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Search results

1000 results found for “Epigen”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Rantes Human, His

    Description:

    Rantes Human Recombinant (CCL5), His Tag

    Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.

    Product # :

    CHM-361

    Price :

    Quantity :

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    Description

    Rantes Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 68 amino acids fragment (24-91) having a total molecular mass of 17.5kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.The Rantes His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Rantes His-Tag protein is supplied in 1x PBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

    • Synonyms

      Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.

    • 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. Please avoid 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.

    Rantes Human His
  • View Data Sheet

    Name :

    SIGLEC5 Human

    Description:

    Sialic Acid Binding Ig Like Lectin 5 Human Recombinant

    Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.

    Product # :

    PRO-2432

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
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    Description

    SIGLEC5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 667 amino acids (17-441a.a.) and having a molecular mass of 74.2kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). SIGLEC5 is expressed with a 239 amino acid hIgG-His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SIGLEC5 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sialic Acid Binding Ig Like Lectin 5, also known as SIGLEC5 is a member of the immunoglobulin superfamily and SIGLEC family. SIGLEC5 contains of 2 Ig-like C2-type domains and 1 Ig-like V-type domain. In addition, SIGLEC5 is expressed by monocytic/myeloid lineage cells. SIGLEC5 is expressed at high levels in peripheral blood leukocytes, spleen, and at lower levels in lymph node, appendix, pancreas, lung, and thymus.

    • Synonyms

      Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.

    • 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

      ADLEKPVYEL QVQKSVTVQE GLCVLVPCSF SYPWRSWYSS PPLYVYWFRD GEIPYYAEVV ATNNPDRRVK PETQGRFRLL GDVQKKNCSL SIGDARMEDT GSYFFRVERG RDVKYSYQQN KLNLEVTALI EKPDIHFLEP LESGRPTRLS CSLPGSCEAG PPLTFSWTGN ALSPLDPETT RSSELTLTPR PEDHGTNLTC QMKRQGAQVT TERTVQLNVS YAPQTITIFR NGIALEILQN TSYLPVLEGQ ALRLLCDAPS NPPAHLSWFQ GSPALNATPI SNTGILELRR VRSAEEGGFT CRAQHPLGFL QIFLNLSVYS LPQLLGPSCS WEAEGLHCRC SFRARPAPSL CWRLEEKPLE GNSSQGSFKV NSSSAGPWAN SSLILHGGLS SDLKVSCKAW NIYGSQSGSV LLLQGRSNLG TGVVPAALLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

    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.

    Siglec5 Human
  • View Data Sheet

    Name :

    SIGLEC10 Human

    Description:

    Sialic Acid Binding Ig Like Lectin 10 Human Recombinant

    SIGLEC10, PRO940, SLG2, SIGLEC-10, Sialic acid-binding Ig-like lectin 10 isoform 3, Siglec-like protein 2.

    Product # :

    PRO-2610

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    SIGLEC10 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 678 amino acids (17-455 a.a.) and having a molecular mass of 75.6kDa. SIGLEC10 is expressed with a 239 hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The SIGLEC10 solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sialic Acid Binding Ig Like Lectin 10(SIGLEC10) is a part of the immunoglobulin superfamily that is expressed on eosinophils, B cells, monocytes and neutrophils. SIGLEC10 is an adhesion molecule that mediates sialic-acid dependent binding to cells.SIGLEC10 is a ligand for CD52, the target of the therapeutic monoclonal antibody Alemtuzumab. Also, it binds to Vascular adhesion protein 1 (VAP-1) and to the co-stimulatory molecule CD24.This binding is modulated by cis interactions of SIGLEC10 with sialated molecules on the same cell.

    • Synonyms

      SIGLEC10, PRO940, SLG2, SIGLEC-10, Sialic acid-binding Ig-like lectin 10 isoform 3, Siglec-like protein 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

      MDGRFWIRVQ ESVMVPEGLC ISVPCSFSYP RQDWTGSTPA YGYWFKAVTE TTKGAPVATN
      HQSREVEMST RGRFQLTGDP AKGNCSLVIR DAQMQDESQY FFRVERGSYV RYNFMNDGFF
      LKVTALTQKP DVYIPETLEP GQPVTVICVF NWAFEECPPP SFSWTGAALS SQGTKPTTSH
      FSVLSFTPRP QDHNTDLTCH VDFSRKGVSA QRTVRLRVAY APRDLVISIS RDNTPALEPQ
      PQGNVPYLEA QKGQFLRLLC AADSQPPATL SWVLQNRVLS SSHPWGPRPL GLELPGVKAG
      DSGRYTCRAE NRLGSQQRAL DLSVQYPPEN LRVMVSQANR TVLENLGNGT SLPVLEGQSL
      CLVCVTHSSP PARLSWTQRG QVLSPSQPSD PGVLELPRVQ VEHEGEFTCH ARHPLGSQHV
      SLSLSVHYKK GLISTAFSNL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR
      TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN
      GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS
      DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

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

    Siglec10 Human
  • View Data Sheet

    Name :

    sRAGE Mouse

    Description:

    Advanced Glycosylation End Product-Specific Receptor Mouse Recombinant

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

    Product # :

    PRO-2781

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
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    • purity
    • More Info

    Description

    sRAGE Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing 317 amino acids (Gly23–Asp333) and having a molecular mass of 34.0kDa. sRAGE Mouse is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    The filtered (0.4µm) concentrated protein solution was lyophilized with PBS, PH 7.4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • 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

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

    • Amino Acid Sequence

      GQNITARIGE PLVLSCKGAP KKPPQQLEWK LNTGRTEAWK VLSPQGGPWD SVARILPNGS LLLPATGIVD EGTFRCRATN RRGKEVKSNY RVRVYQIPGK PEIVDPASEL TASVPNKVGT CVSEGSYPAG TLSWHLDGKL LIPDGKETLV KEETRRHPET GLFTLRSELT VIPTQGGTHP TFSCSFSLGL PRRRPLNTAP IQLRVREPGP PEGIQLLVEP EGGIVAPGGT VTLTCAISAQ PPPQVHWIKD GAPLPLAPSP VLLLPEVGHE DEGTYSCVAT HPSHGPQESP PVSIRVTETG DEGPAEGEGL DHHHHHH.

    • Background

      The soluble receptor for advanced glycation end products, sRAGE, is a multifunctional protein known for its involvement in diverse physiological processes, including inflammation, aging, and chronic diseases. Research using mouse models has been instrumental in unraveling the complexities of sRAGE biology and its implications for health and disease. This study aims to provide a comprehensive exploration of sRAGE in mouse physiology, shedding light on its various functions and potential applications in understanding aging and disease mechanisms.

      The primary objective of this research is to elucidate the impact of sRAGE in mouse models on aging processes. In vivo experiments utilizing genetically modified mice with altered sRAGE expression will be conducted to investigate how sRAGE influences the aging process, including effects on tissue homeostasis, oxidative stress, and longevity. Understanding these mechanisms is fundamental for deciphering the role of sRAGE in age-related diseases.

      The second objective is to assess the clinical relevance of sRAGE in mouse models of chronic diseases. Mouse models of diseases such as diabetes, Alzheimer's disease, and cancer will be employed to explore how sRAGE modulation affects disease progression, inflammation, and tissue damage. These investigations may provide valuable insights into potential therapeutic strategies targeting sRAGE in various chronic diseases.

      The third objective is to explore the broader implications of sRAGE in mouse physiology, including its effects on immunity, tissue repair, and metabolic regulation. Research will investigate its roles in immune cell function, wound healing, and glucose homeostasis. Understanding the multifaceted properties of sRAGE in mouse models may open new avenues for therapeutic interventions in various health and disease contexts.

      By delving into the diverse functions of sRAGE in mouse physiology, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for age-related diseases and chronic conditions influenced by sRAGE.

    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.

    Srage Mouse
  • View Data Sheet

    Name :

    ICOSLG Human

    Description:

    Inducible T-Cell Costimulator Ligand Human Recombinant

    Inducible T-Cell Costimulator Ligand, B7-Related Protein 1, B7 Homolog 2, B7-Like Protein Gl50, B7 Homologue 2, B7RP-1, ICOSL, B7-H2, B7RP1, B7H2, Transmembrane Protein B7-H2 ICOS Ligand, Inducible T-Cell Co-Stimulator Ligand, CD275 Antigen, ICOS Ligand, KIAA0653, ICOS-L, CD275, LICOS, GL50, ICOS ligand, B7 homolog 2, B7-H2, B7-like protein Gl50, B7-related protein 1, B7RP-1.

    Product # :

    PRO-2431

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    Description

    ICOSLG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 480 amino acids (19-256a.a.) and having a molecular mass of 53.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ICOSLG is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inducible T-Cell Costimulator Ligand also known as ICOSLG, is part of the B7 family of co-stimulatory molecules related to B7-1 and B7-2. ICOSLG is a transmembrane glycoprotein with extracellular IgV and IgC domains, in addition it binds to ICOS on activated T cells. The dependent signaling of ICOSLG takes part in a proliferative response.

    • Synonyms

      Inducible T-Cell Costimulator Ligand, B7-Related Protein 1, B7 Homolog 2, B7-Like Protein Gl50, B7 Homologue 2, B7RP-1, ICOSL, B7-H2, B7RP1, B7H2, Transmembrane Protein B7-H2 ICOS Ligand, Inducible T-Cell Co-Stimulator Ligand, CD275 Antigen, ICOS Ligand, KIAA0653, ICOS-L, CD275, LICOS, GL50, ICOS ligand, B7 homolog 2, B7-H2, B7-like protein Gl50, B7-related protein 1, B7RP-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

      ADPDTQEKEV RAMVGSDVEL SCACPEGSRF DLNDVYVYWQ TSESKTVVTY HIPQNSSLEN VDSRYRNRAL MSPAGMLRGD FSLRLFNVTP QDEQKFHCLV LSQSLGFQEV LSVEVTLHVA ANFSVPVVSA PHSPSQDELT FTCTSINGYP RPNVYWINKT DNSLLDQALQ NDTVFLNMRG LYDVVSVLRI ARTPSVNIGC CIENVLLQQN LTVGSQTGND IGERDKITEN PVSTGEKNAA TLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.

    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.

    Icoslg Human
  • View Data Sheet

    Name :

    SURF1 Human

    Description:

    Surfeit-1 Human Recombinant

    SURF1, SURF-1, Surfeit locus protein 1, Surfeit 1.

    Product # :

    PRO-764

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    Description

    Surfeit-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 215 amino acids (80-273 a.a.) and having a molecular mass of 24.3 kDa. The Surfeit-1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Surfeit-1 solution contains 20 mM Tris-HCl buffer (pH 8.0), 0.1M Nacl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SURF1 plays a role in the biogenesis of the COX complex. SURF1 is found in the inner mitochondrial membrane and takes part in the biogenesis of the cytochrome c oxidase complex. SURF1 is shares a bidirectional promoter with SURF2 on the opposite strand. Defects in this SURF1 cause Leigh syndrome, a rigorous neurological disorder that is generally associated with systemic cytochrome c oxidase deficiency.

    • Synonyms

      SURF1, SURF-1, Surfeit locus protein 1, Surfeit 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQVQRRKWKL NLIAELESRV LAEPVPLPAD PMELKNLEYR PVKVRGCFDH SKELYMMPRT MVDPVREARE GGLISSSTQS GAYVVTPFHC TDLGVTILVN RGFVPRKKVN PETRQKGQIE GEVDLIGMVR LTETRQPFVP ENNPERNHWH YRDLEAMARI TGAEPIFIDA NFQSTVPGGP IGGQTRVTLR NEHLQ.

    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.

    Surf1 Human
  • View Data Sheet

    Name :

    MOG Antibody

    Description:

    myelin oligodendrocyte glycoprotein, Mouse Antibody

    MGC26137, MOG, MYELIN-OLIGODENDROCYTE GLYCOPROTEIN.

    Product # :

    ANT-199

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    Formulation

    1mg/ml in PBS (after reconstitution).

    More Info

    • Introduction

      MOG is a membrane protein expressed on the oligodendrocyte cell surface and the outermost surface of myelin sheaths. Due to this localization, it is a primary target antigen involved in immune-mediated demyelination. MOG is involved in completion and maintenance of the myelin sheath and in cell-cell communication. Alternatively spliced transcript variants encoding different isoforms have been identified Minor component of the myelin sheath is involved in completion and/or maintenance of the myelin sheath and in cell- cell communication.

    • Synonyms

      MGC26137, MOG, MYELIN-OLIGODENDROCYTE GLYCOPROTEIN.

    • Solubility

      Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      synthetic pMOG 35-55.

    • Ig Subclass

      mouse IgG1.

    • Clone

      NYRMOG.

    • Applications

      Direct ELISA, Western Blot, Immuneprecipitation, immunohistochemistry.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Antibody Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    • Purification Method

      Ion exchange column.

    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.

    Mog Antibody
  • View Data Sheet

    Name :

    Thymosin beta 4

    Description:

    Thymosin β4

    Thymosin beta-4. TB500, TB-500

    Product # :

    HOR-275

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    Description

    Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.

    Formulation

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

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.

    • Synonyms

      Thymosin beta-4. TB500, TB-500

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.

    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.

    Thymosin Beta 4
  • View Data Sheet

    Name :

    VEGF (121 a.a.) Human

    Description:

    Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant

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

    Product # :

    CYT-343

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    Description

    Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor -121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR R

    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.

    Vegf121 Human
  • View Data Sheet

    Name :

    VEGF (121 a.a.) Mouse

    Description:

    Vascular Endothelial Growth Factor (121 a.a.) Mouse Recombinant

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

    Product # :

    CYT-574

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    Description

    Vascular Endothelial Growth Factor-121 Mouse Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 28.4 kDa.Recombinant Mouse VEGF-121 is a truncated version of Murine VEGF-165.The VEGF-121 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized VEGF-121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 VEGF-121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKRPR R.

    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.

    Vegf121 Mouse
  • View Data Sheet

    Name :

    CA10 Human

    Description:

    Carbonic Anhydrase X Human Recombinant

    Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.

    Product # :

    ENZ-1189

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    Description

    CA10 Human Recombinant is a single, glycosylated polypeptide chain containing 317 amino acids (22-328a.a) and having a molecular mass of 36.3kDa (calculated). CA10 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    CA10 protein solution (0.5mg/ml) is filtered in Phosphate-Buffered Saline pH 7.4 and 10% (w/v) glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH8.0 at 37℃.

    More Info

    • Synonyms

      Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      DGSMQQNSPK IHEGWWAYKE VVQGSFVPVP SFWGLVNSAW NLCSVGKRQS PVNIETSHMI FDPFLTPLRI NTGGRKVSGT MYNTGRHVSL RLDKEHLVNI SGGPMTYSHR LEEIRLHFGS EDSQGSEHLL NGQAFSGEVQ LIHYNHELYT NVTEAAKSPN GLVVVSIFIK VSDSSNPFLN RMLNRDTITR ITYKNDAYLL QGLNIEELYP ETSSFITYDG SMTIPPCYET ASWIIMNKPV YITRMQMHSL RLLSQNQPSQ IFLSMSDNFR PVQPLNNRCI RTNINFSLQG KDCPNNRAQK LQYRVNEWLL KHHHHHH

    • Background

      Carbonic anhydrases (CAs) are a family of enzymes that play a crucial role in regulating pH balance and carbon dioxide transport in various tissues and organs. Carbonic anhydrase X (CA10) is a less-studied member of this family, and this research aims to explore its structure, function, and implications in metabolism and disease. Understanding the molecular mechanisms and regulatory roles of CA10 can provide valuable insights into its potential as a therapeutic target for various disorders.

      Structure and Expression of Carbonic Anhydrase X:

      CA10, also known as mitochondrial carbonic anhydrase, is a membrane-associated protein predominantly found in the mitochondria of various tissues, including the liver, kidney, and brain. It possesses the characteristic zinc-binding catalytic domain found in other CAs. However, CA10 has distinct features, including a unique N-terminal mitochondrial targeting sequence, suggesting its specific role within mitochondria.

      Role of Carbonic Anhydrase X in Metabolism:

      CA10 is involved in the regulation of pH and bicarbonate concentrations within the mitochondrial matrix, impacting mitochondrial metabolism. It catalyzes the reversible hydration of carbon dioxide to bicarbonate, facilitating the exchange of carbon dioxide between the mitochondria and the cytoplasm. This process is vital for maintaining acid-base homeostasis and efficient energy production through oxidative phosphorylation.

      Implications of Carbonic Anhydrase X in Disease:

      Emerging evidence suggests that CA10 may be implicated in various pathological conditions. Alterations in CA10 expression or activity have been associated with metabolic disorders, including obesity and diabetes. Furthermore, dysregulation of mitochondrial function and pH homeostasis, in which CA10 plays a role, have been linked to neurodegenerative diseases, cancer, and cardiovascular disorders. Elucidating the precise contributions of CA10 in these pathologies is an area of active investigation.

      Therapeutic Potential of Carbonic Anhydrase X:

      The unique properties and expression patterns of CA10 make it an intriguing target for therapeutic interventions. Modulating CA10 activity or expression could have implications in metabolic disorders, where the manipulation of mitochondrial function and pH regulation could offer therapeutic benefits. Developing selective inhibitors or activators of CA10 could be explored to regulate its enzymatic activity and modulate mitochondrial metabolism.

      Challenges and Future Directions:

      Although CA10 shows promise as a therapeutic target, several challenges remain. The elucidation of the precise regulatory mechanisms and signaling pathways involving CA10 within mitochondria is necessary for a comprehensive understanding of its function. Additionally, the development of specific modulators that selectively target CA10 without affecting other CAs or disrupting physiological processes is a critical consideration.

      Conclusion:

      The study of CA10 protein provides valuable insights into its distinct role in mitochondrial metabolism and disease pathogenesis. Understanding the molecular mechanisms and functional implications of CA10 opens avenues for the development of targeted therapies for metabolic disorders, neurodegenerative diseases, cancer, and cardiovascular disorders. Further research on CA10, its interactions, and its modulation in pathological conditions will contribute to the development of novel therapeutic interventions to improve patient outcomes.

    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.

    Ca10 Human
  • View Data Sheet

    Name :

    hCG Protein

    Description:

    Chorionic Gonadotropin Human

    Chorionic gonadotropin, hCG, CG.

    Product # :

    HOR-250

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    • Activity Assay

    Description

    Human Chorionic Gonadotropin is produced from a sterile preparation of placental glucoprotein urine of pregnant women having a total molecular mass of 36,700 Dalton. The hCG consists of 237 amino acids, a chain-92 amino acids and b chain-145 amino acids. The hCG is purified by proprietary chromatographic techniques.

    Source

    Urine of pregnant women.

    Formulation

    The hCG was lyophilized with no additives.

    Biological Activity

    The activity was found to be 5212IU/mg.

    Activity Assay

    hcg activity assay - Product image 1
    hcg bioactivity assay - Product image 2

    More Info

    • Introduction

      Human chorionic gonadotropin (hCG) is a peptide hormone produced in pregnancy, that is made by the embryosoon after conception and later by the syncytiotrophoblast(part of the placenta). Its role is to prevent the disintegration of the corpus luteumof the ovaryand thereby maintain progesterone production that is critical for a pregnancy in humans. hCG may have additional functions, for instance it is thought that it affects the immune tolerance of the pregnancy. Early pregnancy testing generally is based on the detection or measurement of hCG.

    • Synonyms

      Chorionic gonadotropin, hCG, CG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Contaminants

      Free of: HbsAg and antibodies to HIV and HCV.

    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.

    Hcg Human
  • View Data Sheet

    Name :

    IFN tau Ovine

    Description:

    IFN-Tau Ovine Recombinant

    IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.

    Product # :

    CYT-377

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    Description

    IFN-Tau Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19914.7 Dalton.The IFN-Tau is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from (1mg/ml) solution containing PBS pH-7.4.

    Purity

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

    Biological Activity

    The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.

    More Info

    • Introduction

      IFN-tau is also known as TP-1 (trophoblast protein-1) is a new class of type I IFN that is secreted by the trophoblast and is the signal for maternal recognition of pregnancy in sheep. IFN- tau has potent immunosuppressive and antiviral activities similar to other type I IFN but is less cytotoxic than IFN-alpha and IFN-beta. The current investigation concerns the effect of recombinant ovine IFN- tau (rOIFN- tau) on the modulation of MHC class I and II expression on cloned mouse cerebrovascular endothelial (CVE) cells.
      IFN-tau induced tyrosine phosphorylation of Stat1 and upregulated the expression of MHC class I on CVE. One proposed action by which type I IFN reduces the relapse rate in MS is via interference with IFN-?-induced MHC class II expression. IFN- tau was shown to downregulate IFN-?-induced MHC class II expression on CVE and, hence, may be of potential therapeutic value in downregulating inflammation in the central nervous system (CNS). IFN- tau did not upregulate the expression of MHC class II on CVE. IFN- tau also inhibited the replication of Theiler's virus in CVE.

    • Synonyms

      IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.

    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.

    Interferon Tau Ovine
  • View Data Sheet

    Name :

    Clusterin Rat

    Description:

    Clusterin Rat Recombinant

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

    Product # :

    CYT-437

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    Description

    The Clusterin Rat His-Tagged Fusion Protein, produced in E.coli, is 26.5kDa protein containing 215 amino acid residues of the APO-J Rat and 25 additional amino acid residues: N-terminal fusion of T7-Tag (16AA) and C-terminal fusion of His-Tag (9AA). (Underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.02M Tris buffer and 0.05M NaCl, pH 7.5.

    Purity

    Greater than 90% as determined by SDS PAGE.

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

    • Physical Appearance

      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 a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MASMTGGQQM GRDPNSSSPF YFWMNGDRID SLLESDRQQS QVLDAMQDSF TRASGIIDTL FQDRFFTHEPQDIHHFSPMG FPHKRPHLLY PKSRLVRSLM PLSHYGPLSF HNMFQPFFDM IHQAQQAMDV QLHSPALQFPDVDFLKEGED DRTVCKEIRH NSTGCLKMKG QCEKCQEILS VDCSTNNPAQ ANLRQELNDS LQVAERLTQQYNELLHSLQS KMLNTSSLLE QALEHHHHHH.

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 26.5kDa.

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

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

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

      What is the amino acid sequence of CLUSTERIN Protein?
      MASMTGGQQM GRDPNSSSPF YFWMNGDRID SLLESDRQQS QVLDAMQDSF TRASGIIDTL FQDRFFTHEPQDIHHFSPMG FPHKRPHLLY PKSRLVRSLM PLSHYGPLSF HNMFQPFFDM IHQAQQAMDV QLHSPALQFPDVDFLKEGED DRTVCKEIRH NSTGCLKMKG QCEKCQEILS VDCSTNNPAQ ANLRQELNDS LQVAERLTQQYNELLHSLQS KMLNTSSLLE QALEHHHHHH.

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

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

    Clusterin Rat
  • View Data Sheet

    Name :

    Bet v 2.0101

    Description:

    Profilin-1 Recombinant

    Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.

    Product # :

    PRO-2283

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    Description

    Recombinant Profilin-1 produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 15,625 Dalton. Bet v 2.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bet v 2.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Profilin-1 (Bet v 2.0101) binds to actin and affects the structure of the cytoskeleton. At high concentrations, profiling-1 averts the polymerization of actin, whereas it augments it at low concentrations. By binding to PIP2, Profilin-1 inhibits the creation of IP3 and DG.

    • Synonyms

      Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

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

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

    Bet V 20101
  • View Data Sheet

    Name :

    ANXA1 Human

    Description:

    Annexin A1 Human Recombinant

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

    Product # :

    PRO-679

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Anxa1 Human
  • View Data Sheet

    Name :

    MIP 5 Human

    Description:

    Macrophage Inflammatory Protein-5 Human Recombinant (CCL15)

    Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.

    Product # :

    CHM-230

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    Description

    Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids and having a molecular mass of 10.1 kDa. The MIP5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIP5 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 100mM NaCl.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.

    • Synonyms

      Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL15 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 MIP5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.

    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 5 Human
  • View Data Sheet

    Name :

    IFNG Canine, His

    Description:

    Interferon-gamma Canine Recombinant, His Tag

    Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma. 

    Product # :

    CYT-1022

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    Description

    IFNG Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids (24-166 a.a) and having a molecular mass of 19.3kDa. IFNG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IFNG protein solution (0.5mg/ml) contains 20mM MES (pH6.0), 20% glycerol, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
      IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.

    • Synonyms

      Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

    • 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 MGSQAMFFKE IENLKEYFNA SNPDVSDGGS LFVDILKKWR EESDKTIIQS QIVSFYLKLF DNFKDNQIIQ RSMDTIKEDM LGKFLNSSTS KREDFLKLIQ IPVNDLQVQR KAINELIKVM NDLSPRSNLR KRKRSQNLFR GRRASK.

    • Background

      What is the molecular weight/Mw of IFNG CANINE, HIS Protein?
      IFNG CANINE, HIS Protein has a total Mw of 19.3kDa.

      What is the source or expression system of IFNG CANINE, HIS Protein?
      Escherichia Coli.

      What is the Purity of IFNG CANINE, HIS Protein?
      IFNG CANINE, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNG CANINE, HIS Protein?
      The biological functionality of IFNG CANINE, HIS Protein will be determined in the future.

      What is the amino acid sequence of IFNG CANINE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSQAMFFKE IENLKEYFNA SNPDVSDGGS LFVDILKKWR EESDKTIIQS QIVSFYLKLF DNFKDNQIIQ RSMDTIKEDM LGKFLNSSTS KREDFLKLIQ IPVNDLQVQR KAINELIKVM NDLSPRSNLR KRKRSQNLFR GRRASK.

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

      What is the endotoxin level for IFNG CANINE, HIS Protein?
      The endotoxin level is minimal, IFNG CANINE, HIS 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.

    Canine Ifng
  • View Data Sheet

    Name :

    Omentin Human

    Description:

    Omentin Human Recombinant

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

    Product # :

    CYT-301

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    Description

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

    Source

    E.Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

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

    Omentin Human
  • View Data Sheet

    Name :

    CEA Human, His

    Description:

    Carcinoembryonic Antigen Human Recombinant, His Tag

    Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.

    Product # :

    PRO-2407

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    Description

    CEA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 659 amino acids (35-685a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-150kDa). CEA is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CEA 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.

    More Info

    • Introduction

      Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
      There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
      The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
      CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
      The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
      Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed.

    • Synonyms

      Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.

    • 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

      KLTIESTPFN VAEGKEVLLL VHNLPQHLFG YSWYKGERVD GNRQIIGYVI GTQQATPGPA YSGREIIYPN ASLLIQNIIQ NDTGFYTLHV IKSDLVNEEA TGQFRVYPEL PKPSISSNNS KPVEDKDAVA FTCEPETQDA TYLWWVNNQS LPVSPRLQLS NGNRTLTLFN VTRNDTASYK CETQNPVSAR RSDSVILNVL YGPDAPTISP LNTSYRSGEN LNLSCHAASN PPAQYSWFVN GTFQQSTQEL FIPNITVNNS GSYTCQAHNS DTGLNRTTVT TITVYAEPPK PFITSNNSNP VEDEDAVALT CEPEIQNTTY LWWVNNQSLP VSPRLQLSND NRTLTLLSVT RNDVGPYECG IQNKLSVDHS DPVILNVLYG PDDPTISPSY TYYRPGVNLS LSCHAASNPP AQYSWLIDGN IQQHTQELFI SNITEKNSGL YTCQANNSAS GHSRTTVKTI TVSAELPKPS ISSNNSKPVE DKDAVAFTCE PEAQNTTYLW WVNGQSLPVS PRLQLSNGNR TLTLFNVTRN DARAYVCGIQ NSVSANRSDP VTLDVLYGPD TPIISPPDSS YLSGANLNLS CHSASNPSPQ YSWRINGIPQ QHTQVLFIAK ITPNNNGTYA CFVSNLATGR NNSIVKSITV SASGTSPGLS ALEHHHHHH.

    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.

    Ceacam5 Human
  • View Data Sheet

    Name :

    EGFL6 Human

    Description:

    EGF Like Domain Multiple 6 Human Recombinant

    EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.

    Product # :

    CYT-974

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    Description

    EGF Like Domain Multiple 6 Human Recombinant produced in HEK cells is a polypeptide chain starting at amino acid Asn at position 22 to amino acid Arg at position 363, fused to an FC, 6 x His-tag at C-terminus, containing a total of 348 amino acids and having a predicted molecular mass of 40-55kDa. The EGFL6 is purified by proprietary chromatographic techniques.

    Source

    HEK (Human embryonic kidney cells).

    Formulation

    The EGFL6 protein was lyophilized from a 0.2µm filtered solution in 20mM MES and 500mM NaCl, pH 6.0 with 5% Trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

    More Info

    • Introduction

      Epidermal Growth Factor­like Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.

    • Synonyms

      EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EGFL6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGFL6 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 EGFL6 in sterile PBS at 500µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential

      Abstract:

      This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.

      Introduction:

      Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.

      Protein Expression and Purification:

      The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.

      Receptor Binding Assays and Ligand Interaction:

      Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.

      Cellular Signaling Pathways and Responses:

      In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.

      Bioinformatics Insights and Structural Modeling:

      Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.

      Therapeutic Implications and Future Prospects:

      EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.

      Challenges and Future Directions:

      Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.

      Conclusion:

      A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.

      What is the molecular weight/Mw of EGFL6 HUMAN Protein?
      EGFL6 HUMAN Protein has a total Mw of 40-55kDa.

      What is the source or expression system of EGFL6 HUMAN Protein?
      HEK (Human embryonic kidney cells).

      What is the Purity of EGFL6 HUMAN Protein?
      EGFL6 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of EGFL6 HUMAN Protein?
      EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

      What is the amino acid sequence of EGFL6 HUMAN Protein?
      EGFL6 HUMAN Protein is composed from 348 amino acids.

      What applications can EGFL6 HUMAN Protein be used in?
      EGFL6 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EGFL6 HUMAN Protein?
      The endotoxin level is minimal, EGFL6 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.

    Egfl6 Human
  • View Data Sheet

    Name :

    EGFR Human Sf9

    Description:

    Epidermal Growth Factor Receptor Sf9 Human Recombinant

    Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.

    Product # :

    PKA-344

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    Description

    The EGFR contains the extracellular domain of the human EGFR (25-647 a.a.) excluding the signal peptide which is cleaved by the insect cells having an approximate Mw of 85kDa. The EGFR is fused to a C-terminal Strep-tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    ErbB1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1x PBS pH-7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, HBEGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.

    • Synonyms

      Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCK LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIAASW SHPQFEK.

    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.

    Egfr Human Sf9
  • View Data Sheet

    Name :

    HBXIP Human

    Description:

    Hepatitis B Virus x Interacting Protein Human Recombinant

    Ragulator complex protein LAMTOR5, Hepatitis B virus X-interacting protein, HBV X-interacting protein, HBX-interacting protein, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5, LAMTOR5, HBXIP, XIP.

    Product # :

    HBV-235

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    • More Info

    Description

    HBXIP Human Recombinant produced in E. coli is a single polypeptide chain containing 197 amino acids (aa 1-173) and having a molecular mass of 20.7kDa.HBXIP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HBXIP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM EDTA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hepatitis B virus x interacting protein (HBXIP) forms a complex with the C-terminus of hepatitis B virus X (HBX) protein. HBXIP negatively regulates HBX activity and changes the replicative life cycle of the virus. Furthermore, HBXIP is involved in bipolar spindle formation and regulates centrosome dynamics and cytokinesis in cells, possibly due to interaction with Dynein light chain. HBXIP is highly expressed in the skeletal and cardiac muscle, followed by pancreas, kidney, liver, brain, placenta and lung. HBXIP has elevated levels in both cancerous and non-cancerous liver tissue of patients with chronic HBV infection compared with hepatic tissue without HBV infection.

    • Synonyms

      Ragulator complex protein LAMTOR5, Hepatitis B virus X-interacting protein, HBV X-interacting protein, HBX-interacting protein, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5, LAMTOR5, HBXIP, XIP.

    • 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 MGSHMEPGAG HLDGHRAGSP SLRQALCDGS AVMFSSKERG RCTVINFVPL EAPLRSTPRS RQVTEACGGE GRAVPLGSEP EWSVGGMEAT LEQHLEDTMK NPSIVGVLCT DSQGLNLGCR GTLSDEHAGV ISVLAQQAAK LTSDPTDIPV VCLESDNGNI MIQKHDGITV AVHKMAS.

    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.

    HBXIP Human
  • View Data Sheet

    Name :

    Leptin Horse

    Description:

    Leptin Horse Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-504

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    Description

    Leptin Horse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Protein content

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

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

    Leptin Horse
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