmembrane Protein 2, Infantile Convulsions And Paroxysmal Choreoathetosis, Dispanin Subfamily B Member 3, DSPB3, BFIC2, BFIS2, DYT10, EKD1, PKC, FICCA, IFITMD1, ICCA.

    Product # :

    PRO-1852

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    Description

    PRRT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 291 amino acids (1-268) and having a molecular mass of 29.7 kDa. PRRT2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The PRRT2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transmembrane protein PRRT2 holds a proline-rich domain in its N-terminal half. PRRT2 is known to be primarily expressed in brain and spinal cord in embryonic and postnatal stages. Alterations in this gene are the cause for paroxysmal kinesigenic dyskinesia. PRRT2 mutations were found in nearly 30% of sporadic PKC patients.

    • Synonyms

      Proline-Rich Transmembrane Protein 2, Infantile Convulsions And Paroxysmal Choreoathetosis, Dispanin Subfamily B Member 3, DSPB3, BFIC2, BFIS2, DYT10, EKD1, PKC, FICCA, IFITMD1, ICCA.

    • 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 MGSMAASSSE ISEMKGVEES PKVPGEGPGH SEAETGPPQV LAGVPDQPEA PQPGPNTTAA PVDSGPKAGL APETTETPAG ASETAQATDL SLSPGGESKA NCSPEDPCQE TVSKPEVSKE ATADQGSRLE SAAPPEPAPE PAPQPDPRPD SQPTPKPALQ PELPTQEDPT PEILSESVGE KQENGAVVPL QAGDGEEGPA PEPHSPPSKK SPPANGAPPR VLQQLVEEDR MRRAHSGHPG SPRGSLSRHP SSQLAGPGVE GGEGTQKPRD Y.

    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.

    Prrt2 Human
  • 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 :

    Cardiac Actin Bovine

    Description:

    Cardiac Actin Bovine

    Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.

    Product # :

    PRO-519

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    Description

    Ultra pure Cardiac Actin having a Molecular mass of 43,000 dalton.

    Source

    Bovine Heart.

    Formulation

    The protein was lyophilized from a 1mg/ml solution containing 10mM Tris-acetate buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% SDS.

    Purity

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

    More Info

    • Introduction

      Alpha-cardiac actin belongs to the actin family which is comprised of three main groups of actin isoforms, alpha, beta, and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Defects in the cardiac actin have been associated with idiopathic dilated cardiomyopathy (IDC) and familial hypertrophic cardiomyopathy (FHC).

    • Synonyms

      Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      Protein standard in 1D and 2D SDS gelelectrophoresis
      Immunoassays
      Immunization.

    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.

    Cardiac Actin
  • View Data Sheet

    Name :

    S100A15 Mouse

    Description:

    S100 Calcium Binding Protein A15 Mouse Recombinant

    Protein S100-A7A, S100 calcium-binding protein A15A, S100 calcium-binding protein A7A.

    Product # :

    PRO-1145

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    Description

    S100A15 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (1-108) and having a molecular mass of 15.0 kDa.S100A15 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The S100A15 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mouse S100A15 is a protein of 104 amino acids with an expected molecular weight of 12,870 Dalton having 2 EF-hand calcium binding sites. The S100A15 expression is upregulated in cultured keratinocytes stimulated to differentiate by calcium or phorbol esters. S100A15 is expressed in the skin and keratinocytes.

    • Synonyms

      Protein S100-A7A, S100 calcium-binding protein A15A, S100 calcium-binding protein A7A.

    • 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 MGSHMPDTPV EDSLFQIIHC FHHYAAREGD KETLSLEELK ALLLDSVPRF MDTLGRRQPY YITELFRAAD KNKDNQICFD EFLYILGKLV KDYHLQFHRQ LCAHYCTEHS LY.

    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.

    S100A15 Mouse
  • View Data Sheet

    Name :

    TYRO3 Mouse

    Description:

    TYRO3 Protein Tyrosine Kinase Mouse Recombinant

    Etk2/tyro3, TK19-2, Tyrosine-protein kinase DTK, Tyrosine-protein kinase RSE, Tyrosine-protein kinase TIF, Tyro3, Dtk, Rse, Tif, AI323366, Brt, Etk-2.

    Product # :

    PKA-120

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    Description

    TYRO3 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 628 amino acids (31-419 aa) and having a molecular mass of 68.9kDa.TYRO3 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The TYRO3 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TYRO3 Protein Tyrosine Kinase or TYRO3 is a transmembrane receptor tyrosine kinase. TYRO3 has crucial role in essential processes such as cell migration, actin reorganization and cell survival. It is activated and signaled by MAPK/ERK and PI3K/AKT that expedites the cellular functions of protein.

    • Synonyms

      Etk2/tyro3, TK19-2, Tyrosine-protein kinase DTK, Tyrosine-protein kinase RSE, Tyrosine-protein kinase TIF, Tyro3, Dtk, Rse, Tif, AI323366, Brt, Etk-2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      AGLKLMGAPV KMTVSQGQPV KLNCSVEGME DPDIHWMKDG TVVQNASQVS ISISEHSWIG LLSLKSVERS DAGLYWCQVK DGEETKISQS VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC EAVGPPEPVT IYWWRGLTKV GGPAPSPSVL NVTGVTQRTE FSCEARNIKG LATSRPAIVR LQAPPAAPFN TTVTTISSYN ASVAWVPGAD GLALLHSCTV QVAHAPGEWE ALAVVVPVPP FTCLLRNLAP ATNYSLRVRC ANALGPSPYG DWVPFQTKGL APARAPQNFH AIRTDSGLIL EWEEVIPEDP GEGPLGPYKL SWVQENGTQD ELMVEGTRAN LTDWDPQKDL ILRVCASNAI GDGPWSQPLV VSSHDHAGRQ GPPHSRTSWL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH

    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.

    Tyro3 Mouse
  • View Data Sheet

    Name :

    PRND Human

    Description:

    Prion Protein 2 Human Recombinant

    Prion protein 2, DOPPEL, DPL, PrPL.

    Product # :

    PRO-018

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    Description

    PRND Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (27-152a.a) and having a molecular mass of 16.9kDa. PRND is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRND protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRND is a membrane glycosylphosphatidylinositol-anchored glycoprotein which exists mainly in testis. PRND is expressed during embryogenesis, although in the central nervous system it is expressed minimally .Mutations in PRND may cause neurological disorders. PRND located on chromosome 20, about 20 kbp downstream of the gene encoding cellular prion protein, to which it is biochemically and structurally analogous.

    • Synonyms

      Prion protein 2, DOPPEL, DPL, PrPL.

    • 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 MGSRGIKHRI KWNRKALPST AQITEAQVAE NRPGAFIKQG RKLDIDFGAE GNRYYEANYW QFPDGIHYNG CSEANVTKEA FVTGCINATQ AANQGEFQKP DNKLHQQVLW RLVQELCSLK HCEFWLERG.

    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.

    Prnd Human
  • View Data Sheet

    Name :

    RAB3IL1 Human

    Description:

    RAB3A Interacting Protein Like 1 Human Recombinant

    GRAB, Rab-3A-interacting-like protein 1, Guanine nucleotide exchange factor for Rab-3A, Rab3A-interacting-like protein 1, Rabin3-like 1.

    Product # :

    PRO-2141

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    Description

    RAB3IL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 405 amino acids (1-382a.a) and having a molecular mass of 45kDa.RAB3IL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RAB3IL1 protein solution (0.25mg/ml) containing Phosphate buffer saline (pH 7.4) and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAB3A Interacting Protein Like 1 (RAB3IL1) is a 382 amino acid protein which is a member of the SEC2 family. RAB3IL1 is a guanine nucleotide exchange factor (GEF) for Rab3A. RAB3IL1 competes for interaction with Rab3A and IHPK1 via its coiled coil domain, which doesn’t involve IHPK1 kinase activity.

    • Synonyms

      GRAB, Rab-3A-interacting-like protein 1, Guanine nucleotide exchange factor for Rab-3A, Rab3A-interacting-like protein 1, Rabin3-like 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMWSGPPQ PDQGLPPPLA AVPVPWKSTD PCQGHRESPG ALVETSAGEE AQGQEGPAAA QLDVLRLRSS SMEIREKGSE FLKEELHRAQ KELKLKDEEC ERLSKVREQL EQELEELTAS LFEEAHKMVR EANMKQAASE KQLKEARGKI DMLQAEVTAL KTLVITSTPA SPNRELHPQL LSPTKAGPRK GHSRHKSTSS TLCPAVCPAA GHTLTPDREG KEVDTILFAE FQAWRESPTL DKTCPFLERV YREDVGPCLD FTMQELSVLV RAAVEDNTLT IEPVASQTLP TVKVAEVDCS STNTCALSGL TRTCRHRIRL GDSKSHYYIS PSSRARITAV CNFFTYIRYI QQGLVRQDAE PMFWEIMRLR KEMSLAKLGF FPQEA.

    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.

    Rab3Il1 Human
  • View Data Sheet

    Name :

    EIF3J Human

    Description:

    Eukaryotic Translation Initiation Factor 3J Human Recombinant

    Eukaryotic translation initiation factor 3 subunit J, Eukaryotic translation initiation factor 3 subunit 1, eIF-3-alpha, eIF3 p35, EIF3J, EIF3S1, eIF3-alpha.

    Product # :

    PRO-970

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    Description

    EIF3J Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (70-258) and having a molecular mass of 24kDa (Molecular weight on SDS-PAGE will appear higher).EIF3J is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF3J solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic translation initiation factor 3 subunit J (EIF3J) is a member of the EIF-3 subunit J family. EIF3 has a crucial role in binding of initiator methionyl-tRNA and mRNA to the 40S ribosomal subunit to produce the 40S initiation complex. EIF3J binds to the aminoacyl (A) site and mRNA access channel of the 40S subunit, setting EIF3J directly in the ribosomal decoding center. In addition, EIF3J interacts with eIF1A and reduces 40S subunit affinity for mRNA. An elevated affinity for mRNA is restored upon enlistment of initiator tRNA, despite the fact EIF3J remains in the mRNA-binding cleft in the presence of tRNA.

    • Synonyms

      Eukaryotic translation initiation factor 3 subunit J, Eukaryotic translation initiation factor 3 subunit 1, eIF-3-alpha, eIF3 p35, EIF3J, EIF3S1, eIF3-alpha.

    • 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 MKISEKKKIA EKIKEKERQQ KKRQEEIKKR LEEPEEPKVL TPEEQLADKL RLKKLQEESD LELAKETFGV NNAVYGIDAM NPSSRDDFTE FGKLLKDKIT QYEKSLYYAS FLEVLVRDVC ISLEIDDLKK ITNSLTVLCS EKQKQEKQSK AKKKKKGVVP GGGLKATMKD DLADYGGYDG GYVQDYEDFM.

    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.

    Eif3J Human
  • View Data Sheet

    Name :

    SNRPC Human

    Description:

    Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant

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

    Product # :

    PRO-1004

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Snrpc Human
  • View Data Sheet

    Name :

    Glycinin

    Description:

    Allergen Ara h 3.0101 Recombinant

    Glycinin, Arah3.

    Product # :

    ALR-008

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    Description

    Recombinant Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa. Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Glycinin is supplied in 20mM HEPES buffer pH-8, 6M Urea and 0.25M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.

    • Synonyms

      Glycinin, Arah3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Glycinin
  • View Data Sheet

    Name :

    PTPRN Human

    Description:

    Protein Tyrosine Phosphatase Receptor Type N Human Recombinant

    Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.

    Product # :

    ENZ-1162

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    Description

    Recombinant Human Protein Tyrosine Phosphatase Receptor Type N produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. PTPRN is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    PTPRN is supplied in 50mM Sodium phosphate (pH 8.0) and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein Tyrosine Phosphatase Receptor Type N (PTPRN) is a catalytically inactive protein and a major target of autoimmune response in diabetes mellitus. The long C-terminal intracellular tail covers the majority of autoantibody epitopes. PTPRN is expressed in neural, neuroendocrine and pancreatic islet cells.

    • Synonyms

      Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.

    • 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. Avoid multiple freeze-thaw cycles.

    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.

    Ptprn Human
  • View Data Sheet

    Name :

    LLO

    Description:

    Listeriolysin-O Recombinant

    Listeriolysin-O, LLO, hlyA.

    Product # :

    PRO-320

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    Description

    LLO is a single, non-glycosylated polypeptide chain containing 529 amino acids and having a molecular mass of 58kDa. (accession number: AAF64524).

    Source

    Escherichia Coli.

    Formulation

    The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, pH 6.4, 1mM DTT, 5% (v/v) glycerol and 0.5M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Hemolytic activity is 8,27E+05  HU/mg of protein where HU means hemolytic activity unit that is the amount of toxin needed to release half the hemoglobin (50% lysis) of the erythrocytes as determined by hemolysin assay.

    More Info

    • Introduction

      Listeriolysin O (aka LLO) is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents and inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes (average pH ~ 5.9) of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, and the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system and antibodies. LLO also brings about dephosphorylation of histone H3 and deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO and is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST's supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO.

    • Synonyms

      Listeriolysin-O, LLO, hlyA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    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.

    Listeriolysin O
  • View Data Sheet

    Name :

    RPS10 Human

    Description:

    Ribosomal Protein S10 Human Recombinant

    DBA9, S10, 40S ribosomal protein S10, RPS10.

    Product # :

    PRO-1409

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    Description

    RPS10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 21kDa. RPS10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RPS10 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribosomes (the organelles that catalyze protein synthesis) consist of a small 40S subunit and a large 60S subunit. Jointly these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPS10 which is is located in the cytoplasm and a part of the S10E family of ribosomal proteins, is a ribosomal protein that is a component of the 40S subunit. Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found.

    • Synonyms

      DBA9, S10, 40S ribosomal protein S10, RPS10.

    • 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 MGSMLMPKKN RIAIYELLFK EGVMVAKKDV HMPKHPELAD KNVPNLHVMK AMQSLKSRGY VKEQFAWRHF YWYLTNEGIQ YLRDYLHLPP EIVPATLRRS RPETGRPRPK GLEGERPARL TRGEADRDTY RRSAVPPGAD KKAEAGAGSA TEFQFRGGFG RGRGQPPQ.

    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.

    Rps10 Human
  • View Data Sheet

    Name :

    KLF7 Human

    Description:

    Kruppel-Like Factor 7 Human Recombinant

    UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.

    Product # :

    PRO-1527

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    Description

    KLF7 Human Recombinant produced in E. coli is a single polypeptide chain containing 325 amino acids (1-302) and having a molecular mass of 35.8kDa. KLF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KLF7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kruppel-Like Factor 7 (KLF7) is a part of the Kruppel-like transcriptional regulator family whose members regulate cell proliferation, differentiation and survival and contain 3 C2H2 zinc fingers at the C-terminus that mediate binding to GC-rich sites. KLF7 contributes to the progression of type 2 diabetes by inhibiting hormone expression and secretion in pancreatic beta-cells and also by deregulating adipocytokine secretion in adipocytes.

    • Synonyms

      UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.

    • 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 MGSMDVLASY SIFQELQLVH DTGYFSALPS LEETWQQTCL ELERYLQTEP RRISETFGED LDCFLHASPP PCIEESFRRL DPLLLPVEAA ICEKSSAVDI LLSRDKLLSE TCLSLQPASS SLDSYTAVNQ AQLNAVTSLT PPSSPELSRH LVKTSQTLSA VDGTVTLKLV AKKAALSSVK VGGVATAAAA VTAAGAVKSG QSDSDQGGLG AEACPENKKR VHRCQFNGCR KVYTKSSHLK AHQRTHTGEK PYKCSWEGCE WRFARSDELT RHYRKHTGAK PFKCNHCDRC FSRSDHLALH MKRHI.

    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.

    Klf7 Human
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