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Search results

1000 results found for “lin protein”

Name

Description

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  • View Data Sheet

    Name :

    CXCL16 Human

    Description:

    CXCL16 Human Recombinant

    Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.

    Product # :

    CHM-029

    Price :

    Quantity :

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    • source
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    Description

    CXCL16 Human Recombinant (30-118 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids and having a molecular mass of 10kDa.The CXCL16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL16 protein was lyophilized from a 0.2µm filtered solution in PBS.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.

    More Info

    • Introduction

      CXC chemokine ligand 16 (CXCL16) is a type I membrane protein, which contains a non-ELR motif-containing CXC chemokine domain in its extracellular region. Human and Mouse CXCL16 share a 70% a.a. sequence similarity within their chemokine domains and 49% overall a.a. sequence identity. Functional CXCL16 can be dropped from the cell surface as an approximately 35kDa soluble protein. CXCR6 is the functional receptor for CXCL16. CXCL16 functions as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), proposing that CXCL16 may be involved in pathophysiology such as atherogenesis. In addition, CXCL16 induces a strong chemotactic response and calcium mobilization. CXCL16 binds to CXCR6/Bonzo.

    • Synonyms

      Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL16 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 CXCL16 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.

    • Background

      What is the molecular weight/Mw of CXCL16 HUMAN Protein?
      CXCL16 HUMAN Protein has a total Mw of 10kDa.

      What is the source or expression system of CXCL16 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL16 HUMAN Protein?
      CXCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL16 HUMAN Protein?
      The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.

      What is the amino acid sequence of CXCL16 HUMAN Protein?
      NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.

      What applications can CXCL16 HUMAN Protein be used in?
      CXCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL16 HUMAN Protein?
      The endotoxin level is minimal, CXCL16 HUMAN 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.

    Cxcl16 Human
  • View Data Sheet

    Name :

    FABP9 Human

    Description:

    Fatty Acid Binding Protein-9 Human Recombinant

    Fatty acid-binding protein 9, Testis lipid-binding protein, TLBP, Testis-type fatty acid-binding protein, T-FABP, FABP9, PERF, PERF15.

    Product # :

    PRO-1088

    Price :

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    • More Info

    Description

    FABP9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-132 a.a) and having a molecular mass of 17.6kDa.FABP9 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fatty acid binding protein 9 (FABP9) belongs to the fatty acid-binding proteins (FABPs) which are a family of small, extremely conserved, cytoplasmic proteins to bind long-chain fatty acids and other hydrophobic ligands. FABP9 is found in midpachytene spermatocytes and round spermatids, and comprises part of the perinuclear theca. FABP9 probably links intracellular membranes and signals abnormal sperm formation during spermatogenesis.

    • Synonyms

      Fatty acid-binding protein 9, Testis lipid-binding protein, TLBP, Testis-type fatty acid-binding protein, T-FABP, FABP9, PERF, PERF15.

    • 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 MGSHMVEPFL GTWKLVSSEN FEDYMKELGV NFAARNMAGL VKPTVTISVD GKMMTIRTES SFQDTKISFK LGEEFDETTA DNRKVKSTIT LENGSMIHVQ KWLGKETTIK RKIVDEKMVV ECKMNNIVST RIYEKV.

    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.

    Fabp9 Human
  • View Data Sheet

    Name :

    TCEA2 Human

    Description:

    Transcription Elongation Factor A (SII)-2 Human Recombinant

    Transcription elongation factor A protein 2, Testis-specific S-II, Transcription elongation factor S-II protein 2, Transcription elongation factor TFIIS.l, TCEA2, TFIIS, Transcription Elongation Factor A (SII) 2.

    Product # :

    PRO-1489

    Price :

    Quantity :

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    Description

    TCEA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a) and having a molecular mass of 36kDa.TCEA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TCEA2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.25M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription Elongation Factor A (SII)- 2 (TCEA2) is located in the nucleus, where it serves as an SII class transcription elongation factor. Elongation factors in this class are responsible for discharging RNA polymerase II ternary complexes from transcriptional arrest at template-encoded arresting sites. TCEA2 interacts with general transcription factor IIB, a basal transcription factor.

    • Synonyms

      Transcription elongation factor A protein 2, Testis-specific S-II, Transcription elongation factor S-II protein 2, Transcription elongation factor TFIIS.l, TCEA2, TFIIS, Transcription Elongation Factor A (SII) 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

      MGSSHHHHHH SSGLVPRGSH MGSMMGKEEE IARIARRLDK MVTKKSAEGA MDLLRELKAM PITLHLLQST RVGMSVNALR KQSSDEEVIA LAKSLIKSWK KLLDASDAKA RERGRGMPLP TSSRDASEAP DPSRKRPELP RAPSTPRITT FPPVPVTCDA VRNKCREMLT AALQTDHDHV AIGADCERLS AQIEECIFRD VGNTDMKYKN RVRSRISNLK DAKNPDLRRN VLCGAITPQQ IAVMTSEEMA SDELKEIRKA MTKEAIREHQ MARTGGTQTD LFTCGKCRKK NCTYTQVQTR SSDEPMTTFV VCNECGNRWK FC.

    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.

    Tcea2 Human
  • View Data Sheet

    Name :

    EDF1 Human

    Description:

    Endothelial Differentiation-Related Factor 1 Human Recombinant

    EDF-1, MBF1, Multiprotein-bridging factor 1.

    Product # :

    PRO-494

    Price :

    Quantity :

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    Description

    EDF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-148 a.a.) and having a molecular mass of 17.4 kDa. The EDF1 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5 mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EDF1 controls endothelial cell differentiation. EDF1 has a role as a bridging protein that interconnects regulatory proteins and the basal transcriptional machinery, thus modulating the transcription of genes that take part in endothelial differentiation. EDF1 binds calmodulin through its IQ domain and controls nitric oxide synthase activity via calmodulin sequestration in the cytoplasm. EDF1 is localized in adult liver, heart, adipose tissues, intestine and pancreas.

    • Synonyms

      EDF-1, MBF1, Multiprotein-bridging factor 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV LGKIERAIGL KLRGKDIGKP IEKGPRAKLE HHHHHH.

    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.

    Edf1 Human
  • View Data Sheet

    Name :

    EFNB3 Human

    Description:

    Ephrin- B3 Human Recombinant

    Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.

    Product # :

    PRO-1169

    Price :

    Quantity :

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    Description

    EFNB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-226 a.a) and having a molecular mass of 24.6kDa.EFNB3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    EFNB3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.

    • Synonyms

      Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.

    • 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 MGSHMLSLEP VYWNSANKRF QAEGGYVLYP QIGDRLDLLC PRARPPGPHS SPNYEFYKLY LVGGAQGRRC EAPPAPNLLL TCDRPDLDLR FTIKFQEYSP NLWGHEFRSH HDYYIIATSD GTREGLESLQ GGVCLTRGMK VLLRVGQSPR GGAVPRKPVS EMPMERDRGA AHSLEPGKEN LPGDPTSNAT SRGAEGPLPP PSMP.

    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.

    Efnb3 Human
  • View Data Sheet

    Name :

    RAET1E Human

    Description:

    Retinoic Acid Early Transcript 1E Human Recombinant

    bA350J20.7, LETAL, N2DL-4, NKG2DL4, RAET1E2, RL-4, ULBP4, NKG2D ligand 4, Retinoic acid early transcript 1E, RAE-1-like transcript 4, Lymphocyte effector toxicity activation ligand, UNQ1867/PRO4303.

    Product # :

    PRO-1293

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    Description

    RAET1E Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (31-225 a.a.) and having a molecular mass of 24.9kDa.RAET1E is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RAET1E protein solution (1mg/ml) contains 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

      RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

    • Synonyms

      bA350J20.7, LETAL, N2DL-4, NKG2DL4, RAET1E2, RL-4, ULBP4, NKG2D ligand 4, Retinoic acid early transcript 1E, RAE-1-like transcript 4, Lymphocyte effector toxicity activation ligand, UNQ1867/PRO4303.

    • 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 MGSMHSLCFN FTIKSLSRPG QPWCEAQVFL NKNLFLQYNS DNNMVKPLGL LGKKVYATST WGELTQTLGE VGRDLRMLLC DIKPQIKTSD PSTLQVEMFC QREAERCTGA SWQFATNGEK SLLFDAMNMT WTVINHEASK IKETWKKDRG LEKYFRKLSK GDCDHWLREF LGHWEAMPEP TVSPVNASDI HWSSSSLPD.

    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.

    Raet1E Human
  • View Data Sheet

    Name :

    CCL9 Mouse

    Description:

    Macrophage Inflammatory Protein-1 Gamma Mouse Recombinant (CCL9)

    CCL9/10, MRP2, CCF18.

    Product # :

    CHM-257

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    Description

    MIP-1 gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 101 amino acids and having a molecular mass of 11.6 kDa. The MIP-1 gamma is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MIP-1 gamma was lyophilized from 1xPBS solution pH-7.4.

    Purity

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

    Biological Activity

    Defined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml, corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Mouse MIP-1 gamma is 75% identical in its amino acid compostion as compared to the rat specie. MIP-1 gamma is a CC chemokine localized in murine blood and a widespread range of murine tissues, without having an identified human homolog. MIP-1 gamma signals through the CCR1 receptor. MIP-1 gamma chemoattracts neutrophils and also inhibits colony formation of bone marrow myeloid immature progenitors. MIP-1 gamma has six cysteines including the four highly conserved cysteine residues present in CC chemokines.

    • Synonyms

      CCL9/10, MRP2, CCF18.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-1 gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL9/10 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 MIP-1 gamma in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QITHATETKE VQSSLKAQQG LEIEMFHMGF QDSSDCCLSY NSRIQCSRFI GYFPTSGGCT RPGIIFISKR GFQVCANPSD RRVQRCIERL EQNSQPRTYK Q.

    • Background

      What is the molecular weight/Mw of CCL9 MOUSE Protein?
      CCL9 MOUSE Protein has a total Mw of 11.6kDa.

      What is the source or expression system of CCL9 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL9 MOUSE Protein?
      CCL9 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL9 MOUSE Protein?
      Defined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml, corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL9 MOUSE Protein?
      QITHATETKE VQSSLKAQQG LEIEMFHMGF QDSSDCCLSY NSRIQCSRFI GYFPTSGGCT RPGIIFISKR GFQVCANPSD RRVQRCIERL EQNSQPRTYK Q.

      What applications can CCL9 MOUSE Protein be used in?
      CCL9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL9 MOUSE Protein?
      The endotoxin level is minimal, CCL9 MOUSE 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.

    Mip 1 Gamma Mouse
  • 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.

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    • 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 :

    TNNI3 Human, (1-210)

    Description:

    Cardiac Troponin-I Human Recombinant (1-210 a.a.)

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    Product # :

    PRO-2591

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    Description

    TNNI3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 26.4 kDa.TNNI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNNI3 protein solution (0.25mg/ml) contains 30% glycerol, 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl, 0.1mMPMSF & 1mM DTT.

    Purity

    Greater than 90.0% as determined by both SDS-PAGE.

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    • Introduction

      Troponin I (TnI), troponin T (TnT) and troponin C (TnC) form the troponin complex of the thin filaments of striated muscle. TnI acts as the inhibitory subunit by blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains 3 genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. The TNNI3 gene encodes the TnI-cardiac protein and isexpressed solely in cardiac muscle tissues. Mutations in the TNNI3 gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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 MGSMADGSSD AAREPRPAPA PIRRRSSNYR AYATEPHAKK KSKISASRKL QLKTLLLQIA KQELEREAEERRGEKGRALS TRCQPLELAG LGFAELQDLC RQLHARVDKV DEERYDIEAK VTKNITEIAD LTQKIFDLRG KFKRPTLRRV RISADAMMQALLGARAKESL DLRAHLKQVK KEDTEKENRE VGDWRKNIDA LSGMEGRKKK FES

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    Cardiac Troponin I
  • View Data Sheet

    Name :

    Collagen-V Bovine

    Description:

    Bovine Collagen-V

    Product # :

    PRO-2677

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    Description

    Bovine Collagen-V is a natural protein purified from bovine placenta. Collagen-V is purified by proprietary chromatographic techniques.

    Source

    Bovine placenta.

    Formulation

    Collagen-V was lyophilized without additives.

    Purity

    > 98.0%.

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    • Introduction

      Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Collagen-V in 20 mM acetic acid not less than 1mg/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.

    Collagen V Bovine
  • View Data Sheet

    Name :

    CEND1 Human

    Description:

    Cell Cycle Exit And Neuronal Differentiation 1 Human Recombinant

    Cell Cycle Exit And Neuronal Differentiation 1, BM88, BM88 Antigen, Cell Cycle Exit And Neuronal Differentiation Protein 1.

    Product # :

    PRO-1823

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    Description

    CEND1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (1-125 a.a) and having a molecular mass of 15.0kDa (molecular size on SDS-PAGE will appear higher).CEND1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CEND1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Cell Cycle Exit And Neuronal Differentiation 1, also known as CEND1, is a neuron-specific protein. CEND1 take part in cell cycle control and neuronal differentiation mechanisms during neonatal SVZ neurogenesis and turn out to be crucial for the transition from neuroblasts to mature neurons when reaching high levels. The similar protein in pig enhances neuroblastoma cell differentiation in vitro and involved in neuronal differentiation in vivo. Multiple pseudogenes have been reported for this gene. The disease neuroblastoma has been associated with CEND1.

    • Synonyms

      Cell Cycle Exit And Neuronal Differentiation 1, BM88, BM88 Antigen, Cell Cycle Exit And Neuronal Differentiation Protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMESRGKS ASSPKPDTKV PQVTTEAKVP PAADGKAPLT KPSKKEAPAE KQQPPAAPTT APAKKTSAKA DPALLNNHSN LKPAPTVPSS PDATPEPKGP GDGAEEDEAA SGGPGGRGPW SCENFNPL

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    Cend1 Human
  • View Data Sheet

    Name :

    MXD3 Human

    Description:

    MAX Dimerization Protein 3 Human Recombinant

    BHLHC13, MAD3, MYX, Max dimerization protein 3, Max dimerizer 3, Class C basic helix-loop-helix protein 13, bHLHc13, Max-associated protein 3, Max-interacting transcriptional repressor MAD3, MXD3 Human, MXD3.

    Product # :

    PRO-1356

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    Description

    MXD3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-206) and having a molecular mass of 25.9 kDa. MXD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MXD3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      MAX Dimerization Protein 3 (MXD3) belongs to the Myc superfamily of basic helix-loop-helix leucine zipper transcriptional regulators. MXD3 forms a heterodimer with the cofactor MAX that connects specific E-box DNA motifs in the promoters of target genes and regulates their transcription. Disturbance of the MAX-MXD3 complex is correlated with uncontrolled cell proliferation and tumorigenesis. Transcript variants of MXD3 encoding different isoforms have been described.

    • Synonyms

      BHLHC13, MAD3, MYX, Max dimerization protein 3, Max dimerizer 3, Class C basic helix-loop-helix protein 13, bHLHc13, Max-associated protein 3, Max-interacting transcriptional repressor MAD3, MXD3 Human, MXD3.

    • 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 MGSMEPLASN IQVLLQAAEF LERREREAEH GYASLCPHRS PGPIHRRKKR PPQAPGAQDS GRSVHNELEK RRRAQLKRCL ERLKQQMPLG ADCARYTTLS LLRRARMHIQ KLEDQEQRAR QLKERLRSKQ QSLQRQLEQL RGLAGAAERE RLRADSLDSS GLSSERSDSD QEELEVDVES LVFGGEAELL RGFVAGQEHS YSHGGGAWL.

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    Mxd3 Human
  • View Data Sheet

    Name :

    SPARC Human, Sf9

    Description:

    Secreted Protein Acidic & Rich in Cysteine Human Recombinant, Sf9

    SPARC, Basement-membrane protein 40, BM-40, Osteonectin, ON, Secreted protein acidic and rich in cysteine, OI17.

    Product # :

    PRO-2623

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    Description

    SPARC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 295 amino acids (18-303 a.a) and having a molecular mass of 33.8kDa.SPARC is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SPARC protein, or secreted protein acidic and rich in cysteine, or osteonectin or basement-membrane protein 40 is a protein that is coded by the SPARC gene in humans. It is a glycoprotein located in bones, that binds to calcium. The osteonectin is secreted from osteoblasts cells when boas are formed, mineralized and promotes the formation and creation of mineral crystals. Asides from calcium, it has been shown that this protein can also bind to collagen.

    • Synonyms

      SPARC, Basement-membrane protein 40, BM-40, Osteonectin, ON, Secreted protein acidic and rich in cysteine, OI17.

    • 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

      ADPAPQQEAL PDETEVVEET VAEVTEVSVG ANPVQVEVGE FDDGAEETEE EVVAENPCQN
      HHCKHGKVCE LDENNTPMCV CQDPTSCPAP IGEFEKVCSN DNKTFDSSCH FFATKCTLEG
      TKKGHKLHLD YIGPCKYIPP CLDSELTEFP LRMRDWLKNV LVTLYERDED NNLLTEKQKL
      RVKKIHENEK RLEAGDHPVE LLARDFEKNY NMYIFPVHWQ FGQLDQHPID GYLSHTELAP
      LRAPLIPMEH CTTRFFETCD LDNDKYIALD EWAGCFGIKQ KDIDKDLVIH HHHHH

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    Sparc Human
  • View Data Sheet

    Name :

    NPM2 Human

    Description:

    Nucleophosmin 2 Human Recombinant

    Nucleophosmin/nucleoplasmin 2, nucleoplasmin-2.

    Product # :

    PRO-1182

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    Description

    NPM2 Human Recombinant produced in E. coli is a single polypeptide chain containing 237 amino acids (1-214) and having a molecular mass of 26.6 kDa.NPM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NPM2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      NPM2 is a member of nucleoplasmin family. NPM2 is a core histones chaperone which takes part in chromatin reprogramming, particularly throughout fertilization and early embryonic development. NPM2 also takes part in sperm DNA decondensation during fertilization.

    • Synonyms

      Nucleophosmin/nucleoplasmin 2, nucleoplasmin-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

      MGSSHHHHHH SSGLVPRGSH MGSMNLSSAS STEEKAVTTV LWGCELSQER RTWTFRPQLE GKQSCRLLLH TICLGEKAKE EMHRVEILPP ANQEDKKMQP VTIASLQASV LPMVSMVGVQ LSPPVTFQLR AGSGPVFLSG QERYEASDLT WEEEEEEEGE EEEEEEEDDE DEDADISLEE
      QSPVKQVKRL VPQKQASVAK KKKLEKEEEE IRASVRDKSP VKKAKATARA KKPGFKK

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    Npm2 Human
  • View Data Sheet

    Name :

    ICAM3 Human

    Description:

    Intercellular Adhesion Molecule-3 Human Recombinant

    ICAM3, Intercellular adhesion molecule 3, ICAM-3, CD50, CDW50, ICAM-R, intercellular adhesion molecule 3 isoform 1

    Product # :

    PRO-2637

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    Description

    ICAM3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 698 amino acids (30-485 a.a) and having a molecular mass of 76.7kDa.ICAM3 is fused to a 242 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The ICAM3 solution (0.25mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by the ability of the immobilized protein to support the adhesion of HL-60 human promyelocytic cells.  When cells are added to Human ICAM-3/CD50 coated plates, the ED50 range ≤4ug/ml.

    More Info

    • Introduction

      ICAM-3/CD50, or CD50 or Cluster of Differentiation 50 is a protein, part of the intercellular adhesion molecule superfamily. every ICAM peptides are type I transmembrane glycoproteins, bind to leukocyte adhesion LFA-1 & has 2-9 immunoglobulinlike C2-type domains. ICAM-3/CD50 can be found in every leukocyte and acts as a crucial ligand for LFA-1 in the start of the immune system response. ICAM-3/CD50 acts as an adhesion molecule and is also a potent signaling protein.

    • Synonyms

      ICAM3, Intercellular adhesion molecule 3, ICAM-3, CD50, CDW50, ICAM-R, intercellular adhesion molecule 3 isoform 1

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADLQEFLLRV EPQNPVLSAG GSLFVNCSTD CPSSEKIALE TSLSKELVAS GMGWAAFNLS NVTGNSRILC SVYCNGSQIT GSSNITVYRL PERVELAPLP PWQPVGQNFT LRCQVEDGSP RTSLTVVLLR WEEELSRQPA VEEPAEVTAT VLASRDDHGA PFSCRTELDM QPQGLGLFVN TSAPRQLRTF VLPVTPPRLV APRFLEVETS WPVDCTLDGL FPASEAQVYL ALGDQMLNAT VMNHGDTLTA TATATARADQ EGAREIVCNV TLGGERREAR ENLTVFSFLG PIVNLSEPTA HEGSTVTVSC MAGARVQVTL DGVPAAAPGQ PAQLQLNATE SDDGRSFFCS ATLEVDGEFL HRNSSVQLRV LYGPKIDRAT CPQHLKWKDK TRHVLQCQAR GNPYPELRCL KEGSSREVPV GIPFFVNVTH NGTYQCQASS SRGKYTLVVV MDIEAGSSHV EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH

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    Icam3 Human
  • View Data Sheet

    Name :

    EGF Mouse, Biotin

    Description:

    Epidermal Growth Factor Mouse Recombinant, Biotin

    Urogastrone, URG, EGF.

    Product # :

    CYT-841

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    Description

    EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.

    Source

    Escherichia Coli.

    Formulation

    The protein (0.5mg/ml) solution contains sterile PBS.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

    More Info

    • Introduction

      Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Should be stored at 4°C.Please do not freeze.

    • Amino Acid Sequence

      MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

    • Background

      Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential

      Abstract:

      This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.

      Introduction:

      Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.

      Protein Engineering and Biotin Conjugation:

      EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.

      Cellular Signaling Amplification:

      The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.

      Cellular Assays and Functional Responses:

      In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.

      Tailored Delivery Strategies:

      The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.

      Regenerative Medicine and Targeted Therapy:

      The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.

      Future Prospects and Challenges:

      While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.

      Conclusion:

      In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.

      What is the molecular weight/Mw of MEGF, BIOTIN Protein?
      MEGF, BIOTIN Protein has a total Mw of 7kDa.

      What is the source or expression system of MEGF, BIOTIN Protein?
      Escherichia Coli.

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

      What is the Biological Activity of MEGF, BIOTIN Protein?
      The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

      What is the amino acid sequence of MEGF, BIOTIN Protein?
      MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

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

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

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    Egf Mouse Biotin
  • View Data Sheet

    Name :

    SDC1 Human

    Description:

    Syndecan-1 Human Recombinant

    Heparan Sulfate proteoglycan fibroblast growth factor receptor, syndecan proteoglycan 1, Syndecan 1, SYND1, CD138 antigen, SDC.

    Product # :

    PRO-1065

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    Description

    SDC1 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (18-254) and having a molecular mass of 27kDa (molecular size on SDS-PAGE will appear higher).SDC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SDC1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD138 takes a part in cell adhesion. CD138 is expressed on the surface of pre-B cells and plasma cells but is absent from mature B cells. SDC1 is a selective marker for B cell lymphoblastic leukemia and lymphoplasmacytoid leukemia. SDC1 is missing from the apoptotic myeloma cells; therefore is a valuable marker for plasma cell and myeloma cells.

    • Synonyms

      Heparan Sulfate proteoglycan fibroblast growth factor receptor, syndecan proteoglycan 1, Syndecan 1, SYND1, CD138 antigen, SDC.

    • 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 MGSHMQPALP QIVATNLPPE DQDGSGDDSD NFSGSGAGAL QDITLSQQTP STWKDTQLLT AIPTSPEPTG LEATAASTST LPAGEGPKEG EAVVLPEVEP GLTAREQEAT PRPRETTQLP TTHQASTTTA TTAQEPATSH PHRDMQPGHH ETSTPAGPSQ ADLHTPHTED GGPSATERAA EDGASSQLPA AEGSGEQDFT FETSGENTAV VAVEPDRRNQ SPVDQGATGA SQGLLDRKEV LG.

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    Sdc1 Human
  • View Data Sheet

    Name :

    ZNF346 Human

    Description:

    Zinc Finger Protein 346 Human Recombinant

    Zinc finger protein 346, JAZ, Zfp346, ZNF346.

    Product # :

    PRO-1685

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    Description

    ZNF346 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-294) and having a molecular mass of 35.3 kDa.ZNF346 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ASCC1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ZNF346 is a nucleolar, zinc finger protein which specially binds to double-stranded RNA or RNA/DNA fusions, instead of DNA alone. Zinc finger domains vital for dsRNA binding and essential for its nucleolar localization. ZNF346 takes part in cell growth and survival.

    • Synonyms

      Zinc finger protein 346, JAZ, Zfp346, ZNF346.

    • 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 MGSMEYPAPA TVQAADGGAA GPYSSSELLE GQEPDGVRFD RERARRLWEA VSGAQPVGRE EVEHMIQKNQ CLFTNTQCKV CCALLISESQ KLAHYQSKKH ANKVKRYLAI HGMETLKGET KKLDSDQKSS RSKDKNQCCP ICNMTFSSPV VAQSHYLGKT HAKNLKLKQQ STKVEALHQN REMIDPDKFC SLCHATFNDP VMAQQHYVGK KHRKQETKLK LMARYGRLAD PAVTDFPAGK GYPCKTCKIV LNSIEQYQAH VSGFKHKNQS PKTVASSLGQ IPMQRQPIQK DSTTLED.

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    Znf346 Human
  • View Data Sheet

    Name :

    IL1RL1 Human, Sf9

    Description:

    Interleukin-1 Receptor Like-1 Human Recombinant, Sf9

    IL33R, Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.

    Product # :

    CYT-984

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    Description

    IL 1RL1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-328 a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 318 amino acids and having a molecular mass of 36.0kDa.IL 1RL1 shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL1RL1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.

    • Synonyms

      IL33R, Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.

    • 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

      KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS LEHHHHHH.

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    Il1Rl1 Human Sf9
  • View Data Sheet

    Name :

    MYL5 Human

    Description:

    Myosin Light Chain 5 Human Recombinant

    Myosin light chain 5, Myosin regulatory light chain 5, Superfast myosin regulatory light chain 2, MYLC2, MyLC-2, MYL5.

    Product # :

    PRO-916

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    Description

    MYL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-132 a.a.) and having a molecular mass of 17.4kDa.MYL5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYL5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 30% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin regulatory light chain 5 (MYL5) is a hexameric ATPase cellular motor protein. Myosin is comprised of 2 heavy chains, 2 nonphosphorylatable alkali light chains, and 2 phosphorylatable regulatory light chains. MYL5 is a regulatory light chain and is expressed in the fetal muscle and in the adult retina, cerebellum, and basal ganglia. The reconstitution of myosin with MYL5 or alkali light chain increases filament velocity to intermediate rates, and the re-addition of both classes of light chains fully reinstates the original sliding pace.

    • Synonyms

      Myosin light chain 5, Myosin regulatory light chain 5, Superfast myosin regulatory light chain 2, MYLC2, MyLC-2, MYL5.

    • 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 MGSHMDQNRD GFIDKEDLKD TYASLGKTNV KDDELDAMLK EASGPINFTM FLNLFGEKLS GTDAEETILN AFKMLDPDGK GKINKEYIKR LLMSQADKMT AEEVDQMFQF ASIDVAGNLD YKALSYVITH GEEKEE.

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    Myl5 Human
  • View Data Sheet

    Name :

    SPOCK3 Mouse

    Description:

    Sparc/Osteonectin 3 Mouse Recombinant

    Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.

    Product # :

    PRO-2328

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    Description

    SPOCK3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (22-436 a.a.) and having a molecular mass of 47.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).SPOCK3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SPOCK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Testican-3 (Spock3) is a nervous system-expressed heparan sulfate proteoglycan belonging to a subgroup of the BM-40/SPARC/osteonectin family, whose role of in brain development is unclear. Spock3 inhibits the processing of pro-matrix metalloproteinase 2(MMP-2) by MT1-MMP and MT3-MMP. Spock3 is mostly confined to the developmental stage of the brain.

    • Synonyms

      Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.

    • 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

      AAAAVAVAGG RSDGGNFLDE KQWLTTISQY DKEVGQWNKF RDEVEDDYFR TWNPGKPFDQ ALDPAKDPCL KTKCSRHKVC ITQDAQTALC ISHRRLTHSM KEVGGSHKQW RGLPSSTCKP CPIAYASPVC GSDGHSYSSQ CKLEYQACVL GKQISIKCEG RCPCPSDKSM NIGRNVKRAC
      SDLEFREVAN RLRDWFKALH ESGSQNKKTK ALLRPERSRF DTSILPICKD SLGWMFNRLD TNYDLLLDQS ELGSIYLDKN EQCTKAFFNS CDTYKDSLIS NNEWCYCFQR QQDPPCHTEL SNIQKRQGIK KLLGQYIPLC DEDGYYKPTQ CHGSVGQCWC VDRYGNEVVG SRINGVADCA
      IDFEISGDFA SGDFREWTDD EGEEDDIMND KDDIEDDDED EGDDDDDGDV HDGYILEHHH HHH

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    Spock3 Mouse
  • View Data Sheet

    Name :

    SLAMF1 Human, Sf9

    Description:

    SLAMF1 Human Recombinant, Sf9

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

    Product # :

    PRO-2393

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    Description

    SLAMF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 226 amino acids (21-237a.a.) and having a molecular mass of 25.3kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).SLAMF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SLAMF1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Slamf1 Human Sf9
  • View Data Sheet

    Name :

    GPC4 511 aa Human

    Description:

    Glypican-4 511 aa Human Recombinant

    Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.

    Product # :

    PRO-2034

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    Description

    Glypican-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala19-Ser529) containing 521 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 58.7kDa.

    Source

    Escherichia Coli.

    Formulation

    Glypican-4 filtered (0.4µm) solution at a concentration of 0.2mg/ml in 20mM Tris buffer, 50mM NaCl, pH 8.0 and 5mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.

    • Synonyms

      Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.

    • Physical Appearance

      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

      MKHHHHHHASALLAAELKSK SCSEVRRLYV SKGFNKNDAP LHEINGDHLK ICPQGSTCCS QEMEEKYSLQ SKDDFKSVVS EQCNHLQAVF ASRYKKFDEF FKELLENAEK SLNDMFVKTY GHLYMQNSEL FKDLFVELKR YYVVGNVNLE EMLNDFWARL LERMFRLVNS QYHFTDEYLE CVSKYTEQLK PFGDVPRKLK LQVTRAFVAA RTFAQGLAVA GDVVSKVSVV NPTAQCTHAL LKMIYCSHCR GLVTVKPCYN YCSNIMRGCL ANQGDLDFEW NNFIDAMLMV AERLEGPFNI ESVMDPIDVK ISDAIMNMQD NSVQVSQKVF QGCGPPKPLP AGRISRSISE SAFSARFRPH HPEERPTTAA GTSLDRLVTD VKEKLKQAKK FWSSLPSNVC NDERMAAGNG NEDDCWNGKG KSRYLFAVTG NGLANQGNNP EVQVDTSKPD ILILRQIMAL RVMTSKMKNA YNGNDVDFFD ISDESSGEGS GSGCEYQQCP SEFDYNATDH AGKSANEKAD 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.

    Gpc4 511 Aa Human
  • View Data Sheet

    Name :

    EFNB1 Human, Sf9

    Description:

    Ephrin-B1 Human Recombinant, Sf9

    Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2. 

    Product # :

    PRO-2543

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EFNB1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.

    • Synonyms

      Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 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

      ADPLAKNLEP VSWSSLNPKF LSGKGLVIYP KIGDKLDIIC PRAEAGRPYE YYKLYLVRPE QAAACSTVLD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL EFKKHHDYYI TSTSNGSLEG LENREGGVCR TRTMKIIMKV GQDPNAVTPE QLTTSRPSKE ADNTVKMATQ APGSRGSLGD
      SDGKHETVNQ EEKSGPGASG GSSGDPDGFF NSKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN
      QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

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

    Ephrin B1
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