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Search results

1000 results found for “collagen”

Name

Description

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  • View Data Sheet

    Name :

    DCUN1D2 Human

    Description:

    DCN1 Defective in Cullin Neddylation 1 Domain Containing 2 Human Recombinant

    DCN1-like protein 2, DCUN1 domain-containing protein 2, Defective in cullin neddylation protein 1-like protein 2, DCUN1D2, C13orf17, DCUN1L2.

    Product # :

    PRO-899

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    Description

    DCUN1D2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259 a.a.) and having a molecular mass of 32.3kDa.DCUN1D2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCUN1D2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DCN1-like protein 2 (DCUN1D2) which contains one DCUN1 domain and 1 UBA-like domain, may have a role in the neddylation of cullins which regulate SCF-type ubiquitin ligase complexes. The gene encoding Dcun1D2 is located on human chromosome 13. Chromosome 13 contains major tumor suppressor genes, including BRCA2 and RB1, which are linked with breast cancer susceptibility and retinoblastoma, respectively.

    • Synonyms

      DCN1-like protein 2, DCUN1 domain-containing protein 2, Defective in cullin neddylation protein 1-like protein 2, DCUN1D2, C13orf17, DCUN1L2.

    • 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 MHKLKSSQKD KVRQFMACTQ AGERTAIYCL TQNEWRLDEA TDSFFQNPDS LHRESMRNAV DKKKLERLYG RYKDPQDENK IGVDGIQQFC DDLSLDPASI SVLVIAWKFR AATQCEFSRK EFLDGMTELG CDSMEKLKAL LPRLEQELKD TAKFKDFYQF
      TFTFAKNPGQ KGLDLEMAVA YWKLVLSGRF KFLDLWNTFL MEHHKRSIPR DTWNLLLDFG NMIADDMSNY DEEGAWPVLI DDFVEYARPV VTGGKRSLF.

    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.

    Dcun1D2 Human
  • View Data Sheet

    Name :

    SERPINC1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade C Member 1 Human Recombinant

    AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1, SERPINC1.

    Product # :

    PRO-1877

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    Description

    SERPINC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (33-464 a.a) and having a molecular mass of 51.4kDa. SERPINC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SERPINC1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serpin Peptidase Inhibitor, Clade C Member 1 (SERPINC1), which is a part of the serpin superfamily, is a plasma protease inhibitor. SERPINC1 inhibits thrombin and other activated serine proteases of the coagulation system, and regulates the blood coagulation cascade. SERPINC1 also inhibits Thrombin and Factors IXa, Xa and XIa. Deficiencies in SERPINC1 can cause ATIII deficiency, an autosomal dominant disease which might lead to a hereditary thrombophilia.

    • Synonyms

      AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1, SERPINC1.

    • 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 MGSHGSPVDI CTAKPRDIPM NPMCIYRSPE KKATEDEGSE QKIPEATNRR VWELSKANSR FATTFYQHLA DSKNDNDNIF LSPLSISTAF AMTKLGACND TLQQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SKLVSANRLF GDKSLTFNET YQDISELVYG AKLQPLDFKE NAEQSRAAIN KWVSNKTEGR ITDVIPSEAI NELTVLVLVN TIYFKGLWKS KFSPENTRKE LFYKADGESC SASMMYQEGK FRYRRVAEGT QVLELPFKGD DITMVLILPK PEKSLAKVEK ELTPEVLQEW LDELEEMMLV VHMPRFRIED GFSLKEQLQD MGLVDLFSPE KSKLPGIVAE GRDDLYVSDA FHKAFLEVNE EGSEAAASTA VVIAGRSLNP NRVTFKANRP FLVFIREVPL NTIIFMGRVA NPCVK.

    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.

    Serpinc1 Human
  • View Data Sheet

    Name :

    ICAM1 Human HEK

    Description:

    Intercellular Adhesion Molecule-1 Human Recombinant HEK

    Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.

    Product # :

    PRO-1643

    Price :

    Quantity :

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    • description
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    Description

    ICAM1 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 461 amino acids (28-480). ICAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    ICAM1 was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues.
      ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH.
      Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions.

    • Synonyms

      Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ICAM1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ICAM1 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 ICAM1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQE
      DSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANL
      TVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAP
      YQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGN
      DSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEV
      TVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELR
      VLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYL
      CRARSTQGEVTRKVTVNVLSPRYEVDHHHHHH.

    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.

    Icam1 Human Hek
  • View Data Sheet

    Name :

    BMP8B Human

    Description:

    Bone Morphogenetic protein-8b Human Recombinant

    Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.

    Product # :

    CYT-830

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    • sds-page

    Description

    BMP8B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (264-402a.a.) and having a molecular mass of 18.1kDa.BMP8B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    BMP8B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    BMP8B-sds-page - Product image 1

    More Info

    • Introduction

      Bone Morphogenetic protein-8b (BMP8B) belongs to a family of secreted signaling molecules which can induce ectopic bone growth. BMP8B is known for having a possible bone inductive activity as it is related to BMP5 and BMP7. BMP8B is the osteoinductive factor accountable for epithelial osteogenesis.

    • Synonyms

      Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.

    • 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 MGSAVRPLRR RQPKKSNELP QANRLPGIFD DVHGSHGRQV CRRHELYVSF QDLGWLDWVI APQGYSAYYC EGECSFPLDS CMNATNHAIL QSLVHLMMPD AVPKACCAPT KLSATSVLYY DSSNNVILRK HRNMVVKACG CH.

    • Background

      Bone Morphogenetic Protein-8B Human Recombinant: Unveiling the Potential for Regenerative Medicine and Tissue Engineering

      Abstract:

      Bone Morphogenetic Protein-8B (BMP-8B) human recombinant is a key member of the bone morphogenetic protein family, renowned for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-8B, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-8B human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine and tissue engineering.

      Introduction:

      Regenerative medicine and tissue engineering offer promising solutions to address the challenges of tissue repair and regeneration. BMP-8B, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper delves into the distinctive features of BMP-8B and presents novel approaches for the production and optimization of BMP-8B human recombinant, aiming to unleash its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-8B is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, thereby initiating intricate intracellular signaling cascades. BMP-8B signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.

      Production of BMP-8B Human Recombinant:

      Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-8B human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-8B. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-8B recombinant protein.

      Potential Therapeutic Applications:

      BMP-8B human recombinant holds immense promise in the field of regenerative medicine and tissue engineering. Its involvement in bone and cartilage formation, muscle regeneration, and wound healing makes it a potential candidate for the treatment of skeletal disorders, muscle injuries, and chronic wounds. Furthermore, the ability of BMP-8B to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-8B human recombinant emerges as a crucial regulator in regenerative medicine and tissue engineering, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. Given its involvement in bone, cartilage, and muscle formation, as well as wound healing, BMP-8B human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.

      What is the molecular weight/Mw of BMP8B Protein?
      BMP8B Protein has a total Mw of 18.1kDa.

      What is the source or expression system of BMP8B Protein?
      Escherichia Coli.

      What is the Purity of BMP8B Protein?
      BMP8B Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP8B Protein?
      The biological functionality of BMP8B Protein will be determined in the future.

      What is the amino acid sequence of BMP8B Protein?
      MGSSHHHHHH SSGLVPRGSH MGSAVRPLRR RQPKKSNELP QANRLPGIFD DVHGSHGRQV CRRHELYVSF QDLGWLDWVI APQGYSAYYC EGECSFPLDS CMNATNHAIL QSLVHLMMPD AVPKACCAPT KLSATSVLYY DSSNNVILRK HRNMVVKACG CH.

      What applications can BMP8B Protein be used in?
      BMP8B Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP8B Protein?
      The endotoxin level is minimal, BMP8B 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.

    Bmp8B Human
  • View Data Sheet

    Name :

    FAIM Human

    Description:

    Fas Apoptotic Inhibitory Molecule Human Recombinant

    FAIM1, Fas Apoptotic Inhibitory Molecule, FAIM2, LFG, NMP35, Fas Apoptotic Inhibitory Molecule 1, FAIM.

    Product # :

    PRO-1742

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    Description

    FAIM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-213aa) and having a molecular mass of 26.4kDa.FAIM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FAIM protein solution (0.5 mg /ml) containing 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

      Fas apoptotic inhibitory molecule, also known as FAIM function as an inducible effector molecule which mediates Fas resistance produced by surface Ig engagement in B cells. In addition FAIM protects against death receptor-triggered apoptosis and regulates B-cell signaling and differentiation. Among the diseases associated with FAIM are hemorrhagic thrombocythemia, and food allergy.

    • Synonyms

      FAIM1, Fas Apoptotic Inhibitory Molecule, FAIM2, LFG, NMP35, Fas Apoptotic Inhibitory Molecule 1, FAIM.

    • 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 MGSMLLPFIR TLPLLCYNHL LVSPDSATLS PPYSLEKMTD LVAVWDVALS DGVHKIEFEH GTTSGKRVVY VDGKEEIRKE WMFKLVGKET FYVGAAKTKA TINIDAISGF AYEYTLEING KSLKKYMEDR SKTTNTWVLH MDGENFRIVL EKDAMDVWCN GKKLETAGEF VDDGTETHFS IGNHDCYIKA VSSGKRKEGI IHTLIVDNRE IPEIAS.

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    Faim Human
  • View Data Sheet

    Name :

    JAM2 Human

    Description:

    Junctional Adhesion Molecule 2 Human Recombinant

    Junctional adhesion molecule B, JAM-B, Junctional adhesion molecule 2, JAM-2, Vascular endothelial junction-associated molecule, VE-JAM, CD322.

    Product # :

    PRO-1336

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    Description

    JAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 241 amino acids (21-238) and having a molecular mass of 26.7kDa. JAM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    JAM2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Junctional Adhesion Molecule 2 (JAM2) is a member of the immunoglobulin superfamily, and the junctional adhesion molecule (JAM) family. JAM2 is a type I membrane protein which is localized at the tight junctions of both epithelial and endothelial cells. JAM2 functions as an adhesive ligand for interacting with various immune cell types, and may have a role in lymphocyte homing to secondary lymphoid organs.

    • Synonyms

      Junctional adhesion molecule B, JAM-B, Junctional adhesion molecule 2, JAM-2, Vascular endothelial junction-associated molecule, VE-JAM, CD322.

    • 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 MGSLGYHKAY GFSAPKDQQV VTAVEYQEAI LACKTPKKTV SSRLEWKKLG RSVSFVYYQQ TLQGDFKNRA EMIDFNIRIK NVTRSDAGKY RCEVSAPSEQ GQNLEEDTVT LEVLVAPAVP SCEVPSSALS GTVVELRCQD KEGNPAPEYT WFKDGIRLLE NPRLGSQSTN SSYTMNTKTG TLQFNTVSKL DTGEYSCEAR NSVGYRRCPG KRMQVDDLNI S.

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    Jam2 Human
  • View Data Sheet

    Name :

    LAIR1 Human

    Description:

    Leukocyte-Associated Ig-Like Receptor 1 Human Recombinant

    Leukocyte-associated immunoglobulin-like receptor 1, LAIR-1, hLAIR1, CD305 antigen, LAIR1, CD305.

    Product # :

    PRO-431

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    Description

    LAIR1 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 105 and having a molecular mass of 11.5 kDa. The extracellular domain of LAIR-1 (22-125aa) was overexpressed in E.coli, and purified by using conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris-HCl (pH7.5) 50mM NaCl and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      LAIR1 is a glycoprotein (~32kDa) expressed on the surface of the majority of human peripheral blood mononuclear leukocytes including T cells, B cells, NK cells, macrophages and dendritic cells. LAIR-1 functions as an inhibitory receptor in NK cells, T cells and B cells. Inhibitory receptors control the immune response to prevent lysis of cells recognized as self. Lair1 consists of a leader sequence, extracellular domain, transmembrane domain, cytoplasmic region.
      LAIR1 is a member of both the immunoglobulin superfamily and the leukocyte-associated inhibitory receptor family. LAIR1 maps to a region of 19q13.4 labeled the leukocyte receptor cluster, which contains at least 29 genes encoding leukocyte-expressed receptors of the immunoglobulin superfamily.

    • Synonyms

      Leukocyte-associated immunoglobulin-like receptor 1, LAIR-1, hLAIR1, CD305 antigen, LAIR1, CD305.

    • 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

      MQEEDLPRPS ISAEPGTVIP LGSHVTFVCR GPVGVQTFRL ERESRSTYND TEDVSQASPSESEARFRIDS VSEGNAGPYR CIYYKPPKWS EQSDYLELLV KETSG.

    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.

    Lair1 Human
  • View Data Sheet

    Name :

    UNC119B Human

    Description:

    UNC-119 Homolog B Human Recombinant

    Unc-119 homolog B (C. elegans), POC7B, POC7 centriolar protein homolog B, MGC5139.

    Product # :

    PRO-1034

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    Description

    UNC119B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-251) and having a molecular mass of 30.3kDa.UNC119B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The UNC119B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      UCN119B is a member of the PDE6D/unc-119 family. UCN119B has a large number of photoreceptors of the retina. Additionaly, UCN119B has a strong homology with the C. elegans unc119 and is able to functionally complement the C. elegans unc119 mutation gene.

    • Synonyms

      Unc-119 homolog B (C. elegans), POC7B, POC7 centriolar protein homolog B, MGC5139.

    • 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 MSGSNPKAAA AASAAGPGGL VAGKEEKKKA GGGVLNRLKA RRQAPHHAAD DGVGAAVTEQ ELLALDTIRP EHVLRLSRVT ENYLCKPEDN IYSIDFTRFK IRDLETGTVL FEIAKPCVSD QEEDEEEGGG DVDISAGRFV RYQFTPAFLR LRTVGATVEF TVGDKPVSNF RMIERHYFRE HLLKNFDFDF GFCIPSSRNT CEHIYEFPQL SEDVIRLMIE NPYETRSDSF YFVDNKLIMH NKADYAYNGG Q

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    Unc119B Human
  • View Data Sheet

    Name :

    CLEC2D Human

    Description:

    C-type Lectin Domain Family 2, Member D Human Recombinant

    C-type lectin domain family 2 member D, CLAX1, LLT11, OCIL.

    Product # :

    PRO-2650

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    Description

    CLEC2D Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (60-191 a.a.) and having a molecular mass of 17.7 kDa. CLEC2D is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CLEC2D solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C-type lectin domain family 2, also referred to CLEC2D, is a receptor for KLRB1 which protects target cells against natural killer cell-mediated lysis.It has been shown that CLEC2Dinhibits osteoclast formation and bone resorption. The protein controls the release of interferon-gamma and contains a transmembrane domain near the N-terminus likewisethe C-type lectin-like extracellular domain.

    • Synonyms

      C-type lectin domain family 2 member D, CLAX1, LLT11, OCIL.

    • 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 MGSRANCHQE PSVCLQAACP ESWIGFQRKC FYFSDDTKNW TSSQRFCDSQ DADLAQVESF QELNFLLRYK GPSDHWIGLS REQGQPWKWI NGTEWTRQFP ILGAGECAYL NDKGASSARH YTERKWICSK SDIHV

    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.

    Clec2D Human
  • View Data Sheet

    Name :

    MAP1LC3B Human

    Description:

    Microtubule-Associated Protein 1 Light Chain 3 Beta Human Recombinant

    Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    Product # :

    PRO-076

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    Description

    MAP1LC3B produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-120a.a.) and having a molecular mass of 16.2kDa.MAP1LC3B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAP1LC3B protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    1mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.

    • Synonyms

      Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    • 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 MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVYASQETFG

    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.

    Map1Lc3B Human
  • View Data Sheet

    Name :

    RARA Human

    Description:

    Retinoic Acid Receptor Alpha Human Recombinant

    Retinoic acid receptor alpha, RAR-alpha, Nuclear receptor subfamily 1 group B member 1,RAR, NR1B1, RARA.

    Product # :

    PRO-596

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    Description

    RARA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 127 amino acids (68-173 a.a.) and having a molecular mass of 14kDa (molecular weight on SDS-PAGE will appear higher). The RARA fused to a 21 amino acid his tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/1ml) contains 20mM Tris-HCl pH-7.5, 0.1M NaCl & 5mM b-mercaptoethanol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Retinoic acid receptor alpha (RAR) belongs to the large family of ligand responsive gene regulatory proteins that includes receptors for steroid and thyroid hormones. These proteins contain two highly conserved domains that are involved in determining their DNA and ligand-binding activities. There are three isotypes of RAR proteins: alpha, beta, and gamma. The RAR proteins are encoded by distinct genetic loci and possess distinct transcriptional properties. Typically, RAR-alpha represses target gene transcription in the absence of hormone, whereas RAR-beta and gamma fail to repress under these conditions. RARA is a receptor for retinoic acid that has profound effects on vertebrate development. Retinoic acid is a morphogen and is a powerful teratogen. RARA controls cell function by directly regulating gene expression.
      Chromosomal aberrations involving RARA cause acute promyelocytic leukemia (APL).

    • Synonyms

      Retinoic acid receptor alpha, RAR-alpha, Nuclear receptor subfamily 1 group B member 1,RAR, NR1B1, RARA.

    • 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 MSEEIVPSPP SPPPLPRIYK PCFVCQDKSS GYHYGVSACE GCKGFFRRSI QKNMVYTCHR DKNCIINKVT RNRCQYCRLQ KCFEVGMSKESVRNDRNKKK KEVPKPE.

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    Rar Alpha Human
  • View Data Sheet

    Name :

    sRAGE Human

    Description:

    Advanced Glycosylation End Product-Specific Receptor Human Recombinant

    Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.

    Product # :

    PRO-600

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    Description

    sRAGE Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 339 amino acids and having a molecular mass of 36.5 kDa. The Human sRAGE is fused to a 14 a.a. His tag at N-Terminus.The Human sRAGE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered (0.4 µm) concentrated (0.5mg/ml) protein solution was lyophilized with 30mM acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      sRAGE is a member of the immunoglobulin superfamily of cell surface molecules. sRAGE is a receptor for various molecules, including the amyloidogenic form of serum amyloid A, amyloid-beta protein, members of the S100/calgranulin superfamily and advanced glycation end products. sRAGE lies within the major histocompatibility complex (MHC) class III region on chromosome 6. Alternative splicing results in two transcript variants encoding different isoforms. sRAGE mediates interactions of nonenzymatic glycosylated proteins which accumulate in vascular tissue during aging & at an increasing rate in diabetes. sRAGE is a receptor for amyloid beta peptide.

    • Synonyms

      Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      Add 0.1M Acetate buffer pH4 to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MRGSHHHHHH GMASAQNITA RIGEPLVLKC KGAPKKPPQR LEWKLNTGRT EAWKVLSPQG GGPWDSVARV LPNGSLFLPAV GIQDEGIFRCQ AMNRNGKETKS NYRVRVYQIP GKPEIVDSASE LTAGVPNKVG TCVSEGSYPA GTLSWHLDGKPL VPNEKGVSVK EQTRRHPETG LFTLQSELMV TPARGGDPRP TFSCSFSPGL PRHRALRTAP IQPRVWEPVPL EEVQLVVEPE GGAVAPGGTV TLTCEVPAQP SPQIHWMKDGVP LPLPPSPVLI LPEIGPQDQG TYSCVATHSS HGPQESRAVS ISIIEPGEEG PTAGEGFDKV REAEDSPQHM

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    Srage Human
  • View Data Sheet

    Name :

    Fibronectin Recombinant, Oryza

    Description:

    Fibronectin, Oryza Human Recombinant

    Product # :

    PRO-2841

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    Description

    Fibronectin Human Recombinant is a single, non-glycosylated polypeptide chain having a molecular mass of 216kDa. The Fibronectin is purified by proprietary chromatographic techniques.

    Source

    Oryza sativa (rice).

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism mainly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

    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.

    Fibronectin Human Protein
  • View Data Sheet

    Name :

    RLN2 Human, Sf9

    Description:

    Relaxin-2 Human Recombinant, Sf9

    Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.

    Product # :

    PRO-2406

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    Description

    RLN2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (25-185a.a.) and having a molecular mass of 19.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).RLN2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RLN2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prorelaxin H2 (RLN2) is a member of the insulin gene superfamily. This family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing oxytocin and vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.

    • Synonyms

      Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.

    • 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

      ADPDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFCHHHHHH.

    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.

    Rln2 Human Sf9
  • View Data Sheet

    Name :

    S100A12 Human

    Description:

    S100 Calcium Binding Protein A12 Human Recombinant

    Extracellular newly identified RAGE-binding protein, Protein S100-A12, CGRP, Calcium-binding protein in amniotic fluid 1, CAAF1, Calgranulin-C, CAGC, EN-RAGE, Neutrophil S100 protein, S100 calcium-binding protein A12, p6, S100A12, MRP6, ENRAGE.

    Product # :

    PRO-152

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    Description

    The Recombinant Human S100A12 produced in E.coli has a molecular mass of 11.63kDa containing 101 amino acid residues of the human S100A12 and fused to a 10 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    S100A12 was filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    More Info

    • Introduction

      S100A12 belongs to the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 family members are localized in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A12 may be involved in specific calcium-dependent signal transduction pathways and its regulatory effect on cytoskeletal components may modulate various neutrophil activities.

    • Synonyms

      Extracellular newly identified RAGE-binding protein, Protein S100-A12, CGRP, Calcium-binding protein in amniotic fluid 1, CAAF1, Calgranulin-C, CAGC, EN-RAGE, Neutrophil S100 protein, S100 calcium-binding protein A12, p6, S100A12, MRP6, ENRAGE.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS TKLEEHLEGI VNIFHQYSVR KGHFDTLSKG ELKQLLTKEL ANTIKNIKDK AVIDEIFQGL DANQDEQVDFQEFISLVAIA LKAAHYHTHK E.

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    S100A12 Human
  • View Data Sheet

    Name :

    S100A3 Human

    Description:

    S100 Calcium Binding Protein A3 Human Recombinant

    S100-A3, S-100E, S100 calcium-binding protein A3, S100E, S-100A3, Protein S100-A3, Protein S-100E, S100A3.

    Product # :

    PRO-755

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    Description

    S100A3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.9kDa.The S100A3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A3 protein at 1mg/ml in 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.2M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.

    • Synonyms

      S100-A3, S-100E, S100 calcium-binding protein A3, S100E, S-100A3, Protein S100-A3, Protein S-100E, S100A3.

    • 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 prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MARPLEQAVA AIVCTFQEYA GRCGDKYKLC QAELKELLQK ELATWTPTEF RECDYNKFMS VLDTNKDCEV DFVEYVRSLA CLCLYCHEYF KDCPSEPPCS 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.

    S100A3 Human
  • View Data Sheet

    Name :

    DCUN1D4 Human

    Description:

    DCN1 Defective in Cullin Neddylation 1 Domain Containing 4 Human Recombinant

    DCN1 Defective In Cullin Neddylation 1 Domain Containing 4, Defective In Cullin Neddylation Protein 1-Like Protein 4, DCUN1 Domain-Containing Protein 4, KIAA0276, DCN1-Like Protein 4.

    Product # :

    PRO-1715

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    Description

    DCUN1D4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 36.5kDa.DCUN1D4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DCUN1D4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DCUN1D4 holds 1 DCUN1 domain.

    • Synonyms

      DCN1 Defective In Cullin Neddylation 1 Domain Containing 4, Defective In Cullin Neddylation Protein 1-Like Protein 4, DCUN1 Domain-Containing Protein 4, KIAA0276, DCN1-Like Protein 4.

    • 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 MGSMHSDAAA VNFQLNSHLS TLANIHKIYH TLNKLNLTED IGQDDHQTGS LRSCSSSDCF NKVMPPRKKR RPASGDDLSA KKSRHDSMYR KYDSTRIKTE EEAFSSKRCL EWFYEYAGTD DVVGPEGMEK FCEDIGVEPE NVVMLVLAWK LDAQNMGYFT LQEWLKGMTS LQCDTTEKLR NTLDYLRSFL NDSTNFKLIY RYAFDFAREK DQRSLDINTA KCMLGLLLGK IWPLFPVFHQ FLEQSKYKVI NKDQWCNVLE FSRTINLDLS NYDEDGAWPV LLDEFVEWYK DKQMS

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    Dcun1D4 Human
  • View Data Sheet

    Name :

    DRG1 Human

    Description:

    Developmentally Regulated GTP Binding Protein 1 Human Recombinant

    Developmentally-regulated GTP-binding protein 1, DRG-1, Neural precursor cell expressed developmentally down-regulated protein 3, NEDD-3, DRG1, NEDD3.

    Product # :

    PRO-885

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    Description

    DRG1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 42.7kDa.DRG1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DRG1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 1mM EDTA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Developmentally-regulated GTP-binding protein 1 (DRG1) is a member of the GTP1/OBG family. DRG1 has a role in cell proliferation and differentiation, as well as in apoptosis, proposing a role in tumor formation and metastasis. Expression of the DRG1 was considerably reduced in breast tumor cells, particularly in patients with lymph node or bone metastasis as compared to those with localized breast cancer. The DRG1 protein is expressed at high levels in the heart, kidney and skeletal muscle and at lower levels in the brain, liver, placenta, lung, colon and spleen.

    • Synonyms

      Developmentally-regulated GTP-binding protein 1, DRG-1, Neural precursor cell expressed developmentally down-regulated protein 3, NEDD-3, DRG1, NEDD3.

    • 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 MSSTLAKIAE IEAEMARTQK NKATAHHLGL LKARLAKLRR ELITPKGGGG GGPGEGFDVA KTGDARIGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGVIRYKG AKIQLLDLPG IIEGAKDGKG RGRQVIAVAR TCNLILIVLD VLKPLGHKKI IENELEGFGI RLNSKPPNIG FKKKDKGGIN LTATCPQSEL DAETVKSILA EYKIHNADVT LRSDATADDL IDVVEGNRVY IPCIYVLNKI DQISIEELDI IYKVPHCVPI SAHHRWNFDD LLEKIWDYLK LVRIYTKPKG QLPDYTSPVV LPYSRTTVED FCMKIHKNLI KEFKYALVWG LSVKHNPQKV GKDHTLEDED VIQIVKK.

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    Drg1 Human
  • View Data Sheet

    Name :

    ARL9 Human

    Description:

    ADP-Ribosylation Factor-Like 9 Human Recombinant

    ADP-ribosylation factor-like protein 9, ARL9.

    Product # :

    PRO-1009

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    Description

    ARL9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (1-123 a.a.) and having a molecular mass of 15.9kDa. ARL9 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARL9 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-ribosylation factor-like protein 9 (ARL9) is a member of to 2 novel subfamilies coding for small GTPases that were found to be highly conserved among eukaryotes.

    • Synonyms

      ADP-ribosylation factor-like protein 9, ARL9.

    • 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 MEFLEIGGSK PFRSYWEMYL SKGLLLIFVV DSADHSRLPE AKKYLHQLIA ANPVLPLVVF ANKQDLEAAY HITDIHEALA LSEVGNDRKM FLFGTYLTKN GSEIPSTMQD AKDLIAQLAA DVQ.

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    Arl9 Human
  • View Data Sheet

    Name :

    IF Human

    Description:

    Intrinsic Factor Human Recombinant

    Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.

    Product # :

    PRO-375

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    Description

    Intrinsic Factor Human Recombinant produced in baculovirus is a glycosylated, polypeptide chain having a molecular mass of 55,000 Dalton. The Intrinsic Factor is fused to a hexa-histidine at the C-terminus and purified by proprietary chromatographic techniques for removal of bound Vitamin B-12.

    Source

    Sf9 Insect Cells.

    Formulation

    The protein solution contains 20mM HEPES pH-8.0, 100mM NaCl and 20% Glycerol.

    Purity

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

    More Info

    • Introduction

      Intrinsic Factor is a member of the cobalamin transport protein family. It encodes a glycoprotein secreted by parietal cells of the gastric mucosa and is required for adequate absorption of vitamin B12 in the terminal ileum. Vitamin B12 is essential for erythrocyte maturation and mutations in the Intrinsic Factor may lead to congenital pernicious anemia. Upon entry into the stomach, vitamin B12 binds to one of two B12 binding proteins present in the gastric fluid. In the less acidic environment of the small intestine, these proteins dissociate from the vitamin, allowing it to bind to intrinsic factor and enter the portal circulation through a receptor in the ileal mucosa specific for the B12-intrinsic factor complex.

    • Synonyms

      Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.

    • Physical Appearance

      Sterile Filtered pink 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.

    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.

    Intrinsic Factor Human
  • View Data Sheet

    Name :

    ATP1B3 Human

    Description:

    ATPaseTransporting Beta 3 Human Recombinant

    ATPase Na+/K+ Transporting Beta 3 Polypeptide, Sodium-Potassium ATPase Subunit Beta 3 (Non-Catalytic), Sodium/Potassium-Transporting ATPase Subunit Beta-3, Sodium/Potassium-Dependent ATPase Subunit Beta-3, Sodium Pump Subunit Beta-3, ATPB-3, Sodium/Potassium-Transporting ATPase Beta-3 Chain, Sodium/Potassium-Dependent ATPase Beta-3 Subunit, Na K-ATPase Beta-3 Polypeptide, CD298 Antigen, CD298, ATP1B3.

    Product # :

    PRO-1962

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    Description

    ATP1B3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (57-279) and having a molecular mass of 27.4 kDa.ATP1B3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ATP1B3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ATPaseTransporting Beta 3 (ATP1B3) is a member of the X(+)/potassium ATPases subunit beta family. ATP1B3 is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The beta subunit controls, by way of assembly of alpha/beta heterodimers, the quantity of sodium pumps transported to the plasma membrane. The precise role of the beta-3 subunit is unknown.

    • Synonyms

      ATPase Na+/K+ Transporting Beta 3 Polypeptide, Sodium-Potassium ATPase Subunit Beta 3 (Non-Catalytic), Sodium/Potassium-Transporting ATPase Subunit Beta-3, Sodium/Potassium-Dependent ATPase Subunit Beta-3, Sodium Pump Subunit Beta-3, ATPB-3, Sodium/Potassium-Transporting ATPase Beta-3 Chain, Sodium/Potassium-Dependent ATPase Beta-3 Subunit, Na K-ATPase Beta-3 Polypeptide, CD298 Antigen, CD298, ATP1B3.

    • 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 MGSTMWVMLQ TLNDEVPKYR DQIPSPGLMV FPKPVTALEY TFSRSDPTSY AGYIEDLKKF LKPYTLEEQK NLTVCPDGAL FEQKGPVYVA CQFPISLLQA CSGMNDPDFG YSQGNPCILV KMNRIIGLKP EGVPRIDCVS KNEDIPNVAV YPHNGMIDLK YFPYYGKKLH VGYLQPLVAV QVSFAPNNTG KEVTVECKID GSANLKSQDD RDKFLGRVMF KITARA.

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    Atp1B3 Human
  • View Data Sheet

    Name :

    EFNA1 Human, HEK

    Description:

    Ephrin A1 Human Recombinant, HEK

    Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    Product # :

    PRO-2477

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    Description

    EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    EFNA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline, pH 7.5 containing 5 % (w/v) trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.

    • Synonyms

      Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. EFNA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      DRHTVFWNSS NPKFRNEDYT IHVQLNDYVD IICPHYEDHS VADAAMEQYI LYLVEHEEYQ LCQPQSKDQV RWQCNRPSAK HGPEKLSEKF QRFTPFTLGK EFKEGHSYYY ISKPIHQHED RCLRLKVTVS GKITHSPQAH DNPQEKRLAA DDPEVRVLHS IGHS HHHHHH.

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    Efna1 Protein
  • View Data Sheet

    Name :

    STYX Human

    Description:

    Serine/Threonine/Tyrosine Interacting Protein Human Recombinant

    Serine/threonine/tyrosine-interacting protein, Protein tyrosine phosphatase-like protein, STYX, FLJ42934.

    Product # :

    ENZ-585

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    Description

    STYX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (1-223) and having a molecular mass of 28kDa.STYX is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The STYX solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 1mM DTT and 0.1M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serine/threonine/tyrosine-interacting protein (STYX) is a member of the protein-tyrosine phosphatase family. STYX contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which makes it catalytically inactive as a phosphatase. On the other hand, the binding pocket is adequately preserved to bind phosphorylated substrates, and may protect them from phosphatases. STYX may have a role in spermiogenesis. STYX is a possible pseudophosphatase.

    • Synonyms

      Serine/threonine/tyrosine-interacting protein, Protein tyrosine phosphatase-like protein, STYX, FLJ42934.

    • 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 MGSHMEDVKL EFPSLPQCKE DAEEWTYPMR REMQEILPGL FLGPYSSAMK SKLPVLQKHG ITHIICIRQN IEANFIKPNF QQLFRYLVLD IADNPVENII RFFPMTKEFI DGSLQMGGKV LVHGNAGISR SAAFVIAYIM ETFGMKYRDA FAYVQERRFC
      INPNAGFVHQ LQEYEAIYLA KLTIQMMSPL QIERSLSVHS GTTGSLKRTH EEEDDFGTMQ VATAQNG.

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    Styx Human
  • View Data Sheet

    Name :

    ESM1 Human, HEK

    Description:

    Endothelial Cell-Specific Molecule 1 Human Recombinant, HEK

    Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan. 

    Product # :

    PRO-2476

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    • More Info

    Description

    ESM1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-184) containing 175 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 19.5kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    ESM1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Endothelial cell-specific molecule 1 (ESM1) is a proteoglycan secreted by endothelial cells (mostly in the human lung and kidney tissues) and its mRNA expression is regulated by inflammatory cytokines. ESM1 has potent implications in lung endothelial cell-leukocyte interactions. In addition, ESM1 expression is detected in various epithelia and in adipocytes. ESM1 is involved in angiogenesis and it also promotes angiogenic sprouting. ESM1 expression is upregulated by TNF alpha, IL1 beta, or lipopolysaccharide and downregulated by IFN gamma. Genetically engineered cells overexpressing ESM1 induce tumor formation, implying that ESM1 might be involved in the pathophysiology of tumor growth in vivo.

    • Synonyms

      Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. ESM1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      WSNNYAVDCP QHCDSSECKS SPRCKRTVLD DCGCCRVCAA GRGETCYRTV SGMDGMKCGP GLRCQPSNGE DPFGEEFGIC KDCPYGTFGM DCRETCNCQS GICDRGTGKC LKFPFFQYSV TKSSNRFVSL TEHDMASGDG NIVREEVVKE NAAGSPVMRK WLNPR HHHHH 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.

    Esm1 Protein
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